CA2523001C - Therapeutic use of anti-cs1 antibodies - Google Patents
Therapeutic use of anti-cs1 antibodies Download PDFInfo
- Publication number
- CA2523001C CA2523001C CA2523001A CA2523001A CA2523001C CA 2523001 C CA2523001 C CA 2523001C CA 2523001 A CA2523001 A CA 2523001A CA 2523001 A CA2523001 A CA 2523001A CA 2523001 C CA2523001 C CA 2523001C
- Authority
- CA
- Canada
- Prior art keywords
- antibody
- seq
- cells
- antibodies
- antigen binding
- Prior art date
- Legal status (The legal status is an assumption and is not a legal conclusion. Google has not performed a legal analysis and makes no representation as to the accuracy of the status listed.)
- Expired - Lifetime
Links
- 230000001225 therapeutic effect Effects 0.000 title description 15
- 230000027455 binding Effects 0.000 claims abstract description 117
- 238000009739 binding Methods 0.000 claims abstract description 115
- 239000012634 fragment Substances 0.000 claims abstract description 70
- 239000000427 antigen Substances 0.000 claims abstract description 63
- 108091007433 antigens Proteins 0.000 claims abstract description 61
- 102000036639 antigens Human genes 0.000 claims abstract description 61
- 206010028980 Neoplasm Diseases 0.000 claims abstract description 52
- 208000023275 Autoimmune disease Diseases 0.000 claims abstract description 44
- 201000011510 cancer Diseases 0.000 claims abstract description 30
- 239000008194 pharmaceutical composition Substances 0.000 claims abstract description 7
- 108090000623 proteins and genes Proteins 0.000 claims description 257
- 102000004169 proteins and genes Human genes 0.000 claims description 165
- 206010035226 Plasma cell myeloma Diseases 0.000 claims description 97
- 125000003275 alpha amino acid group Chemical group 0.000 claims description 89
- 201000000050 myeloid neoplasm Diseases 0.000 claims description 73
- 238000011282 treatment Methods 0.000 claims description 61
- 108060003951 Immunoglobulin Proteins 0.000 claims description 47
- 102000018358 immunoglobulin Human genes 0.000 claims description 47
- 208000022559 Inflammatory bowel disease Diseases 0.000 claims description 42
- 208000034578 Multiple myelomas Diseases 0.000 claims description 29
- 150000001875 compounds Chemical class 0.000 claims description 29
- 210000004408 hybridoma Anatomy 0.000 claims description 27
- 210000004180 plasmocyte Anatomy 0.000 claims description 27
- 238000001514 detection method Methods 0.000 claims description 24
- 230000007423 decrease Effects 0.000 claims description 23
- 239000012636 effector Substances 0.000 claims description 23
- 206010039073 rheumatoid arthritis Diseases 0.000 claims description 23
- 230000028327 secretion Effects 0.000 claims description 20
- 239000000758 substrate Substances 0.000 claims description 18
- 206010025135 lupus erythematosus Diseases 0.000 claims description 17
- 102000004190 Enzymes Human genes 0.000 claims description 14
- 108090000790 Enzymes Proteins 0.000 claims description 14
- 210000000988 bone and bone Anatomy 0.000 claims description 11
- 206010020631 Hypergammaglobulinaemia benign monoclonal Diseases 0.000 claims description 7
- 201000005328 monoclonal gammopathy of uncertain significance Diseases 0.000 claims description 7
- 208000010626 plasma cell neoplasm Diseases 0.000 claims description 7
- 239000007850 fluorescent dye Substances 0.000 claims description 6
- 230000002285 radioactive effect Effects 0.000 claims description 6
- 208000007452 Plasmacytoma Diseases 0.000 claims description 5
- 208000033559 Waldenström macroglobulinemia Diseases 0.000 claims description 5
- 208000010839 B-cell chronic lymphocytic leukemia Diseases 0.000 claims description 4
- 239000003242 anti bacterial agent Substances 0.000 claims description 4
- 206010028417 myasthenia gravis Diseases 0.000 claims description 4
- 208000011580 syndromic disease Diseases 0.000 claims description 4
- 239000003053 toxin Substances 0.000 claims description 4
- 231100000765 toxin Toxicity 0.000 claims description 4
- 108700012359 toxins Proteins 0.000 claims description 4
- 208000023761 AL amyloidosis Diseases 0.000 claims description 3
- 208000035186 Hemolytic Autoimmune Anemia Diseases 0.000 claims description 3
- 208000005531 Immunoglobulin Light-chain Amyloidosis Diseases 0.000 claims description 3
- 208000031422 Lymphocytic Chronic B-Cell Leukemia Diseases 0.000 claims description 3
- 206010036673 Primary amyloidosis Diseases 0.000 claims description 3
- 229940127089 cytotoxic agent Drugs 0.000 claims description 3
- 239000003937 drug carrier Substances 0.000 claims description 3
- 201000006569 extramedullary plasmacytoma Diseases 0.000 claims description 3
- 208000025750 heavy chain disease Diseases 0.000 claims description 3
- 201000000564 macroglobulinemia Diseases 0.000 claims description 3
- 102000004882 Lipase Human genes 0.000 claims description 2
- 108090001060 Lipase Proteins 0.000 claims description 2
- 239000004367 Lipase Substances 0.000 claims description 2
- 239000002246 antineoplastic agent Substances 0.000 claims description 2
- 208000032852 chronic lymphocytic leukemia Diseases 0.000 claims description 2
- 235000019421 lipase Nutrition 0.000 claims description 2
- 230000009885 systemic effect Effects 0.000 claims description 2
- 238000012875 competitive assay Methods 0.000 claims 2
- 201000000448 autoimmune hemolytic anemia Diseases 0.000 claims 1
- 230000003115 biocidal effect Effects 0.000 claims 1
- 239000002254 cytotoxic agent Substances 0.000 claims 1
- 231100000599 cytotoxic agent Toxicity 0.000 claims 1
- 206010043554 thrombocytopenia Diseases 0.000 claims 1
- 238000000034 method Methods 0.000 abstract description 111
- 208000037265 diseases, disorders, signs and symptoms Diseases 0.000 abstract description 48
- 239000005557 antagonist Substances 0.000 abstract description 35
- 201000010099 disease Diseases 0.000 abstract description 32
- 230000004071 biological effect Effects 0.000 abstract description 11
- 101000633784 Homo sapiens SLAM family member 7 Proteins 0.000 abstract description 5
- 210000004027 cell Anatomy 0.000 description 297
- 150000007523 nucleic acids Chemical class 0.000 description 150
- 235000018102 proteins Nutrition 0.000 description 147
- 102000039446 nucleic acids Human genes 0.000 description 133
- 108020004707 nucleic acids Proteins 0.000 description 133
- 230000014509 gene expression Effects 0.000 description 132
- 241000282414 Homo sapiens Species 0.000 description 104
- 108090000765 processed proteins & peptides Proteins 0.000 description 82
- 239000000523 sample Substances 0.000 description 76
- 102000004196 processed proteins & peptides Human genes 0.000 description 74
- 229920001184 polypeptide Polymers 0.000 description 73
- 210000003719 b-lymphocyte Anatomy 0.000 description 62
- 239000002299 complementary DNA Substances 0.000 description 62
- 235000001014 amino acid Nutrition 0.000 description 60
- 108091034117 Oligonucleotide Proteins 0.000 description 57
- 238000004519 manufacturing process Methods 0.000 description 54
- 229940024606 amino acid Drugs 0.000 description 53
- 150000001413 amino acids Chemical class 0.000 description 52
- 210000001519 tissue Anatomy 0.000 description 50
- LFQSCWFLJHTTHZ-UHFFFAOYSA-N Ethanol Chemical compound CCO LFQSCWFLJHTTHZ-UHFFFAOYSA-N 0.000 description 49
- 241000699670 Mus sp. Species 0.000 description 48
- 108091032973 (ribonucleotides)n+m Proteins 0.000 description 47
- 241000699666 Mus <mouse, genus> Species 0.000 description 46
- 210000003819 peripheral blood mononuclear cell Anatomy 0.000 description 42
- 238000009396 hybridization Methods 0.000 description 41
- 238000003752 polymerase chain reaction Methods 0.000 description 41
- 238000003556 assay Methods 0.000 description 40
- 229960004137 elotuzumab Drugs 0.000 description 39
- 239000000203 mixture Substances 0.000 description 38
- 108020004414 DNA Proteins 0.000 description 36
- 239000013604 expression vector Substances 0.000 description 35
- 239000013615 primer Substances 0.000 description 33
- 230000001965 increasing effect Effects 0.000 description 32
- 108020004999 messenger RNA Proteins 0.000 description 28
- 230000000694 effects Effects 0.000 description 25
- 238000000338 in vitro Methods 0.000 description 25
- 125000003729 nucleotide group Chemical group 0.000 description 25
- 238000006467 substitution reaction Methods 0.000 description 25
- 108010047041 Complementarity Determining Regions Proteins 0.000 description 24
- 239000000872 buffer Substances 0.000 description 24
- 239000002773 nucleotide Substances 0.000 description 24
- 238000010186 staining Methods 0.000 description 24
- 210000000265 leukocyte Anatomy 0.000 description 23
- 238000002965 ELISA Methods 0.000 description 22
- 231100000135 cytotoxicity Toxicity 0.000 description 22
- 238000007737 ion beam deposition Methods 0.000 description 22
- 239000013598 vector Substances 0.000 description 22
- 230000003013 cytotoxicity Effects 0.000 description 21
- 208000002551 irritable bowel syndrome Diseases 0.000 description 21
- 208000024891 symptom Diseases 0.000 description 21
- XLYOFNOQVPJJNP-UHFFFAOYSA-N water Chemical compound O XLYOFNOQVPJJNP-UHFFFAOYSA-N 0.000 description 21
- 210000004698 lymphocyte Anatomy 0.000 description 20
- 210000005259 peripheral blood Anatomy 0.000 description 19
- 239000011886 peripheral blood Substances 0.000 description 19
- 239000000126 substance Substances 0.000 description 19
- 238000012360 testing method Methods 0.000 description 19
- 238000001727 in vivo Methods 0.000 description 18
- -1 CD 24 Proteins 0.000 description 17
- 208000011231 Crohn disease Diseases 0.000 description 17
- 230000010056 antibody-dependent cellular cytotoxicity Effects 0.000 description 17
- 108020001507 fusion proteins Proteins 0.000 description 17
- 102000037865 fusion proteins Human genes 0.000 description 17
- 108091003079 Bovine Serum Albumin Proteins 0.000 description 16
- 108010033737 Pokeweed Mitogens Proteins 0.000 description 16
- 210000001185 bone marrow Anatomy 0.000 description 16
- 230000000295 complement effect Effects 0.000 description 16
- 208000035475 disorder Diseases 0.000 description 16
- 210000002381 plasma Anatomy 0.000 description 16
- 241001465754 Metazoa Species 0.000 description 15
- 210000001744 T-lymphocyte Anatomy 0.000 description 15
- 230000000875 corresponding effect Effects 0.000 description 15
- 230000035772 mutation Effects 0.000 description 15
- 208000031223 plasma cell leukemia Diseases 0.000 description 15
- 239000013612 plasmid Substances 0.000 description 15
- 238000000746 purification Methods 0.000 description 15
- 238000003753 real-time PCR Methods 0.000 description 15
- 108020004711 Nucleic Acid Probes Proteins 0.000 description 14
- 238000004458 analytical method Methods 0.000 description 14
- 238000004422 calculation algorithm Methods 0.000 description 14
- 239000002853 nucleic acid probe Substances 0.000 description 14
- 230000002829 reductive effect Effects 0.000 description 14
- 108020004705 Codon Proteins 0.000 description 13
- 238000000018 DNA microarray Methods 0.000 description 13
- 108091028043 Nucleic acid sequence Proteins 0.000 description 13
- 230000003321 amplification Effects 0.000 description 13
- 238000006243 chemical reaction Methods 0.000 description 13
- 239000003153 chemical reaction reagent Substances 0.000 description 13
- 238000003745 diagnosis Methods 0.000 description 13
- 229940088598 enzyme Drugs 0.000 description 13
- 230000001939 inductive effect Effects 0.000 description 13
- 239000000463 material Substances 0.000 description 13
- 238000003199 nucleic acid amplification method Methods 0.000 description 13
- 239000000047 product Substances 0.000 description 13
- 230000001105 regulatory effect Effects 0.000 description 13
- 238000012216 screening Methods 0.000 description 13
- 238000013518 transcription Methods 0.000 description 13
- 230000035897 transcription Effects 0.000 description 13
- YBJHBAHKTGYVGT-ZKWXMUAHSA-N (+)-Biotin Chemical compound N1C(=O)N[C@@H]2[C@H](CCCCC(=O)O)SC[C@@H]21 YBJHBAHKTGYVGT-ZKWXMUAHSA-N 0.000 description 12
- 206010009900 Colitis ulcerative Diseases 0.000 description 12
- 108091093037 Peptide nucleic acid Proteins 0.000 description 12
- 201000006704 Ulcerative Colitis Diseases 0.000 description 12
- 230000013595 glycosylation Effects 0.000 description 12
- 238000006206 glycosylation reaction Methods 0.000 description 12
- 102000040430 polynucleotide Human genes 0.000 description 12
- 108091033319 polynucleotide Proteins 0.000 description 12
- 239000002157 polynucleotide Substances 0.000 description 12
- 239000006228 supernatant Substances 0.000 description 12
- 238000005406 washing Methods 0.000 description 12
- 108010021625 Immunoglobulin Fragments Proteins 0.000 description 11
- 102000008394 Immunoglobulin Fragments Human genes 0.000 description 11
- 238000013459 approach Methods 0.000 description 11
- 239000003795 chemical substances by application Substances 0.000 description 11
- 230000006378 damage Effects 0.000 description 11
- 239000003814 drug Substances 0.000 description 11
- 230000004048 modification Effects 0.000 description 11
- 238000012986 modification Methods 0.000 description 11
- 210000002966 serum Anatomy 0.000 description 11
- 239000007787 solid Substances 0.000 description 11
- 101150034556 CS1 gene Proteins 0.000 description 10
- 241000124008 Mammalia Species 0.000 description 10
- JLCPHMBAVCMARE-UHFFFAOYSA-N [3-[[3-[[3-[[3-[[3-[[3-[[3-[[3-[[3-[[3-[[3-[[5-(2-amino-6-oxo-1H-purin-9-yl)-3-[[3-[[3-[[3-[[3-[[3-[[5-(2-amino-6-oxo-1H-purin-9-yl)-3-[[5-(2-amino-6-oxo-1H-purin-9-yl)-3-hydroxyoxolan-2-yl]methoxy-hydroxyphosphoryl]oxyoxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(5-methyl-2,4-dioxopyrimidin-1-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(6-aminopurin-9-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(6-aminopurin-9-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(6-aminopurin-9-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(6-aminopurin-9-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxyoxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(5-methyl-2,4-dioxopyrimidin-1-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(4-amino-2-oxopyrimidin-1-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(5-methyl-2,4-dioxopyrimidin-1-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(5-methyl-2,4-dioxopyrimidin-1-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(6-aminopurin-9-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(6-aminopurin-9-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(4-amino-2-oxopyrimidin-1-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(4-amino-2-oxopyrimidin-1-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(4-amino-2-oxopyrimidin-1-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(6-aminopurin-9-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(4-amino-2-oxopyrimidin-1-yl)oxolan-2-yl]methyl [5-(6-aminopurin-9-yl)-2-(hydroxymethyl)oxolan-3-yl] hydrogen phosphate Polymers Cc1cn(C2CC(OP(O)(=O)OCC3OC(CC3OP(O)(=O)OCC3OC(CC3O)n3cnc4c3nc(N)[nH]c4=O)n3cnc4c3nc(N)[nH]c4=O)C(COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3CO)n3cnc4c(N)ncnc34)n3ccc(N)nc3=O)n3cnc4c(N)ncnc34)n3ccc(N)nc3=O)n3ccc(N)nc3=O)n3ccc(N)nc3=O)n3cnc4c(N)ncnc34)n3cnc4c(N)ncnc34)n3cc(C)c(=O)[nH]c3=O)n3cc(C)c(=O)[nH]c3=O)n3ccc(N)nc3=O)n3cc(C)c(=O)[nH]c3=O)n3cnc4c3nc(N)[nH]c4=O)n3cnc4c(N)ncnc34)n3cnc4c(N)ncnc34)n3cnc4c(N)ncnc34)n3cnc4c(N)ncnc34)O2)c(=O)[nH]c1=O JLCPHMBAVCMARE-UHFFFAOYSA-N 0.000 description 10
- 239000012472 biological sample Substances 0.000 description 10
- 230000001413 cellular effect Effects 0.000 description 10
- 230000008859 change Effects 0.000 description 10
- 230000003247 decreasing effect Effects 0.000 description 10
- 239000000499 gel Substances 0.000 description 10
- 230000006698 induction Effects 0.000 description 10
- 238000004393 prognosis Methods 0.000 description 10
- 238000002560 therapeutic procedure Methods 0.000 description 10
- 101710178046 Chorismate synthase 1 Proteins 0.000 description 9
- 101710152695 Cysteine synthase 1 Proteins 0.000 description 9
- DHMQDGOQFOQNFH-UHFFFAOYSA-N Glycine Chemical compound NCC(O)=O DHMQDGOQFOQNFH-UHFFFAOYSA-N 0.000 description 9
- 102100032831 Protein ITPRID2 Human genes 0.000 description 9
- 241000700159 Rattus Species 0.000 description 9
- 125000000539 amino acid group Chemical group 0.000 description 9
- 230000001580 bacterial effect Effects 0.000 description 9
- 210000004369 blood Anatomy 0.000 description 9
- 239000008280 blood Substances 0.000 description 9
- 238000010367 cloning Methods 0.000 description 9
- 230000009089 cytolysis Effects 0.000 description 9
- 238000012217 deletion Methods 0.000 description 9
- 230000037430 deletion Effects 0.000 description 9
- 238000011161 development Methods 0.000 description 9
- 230000018109 developmental process Effects 0.000 description 9
- 239000012091 fetal bovine serum Substances 0.000 description 9
- 230000001900 immune effect Effects 0.000 description 9
- 238000003780 insertion Methods 0.000 description 9
- 230000037431 insertion Effects 0.000 description 9
- 125000005647 linker group Chemical group 0.000 description 9
- 238000012544 monitoring process Methods 0.000 description 9
- 239000002777 nucleoside Substances 0.000 description 9
- 239000000243 solution Substances 0.000 description 9
- 238000010561 standard procedure Methods 0.000 description 9
- 239000011534 wash buffer Substances 0.000 description 9
- NFGXHKASABOEEW-UHFFFAOYSA-N 1-methylethyl 11-methoxy-3,7,11-trimethyl-2,4-dodecadienoate Chemical compound COC(C)(C)CCCC(C)CC=CC(C)=CC(=O)OC(C)C NFGXHKASABOEEW-UHFFFAOYSA-N 0.000 description 8
- 206010057248 Cell death Diseases 0.000 description 8
- 108091026890 Coding region Proteins 0.000 description 8
- 206010061218 Inflammation Diseases 0.000 description 8
- 102000003855 L-lactate dehydrogenase Human genes 0.000 description 8
- 108700023483 L-lactate dehydrogenases Proteins 0.000 description 8
- 108091005461 Nucleic proteins Proteins 0.000 description 8
- ISWSIDIOOBJBQZ-UHFFFAOYSA-N Phenol Chemical compound OC1=CC=CC=C1 ISWSIDIOOBJBQZ-UHFFFAOYSA-N 0.000 description 8
- 240000004808 Saccharomyces cerevisiae Species 0.000 description 8
- 235000014680 Saccharomyces cerevisiae Nutrition 0.000 description 8
- 108010090804 Streptavidin Proteins 0.000 description 8
- 238000007792 addition Methods 0.000 description 8
- 238000010171 animal model Methods 0.000 description 8
- 230000006907 apoptotic process Effects 0.000 description 8
- 238000005516 engineering process Methods 0.000 description 8
- 238000002474 experimental method Methods 0.000 description 8
- 230000006870 function Effects 0.000 description 8
- 230000004927 fusion Effects 0.000 description 8
- 230000012010 growth Effects 0.000 description 8
- 230000004054 inflammatory process Effects 0.000 description 8
- 210000003734 kidney Anatomy 0.000 description 8
- 238000002372 labelling Methods 0.000 description 8
- 230000001404 mediated effect Effects 0.000 description 8
- 239000008188 pellet Substances 0.000 description 8
- 230000035755 proliferation Effects 0.000 description 8
- 230000003827 upregulation Effects 0.000 description 8
- 241000894006 Bacteria Species 0.000 description 7
- 241000588724 Escherichia coli Species 0.000 description 7
- 241000238631 Hexapoda Species 0.000 description 7
- 101000633785 Mus musculus SLAM family member 7 Proteins 0.000 description 7
- 230000004075 alteration Effects 0.000 description 7
- 230000015572 biosynthetic process Effects 0.000 description 7
- 210000001772 blood platelet Anatomy 0.000 description 7
- 229940098773 bovine serum albumin Drugs 0.000 description 7
- 150000001720 carbohydrates Chemical class 0.000 description 7
- 238000009826 distribution Methods 0.000 description 7
- 230000002068 genetic effect Effects 0.000 description 7
- 229940124452 immunizing agent Drugs 0.000 description 7
- 230000005764 inhibitory process Effects 0.000 description 7
- 210000001165 lymph node Anatomy 0.000 description 7
- 239000003550 marker Substances 0.000 description 7
- 238000010172 mouse model Methods 0.000 description 7
- 210000000822 natural killer cell Anatomy 0.000 description 7
- 239000013642 negative control Substances 0.000 description 7
- 238000010606 normalization Methods 0.000 description 7
- 238000002360 preparation method Methods 0.000 description 7
- 230000009467 reduction Effects 0.000 description 7
- 241000894007 species Species 0.000 description 7
- 238000001890 transfection Methods 0.000 description 7
- 108020004463 18S ribosomal RNA Proteins 0.000 description 6
- HEDRZPFGACZZDS-UHFFFAOYSA-N Chloroform Chemical compound ClC(Cl)Cl HEDRZPFGACZZDS-UHFFFAOYSA-N 0.000 description 6
- SHZGCJCMOBCMKK-UHFFFAOYSA-N D-mannomethylose Natural products CC1OC(O)C(O)C(O)C1O SHZGCJCMOBCMKK-UHFFFAOYSA-N 0.000 description 6
- ZHNUHDYFZUAESO-UHFFFAOYSA-N Formamide Chemical compound NC=O ZHNUHDYFZUAESO-UHFFFAOYSA-N 0.000 description 6
- PNNNRSAQSRJVSB-SLPGGIOYSA-N Fucose Natural products C[C@H](O)[C@@H](O)[C@H](O)[C@H](O)C=O PNNNRSAQSRJVSB-SLPGGIOYSA-N 0.000 description 6
- QNAYBMKLOCPYGJ-REOHCLBHSA-N L-alanine Chemical compound C[C@H](N)C(O)=O QNAYBMKLOCPYGJ-REOHCLBHSA-N 0.000 description 6
- SHZGCJCMOBCMKK-DHVFOXMCSA-N L-fucopyranose Chemical compound C[C@@H]1OC(O)[C@@H](O)[C@H](O)[C@@H]1O SHZGCJCMOBCMKK-DHVFOXMCSA-N 0.000 description 6
- MUBZPKHOEPUJKR-UHFFFAOYSA-N Oxalic acid Chemical compound OC(=O)C(O)=O MUBZPKHOEPUJKR-UHFFFAOYSA-N 0.000 description 6
- 108010004729 Phycoerythrin Proteins 0.000 description 6
- 239000004698 Polyethylene Substances 0.000 description 6
- 241000283984 Rodentia Species 0.000 description 6
- FAPWRFPIFSIZLT-UHFFFAOYSA-M Sodium chloride Chemical compound [Na+].[Cl-] FAPWRFPIFSIZLT-UHFFFAOYSA-M 0.000 description 6
- HEMHJVSKTPXQMS-UHFFFAOYSA-M Sodium hydroxide Chemical compound [OH-].[Na+] HEMHJVSKTPXQMS-UHFFFAOYSA-M 0.000 description 6
- 238000002835 absorbance Methods 0.000 description 6
- 230000004913 activation Effects 0.000 description 6
- 210000005058 airway cell Anatomy 0.000 description 6
- 235000004279 alanine Nutrition 0.000 description 6
- 125000003277 amino group Chemical group 0.000 description 6
- 230000000692 anti-sense effect Effects 0.000 description 6
- 229960002685 biotin Drugs 0.000 description 6
- 235000020958 biotin Nutrition 0.000 description 6
- 239000011616 biotin Substances 0.000 description 6
- 238000004113 cell culture Methods 0.000 description 6
- 230000001186 cumulative effect Effects 0.000 description 6
- 230000002950 deficient Effects 0.000 description 6
- 210000003743 erythrocyte Anatomy 0.000 description 6
- 238000006062 fragmentation reaction Methods 0.000 description 6
- FDGQSTZJBFJUBT-UHFFFAOYSA-N hypoxanthine Chemical compound O=C1NC=NC2=C1NC=N2 FDGQSTZJBFJUBT-UHFFFAOYSA-N 0.000 description 6
- 230000002637 immunotoxin Effects 0.000 description 6
- 239000002596 immunotoxin Substances 0.000 description 6
- 229940051026 immunotoxin Drugs 0.000 description 6
- 231100000608 immunotoxin Toxicity 0.000 description 6
- 238000002347 injection Methods 0.000 description 6
- 239000007924 injection Substances 0.000 description 6
- 210000002429 large intestine Anatomy 0.000 description 6
- 210000004962 mammalian cell Anatomy 0.000 description 6
- 238000002703 mutagenesis Methods 0.000 description 6
- 231100000350 mutagenesis Toxicity 0.000 description 6
- 150000003833 nucleoside derivatives Chemical class 0.000 description 6
- 229920000642 polymer Polymers 0.000 description 6
- 238000011160 research Methods 0.000 description 6
- 210000000952 spleen Anatomy 0.000 description 6
- 102000017420 CD3 protein, epsilon/gamma/delta subunit Human genes 0.000 description 5
- 108050005493 CD3 protein, epsilon/gamma/delta subunit Proteins 0.000 description 5
- 241000283707 Capra Species 0.000 description 5
- 108020004635 Complementary DNA Proteins 0.000 description 5
- 239000006144 Dulbecco’s modified Eagle's medium Substances 0.000 description 5
- 108700024394 Exon Proteins 0.000 description 5
- 108010087819 Fc receptors Proteins 0.000 description 5
- 102000009109 Fc receptors Human genes 0.000 description 5
- 239000004471 Glycine Substances 0.000 description 5
- 101000581981 Homo sapiens Neural cell adhesion molecule 1 Proteins 0.000 description 5
- 108010054477 Immunoglobulin Fab Fragments Proteins 0.000 description 5
- 102000001706 Immunoglobulin Fab Fragments Human genes 0.000 description 5
- 101710085938 Matrix protein Proteins 0.000 description 5
- 101710127721 Membrane protein Proteins 0.000 description 5
- 241001529936 Murinae Species 0.000 description 5
- 241000699660 Mus musculus Species 0.000 description 5
- 102100032965 Myomesin-2 Human genes 0.000 description 5
- 102100027347 Neural cell adhesion molecule 1 Human genes 0.000 description 5
- 108020004511 Recombinant DNA Proteins 0.000 description 5
- AYFVYJQAPQTCCC-UHFFFAOYSA-N Threonine Natural products CC(O)C(N)C(O)=O AYFVYJQAPQTCCC-UHFFFAOYSA-N 0.000 description 5
- 239000004473 Threonine Substances 0.000 description 5
- 239000002671 adjuvant Substances 0.000 description 5
- 230000001363 autoimmune Effects 0.000 description 5
- 230000000903 blocking effect Effects 0.000 description 5
- 210000004556 brain Anatomy 0.000 description 5
- 238000002512 chemotherapy Methods 0.000 description 5
- 206010009887 colitis Diseases 0.000 description 5
- 229940079593 drug Drugs 0.000 description 5
- 239000012149 elution buffer Substances 0.000 description 5
- 239000002158 endotoxin Substances 0.000 description 5
- 239000003623 enhancer Substances 0.000 description 5
- 230000002255 enzymatic effect Effects 0.000 description 5
- MHMNJMPURVTYEJ-UHFFFAOYSA-N fluorescein-5-isothiocyanate Chemical compound O1C(=O)C2=CC(N=C=S)=CC=C2C21C1=CC=C(O)C=C1OC1=CC(O)=CC=C21 MHMNJMPURVTYEJ-UHFFFAOYSA-N 0.000 description 5
- 238000013467 fragmentation Methods 0.000 description 5
- 210000002216 heart Anatomy 0.000 description 5
- 230000002163 immunogen Effects 0.000 description 5
- 238000007912 intraperitoneal administration Methods 0.000 description 5
- 230000003902 lesion Effects 0.000 description 5
- 229920006008 lipopolysaccharide Polymers 0.000 description 5
- 210000004072 lung Anatomy 0.000 description 5
- 210000002540 macrophage Anatomy 0.000 description 5
- 239000002609 medium Substances 0.000 description 5
- 238000002493 microarray Methods 0.000 description 5
- 210000000056 organ Anatomy 0.000 description 5
- 238000011002 quantification Methods 0.000 description 5
- 210000000813 small intestine Anatomy 0.000 description 5
- 238000003786 synthesis reaction Methods 0.000 description 5
- 229940124597 therapeutic agent Drugs 0.000 description 5
- 230000002103 transcriptional effect Effects 0.000 description 5
- 230000009261 transgenic effect Effects 0.000 description 5
- 238000011830 transgenic mouse model Methods 0.000 description 5
- 102100024222 B-lymphocyte antigen CD19 Human genes 0.000 description 4
- 206010012735 Diarrhoea Diseases 0.000 description 4
- KCXVZYZYPLLWCC-UHFFFAOYSA-N EDTA Chemical compound OC(=O)CN(CC(O)=O)CCN(CC(O)=O)CC(O)=O KCXVZYZYPLLWCC-UHFFFAOYSA-N 0.000 description 4
- 238000012413 Fluorescence activated cell sorting analysis Methods 0.000 description 4
- 101000980825 Homo sapiens B-lymphocyte antigen CD19 Proteins 0.000 description 4
- 101000946889 Homo sapiens Monocyte differentiation antigen CD14 Proteins 0.000 description 4
- 108010091358 Hypoxanthine Phosphoribosyltransferase Proteins 0.000 description 4
- FFEARJCKVFRZRR-BYPYZUCNSA-N L-methionine Chemical group CSCC[C@H](N)C(O)=O FFEARJCKVFRZRR-BYPYZUCNSA-N 0.000 description 4
- AYFVYJQAPQTCCC-GBXIJSLDSA-N L-threonine Chemical compound C[C@@H](O)[C@H](N)C(O)=O AYFVYJQAPQTCCC-GBXIJSLDSA-N 0.000 description 4
- KDXKERNSBIXSRK-UHFFFAOYSA-N Lysine Natural products NCCCCC(N)C(O)=O KDXKERNSBIXSRK-UHFFFAOYSA-N 0.000 description 4
- 239000004472 Lysine Substances 0.000 description 4
- 102100035877 Monocyte differentiation antigen CD14 Human genes 0.000 description 4
- 108010045503 Myeloma Proteins Proteins 0.000 description 4
- 102000005717 Myeloma Proteins Human genes 0.000 description 4
- 230000004988 N-glycosylation Effects 0.000 description 4
- 239000004677 Nylon Substances 0.000 description 4
- 108700026244 Open Reading Frames Proteins 0.000 description 4
- 108010047620 Phytohemagglutinins Proteins 0.000 description 4
- 108010076504 Protein Sorting Signals Proteins 0.000 description 4
- 201000004681 Psoriasis Diseases 0.000 description 4
- 239000006146 Roswell Park Memorial Institute medium Substances 0.000 description 4
- 238000011579 SCID mouse model Methods 0.000 description 4
- 102100029198 SLAM family member 7 Human genes 0.000 description 4
- MTCFGRXMJLQNBG-UHFFFAOYSA-N Serine Natural products OCC(N)C(O)=O MTCFGRXMJLQNBG-UHFFFAOYSA-N 0.000 description 4
- VYPSYNLAJGMNEJ-UHFFFAOYSA-N Silicium dioxide Chemical compound O=[Si]=O VYPSYNLAJGMNEJ-UHFFFAOYSA-N 0.000 description 4
- 102100036011 T-cell surface glycoprotein CD4 Human genes 0.000 description 4
- IQFYYKKMVGJFEH-XLPZGREQSA-N Thymidine Chemical compound O=C1NC(=O)C(C)=CN1[C@@H]1O[C@H](CO)[C@@H](O)C1 IQFYYKKMVGJFEH-XLPZGREQSA-N 0.000 description 4
- 230000002159 abnormal effect Effects 0.000 description 4
- 238000012197 amplification kit Methods 0.000 description 4
- 238000003491 array Methods 0.000 description 4
- 210000000649 b-lymphocyte subset Anatomy 0.000 description 4
- 210000000481 breast Anatomy 0.000 description 4
- 238000010804 cDNA synthesis Methods 0.000 description 4
- 125000003178 carboxy group Chemical group [H]OC(*)=O 0.000 description 4
- 238000012512 characterization method Methods 0.000 description 4
- 238000003776 cleavage reaction Methods 0.000 description 4
- 210000004922 colonic epithelial cell Anatomy 0.000 description 4
- 230000034994 death Effects 0.000 description 4
- 238000010790 dilution Methods 0.000 description 4
- 239000012895 dilution Substances 0.000 description 4
- 238000010828 elution Methods 0.000 description 4
- 210000001671 embryonic stem cell Anatomy 0.000 description 4
- 230000007613 environmental effect Effects 0.000 description 4
- 238000011156 evaluation Methods 0.000 description 4
- 125000000524 functional group Chemical group 0.000 description 4
- 210000001035 gastrointestinal tract Anatomy 0.000 description 4
- 239000001963 growth medium Substances 0.000 description 4
- 239000001257 hydrogen Substances 0.000 description 4
- 229910052739 hydrogen Inorganic materials 0.000 description 4
- 230000028993 immune response Effects 0.000 description 4
- 230000016784 immunoglobulin production Effects 0.000 description 4
- 229940072221 immunoglobulins Drugs 0.000 description 4
- 230000002401 inhibitory effect Effects 0.000 description 4
- 230000003993 interaction Effects 0.000 description 4
- 210000003292 kidney cell Anatomy 0.000 description 4
- 210000004185 liver Anatomy 0.000 description 4
- 230000007774 longterm Effects 0.000 description 4
- 210000001161 mammalian embryo Anatomy 0.000 description 4
- 239000011159 matrix material Substances 0.000 description 4
- 239000012528 membrane Substances 0.000 description 4
- 229930182817 methionine Chemical group 0.000 description 4
- 210000004877 mucosa Anatomy 0.000 description 4
- 230000003472 neutralizing effect Effects 0.000 description 4
- 125000003835 nucleoside group Chemical group 0.000 description 4
- 229920001778 nylon Polymers 0.000 description 4
- 210000002741 palatine tonsil Anatomy 0.000 description 4
- 230000001885 phytohemagglutinin Effects 0.000 description 4
- 238000001742 protein purification Methods 0.000 description 4
- 108091008146 restriction endonucleases Proteins 0.000 description 4
- 238000010839 reverse transcription Methods 0.000 description 4
- 150000003839 salts Chemical class 0.000 description 4
- 230000007017 scission Effects 0.000 description 4
- 230000002269 spontaneous effect Effects 0.000 description 4
- 238000003153 stable transfection Methods 0.000 description 4
- 230000000638 stimulation Effects 0.000 description 4
- 238000007920 subcutaneous administration Methods 0.000 description 4
- 238000013519 translation Methods 0.000 description 4
- 238000011269 treatment regimen Methods 0.000 description 4
- NHJVRSWLHSJWIN-UHFFFAOYSA-N 2,4,6-trinitrobenzenesulfonic acid Chemical compound OS(=O)(=O)C1=C([N+]([O-])=O)C=C([N+]([O-])=O)C=C1[N+]([O-])=O NHJVRSWLHSJWIN-UHFFFAOYSA-N 0.000 description 3
- 239000004475 Arginine Substances 0.000 description 3
- 241000283690 Bos taurus Species 0.000 description 3
- 108010032001 CS1 peptide Proteins 0.000 description 3
- 241000699800 Cricetinae Species 0.000 description 3
- 238000001712 DNA sequencing Methods 0.000 description 3
- WQZGKKKJIJFFOK-GASJEMHNSA-N Glucose Natural products OC[C@H]1OC(O)[C@H](O)[C@@H](O)[C@@H]1O WQZGKKKJIJFFOK-GASJEMHNSA-N 0.000 description 3
- 102000012153 HLA-B27 Antigen Human genes 0.000 description 3
- 108010061486 HLA-B27 Antigen Proteins 0.000 description 3
- 208000037147 Hypercalcaemia Diseases 0.000 description 3
- UGQMRVRMYYASKQ-UHFFFAOYSA-N Hypoxanthine nucleoside Natural products OC1C(O)C(CO)OC1N1C(NC=NC2=O)=C2N=C1 UGQMRVRMYYASKQ-UHFFFAOYSA-N 0.000 description 3
- 102100029098 Hypoxanthine-guanine phosphoribosyltransferase Human genes 0.000 description 3
- 229930010555 Inosine Natural products 0.000 description 3
- UGQMRVRMYYASKQ-KQYNXXCUSA-N Inosine Chemical compound O[C@@H]1[C@H](O)[C@@H](CO)O[C@H]1N1C2=NC=NC(O)=C2N=C1 UGQMRVRMYYASKQ-KQYNXXCUSA-N 0.000 description 3
- HNDVDQJCIGZPNO-YFKPBYRVSA-N L-histidine Chemical compound OC(=O)[C@@H](N)CC1=CN=CN1 HNDVDQJCIGZPNO-YFKPBYRVSA-N 0.000 description 3
- ROHFNLRQFUQHCH-YFKPBYRVSA-N L-leucine Chemical compound CC(C)C[C@H](N)C(O)=O ROHFNLRQFUQHCH-YFKPBYRVSA-N 0.000 description 3
- COLNVLDHVKWLRT-QMMMGPOBSA-N L-phenylalanine Chemical compound OC(=O)[C@@H](N)CC1=CC=CC=C1 COLNVLDHVKWLRT-QMMMGPOBSA-N 0.000 description 3
- QIVBCDIJIAJPQS-VIFPVBQESA-N L-tryptophane Chemical compound C1=CC=C2C(C[C@H](N)C(O)=O)=CNC2=C1 QIVBCDIJIAJPQS-VIFPVBQESA-N 0.000 description 3
- ROHFNLRQFUQHCH-UHFFFAOYSA-N Leucine Natural products CC(C)CC(N)C(O)=O ROHFNLRQFUQHCH-UHFFFAOYSA-N 0.000 description 3
- 208000015914 Non-Hodgkin lymphomas Diseases 0.000 description 3
- 239000002202 Polyethylene glycol Substances 0.000 description 3
- 241000288906 Primates Species 0.000 description 3
- 239000012979 RPMI medium Substances 0.000 description 3
- 206010038063 Rectal haemorrhage Diseases 0.000 description 3
- 101710083287 SLAM family member 7 Proteins 0.000 description 3
- 208000021386 Sjogren Syndrome Diseases 0.000 description 3
- QIVBCDIJIAJPQS-UHFFFAOYSA-N Tryptophan Natural products C1=CC=C2C(CC(N)C(O)=O)=CNC2=C1 QIVBCDIJIAJPQS-UHFFFAOYSA-N 0.000 description 3
- 208000025865 Ulcer Diseases 0.000 description 3
- 241000700605 Viruses Species 0.000 description 3
- 239000002253 acid Substances 0.000 description 3
- 150000007513 acids Chemical class 0.000 description 3
- 239000000654 additive Substances 0.000 description 3
- 208000007502 anemia Diseases 0.000 description 3
- 210000004102 animal cell Anatomy 0.000 description 3
- 238000000137 annealing Methods 0.000 description 3
- 229940088710 antibiotic agent Drugs 0.000 description 3
- ODKSFYDXXFIFQN-UHFFFAOYSA-N arginine Natural products OC(=O)C(N)CCCNC(N)=N ODKSFYDXXFIFQN-UHFFFAOYSA-N 0.000 description 3
- 230000008901 benefit Effects 0.000 description 3
- 102000015736 beta 2-Microglobulin Human genes 0.000 description 3
- 108010081355 beta 2-Microglobulin Proteins 0.000 description 3
- 230000001588 bifunctional effect Effects 0.000 description 3
- 210000002798 bone marrow cell Anatomy 0.000 description 3
- 235000014633 carbohydrates Nutrition 0.000 description 3
- 230000010261 cell growth Effects 0.000 description 3
- 230000003833 cell viability Effects 0.000 description 3
- 230000001684 chronic effect Effects 0.000 description 3
- 238000010168 coupling process Methods 0.000 description 3
- 238000004132 cross linking Methods 0.000 description 3
- 201000003278 cryoglobulinemia Diseases 0.000 description 3
- NXAKDBCNODQXBZ-YSZCVPRFSA-N cs1 peptide Chemical compound C([C@@H](C(=O)NCC(=O)N1CCC[C@H]1C(=O)N[C@@H](CCC(O)=O)C(=O)N[C@@H]([C@@H](C)CC)C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](CC(O)=O)C(=O)N[C@@H](C(C)C)C(=O)N1[C@@H](CCC1)C(=O)N[C@@H](CO)C(=O)N[C@@H]([C@@H](C)O)C(O)=O)NC(=O)[C@H](CC(C)C)NC(=O)[C@H](CC(N)=O)NC(=O)[C@H]1N(CCC1)C(=O)[C@H](CC=1NC=NC=1)NC(=O)[C@H]1N(CCC1)C(=O)[C@H](CC(C)C)NC(=O)[C@@H](NC(=O)[C@@H](NC(=O)[C@H](CC(C)C)NC(=O)[C@H](CCC(N)=O)NC(=O)[C@H]1N(CCC1)C(=O)[C@H](CC(C)C)NC(=O)[C@H](CCC(O)=O)NC(=O)[C@@H](N)CC(O)=O)C(C)C)[C@@H](C)O)C1=CN=CN1 NXAKDBCNODQXBZ-YSZCVPRFSA-N 0.000 description 3
- 230000001419 dependent effect Effects 0.000 description 3
- 238000002405 diagnostic procedure Methods 0.000 description 3
- 239000000539 dimer Substances 0.000 description 3
- 210000003811 finger Anatomy 0.000 description 3
- 238000000684 flow cytometry Methods 0.000 description 3
- 238000010353 genetic engineering Methods 0.000 description 3
- 210000004602 germ cell Anatomy 0.000 description 3
- 239000011521 glass Substances 0.000 description 3
- 239000008103 glucose Substances 0.000 description 3
- 238000003306 harvesting Methods 0.000 description 3
- 230000036541 health Effects 0.000 description 3
- 210000005260 human cell Anatomy 0.000 description 3
- 230000000148 hypercalcaemia Effects 0.000 description 3
- 208000030915 hypercalcemia disease Diseases 0.000 description 3
- 238000003384 imaging method Methods 0.000 description 3
- 230000002998 immunogenetic effect Effects 0.000 description 3
- 238000003364 immunohistochemistry Methods 0.000 description 3
- 238000011065 in-situ storage Methods 0.000 description 3
- 238000011534 incubation Methods 0.000 description 3
- 208000027866 inflammatory disease Diseases 0.000 description 3
- 230000000977 initiatory effect Effects 0.000 description 3
- 229960003786 inosine Drugs 0.000 description 3
- 238000002955 isolation Methods 0.000 description 3
- 208000032839 leukemia Diseases 0.000 description 3
- 210000005229 liver cell Anatomy 0.000 description 3
- 210000003563 lymphoid tissue Anatomy 0.000 description 3
- 210000004379 membrane Anatomy 0.000 description 3
- 210000001616 monocyte Anatomy 0.000 description 3
- 239000000178 monomer Substances 0.000 description 3
- 201000006417 multiple sclerosis Diseases 0.000 description 3
- 210000000581 natural killer T-cell Anatomy 0.000 description 3
- 230000008520 organization Effects 0.000 description 3
- 230000001575 pathological effect Effects 0.000 description 3
- 230000007170 pathology Effects 0.000 description 3
- 238000002823 phage display Methods 0.000 description 3
- COLNVLDHVKWLRT-UHFFFAOYSA-N phenylalanine Natural products OC(=O)C(N)CC1=CC=CC=C1 COLNVLDHVKWLRT-UHFFFAOYSA-N 0.000 description 3
- 239000004033 plastic Substances 0.000 description 3
- 229920003023 plastic Polymers 0.000 description 3
- 229920001223 polyethylene glycol Polymers 0.000 description 3
- 210000005267 prostate cell Anatomy 0.000 description 3
- 239000011541 reaction mixture Substances 0.000 description 3
- 230000008929 regeneration Effects 0.000 description 3
- 238000011069 regeneration method Methods 0.000 description 3
- 230000010076 replication Effects 0.000 description 3
- 230000004044 response Effects 0.000 description 3
- 230000035945 sensitivity Effects 0.000 description 3
- 238000012163 sequencing technique Methods 0.000 description 3
- 238000002741 site-directed mutagenesis Methods 0.000 description 3
- 210000002027 skeletal muscle Anatomy 0.000 description 3
- 150000003384 small molecules Chemical class 0.000 description 3
- 235000000346 sugar Nutrition 0.000 description 3
- 210000001258 synovial membrane Anatomy 0.000 description 3
- 125000000341 threoninyl group Chemical group [H]OC([H])(C([H])([H])[H])C([H])(N([H])[H])C(*)=O 0.000 description 3
- 210000003371 toe Anatomy 0.000 description 3
- MTCFGRXMJLQNBG-REOHCLBHSA-N (2S)-2-Amino-3-hydroxypropansäure Chemical compound OC[C@H](N)C(O)=O MTCFGRXMJLQNBG-REOHCLBHSA-N 0.000 description 2
- LMDZBCPBFSXMTL-UHFFFAOYSA-N 1-ethyl-3-(3-dimethylaminopropyl)carbodiimide Chemical compound CCN=C=NCCCN(C)C LMDZBCPBFSXMTL-UHFFFAOYSA-N 0.000 description 2
- HZAXFHJVJLSVMW-UHFFFAOYSA-N 2-Aminoethan-1-ol Chemical compound NCCO HZAXFHJVJLSVMW-UHFFFAOYSA-N 0.000 description 2
- TVZGACDUOSZQKY-LBPRGKRZSA-N 4-aminofolic acid Chemical compound C1=NC2=NC(N)=NC(N)=C2N=C1CNC1=CC=C(C(=O)N[C@@H](CCC(O)=O)C(O)=O)C=C1 TVZGACDUOSZQKY-LBPRGKRZSA-N 0.000 description 2
- LRFVTYWOQMYALW-UHFFFAOYSA-N 9H-xanthine Chemical compound O=C1NC(=O)NC2=C1NC=N2 LRFVTYWOQMYALW-UHFFFAOYSA-N 0.000 description 2
- 102100031585 ADP-ribosyl cyclase/cyclic ADP-ribose hydrolase 1 Human genes 0.000 description 2
- 208000004998 Abdominal Pain Diseases 0.000 description 2
- 208000031261 Acute myeloid leukaemia Diseases 0.000 description 2
- 102000002260 Alkaline Phosphatase Human genes 0.000 description 2
- 108020004774 Alkaline Phosphatase Proteins 0.000 description 2
- 108700028369 Alleles Proteins 0.000 description 2
- XKRFYHLGVUSROY-UHFFFAOYSA-N Argon Chemical compound [Ar] XKRFYHLGVUSROY-UHFFFAOYSA-N 0.000 description 2
- DCXYFEDJOCDNAF-UHFFFAOYSA-N Asparagine Natural products OC(=O)C(N)CC(N)=O DCXYFEDJOCDNAF-UHFFFAOYSA-N 0.000 description 2
- 102100022005 B-lymphocyte antigen CD20 Human genes 0.000 description 2
- 244000063299 Bacillus subtilis Species 0.000 description 2
- 235000014469 Bacillus subtilis Nutrition 0.000 description 2
- DWRXFEITVBNRMK-UHFFFAOYSA-N Beta-D-1-Arabinofuranosylthymine Natural products O=C1NC(=O)C(C)=CN1C1C(O)C(O)C(CO)O1 DWRXFEITVBNRMK-UHFFFAOYSA-N 0.000 description 2
- 102100037904 CD9 antigen Human genes 0.000 description 2
- OYPRJOBELJOOCE-UHFFFAOYSA-N Calcium Chemical compound [Ca] OYPRJOBELJOOCE-UHFFFAOYSA-N 0.000 description 2
- OKTJSMMVPCPJKN-UHFFFAOYSA-N Carbon Chemical compound [C] OKTJSMMVPCPJKN-UHFFFAOYSA-N 0.000 description 2
- 206010008479 Chest Pain Diseases 0.000 description 2
- 208000011038 Cold agglutinin disease Diseases 0.000 description 2
- 206010009868 Cold type haemolytic anaemia Diseases 0.000 description 2
- 206010009944 Colon cancer Diseases 0.000 description 2
- 206010010305 Confusional state Diseases 0.000 description 2
- 239000004971 Cross linker Substances 0.000 description 2
- 208000019707 Cryoglobulinemic vasculitis Diseases 0.000 description 2
- 102100033215 DNA nucleotidylexotransferase Human genes 0.000 description 2
- 108010008286 DNA nucleotidylexotransferase Proteins 0.000 description 2
- 239000003155 DNA primer Substances 0.000 description 2
- BWGNESOTFCXPMA-UHFFFAOYSA-N Dihydrogen disulfide Chemical compound SS BWGNESOTFCXPMA-UHFFFAOYSA-N 0.000 description 2
- AOJJSUZBOXZQNB-TZSSRYMLSA-N Doxorubicin Chemical compound O([C@H]1C[C@@](O)(CC=2C(O)=C3C(=O)C=4C=CC=C(C=4C(=O)C3=C(O)C=21)OC)C(=O)CO)[C@H]1C[C@H](N)[C@H](O)[C@H](C)O1 AOJJSUZBOXZQNB-TZSSRYMLSA-N 0.000 description 2
- 208000000059 Dyspnea Diseases 0.000 description 2
- 206010013975 Dyspnoeas Diseases 0.000 description 2
- ULGZDMOVFRHVEP-RWJQBGPGSA-N Erythromycin Chemical compound O([C@@H]1[C@@H](C)C(=O)O[C@@H]([C@@]([C@H](O)[C@@H](C)C(=O)[C@H](C)C[C@@](C)(O)[C@H](O[C@H]2[C@@H]([C@H](C[C@@H](C)O2)N(C)C)O)[C@H]1C)(C)O)CC)[C@H]1C[C@@](C)(OC)[C@@H](O)[C@H](C)O1 ULGZDMOVFRHVEP-RWJQBGPGSA-N 0.000 description 2
- 229920001917 Ficoll Polymers 0.000 description 2
- BJGNCJDXODQBOB-UHFFFAOYSA-N Fivefly Luciferin Natural products OC(=O)C1CSC(C=2SC3=CC(O)=CC=C3N=2)=N1 BJGNCJDXODQBOB-UHFFFAOYSA-N 0.000 description 2
- 208000018522 Gastrointestinal disease Diseases 0.000 description 2
- 208000015872 Gaucher disease Diseases 0.000 description 2
- 208000034826 Genetic Predisposition to Disease Diseases 0.000 description 2
- WHUUTDBJXJRKMK-UHFFFAOYSA-N Glutamic acid Natural products OC(=O)C(N)CCC(O)=O WHUUTDBJXJRKMK-UHFFFAOYSA-N 0.000 description 2
- 102000005744 Glycoside Hydrolases Human genes 0.000 description 2
- 108010031186 Glycoside Hydrolases Proteins 0.000 description 2
- 102000006354 HLA-DR Antigens Human genes 0.000 description 2
- 108010058597 HLA-DR Antigens Proteins 0.000 description 2
- WZUVPPKBWHMQCE-UHFFFAOYSA-N Haematoxylin Chemical compound C12=CC(O)=C(O)C=C2CC2(O)C1C1=CC=C(O)C(O)=C1OC2 WZUVPPKBWHMQCE-UHFFFAOYSA-N 0.000 description 2
- 206010019233 Headaches Diseases 0.000 description 2
- 241000282412 Homo Species 0.000 description 2
- 101000777636 Homo sapiens ADP-ribosyl cyclase/cyclic ADP-ribose hydrolase 1 Proteins 0.000 description 2
- 101000897405 Homo sapiens B-lymphocyte antigen CD20 Proteins 0.000 description 2
- 101000738354 Homo sapiens CD9 antigen Proteins 0.000 description 2
- 101001125026 Homo sapiens Nucleotide-binding oligomerization domain-containing protein 2 Proteins 0.000 description 2
- 101000934346 Homo sapiens T-cell surface antigen CD2 Proteins 0.000 description 2
- 101000716102 Homo sapiens T-cell surface glycoprotein CD4 Proteins 0.000 description 2
- 208000019758 Hypergammaglobulinemia Diseases 0.000 description 2
- 206010021245 Idiopathic thrombocytopenic purpura Diseases 0.000 description 2
- 108700005091 Immunoglobulin Genes Proteins 0.000 description 2
- 108010067060 Immunoglobulin Variable Region Proteins 0.000 description 2
- 102000017727 Immunoglobulin Variable Region Human genes 0.000 description 2
- 102100034343 Integrase Human genes 0.000 description 2
- 102000000588 Interleukin-2 Human genes 0.000 description 2
- 108010002350 Interleukin-2 Proteins 0.000 description 2
- ODKSFYDXXFIFQN-BYPYZUCNSA-P L-argininium(2+) Chemical compound NC(=[NH2+])NCCC[C@H]([NH3+])C(O)=O ODKSFYDXXFIFQN-BYPYZUCNSA-P 0.000 description 2
- DCXYFEDJOCDNAF-REOHCLBHSA-N L-asparagine Chemical compound OC(=O)[C@@H](N)CC(N)=O DCXYFEDJOCDNAF-REOHCLBHSA-N 0.000 description 2
- CKLJMWTZIZZHCS-REOHCLBHSA-N L-aspartic acid Chemical compound OC(=O)[C@@H](N)CC(O)=O CKLJMWTZIZZHCS-REOHCLBHSA-N 0.000 description 2
- AGPKZVBTJJNPAG-WHFBIAKZSA-N L-isoleucine Chemical compound CC[C@H](C)[C@H](N)C(O)=O AGPKZVBTJJNPAG-WHFBIAKZSA-N 0.000 description 2
- KDXKERNSBIXSRK-YFKPBYRVSA-N L-lysine Chemical compound NCCCC[C@H](N)C(O)=O KDXKERNSBIXSRK-YFKPBYRVSA-N 0.000 description 2
- LRQKBLKVPFOOQJ-YFKPBYRVSA-N L-norleucine Chemical group CCCC[C@H]([NH3+])C([O-])=O LRQKBLKVPFOOQJ-YFKPBYRVSA-N 0.000 description 2
- KZSNJWFQEVHDMF-BYPYZUCNSA-N L-valine Chemical compound CC(C)[C@H](N)C(O)=O KZSNJWFQEVHDMF-BYPYZUCNSA-N 0.000 description 2
- 206010055046 Lichen myxoedematosus Diseases 0.000 description 2
- 101100236305 Mus musculus Ly9 gene Proteins 0.000 description 2
- 102000003729 Neprilysin Human genes 0.000 description 2
- 108090000028 Neprilysin Proteins 0.000 description 2
- 102100029441 Nucleotide-binding oligomerization domain-containing protein 2 Human genes 0.000 description 2
- 108020005187 Oligonucleotide Probes Proteins 0.000 description 2
- 108700020796 Oncogene Proteins 0.000 description 2
- 241000283973 Oryctolagus cuniculus Species 0.000 description 2
- 238000012408 PCR amplification Methods 0.000 description 2
- 229910019142 PO4 Inorganic materials 0.000 description 2
- 208000037273 Pathologic Processes Diseases 0.000 description 2
- 241000276498 Pollachius virens Species 0.000 description 2
- 229920001213 Polysorbate 20 Polymers 0.000 description 2
- WCUXLLCKKVVCTQ-UHFFFAOYSA-M Potassium chloride Chemical compound [Cl-].[K+] WCUXLLCKKVVCTQ-UHFFFAOYSA-M 0.000 description 2
- ONIBWKKTOPOVIA-UHFFFAOYSA-N Proline Natural products OC(=O)C1CCCN1 ONIBWKKTOPOVIA-UHFFFAOYSA-N 0.000 description 2
- 208000012322 Raynaud phenomenon Diseases 0.000 description 2
- 102000007056 Recombinant Fusion Proteins Human genes 0.000 description 2
- 108010008281 Recombinant Fusion Proteins Proteins 0.000 description 2
- 238000010818 SYBR green PCR Master Mix Methods 0.000 description 2
- 208000001941 Scleromyxedema Diseases 0.000 description 2
- 241000700584 Simplexvirus Species 0.000 description 2
- FKNQFGJONOIPTF-UHFFFAOYSA-N Sodium cation Chemical compound [Na+] FKNQFGJONOIPTF-UHFFFAOYSA-N 0.000 description 2
- 241000194017 Streptococcus Species 0.000 description 2
- PPBRXRYQALVLMV-UHFFFAOYSA-N Styrene Chemical compound C=CC1=CC=CC=C1 PPBRXRYQALVLMV-UHFFFAOYSA-N 0.000 description 2
- 101710120037 Toxin CcdB Proteins 0.000 description 2
- ISAKRJDGNUQOIC-UHFFFAOYSA-N Uracil Chemical compound O=C1C=CNC(=O)N1 ISAKRJDGNUQOIC-UHFFFAOYSA-N 0.000 description 2
- KZSNJWFQEVHDMF-UHFFFAOYSA-N Valine Natural products CC(C)C(N)C(O)=O KZSNJWFQEVHDMF-UHFFFAOYSA-N 0.000 description 2
- 108700005077 Viral Genes Proteins 0.000 description 2
- 230000021736 acetylation Effects 0.000 description 2
- 238000006640 acetylation reaction Methods 0.000 description 2
- 239000011543 agarose gel Substances 0.000 description 2
- 150000001412 amines Chemical group 0.000 description 2
- 229960003896 aminopterin Drugs 0.000 description 2
- 238000012870 ammonium sulfate precipitation Methods 0.000 description 2
- 239000012491 analyte Substances 0.000 description 2
- 239000008365 aqueous carrier Substances 0.000 description 2
- 235000009582 asparagine Nutrition 0.000 description 2
- 229960001230 asparagine Drugs 0.000 description 2
- 235000003704 aspartic acid Nutrition 0.000 description 2
- 201000003710 autoimmune thrombocytopenic purpura Diseases 0.000 description 2
- 230000005784 autoimmunity Effects 0.000 description 2
- OHDRQQURAXLVGJ-HLVWOLMTSA-N azane;(2e)-3-ethyl-2-[(e)-(3-ethyl-6-sulfo-1,3-benzothiazol-2-ylidene)hydrazinylidene]-1,3-benzothiazole-6-sulfonic acid Chemical compound [NH4+].[NH4+].S/1C2=CC(S([O-])(=O)=O)=CC=C2N(CC)C\1=N/N=C1/SC2=CC(S([O-])(=O)=O)=CC=C2N1CC OHDRQQURAXLVGJ-HLVWOLMTSA-N 0.000 description 2
- 239000011324 bead Substances 0.000 description 2
- IQFYYKKMVGJFEH-UHFFFAOYSA-N beta-L-thymidine Natural products O=C1NC(=O)C(C)=CN1C1OC(CO)C(O)C1 IQFYYKKMVGJFEH-UHFFFAOYSA-N 0.000 description 2
- OQFSQFPPLPISGP-UHFFFAOYSA-N beta-carboxyaspartic acid Natural products OC(=O)C(N)C(C(O)=O)C(O)=O OQFSQFPPLPISGP-UHFFFAOYSA-N 0.000 description 2
- 239000012148 binding buffer Substances 0.000 description 2
- 238000001574 biopsy Methods 0.000 description 2
- 230000017531 blood circulation Effects 0.000 description 2
- 238000010322 bone marrow transplantation Methods 0.000 description 2
- 238000009395 breeding Methods 0.000 description 2
- 230000001488 breeding effect Effects 0.000 description 2
- 239000011575 calcium Substances 0.000 description 2
- 229910052791 calcium Inorganic materials 0.000 description 2
- 229910052799 carbon Inorganic materials 0.000 description 2
- 231100000357 carcinogen Toxicity 0.000 description 2
- 239000003183 carcinogenic agent Substances 0.000 description 2
- 230000007910 cell fusion Effects 0.000 description 2
- 238000005119 centrifugation Methods 0.000 description 2
- 238000004587 chromatography analysis Methods 0.000 description 2
- 230000006690 co-activation Effects 0.000 description 2
- 210000001072 colon Anatomy 0.000 description 2
- 230000000112 colonic effect Effects 0.000 description 2
- 239000000470 constituent Substances 0.000 description 2
- 238000010276 construction Methods 0.000 description 2
- 238000007796 conventional method Methods 0.000 description 2
- 230000008878 coupling Effects 0.000 description 2
- 238000005859 coupling reaction Methods 0.000 description 2
- DDRJAANPRJIHGJ-UHFFFAOYSA-N creatinine Chemical compound CN1CC(=O)NC1=N DDRJAANPRJIHGJ-UHFFFAOYSA-N 0.000 description 2
- 239000012228 culture supernatant Substances 0.000 description 2
- 235000018417 cysteine Nutrition 0.000 description 2
- XUJNEKJLAYXESH-UHFFFAOYSA-N cysteine Natural products SCC(N)C(O)=O XUJNEKJLAYXESH-UHFFFAOYSA-N 0.000 description 2
- OPTASPLRGRRNAP-UHFFFAOYSA-N cytosine Chemical compound NC=1C=CNC(=O)N=1 OPTASPLRGRRNAP-UHFFFAOYSA-N 0.000 description 2
- SUYVUBYJARFZHO-RRKCRQDMSA-N dATP Chemical compound C1=NC=2C(N)=NC=NC=2N1[C@H]1C[C@H](O)[C@@H](COP(O)(=O)OP(O)(=O)OP(O)(O)=O)O1 SUYVUBYJARFZHO-RRKCRQDMSA-N 0.000 description 2
- SUYVUBYJARFZHO-UHFFFAOYSA-N dATP Natural products C1=NC=2C(N)=NC=NC=2N1C1CC(O)C(COP(O)(=O)OP(O)(=O)OP(O)(O)=O)O1 SUYVUBYJARFZHO-UHFFFAOYSA-N 0.000 description 2
- RGWHQCVHVJXOKC-SHYZEUOFSA-J dCTP(4-) Chemical compound O=C1N=C(N)C=CN1[C@@H]1O[C@H](COP([O-])(=O)OP([O-])(=O)OP([O-])([O-])=O)[C@@H](O)C1 RGWHQCVHVJXOKC-SHYZEUOFSA-J 0.000 description 2
- HAAZLUGHYHWQIW-KVQBGUIXSA-N dGTP Chemical compound C1=NC=2C(=O)NC(N)=NC=2N1[C@H]1C[C@H](O)[C@@H](COP(O)(=O)OP(O)(=O)OP(O)(O)=O)O1 HAAZLUGHYHWQIW-KVQBGUIXSA-N 0.000 description 2
- NHVNXKFIZYSCEB-XLPZGREQSA-N dTTP Chemical compound O=C1NC(=O)C(C)=CN1[C@@H]1O[C@H](COP(O)(=O)OP(O)(=O)OP(O)(O)=O)[C@@H](O)C1 NHVNXKFIZYSCEB-XLPZGREQSA-N 0.000 description 2
- 210000004443 dendritic cell Anatomy 0.000 description 2
- 238000013461 design Methods 0.000 description 2
- 230000004069 differentiation Effects 0.000 description 2
- 230000029087 digestion Effects 0.000 description 2
- NAGJZTKCGNOGPW-UHFFFAOYSA-K dioxido-sulfanylidene-sulfido-$l^{5}-phosphane Chemical compound [O-]P([O-])([S-])=S NAGJZTKCGNOGPW-UHFFFAOYSA-K 0.000 description 2
- 238000010494 dissociation reaction Methods 0.000 description 2
- 230000005593 dissociations Effects 0.000 description 2
- 230000003828 downregulation Effects 0.000 description 2
- 210000005069 ears Anatomy 0.000 description 2
- 238000004520 electroporation Methods 0.000 description 2
- 210000002257 embryonic structure Anatomy 0.000 description 2
- 108010030074 endodeoxyribonuclease MluI Proteins 0.000 description 2
- 210000002889 endothelial cell Anatomy 0.000 description 2
- 201000010063 epididymitis Diseases 0.000 description 2
- 239000003797 essential amino acid Substances 0.000 description 2
- 235000020776 essential amino acid Nutrition 0.000 description 2
- 150000002148 esters Chemical class 0.000 description 2
- 210000003527 eukaryotic cell Anatomy 0.000 description 2
- 206010016256 fatigue Diseases 0.000 description 2
- 239000012997 ficoll-paque Substances 0.000 description 2
- 239000006260 foam Substances 0.000 description 2
- 238000009472 formulation Methods 0.000 description 2
- 230000005714 functional activity Effects 0.000 description 2
- 230000002496 gastric effect Effects 0.000 description 2
- 238000001502 gel electrophoresis Methods 0.000 description 2
- 235000013922 glutamic acid Nutrition 0.000 description 2
- UYTPUPDQBNUYGX-UHFFFAOYSA-N guanine Chemical compound O=C1NC(N)=NC2=C1N=CN2 UYTPUPDQBNUYGX-UHFFFAOYSA-N 0.000 description 2
- 231100000869 headache Toxicity 0.000 description 2
- 208000007475 hemolytic anemia Diseases 0.000 description 2
- 229940094991 herring sperm dna Drugs 0.000 description 2
- HNDVDQJCIGZPNO-UHFFFAOYSA-N histidine Natural products OC(=O)C(N)CC1=CN=CN1 HNDVDQJCIGZPNO-UHFFFAOYSA-N 0.000 description 2
- 230000002962 histologic effect Effects 0.000 description 2
- 238000002744 homologous recombination Methods 0.000 description 2
- 230000006801 homologous recombination Effects 0.000 description 2
- 230000002209 hydrophobic effect Effects 0.000 description 2
- 230000003100 immobilizing effect Effects 0.000 description 2
- 210000000987 immune system Anatomy 0.000 description 2
- 230000003053 immunization Effects 0.000 description 2
- 238000002649 immunization Methods 0.000 description 2
- 238000003018 immunoassay Methods 0.000 description 2
- 238000003119 immunoblot Methods 0.000 description 2
- 239000003018 immunosuppressive agent Substances 0.000 description 2
- 230000001976 improved effect Effects 0.000 description 2
- 238000007901 in situ hybridization Methods 0.000 description 2
- 238000000099 in vitro assay Methods 0.000 description 2
- 208000015181 infectious disease Diseases 0.000 description 2
- 230000002757 inflammatory effect Effects 0.000 description 2
- 230000028709 inflammatory response Effects 0.000 description 2
- 238000001802 infusion Methods 0.000 description 2
- 239000003112 inhibitor Substances 0.000 description 2
- 238000011835 investigation Methods 0.000 description 2
- PHTQWCKDNZKARW-UHFFFAOYSA-N isoamylol Chemical compound CC(C)CCO PHTQWCKDNZKARW-UHFFFAOYSA-N 0.000 description 2
- DRAVOWXCEBXPTN-UHFFFAOYSA-N isoguanine Chemical compound NC1=NC(=O)NC2=C1NC=N2 DRAVOWXCEBXPTN-UHFFFAOYSA-N 0.000 description 2
- AGPKZVBTJJNPAG-UHFFFAOYSA-N isoleucine Natural products CCC(C)C(N)C(O)=O AGPKZVBTJJNPAG-UHFFFAOYSA-N 0.000 description 2
- 229960000310 isoleucine Drugs 0.000 description 2
- 208000019207 lichen myxedematosus Diseases 0.000 description 2
- 239000003446 ligand Substances 0.000 description 2
- 238000007834 ligase chain reaction Methods 0.000 description 2
- 230000003211 malignant effect Effects 0.000 description 2
- 210000003519 mature b lymphocyte Anatomy 0.000 description 2
- 238000005259 measurement Methods 0.000 description 2
- 230000007246 mechanism Effects 0.000 description 2
- 238000002844 melting Methods 0.000 description 2
- 230000008018 melting Effects 0.000 description 2
- 210000001806 memory b lymphocyte Anatomy 0.000 description 2
- 229910052751 metal Inorganic materials 0.000 description 2
- 239000002184 metal Substances 0.000 description 2
- MYWUZJCMWCOHBA-VIFPVBQESA-N methamphetamine Chemical compound CN[C@@H](C)CC1=CC=CC=C1 MYWUZJCMWCOHBA-VIFPVBQESA-N 0.000 description 2
- 102000035118 modified proteins Human genes 0.000 description 2
- 108091005573 modified proteins Proteins 0.000 description 2
- 210000001331 nose Anatomy 0.000 description 2
- 239000002751 oligonucleotide probe Substances 0.000 description 2
- 230000003287 optical effect Effects 0.000 description 2
- 230000002018 overexpression Effects 0.000 description 2
- 235000006408 oxalic acid Nutrition 0.000 description 2
- 238000007911 parenteral administration Methods 0.000 description 2
- 239000002245 particle Substances 0.000 description 2
- 230000001717 pathogenic effect Effects 0.000 description 2
- 230000009054 pathological process Effects 0.000 description 2
- 230000000149 penetrating effect Effects 0.000 description 2
- 210000004976 peripheral blood cell Anatomy 0.000 description 2
- 102000013415 peroxidase activity proteins Human genes 0.000 description 2
- 108040007629 peroxidase activity proteins Proteins 0.000 description 2
- NBIIXXVUZAFLBC-UHFFFAOYSA-K phosphate Chemical compound [O-]P([O-])([O-])=O NBIIXXVUZAFLBC-UHFFFAOYSA-K 0.000 description 2
- 239000010452 phosphate Substances 0.000 description 2
- 150000004713 phosphodiesters Chemical group 0.000 description 2
- PTMHPRAIXMAOOB-UHFFFAOYSA-L phosphoramidate Chemical compound NP([O-])([O-])=O PTMHPRAIXMAOOB-UHFFFAOYSA-L 0.000 description 2
- 230000026731 phosphorylation Effects 0.000 description 2
- 238000006366 phosphorylation reaction Methods 0.000 description 2
- 230000008488 polyadenylation Effects 0.000 description 2
- 239000000256 polyoxyethylene sorbitan monolaurate Substances 0.000 description 2
- 235000010486 polyoxyethylene sorbitan monolaurate Nutrition 0.000 description 2
- 238000001556 precipitation Methods 0.000 description 2
- 230000002265 prevention Effects 0.000 description 2
- XOJVVFBFDXDTEG-UHFFFAOYSA-N pristane Chemical compound CC(C)CCCC(C)CCCC(C)CCCC(C)C XOJVVFBFDXDTEG-UHFFFAOYSA-N 0.000 description 2
- 230000008569 process Effects 0.000 description 2
- 238000000159 protein binding assay Methods 0.000 description 2
- 238000010791 quenching Methods 0.000 description 2
- 230000000171 quenching effect Effects 0.000 description 2
- 230000005855 radiation Effects 0.000 description 2
- 230000009257 reactivity Effects 0.000 description 2
- 102000005962 receptors Human genes 0.000 description 2
- 108020003175 receptors Proteins 0.000 description 2
- 239000012557 regeneration buffer Substances 0.000 description 2
- 239000011347 resin Substances 0.000 description 2
- 229920005989 resin Polymers 0.000 description 2
- 230000000717 retained effect Effects 0.000 description 2
- 230000001177 retroviral effect Effects 0.000 description 2
- 150000003290 ribose derivatives Chemical group 0.000 description 2
- 210000003705 ribosome Anatomy 0.000 description 2
- 238000007423 screening assay Methods 0.000 description 2
- 230000003248 secreting effect Effects 0.000 description 2
- 238000000926 separation method Methods 0.000 description 2
- 208000013220 shortness of breath Diseases 0.000 description 2
- 239000000377 silicon dioxide Substances 0.000 description 2
- 210000003491 skin Anatomy 0.000 description 2
- 239000011780 sodium chloride Substances 0.000 description 2
- 229910001415 sodium ion Inorganic materials 0.000 description 2
- 210000000278 spinal cord Anatomy 0.000 description 2
- 150000003431 steroids Chemical class 0.000 description 2
- UCSJYZPVAKXKNQ-HZYVHMACSA-N streptomycin Chemical compound CN[C@H]1[C@H](O)[C@@H](O)[C@H](CO)O[C@H]1O[C@@H]1[C@](C=O)(O)[C@H](C)O[C@H]1O[C@@H]1[C@@H](NC(N)=N)[C@H](O)[C@@H](NC(N)=N)[C@H](O)[C@H]1O UCSJYZPVAKXKNQ-HZYVHMACSA-N 0.000 description 2
- 150000008163 sugars Chemical class 0.000 description 2
- 239000013589 supplement Substances 0.000 description 2
- 208000001608 teratocarcinoma Diseases 0.000 description 2
- RYYWUUFWQRZTIU-UHFFFAOYSA-K thiophosphate Chemical compound [O-]P([O-])([O-])=S RYYWUUFWQRZTIU-UHFFFAOYSA-K 0.000 description 2
- 229940104230 thymidine Drugs 0.000 description 2
- RWQNBRDOKXIBIV-UHFFFAOYSA-N thymine Chemical compound CC1=CNC(=O)NC1=O RWQNBRDOKXIBIV-UHFFFAOYSA-N 0.000 description 2
- 230000009466 transformation Effects 0.000 description 2
- 210000004881 tumor cell Anatomy 0.000 description 2
- 230000004614 tumor growth Effects 0.000 description 2
- 230000036269 ulceration Effects 0.000 description 2
- 210000002700 urine Anatomy 0.000 description 2
- 229960005486 vaccine Drugs 0.000 description 2
- 239000004474 valine Substances 0.000 description 2
- 238000011179 visual inspection Methods 0.000 description 2
- 239000008215 water for injection Substances 0.000 description 2
- 230000003442 weekly effect Effects 0.000 description 2
- 230000004580 weight loss Effects 0.000 description 2
- 208000016261 weight loss Diseases 0.000 description 2
- 238000001262 western blot Methods 0.000 description 2
- 210000005253 yeast cell Anatomy 0.000 description 2
- HDTRYLNUVZCQOY-UHFFFAOYSA-N α-D-glucopyranosyl-α-D-glucopyranoside Natural products OC1C(O)C(O)C(CO)OC1OC1C(O)C(O)C(O)C(CO)O1 HDTRYLNUVZCQOY-UHFFFAOYSA-N 0.000 description 1
- FXYPGCIGRDZWNR-UHFFFAOYSA-N (2,5-dioxopyrrolidin-1-yl) 3-[[3-(2,5-dioxopyrrolidin-1-yl)oxy-3-oxopropyl]disulfanyl]propanoate Chemical compound O=C1CCC(=O)N1OC(=O)CCSSCCC(=O)ON1C(=O)CCC1=O FXYPGCIGRDZWNR-UHFFFAOYSA-N 0.000 description 1
- UKAUYVFTDYCKQA-UHFFFAOYSA-N -2-Amino-4-hydroxybutanoic acid Natural products OC(=O)C(N)CCO UKAUYVFTDYCKQA-UHFFFAOYSA-N 0.000 description 1
- 125000003287 1H-imidazol-4-ylmethyl group Chemical group [H]N1C([H])=NC(C([H])([H])[*])=C1[H] 0.000 description 1
- 150000003923 2,5-pyrrolediones Chemical class 0.000 description 1
- WDLHEUQWTUUMMA-UHFFFAOYSA-N 2,6,10,12-tetramethylpentadecane Chemical compound CCCC(C)CC(C)CCCC(C)CCCC(C)C WDLHEUQWTUUMMA-UHFFFAOYSA-N 0.000 description 1
- JKMHFZQWWAIEOD-UHFFFAOYSA-N 2-[4-(2-hydroxyethyl)piperazin-1-yl]ethanesulfonic acid Chemical compound OCC[NH+]1CCN(CCS([O-])(=O)=O)CC1 JKMHFZQWWAIEOD-UHFFFAOYSA-N 0.000 description 1
- GOJUJUVQIVIZAV-UHFFFAOYSA-N 2-amino-4,6-dichloropyrimidine-5-carbaldehyde Chemical group NC1=NC(Cl)=C(C=O)C(Cl)=N1 GOJUJUVQIVIZAV-UHFFFAOYSA-N 0.000 description 1
- XQCZBXHVTFVIFE-UHFFFAOYSA-N 2-amino-4-hydroxypyrimidine Chemical compound NC1=NC=CC(O)=N1 XQCZBXHVTFVIFE-UHFFFAOYSA-N 0.000 description 1
- JRYMOPZHXMVHTA-DAGMQNCNSA-N 2-amino-7-[(2r,3r,4s,5r)-3,4-dihydroxy-5-(hydroxymethyl)oxolan-2-yl]-1h-pyrrolo[2,3-d]pyrimidin-4-one Chemical compound C1=CC=2C(=O)NC(N)=NC=2N1[C@@H]1O[C@H](CO)[C@@H](O)[C@H]1O JRYMOPZHXMVHTA-DAGMQNCNSA-N 0.000 description 1
- OZDAOHVKBFBBMZ-UHFFFAOYSA-N 2-aminopentanedioic acid;hydrate Chemical compound O.OC(=O)C(N)CCC(O)=O OZDAOHVKBFBBMZ-UHFFFAOYSA-N 0.000 description 1
- NLPWSMKACWGINL-UHFFFAOYSA-N 4-azido-2-hydroxybenzoic acid Chemical compound OC(=O)C1=CC=C(N=[N+]=[N-])C=C1O NLPWSMKACWGINL-UHFFFAOYSA-N 0.000 description 1
- QRXMUCSWCMTJGU-UHFFFAOYSA-N 5-bromo-4-chloro-3-indolyl phosphate Chemical compound C1=C(Br)C(Cl)=C2C(OP(O)(=O)O)=CNC2=C1 QRXMUCSWCMTJGU-UHFFFAOYSA-N 0.000 description 1
- 102100040623 60S ribosomal protein L41 Human genes 0.000 description 1
- 206010000097 Abdominal tenderness Diseases 0.000 description 1
- QTBSBXVTEAMEQO-UHFFFAOYSA-M Acetate Chemical compound CC([O-])=O QTBSBXVTEAMEQO-UHFFFAOYSA-M 0.000 description 1
- 241000251468 Actinopterygii Species 0.000 description 1
- 208000026872 Addison Disease Diseases 0.000 description 1
- 229930024421 Adenine Natural products 0.000 description 1
- GFFGJBXGBJISGV-UHFFFAOYSA-N Adenine Chemical compound NC1=NC=NC2=C1N=CN2 GFFGJBXGBJISGV-UHFFFAOYSA-N 0.000 description 1
- 229920000936 Agarose Polymers 0.000 description 1
- 108010088751 Albumins Proteins 0.000 description 1
- 102000009027 Albumins Human genes 0.000 description 1
- 102100035248 Alpha-(1,3)-fucosyltransferase 4 Human genes 0.000 description 1
- 102100021266 Alpha-(1,6)-fucosyltransferase Human genes 0.000 description 1
- 102100022749 Aminopeptidase N Human genes 0.000 description 1
- USFZMSVCRYTOJT-UHFFFAOYSA-N Ammonium acetate Chemical compound N.CC(O)=O USFZMSVCRYTOJT-UHFFFAOYSA-N 0.000 description 1
- 239000005695 Ammonium acetate Substances 0.000 description 1
- 102000000412 Annexin Human genes 0.000 description 1
- 108050008874 Annexin Proteins 0.000 description 1
- 241000203069 Archaea Species 0.000 description 1
- MIAIYIMCGDSXLY-UHFFFAOYSA-N Armexin Natural products CC(=O)OC1CC(OC(=O)C)C2(C)CCC3C(OC(=O)C3=C)C2=C1C MIAIYIMCGDSXLY-UHFFFAOYSA-N 0.000 description 1
- 206010003694 Atrophy Diseases 0.000 description 1
- 102100022717 Atypical chemokine receptor 1 Human genes 0.000 description 1
- 206010003827 Autoimmune hepatitis Diseases 0.000 description 1
- 108020004513 Bacterial RNA Proteins 0.000 description 1
- 208000023328 Basedow disease Diseases 0.000 description 1
- 108700004676 Bence Jones Proteins 0.000 description 1
- 102100026189 Beta-galactosidase Human genes 0.000 description 1
- 206010061728 Bone lesion Diseases 0.000 description 1
- 208000018084 Bone neoplasm Diseases 0.000 description 1
- 206010006002 Bone pain Diseases 0.000 description 1
- 125000001433 C-terminal amino-acid group Chemical group 0.000 description 1
- 238000011746 C57BL/6J (JAX™ mouse strain) Methods 0.000 description 1
- 102100027207 CD27 antigen Human genes 0.000 description 1
- 210000001266 CD8-positive T-lymphocyte Anatomy 0.000 description 1
- UXVMQQNJUSDDNG-UHFFFAOYSA-L Calcium chloride Chemical compound [Cl-].[Cl-].[Ca+2] UXVMQQNJUSDDNG-UHFFFAOYSA-L 0.000 description 1
- 241000222122 Candida albicans Species 0.000 description 1
- 241000222128 Candida maltosa Species 0.000 description 1
- 102000014914 Carrier Proteins Human genes 0.000 description 1
- 108010078791 Carrier Proteins Proteins 0.000 description 1
- 241000700199 Cavia porcellus Species 0.000 description 1
- 102000000844 Cell Surface Receptors Human genes 0.000 description 1
- 108010001857 Cell Surface Receptors Proteins 0.000 description 1
- 231100000023 Cell-mediated cytotoxicity Toxicity 0.000 description 1
- 206010057250 Cell-mediated cytotoxicity Diseases 0.000 description 1
- 102000019034 Chemokines Human genes 0.000 description 1
- 108010012236 Chemokines Proteins 0.000 description 1
- 206010061764 Chromosomal deletion Diseases 0.000 description 1
- KRKNYBCHXYNGOX-UHFFFAOYSA-K Citrate Chemical compound [O-]C(=O)CC(O)(CC([O-])=O)C([O-])=O KRKNYBCHXYNGOX-UHFFFAOYSA-K 0.000 description 1
- 206010053567 Coagulopathies Diseases 0.000 description 1
- 208000001333 Colorectal Neoplasms Diseases 0.000 description 1
- 108010062580 Concanavalin A Proteins 0.000 description 1
- 208000032170 Congenital Abnormalities Diseases 0.000 description 1
- 241000557626 Corvus corax Species 0.000 description 1
- 102000036364 Cullin Ring E3 Ligases Human genes 0.000 description 1
- CMSMOCZEIVJLDB-UHFFFAOYSA-N Cyclophosphamide Chemical compound ClCCN(CCCl)P1(=O)NCCCO1 CMSMOCZEIVJLDB-UHFFFAOYSA-N 0.000 description 1
- IGXWBGJHJZYPQS-SSDOTTSWSA-N D-Luciferin Chemical compound OC(=O)[C@H]1CSC(C=2SC3=CC=C(O)C=C3N=2)=N1 IGXWBGJHJZYPQS-SSDOTTSWSA-N 0.000 description 1
- 102000016185 DNA ligase 4 Human genes 0.000 description 1
- 108050004671 DNA ligase 4 Proteins 0.000 description 1
- 108050009160 DNA polymerase 1 Proteins 0.000 description 1
- 108010014303 DNA-directed DNA polymerase Proteins 0.000 description 1
- 102000016928 DNA-directed DNA polymerase Human genes 0.000 description 1
- 102000004163 DNA-directed RNA polymerases Human genes 0.000 description 1
- CYCGRDQQIOGCKX-UHFFFAOYSA-N Dehydro-luciferin Natural products OC(=O)C1=CSC(C=2SC3=CC(O)=CC=C3N=2)=N1 CYCGRDQQIOGCKX-UHFFFAOYSA-N 0.000 description 1
- 108010053770 Deoxyribonucleases Proteins 0.000 description 1
- 102000016911 Deoxyribonucleases Human genes 0.000 description 1
- AHCYMLUZIRLXAA-SHYZEUOFSA-N Deoxyuridine 5'-triphosphate Chemical compound O1[C@H](COP(O)(=O)OP(O)(=O)OP(O)(O)=O)[C@@H](O)C[C@@H]1N1C(=O)NC(=O)C=C1 AHCYMLUZIRLXAA-SHYZEUOFSA-N 0.000 description 1
- 201000004624 Dermatitis Diseases 0.000 description 1
- 206010012438 Dermatitis atopic Diseases 0.000 description 1
- 229920002307 Dextran Polymers 0.000 description 1
- SHIBSTMRCDJXLN-UHFFFAOYSA-N Digoxigenin Natural products C1CC(C2C(C3(C)CCC(O)CC3CC2)CC2O)(O)C2(C)C1C1=CC(=O)OC1 SHIBSTMRCDJXLN-UHFFFAOYSA-N 0.000 description 1
- 238000012286 ELISA Assay Methods 0.000 description 1
- 102100029722 Ectonucleoside triphosphate diphosphohydrolase 1 Human genes 0.000 description 1
- 241000196324 Embryophyta Species 0.000 description 1
- 101710202200 Endolysin A Proteins 0.000 description 1
- 108010042407 Endonucleases Proteins 0.000 description 1
- 102000004533 Endonucleases Human genes 0.000 description 1
- 206010014989 Epidermolysis bullosa Diseases 0.000 description 1
- 241000283073 Equus caballus Species 0.000 description 1
- 108091029865 Exogenous DNA Proteins 0.000 description 1
- 108010008177 Fd immunoglobulins Proteins 0.000 description 1
- 241000282326 Felis catus Species 0.000 description 1
- 241000192125 Firmicutes Species 0.000 description 1
- 241000233866 Fungi Species 0.000 description 1
- 241000287828 Gallus gallus Species 0.000 description 1
- 208000003098 Ganglion Cysts Diseases 0.000 description 1
- 206010018364 Glomerulonephritis Diseases 0.000 description 1
- SXRSQZLOMIGNAQ-UHFFFAOYSA-N Glutaraldehyde Chemical compound O=CCCCC=O SXRSQZLOMIGNAQ-UHFFFAOYSA-N 0.000 description 1
- 244000068988 Glycine max Species 0.000 description 1
- 235000010469 Glycine max Nutrition 0.000 description 1
- 102100035716 Glycophorin-A Human genes 0.000 description 1
- 108091005250 Glycophorins Proteins 0.000 description 1
- 208000015023 Graves' disease Diseases 0.000 description 1
- 208000035895 Guillain-Barré syndrome Diseases 0.000 description 1
- HVLSXIKZNLPZJJ-TXZCQADKSA-N HA peptide Chemical compound C([C@@H](C(=O)N[C@@H](CC(O)=O)C(=O)N[C@@H](C(C)C)C(=O)N1[C@@H](CCC1)C(=O)N[C@@H](CC(O)=O)C(=O)N[C@@H](CC=1C=CC(O)=CC=1)C(=O)N[C@@H](C)C(O)=O)NC(=O)[C@H]1N(CCC1)C(=O)[C@@H](N)CC=1C=CC(O)=CC=1)C1=CC=C(O)C=C1 HVLSXIKZNLPZJJ-TXZCQADKSA-N 0.000 description 1
- 208000001204 Hashimoto Disease Diseases 0.000 description 1
- 208000030836 Hashimoto thyroiditis Diseases 0.000 description 1
- 208000002250 Hematologic Neoplasms Diseases 0.000 description 1
- 102100031573 Hematopoietic progenitor cell antigen CD34 Human genes 0.000 description 1
- 208000032843 Hemorrhage Diseases 0.000 description 1
- 229920000209 Hexadimethrine bromide Polymers 0.000 description 1
- LYCVKHSJGDMDLM-LURJTMIESA-N His-Gly Chemical compound OC(=O)CNC(=O)[C@@H](N)CC1=CN=CN1 LYCVKHSJGDMDLM-LURJTMIESA-N 0.000 description 1
- 208000017604 Hodgkin disease Diseases 0.000 description 1
- 208000021519 Hodgkin lymphoma Diseases 0.000 description 1
- 208000010747 Hodgkins lymphoma Diseases 0.000 description 1
- 101000674326 Homo sapiens 60S ribosomal protein L41 Proteins 0.000 description 1
- 101001022185 Homo sapiens Alpha-(1,3)-fucosyltransferase 4 Proteins 0.000 description 1
- 101000819490 Homo sapiens Alpha-(1,6)-fucosyltransferase Proteins 0.000 description 1
- 101000757160 Homo sapiens Aminopeptidase N Proteins 0.000 description 1
- 101000678879 Homo sapiens Atypical chemokine receptor 1 Proteins 0.000 description 1
- 101100383038 Homo sapiens CD19 gene Proteins 0.000 description 1
- 101000914511 Homo sapiens CD27 antigen Proteins 0.000 description 1
- 101001012447 Homo sapiens Ectonucleoside triphosphate diphosphohydrolase 1 Proteins 0.000 description 1
- 101000777663 Homo sapiens Hematopoietic progenitor cell antigen CD34 Proteins 0.000 description 1
- 101001078143 Homo sapiens Integrin alpha-IIb Proteins 0.000 description 1
- 101000599852 Homo sapiens Intercellular adhesion molecule 1 Proteins 0.000 description 1
- 101001057504 Homo sapiens Interferon-stimulated gene 20 kDa protein Proteins 0.000 description 1
- 101001055144 Homo sapiens Interleukin-2 receptor subunit alpha Proteins 0.000 description 1
- 101000878605 Homo sapiens Low affinity immunoglobulin epsilon Fc receptor Proteins 0.000 description 1
- 101000917858 Homo sapiens Low affinity immunoglobulin gamma Fc region receptor III-A Proteins 0.000 description 1
- 101000917839 Homo sapiens Low affinity immunoglobulin gamma Fc region receptor III-B Proteins 0.000 description 1
- 101001063392 Homo sapiens Lymphocyte function-associated antigen 3 Proteins 0.000 description 1
- 101000934338 Homo sapiens Myeloid cell surface antigen CD33 Proteins 0.000 description 1
- 101000994307 Homo sapiens Protein ITPRID2 Proteins 0.000 description 1
- 101000633780 Homo sapiens Signaling lymphocytic activation molecule Proteins 0.000 description 1
- 101000835093 Homo sapiens Transferrin receptor protein 1 Proteins 0.000 description 1
- 101001074035 Homo sapiens Zinc finger protein GLI2 Proteins 0.000 description 1
- 108010001336 Horseradish Peroxidase Proteins 0.000 description 1
- 108091006905 Human Serum Albumin Proteins 0.000 description 1
- 102000008100 Human Serum Albumin Human genes 0.000 description 1
- PMMYEEVYMWASQN-DMTCNVIQSA-N Hydroxyproline Chemical compound O[C@H]1CN[C@H](C(O)=O)C1 PMMYEEVYMWASQN-DMTCNVIQSA-N 0.000 description 1
- 206010051151 Hyperviscosity syndrome Diseases 0.000 description 1
- 102000009786 Immunoglobulin Constant Regions Human genes 0.000 description 1
- 108010009817 Immunoglobulin Constant Regions Proteins 0.000 description 1
- 102000012745 Immunoglobulin Subunits Human genes 0.000 description 1
- 108010079585 Immunoglobulin Subunits Proteins 0.000 description 1
- 206010062016 Immunosuppression Diseases 0.000 description 1
- 101710203526 Integrase Proteins 0.000 description 1
- 102100025306 Integrin alpha-IIb Human genes 0.000 description 1
- 102100037877 Intercellular adhesion molecule 1 Human genes 0.000 description 1
- 102100027268 Interferon-stimulated gene 20 kDa protein Human genes 0.000 description 1
- 108090000174 Interleukin-10 Proteins 0.000 description 1
- 102000004889 Interleukin-6 Human genes 0.000 description 1
- 108090001005 Interleukin-6 Proteins 0.000 description 1
- 244000285963 Kluyveromyces fragilis Species 0.000 description 1
- 235000014663 Kluyveromyces fragilis Nutrition 0.000 description 1
- 241000235058 Komagataella pastoris Species 0.000 description 1
- XUJNEKJLAYXESH-REOHCLBHSA-N L-Cysteine Chemical compound SC[C@H](N)C(O)=O XUJNEKJLAYXESH-REOHCLBHSA-N 0.000 description 1
- ONIBWKKTOPOVIA-BYPYZUCNSA-N L-Proline Chemical compound OC(=O)[C@@H]1CCCN1 ONIBWKKTOPOVIA-BYPYZUCNSA-N 0.000 description 1
- UKAUYVFTDYCKQA-VKHMYHEASA-N L-homoserine Chemical group OC(=O)[C@@H](N)CCO UKAUYVFTDYCKQA-VKHMYHEASA-N 0.000 description 1
- QEFRNWWLZKMPFJ-ZXPFJRLXSA-N L-methionine (R)-S-oxide Chemical group C[S@@](=O)CC[C@H]([NH3+])C([O-])=O QEFRNWWLZKMPFJ-ZXPFJRLXSA-N 0.000 description 1
- QEFRNWWLZKMPFJ-UHFFFAOYSA-N L-methionine sulphoxide Chemical group CS(=O)CCC(N)C(O)=O QEFRNWWLZKMPFJ-UHFFFAOYSA-N 0.000 description 1
- OUYCCCASQSFEME-QMMMGPOBSA-N L-tyrosine Chemical compound OC(=O)[C@@H](N)CC1=CC=C(O)C=C1 OUYCCCASQSFEME-QMMMGPOBSA-N 0.000 description 1
- 241000270322 Lepidosauria Species 0.000 description 1
- 208000012309 Linear IgA disease Diseases 0.000 description 1
- 102100038007 Low affinity immunoglobulin epsilon Fc receptor Human genes 0.000 description 1
- 102100029185 Low affinity immunoglobulin gamma Fc region receptor III-B Human genes 0.000 description 1
- DDWFXDSYGUXRAY-UHFFFAOYSA-N Luciferin Natural products CCc1c(C)c(CC2NC(=O)C(=C2C=C)C)[nH]c1Cc3[nH]c4C(=C5/NC(CC(=O)O)C(C)C5CC(=O)O)CC(=O)c4c3C DDWFXDSYGUXRAY-UHFFFAOYSA-N 0.000 description 1
- 239000006142 Luria-Bertani Agar Substances 0.000 description 1
- 102100030984 Lymphocyte function-associated antigen 3 Human genes 0.000 description 1
- FYYHWMGAXLPEAU-UHFFFAOYSA-N Magnesium Chemical compound [Mg] FYYHWMGAXLPEAU-UHFFFAOYSA-N 0.000 description 1
- YALRCXHVQYBSJC-UHFFFAOYSA-N Mammea A/AB Chemical compound C12=C(O)C(C(=O)C(C)CC)=C(O)C(CC=C(C)C)=C2OC(=O)C=C1C1=CC=CC=C1 YALRCXHVQYBSJC-UHFFFAOYSA-N 0.000 description 1
- 102000018697 Membrane Proteins Human genes 0.000 description 1
- 108010052285 Membrane Proteins Proteins 0.000 description 1
- 206010027476 Metastases Diseases 0.000 description 1
- 206010049567 Miller Fisher syndrome Diseases 0.000 description 1
- 101710154541 Modulator protein Proteins 0.000 description 1
- 241000713333 Mouse mammary tumor virus Species 0.000 description 1
- 206010048723 Multiple-drug resistance Diseases 0.000 description 1
- 101100370002 Mus musculus Tnfsf14 gene Proteins 0.000 description 1
- 101710135898 Myc proto-oncogene protein Proteins 0.000 description 1
- 102100038895 Myc proto-oncogene protein Human genes 0.000 description 1
- 208000033776 Myeloid Acute Leukemia Diseases 0.000 description 1
- 102100025243 Myeloid cell surface antigen CD33 Human genes 0.000 description 1
- NQTADLQHYWFPDB-UHFFFAOYSA-N N-Hydroxysuccinimide Chemical class ON1C(=O)CCC1=O NQTADLQHYWFPDB-UHFFFAOYSA-N 0.000 description 1
- 229930193140 Neomycin Natural products 0.000 description 1
- 241000221960 Neurospora Species 0.000 description 1
- 101100384865 Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987) cot-1 gene Proteins 0.000 description 1
- 101100353526 Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987) pca-2 gene Proteins 0.000 description 1
- 239000000020 Nitrocellulose Substances 0.000 description 1
- 101710163270 Nuclease Proteins 0.000 description 1
- 241000320412 Ogataea angusta Species 0.000 description 1
- 102000043276 Oncogene Human genes 0.000 description 1
- 208000001132 Osteoporosis Diseases 0.000 description 1
- 208000002193 Pain Diseases 0.000 description 1
- 241000282577 Pan troglodytes Species 0.000 description 1
- 101100202644 Parasynechococcus marenigrum (strain WH8102) bsmB gene Proteins 0.000 description 1
- 241001494479 Pecora Species 0.000 description 1
- 206010034277 Pemphigoid Diseases 0.000 description 1
- 201000011152 Pemphigus Diseases 0.000 description 1
- 241000721454 Pemphigus Species 0.000 description 1
- 229930182555 Penicillin Natural products 0.000 description 1
- JGSARLDLIJGVTE-MBNYWOFBSA-N Penicillin G Chemical compound N([C@H]1[C@H]2SC([C@@H](N2C1=O)C(O)=O)(C)C)C(=O)CC1=CC=CC=C1 JGSARLDLIJGVTE-MBNYWOFBSA-N 0.000 description 1
- 102000057297 Pepsin A Human genes 0.000 description 1
- 108090000284 Pepsin A Proteins 0.000 description 1
- 102000035195 Peptidases Human genes 0.000 description 1
- 108091005804 Peptidases Proteins 0.000 description 1
- 240000007643 Phytolacca americana Species 0.000 description 1
- 235000009074 Phytolacca americana Nutrition 0.000 description 1
- 241000235648 Pichia Species 0.000 description 1
- 229920002535 Polyethylene Glycol 1500 Polymers 0.000 description 1
- 239000004743 Polypropylene Substances 0.000 description 1
- 239000004793 Polystyrene Substances 0.000 description 1
- 206010036790 Productive cough Diseases 0.000 description 1
- 206010037660 Pyrexia Diseases 0.000 description 1
- 238000012341 Quantitative reverse-transcriptase PCR Methods 0.000 description 1
- 108020004518 RNA Probes Proteins 0.000 description 1
- 238000002123 RNA extraction Methods 0.000 description 1
- 239000003391 RNA probe Substances 0.000 description 1
- 230000006819 RNA synthesis Effects 0.000 description 1
- 108010092799 RNA-directed DNA polymerase Proteins 0.000 description 1
- 108091030071 RNAI Proteins 0.000 description 1
- 206010057071 Rectal tenesmus Diseases 0.000 description 1
- 208000001647 Renal Insufficiency Diseases 0.000 description 1
- 108010073443 Ribi adjuvant Proteins 0.000 description 1
- 102000006382 Ribonucleases Human genes 0.000 description 1
- 108010083644 Ribonucleases Proteins 0.000 description 1
- 108091028664 Ribonucleotide Proteins 0.000 description 1
- 108091006629 SLC13A2 Proteins 0.000 description 1
- 241000235347 Schizosaccharomyces pombe Species 0.000 description 1
- 206010039710 Scleroderma Diseases 0.000 description 1
- XUIMIQQOPSSXEZ-UHFFFAOYSA-N Silicon Chemical compound [Si] XUIMIQQOPSSXEZ-UHFFFAOYSA-N 0.000 description 1
- 101100043635 Solanum tuberosum SS2 gene Proteins 0.000 description 1
- 208000006045 Spondylarthropathies Diseases 0.000 description 1
- 208000005250 Spontaneous Fractures Diseases 0.000 description 1
- 238000000692 Student's t-test Methods 0.000 description 1
- 241000282898 Sus scrofa Species 0.000 description 1
- 208000005400 Synovial Cyst Diseases 0.000 description 1
- 108091008874 T cell receptors Proteins 0.000 description 1
- 102000016266 T-Cell Antigen Receptors Human genes 0.000 description 1
- 102100025237 T-cell surface antigen CD2 Human genes 0.000 description 1
- 239000004098 Tetracycline Substances 0.000 description 1
- 108010034949 Thyroglobulin Proteins 0.000 description 1
- 102000009843 Thyroglobulin Human genes 0.000 description 1
- 102000040945 Transcription factor Human genes 0.000 description 1
- 108091023040 Transcription factor Proteins 0.000 description 1
- 101710150448 Transcriptional regulator Myc Proteins 0.000 description 1
- 102100026144 Transferrin receptor protein 1 Human genes 0.000 description 1
- 108700019146 Transgenes Proteins 0.000 description 1
- HDTRYLNUVZCQOY-WSWWMNSNSA-N Trehalose Natural products O[C@@H]1[C@@H](O)[C@@H](O)[C@@H](CO)O[C@@H]1O[C@@H]1[C@H](O)[C@@H](O)[C@@H](O)[C@@H](CO)O1 HDTRYLNUVZCQOY-WSWWMNSNSA-N 0.000 description 1
- 241000009298 Trigla lyra Species 0.000 description 1
- 101710162629 Trypsin inhibitor Proteins 0.000 description 1
- 229940122618 Trypsin inhibitor Drugs 0.000 description 1
- 102000004243 Tubulin Human genes 0.000 description 1
- 108090000704 Tubulin Proteins 0.000 description 1
- 102100040245 Tumor necrosis factor receptor superfamily member 5 Human genes 0.000 description 1
- 206010046851 Uveitis Diseases 0.000 description 1
- 206010047115 Vasculitis Diseases 0.000 description 1
- 241000251539 Vertebrata <Metazoa> Species 0.000 description 1
- 208000036142 Viral infection Diseases 0.000 description 1
- 238000002441 X-ray diffraction Methods 0.000 description 1
- 241000235015 Yarrowia lipolytica Species 0.000 description 1
- 102100035558 Zinc finger protein GLI2 Human genes 0.000 description 1
- 230000001594 aberrant effect Effects 0.000 description 1
- 230000005856 abnormality Effects 0.000 description 1
- 238000009825 accumulation Methods 0.000 description 1
- 229920006397 acrylic thermoplastic Polymers 0.000 description 1
- 239000012190 activator Substances 0.000 description 1
- 239000013543 active substance Substances 0.000 description 1
- 229960000643 adenine Drugs 0.000 description 1
- 210000004100 adrenal gland Anatomy 0.000 description 1
- 238000001042 affinity chromatography Methods 0.000 description 1
- 238000001261 affinity purification Methods 0.000 description 1
- 230000002776 aggregation Effects 0.000 description 1
- 238000004220 aggregation Methods 0.000 description 1
- 239000000556 agonist Substances 0.000 description 1
- PPQRONHOSHZGFQ-LMVFSUKVSA-N aldehydo-D-ribose 5-phosphate Chemical group OP(=O)(O)OC[C@@H](O)[C@@H](O)[C@@H](O)C=O PPQRONHOSHZGFQ-LMVFSUKVSA-N 0.000 description 1
- 125000000217 alkyl group Chemical group 0.000 description 1
- HDTRYLNUVZCQOY-LIZSDCNHSA-N alpha,alpha-trehalose Chemical compound O[C@@H]1[C@@H](O)[C@H](O)[C@@H](CO)O[C@@H]1O[C@@H]1[C@H](O)[C@@H](O)[C@H](O)[C@@H](CO)O1 HDTRYLNUVZCQOY-LIZSDCNHSA-N 0.000 description 1
- 230000009435 amidation Effects 0.000 description 1
- 238000007112 amidation reaction Methods 0.000 description 1
- 229940043376 ammonium acetate Drugs 0.000 description 1
- 235000019257 ammonium acetate Nutrition 0.000 description 1
- 229960000723 ampicillin Drugs 0.000 description 1
- AVKUERGKIZMTKX-NJBDSQKTSA-N ampicillin Chemical compound C1([C@@H](N)C(=O)N[C@H]2[C@H]3SC([C@@H](N3C2=O)C(O)=O)(C)C)=CC=CC=C1 AVKUERGKIZMTKX-NJBDSQKTSA-N 0.000 description 1
- 230000033115 angiogenesis Effects 0.000 description 1
- 230000003172 anti-dna Effects 0.000 description 1
- 230000000890 antigenic effect Effects 0.000 description 1
- 239000003430 antimalarial agent Substances 0.000 description 1
- 210000000436 anus Anatomy 0.000 description 1
- 210000000709 aorta Anatomy 0.000 description 1
- 210000001765 aortic valve Anatomy 0.000 description 1
- 239000007864 aqueous solution Substances 0.000 description 1
- 229910052786 argon Inorganic materials 0.000 description 1
- 125000000613 asparagine group Chemical group N[C@@H](CC(N)=O)C(=O)* 0.000 description 1
- 208000006673 asthma Diseases 0.000 description 1
- 201000008937 atopic dermatitis Diseases 0.000 description 1
- 230000037444 atrophy Effects 0.000 description 1
- 238000011888 autopsy Methods 0.000 description 1
- 238000000376 autoradiography Methods 0.000 description 1
- 235000013405 beer Nutrition 0.000 description 1
- WQZGKKKJIJFFOK-VFUOTHLCSA-N beta-D-glucose Chemical compound OC[C@H]1O[C@@H](O)[C@H](O)[C@@H](O)[C@@H]1O WQZGKKKJIJFFOK-VFUOTHLCSA-N 0.000 description 1
- 108010005774 beta-Galactosidase Proteins 0.000 description 1
- 238000013357 binding ELISA Methods 0.000 description 1
- 230000008512 biological response Effects 0.000 description 1
- 229960000074 biopharmaceutical Drugs 0.000 description 1
- 230000001851 biosynthetic effect Effects 0.000 description 1
- 230000006696 biosynthetic metabolic pathway Effects 0.000 description 1
- 208000034158 bleeding Diseases 0.000 description 1
- 230000000740 bleeding effect Effects 0.000 description 1
- 239000002981 blocking agent Substances 0.000 description 1
- 230000023555 blood coagulation Effects 0.000 description 1
- 238000009534 blood test Methods 0.000 description 1
- 210000004204 blood vessel Anatomy 0.000 description 1
- 238000006664 bond formation reaction Methods 0.000 description 1
- 210000002449 bone cell Anatomy 0.000 description 1
- 230000037182 bone density Effects 0.000 description 1
- 238000009583 bone marrow aspiration Methods 0.000 description 1
- 210000000621 bronchi Anatomy 0.000 description 1
- 239000008366 buffered solution Substances 0.000 description 1
- 208000000594 bullous pemphigoid Diseases 0.000 description 1
- 210000004899 c-terminal region Anatomy 0.000 description 1
- 239000001110 calcium chloride Substances 0.000 description 1
- 229910001628 calcium chloride Inorganic materials 0.000 description 1
- 239000001506 calcium phosphate Substances 0.000 description 1
- 229910000389 calcium phosphate Inorganic materials 0.000 description 1
- 235000011010 calcium phosphates Nutrition 0.000 description 1
- 229940095731 candida albicans Drugs 0.000 description 1
- 239000011545 carbonate/bicarbonate buffer Substances 0.000 description 1
- 230000015556 catabolic process Effects 0.000 description 1
- 210000004970 cd4 cell Anatomy 0.000 description 1
- 238000000423 cell based assay Methods 0.000 description 1
- 230000030833 cell death Effects 0.000 description 1
- 210000000170 cell membrane Anatomy 0.000 description 1
- 230000005890 cell-mediated cytotoxicity Effects 0.000 description 1
- 230000036755 cellular response Effects 0.000 description 1
- 210000003679 cervix uteri Anatomy 0.000 description 1
- 230000009920 chelation Effects 0.000 description 1
- 238000009614 chemical analysis method Methods 0.000 description 1
- 239000002975 chemoattractant Substances 0.000 description 1
- 239000012829 chemotherapy agent Substances 0.000 description 1
- 238000009104 chemotherapy regimen Methods 0.000 description 1
- 229960004630 chlorambucil Drugs 0.000 description 1
- JCKYGMPEJWAADB-UHFFFAOYSA-N chlorambucil Chemical compound OC(=O)CCCC1=CC=C(N(CCCl)CCCl)C=C1 JCKYGMPEJWAADB-UHFFFAOYSA-N 0.000 description 1
- 229960005091 chloramphenicol Drugs 0.000 description 1
- WIIZWVCIJKGZOK-RKDXNWHRSA-N chloramphenicol Chemical compound ClC(Cl)C(=O)N[C@H](CO)[C@H](O)C1=CC=C([N+]([O-])=O)C=C1 WIIZWVCIJKGZOK-RKDXNWHRSA-N 0.000 description 1
- UHZZMRAGKVHANO-UHFFFAOYSA-M chlormequat chloride Chemical compound [Cl-].C[N+](C)(C)CCCl UHZZMRAGKVHANO-UHFFFAOYSA-M 0.000 description 1
- 238000011098 chromatofocusing Methods 0.000 description 1
- 239000003593 chromogenic compound Substances 0.000 description 1
- 208000019902 chronic diarrheal disease Diseases 0.000 description 1
- 208000025302 chronic primary adrenal insufficiency Diseases 0.000 description 1
- 238000004140 cleaning Methods 0.000 description 1
- 238000009535 clinical urine test Methods 0.000 description 1
- 230000035602 clotting Effects 0.000 description 1
- 230000008951 colonic inflammation Effects 0.000 description 1
- 238000004440 column chromatography Methods 0.000 description 1
- 238000005056 compaction Methods 0.000 description 1
- 238000004590 computer program Methods 0.000 description 1
- 238000005094 computer simulation Methods 0.000 description 1
- 238000012790 confirmation Methods 0.000 description 1
- 230000001268 conjugating effect Effects 0.000 description 1
- 239000000356 contaminant Substances 0.000 description 1
- 229920001577 copolymer Polymers 0.000 description 1
- 210000004351 coronary vessel Anatomy 0.000 description 1
- 230000002596 correlated effect Effects 0.000 description 1
- 229940109239 creatinine Drugs 0.000 description 1
- 230000002089 crippling effect Effects 0.000 description 1
- 239000003431 cross linking reagent Substances 0.000 description 1
- 230000009260 cross reactivity Effects 0.000 description 1
- 210000004748 cultured cell Anatomy 0.000 description 1
- 238000012258 culturing Methods 0.000 description 1
- 230000001351 cycling effect Effects 0.000 description 1
- 229960004397 cyclophosphamide Drugs 0.000 description 1
- 230000016396 cytokine production Effects 0.000 description 1
- 229940104302 cytosine Drugs 0.000 description 1
- 231100000433 cytotoxic Toxicity 0.000 description 1
- 230000001472 cytotoxic effect Effects 0.000 description 1
- 238000002784 cytotoxicity assay Methods 0.000 description 1
- 231100000263 cytotoxicity test Toxicity 0.000 description 1
- 230000006240 deamidation Effects 0.000 description 1
- 230000007547 defect Effects 0.000 description 1
- 230000022811 deglycosylation Effects 0.000 description 1
- 238000006731 degradation reaction Methods 0.000 description 1
- 230000003111 delayed effect Effects 0.000 description 1
- 238000004925 denaturation Methods 0.000 description 1
- 230000036425 denaturation Effects 0.000 description 1
- 238000001212 derivatisation Methods 0.000 description 1
- 230000000368 destabilizing effect Effects 0.000 description 1
- 230000009025 developmental regulation Effects 0.000 description 1
- 229960003957 dexamethasone Drugs 0.000 description 1
- UREBDLICKHMUKA-CXSFZGCWSA-N dexamethasone Chemical compound C1CC2=CC(=O)C=C[C@]2(C)[C@]2(F)[C@@H]1[C@@H]1C[C@@H](C)[C@@](C(=O)CO)(O)[C@@]1(C)C[C@@H]2O UREBDLICKHMUKA-CXSFZGCWSA-N 0.000 description 1
- 229950006137 dexfosfoserine Drugs 0.000 description 1
- 206010012601 diabetes mellitus Diseases 0.000 description 1
- 238000012631 diagnostic technique Methods 0.000 description 1
- 210000000188 diaphragm Anatomy 0.000 description 1
- QONQRTHLHBTMGP-UHFFFAOYSA-N digitoxigenin Natural products CC12CCC(C3(CCC(O)CC3CC3)C)C3C11OC1CC2C1=CC(=O)OC1 QONQRTHLHBTMGP-UHFFFAOYSA-N 0.000 description 1
- SHIBSTMRCDJXLN-KCZCNTNESA-N digoxigenin Chemical compound C1([C@@H]2[C@@]3([C@@](CC2)(O)[C@H]2[C@@H]([C@@]4(C)CC[C@H](O)C[C@H]4CC2)C[C@H]3O)C)=CC(=O)OC1 SHIBSTMRCDJXLN-KCZCNTNESA-N 0.000 description 1
- XPPKVPWEQAFLFU-UHFFFAOYSA-J diphosphate(4-) Chemical compound [O-]P([O-])(=O)OP([O-])([O-])=O XPPKVPWEQAFLFU-UHFFFAOYSA-J 0.000 description 1
- 235000011180 diphosphates Nutrition 0.000 description 1
- UKWLRLAKGMZXJC-QIECWBMSSA-L disodium;[4-chloro-3-[(3r,5s)-1-chloro-3'-methoxyspiro[adamantane-4,4'-dioxetane]-3'-yl]phenyl] phosphate Chemical compound [Na+].[Na+].O1OC2([C@@H]3CC4C[C@H]2CC(Cl)(C4)C3)C1(OC)C1=CC(OP([O-])([O-])=O)=CC=C1Cl UKWLRLAKGMZXJC-QIECWBMSSA-L 0.000 description 1
- PMMYEEVYMWASQN-UHFFFAOYSA-N dl-hydroxyproline Natural products OC1C[NH2+]C(C([O-])=O)C1 PMMYEEVYMWASQN-UHFFFAOYSA-N 0.000 description 1
- 229960004679 doxorubicin Drugs 0.000 description 1
- 238000001962 electrophoresis Methods 0.000 description 1
- 238000005538 encapsulation Methods 0.000 description 1
- 210000004696 endometrium Anatomy 0.000 description 1
- 230000009144 enzymatic modification Effects 0.000 description 1
- 238000006911 enzymatic reaction Methods 0.000 description 1
- 210000000918 epididymis Anatomy 0.000 description 1
- 210000002919 epithelial cell Anatomy 0.000 description 1
- 208000037888 epithelial cell injury Diseases 0.000 description 1
- 210000000267 erythroid cell Anatomy 0.000 description 1
- 229960003276 erythromycin Drugs 0.000 description 1
- 210000003238 esophagus Anatomy 0.000 description 1
- 238000012869 ethanol precipitation Methods 0.000 description 1
- 210000003414 extremity Anatomy 0.000 description 1
- 208000030533 eye disease Diseases 0.000 description 1
- 230000001605 fetal effect Effects 0.000 description 1
- 235000019688 fish Nutrition 0.000 description 1
- 239000012530 fluid Substances 0.000 description 1
- 231100000221 frame shift mutation induction Toxicity 0.000 description 1
- 230000037433 frameshift Effects 0.000 description 1
- 230000033581 fucosylation Effects 0.000 description 1
- 210000000232 gallbladder Anatomy 0.000 description 1
- 230000009368 gene silencing by RNA Effects 0.000 description 1
- 238000001415 gene therapy Methods 0.000 description 1
- 229960001031 glucose Drugs 0.000 description 1
- 239000004220 glutamic acid Substances 0.000 description 1
- 125000000291 glutamic acid group Chemical group N[C@@H](CCC(O)=O)C(=O)* 0.000 description 1
- ZDXPYRJPNDTMRX-UHFFFAOYSA-N glutamine Natural products OC(=O)C(N)CCC(N)=O ZDXPYRJPNDTMRX-UHFFFAOYSA-N 0.000 description 1
- 125000000404 glutamine group Chemical group N[C@@H](CCC(N)=O)C(=O)* 0.000 description 1
- 150000004676 glycans Chemical class 0.000 description 1
- 229930182470 glycoside Natural products 0.000 description 1
- 150000002338 glycosides Chemical class 0.000 description 1
- 229930004094 glycosylphosphatidylinositol Natural products 0.000 description 1
- 230000036449 good health Effects 0.000 description 1
- 210000003714 granulocyte Anatomy 0.000 description 1
- 239000003102 growth factor Substances 0.000 description 1
- 201000005787 hematologic cancer Diseases 0.000 description 1
- 208000024200 hematopoietic and lymphoid system neoplasm Diseases 0.000 description 1
- 125000004404 heteroalkyl group Chemical group 0.000 description 1
- 238000004128 high performance liquid chromatography Methods 0.000 description 1
- 238000013537 high throughput screening Methods 0.000 description 1
- 239000005556 hormone Substances 0.000 description 1
- 229940088597 hormone Drugs 0.000 description 1
- 102000053426 human ITPRID2 Human genes 0.000 description 1
- 125000004435 hydrogen atom Chemical group [H]* 0.000 description 1
- 125000001165 hydrophobic group Chemical group 0.000 description 1
- 125000002887 hydroxy group Chemical group [H]O* 0.000 description 1
- 230000033444 hydroxylation Effects 0.000 description 1
- 238000005805 hydroxylation reaction Methods 0.000 description 1
- 229960002591 hydroxyproline Drugs 0.000 description 1
- 150000002463 imidates Chemical class 0.000 description 1
- 230000000984 immunochemical effect Effects 0.000 description 1
- 238000010324 immunological assay Methods 0.000 description 1
- 239000002955 immunomodulating agent Substances 0.000 description 1
- 229940121354 immunomodulator Drugs 0.000 description 1
- 230000008975 immunomodulatory function Effects 0.000 description 1
- 238000001114 immunoprecipitation Methods 0.000 description 1
- 230000004957 immunoregulator effect Effects 0.000 description 1
- 230000001506 immunosuppresive effect Effects 0.000 description 1
- 229940125721 immunosuppressive agent Drugs 0.000 description 1
- 229940124589 immunosuppressive drug Drugs 0.000 description 1
- 230000006872 improvement Effects 0.000 description 1
- 230000002779 inactivation Effects 0.000 description 1
- 238000010348 incorporation Methods 0.000 description 1
- 208000027138 indeterminate colitis Diseases 0.000 description 1
- 210000005007 innate immune system Anatomy 0.000 description 1
- 238000011081 inoculation Methods 0.000 description 1
- 238000007689 inspection Methods 0.000 description 1
- 230000000968 intestinal effect Effects 0.000 description 1
- 210000002490 intestinal epithelial cell Anatomy 0.000 description 1
- 210000000936 intestine Anatomy 0.000 description 1
- 230000003834 intracellular effect Effects 0.000 description 1
- 238000007918 intramuscular administration Methods 0.000 description 1
- 238000010255 intramuscular injection Methods 0.000 description 1
- 239000007928 intraperitoneal injection Substances 0.000 description 1
- 238000001990 intravenous administration Methods 0.000 description 1
- 238000010253 intravenous injection Methods 0.000 description 1
- 238000005342 ion exchange Methods 0.000 description 1
- 238000001155 isoelectric focusing Methods 0.000 description 1
- 230000000155 isotopic effect Effects 0.000 description 1
- 238000005304 joining Methods 0.000 description 1
- 210000005067 joint tissue Anatomy 0.000 description 1
- 229960000318 kanamycin Drugs 0.000 description 1
- 229930027917 kanamycin Natural products 0.000 description 1
- SBUJHOSQTJFQJX-NOAMYHISSA-N kanamycin Chemical compound O[C@@H]1[C@@H](O)[C@H](O)[C@@H](CN)O[C@@H]1O[C@H]1[C@H](O)[C@@H](O[C@@H]2[C@@H]([C@@H](N)[C@H](O)[C@@H](CO)O2)O)[C@H](N)C[C@@H]1N SBUJHOSQTJFQJX-NOAMYHISSA-N 0.000 description 1
- 229930182823 kanamycin A Natural products 0.000 description 1
- 108010045069 keyhole-limpet hemocyanin Proteins 0.000 description 1
- 201000006370 kidney failure Diseases 0.000 description 1
- 230000003907 kidney function Effects 0.000 description 1
- 238000012933 kinetic analysis Methods 0.000 description 1
- 238000011005 laboratory method Methods 0.000 description 1
- 238000002843 lactate dehydrogenase assay Methods 0.000 description 1
- 210000000867 larynx Anatomy 0.000 description 1
- 230000002045 lasting effect Effects 0.000 description 1
- 238000012917 library technology Methods 0.000 description 1
- 210000000088 lip Anatomy 0.000 description 1
- 239000002502 liposome Substances 0.000 description 1
- 244000144972 livestock Species 0.000 description 1
- 210000005210 lymphoid organ Anatomy 0.000 description 1
- 239000012139 lysis buffer Substances 0.000 description 1
- 230000002101 lytic effect Effects 0.000 description 1
- 229920002521 macromolecule Polymers 0.000 description 1
- 239000011777 magnesium Substances 0.000 description 1
- 229910052749 magnesium Inorganic materials 0.000 description 1
- 238000012423 maintenance Methods 0.000 description 1
- 230000036210 malignancy Effects 0.000 description 1
- 238000013507 mapping Methods 0.000 description 1
- 238000004949 mass spectrometry Methods 0.000 description 1
- MIKKOBKEXMRYFQ-WZTVWXICSA-N meglumine amidotrizoate Chemical compound C[NH2+]C[C@H](O)[C@@H](O)[C@H](O)[C@H](O)CO.CC(=O)NC1=C(I)C(NC(C)=O)=C(I)C(C([O-])=O)=C1I MIKKOBKEXMRYFQ-WZTVWXICSA-N 0.000 description 1
- 229960001924 melphalan Drugs 0.000 description 1
- SGDBTWWWUNNDEQ-LBPRGKRZSA-N melphalan Chemical compound OC(=O)[C@@H](N)CC1=CC=C(N(CCCl)CCCl)C=C1 SGDBTWWWUNNDEQ-LBPRGKRZSA-N 0.000 description 1
- 150000002739 metals Chemical class 0.000 description 1
- 230000009401 metastasis Effects 0.000 description 1
- YCXSYMVGMXQYNT-UHFFFAOYSA-N methyl 3-[(4-azidophenyl)disulfanyl]propanimidate Chemical compound COC(=N)CCSSC1=CC=C(N=[N+]=[N-])C=C1 YCXSYMVGMXQYNT-UHFFFAOYSA-N 0.000 description 1
- 230000011987 methylation Effects 0.000 description 1
- 238000007069 methylation reaction Methods 0.000 description 1
- 125000006357 methylene carbonyl group Chemical group [H]C([H])([*:1])C([*:2])=O 0.000 description 1
- LSDPWZHWYPCBBB-UHFFFAOYSA-O methylsulfide anion Chemical compound [SH2+]C LSDPWZHWYPCBBB-UHFFFAOYSA-O 0.000 description 1
- 239000010445 mica Substances 0.000 description 1
- 229910052618 mica group Inorganic materials 0.000 description 1
- HPNSFSBZBAHARI-UHFFFAOYSA-N micophenolic acid Natural products OC1=C(CC=C(C)CCC(O)=O)C(OC)=C(C)C2=C1C(=O)OC2 HPNSFSBZBAHARI-UHFFFAOYSA-N 0.000 description 1
- 238000010208 microarray analysis Methods 0.000 description 1
- 238000000520 microinjection Methods 0.000 description 1
- 108091005601 modified peptides Proteins 0.000 description 1
- 238000001823 molecular biology technique Methods 0.000 description 1
- 210000005087 mononuclear cell Anatomy 0.000 description 1
- 229940035032 monophosphoryl lipid a Drugs 0.000 description 1
- 230000004660 morphological change Effects 0.000 description 1
- 210000002200 mouth mucosa Anatomy 0.000 description 1
- 210000003097 mucus Anatomy 0.000 description 1
- 238000011527 multiparameter analysis Methods 0.000 description 1
- 210000003205 muscle Anatomy 0.000 description 1
- 230000000869 mutational effect Effects 0.000 description 1
- 229960000951 mycophenolic acid Drugs 0.000 description 1
- HPNSFSBZBAHARI-RUDMXATFSA-N mycophenolic acid Chemical compound OC1=C(C\C=C(/C)CCC(O)=O)C(OC)=C(C)C2=C1C(=O)OC2 HPNSFSBZBAHARI-RUDMXATFSA-N 0.000 description 1
- 230000002107 myocardial effect Effects 0.000 description 1
- 210000000754 myometrium Anatomy 0.000 description 1
- 230000031942 natural killer cell mediated cytotoxicity Effects 0.000 description 1
- 229960004927 neomycin Drugs 0.000 description 1
- 231100000417 nephrotoxicity Toxicity 0.000 description 1
- 230000007935 neutral effect Effects 0.000 description 1
- JPXMTWWFLBLUCD-UHFFFAOYSA-N nitro blue tetrazolium(2+) Chemical compound COC1=CC(C=2C=C(OC)C(=CC=2)[N+]=2N(N=C(N=2)C=2C=CC=CC=2)C=2C=CC(=CC=2)[N+]([O-])=O)=CC=C1[N+]1=NC(C=2C=CC=CC=2)=NN1C1=CC=C([N+]([O-])=O)C=C1 JPXMTWWFLBLUCD-UHFFFAOYSA-N 0.000 description 1
- 229920001220 nitrocellulos Polymers 0.000 description 1
- 238000007826 nucleic acid assay Methods 0.000 description 1
- 231100000862 numbness Toxicity 0.000 description 1
- 230000000414 obstructive effect Effects 0.000 description 1
- 229920002113 octoxynol Polymers 0.000 description 1
- 239000003921 oil Substances 0.000 description 1
- 238000002966 oligonucleotide array Methods 0.000 description 1
- 238000005457 optimization Methods 0.000 description 1
- 210000002997 osteoclast Anatomy 0.000 description 1
- 230000000010 osteolytic effect Effects 0.000 description 1
- 229940045681 other alkylating agent in atc Drugs 0.000 description 1
- 210000001672 ovary Anatomy 0.000 description 1
- 125000004043 oxo group Chemical group O=* 0.000 description 1
- 210000000496 pancreas Anatomy 0.000 description 1
- 230000000849 parathyroid Effects 0.000 description 1
- 230000036961 partial effect Effects 0.000 description 1
- 239000013610 patient sample Substances 0.000 description 1
- 201000001976 pemphigus vulgaris Diseases 0.000 description 1
- 229940049954 penicillin Drugs 0.000 description 1
- 229940111202 pepsin Drugs 0.000 description 1
- 210000005105 peripheral blood lymphocyte Anatomy 0.000 description 1
- 210000001322 periplasm Anatomy 0.000 description 1
- 210000001986 peyer's patch Anatomy 0.000 description 1
- 239000000546 pharmaceutical excipient Substances 0.000 description 1
- 230000002186 photoactivation Effects 0.000 description 1
- 210000002826 placenta Anatomy 0.000 description 1
- 239000013600 plasmid vector Substances 0.000 description 1
- 230000010118 platelet activation Effects 0.000 description 1
- 229920003229 poly(methyl methacrylate) Polymers 0.000 description 1
- 238000002264 polyacrylamide gel electrophoresis Methods 0.000 description 1
- 229920001748 polybutylene Polymers 0.000 description 1
- 229920000573 polyethylene Polymers 0.000 description 1
- 239000000244 polyoxyethylene sorbitan monooleate Substances 0.000 description 1
- 235000010482 polyoxyethylene sorbitan monooleate Nutrition 0.000 description 1
- 210000004896 polypeptide structure Anatomy 0.000 description 1
- 229920001155 polypropylene Polymers 0.000 description 1
- 229920001451 polypropylene glycol Polymers 0.000 description 1
- 229920001282 polysaccharide Polymers 0.000 description 1
- 239000005017 polysaccharide Substances 0.000 description 1
- 229920000053 polysorbate 80 Polymers 0.000 description 1
- 229940068968 polysorbate 80 Drugs 0.000 description 1
- 229920002223 polystyrene Polymers 0.000 description 1
- 229920002635 polyurethane Polymers 0.000 description 1
- 239000004814 polyurethane Substances 0.000 description 1
- 238000010837 poor prognosis Methods 0.000 description 1
- 239000013641 positive control Substances 0.000 description 1
- 230000001323 posttranslational effect Effects 0.000 description 1
- SCVFZCLFOSHCOH-UHFFFAOYSA-M potassium acetate Chemical compound [K+].CC([O-])=O SCVFZCLFOSHCOH-UHFFFAOYSA-M 0.000 description 1
- 239000001103 potassium chloride Substances 0.000 description 1
- 235000011164 potassium chloride Nutrition 0.000 description 1
- 239000002244 precipitate Substances 0.000 description 1
- 229960004618 prednisone Drugs 0.000 description 1
- XOFYZVNMUHMLCC-ZPOLXVRWSA-N prednisone Chemical compound O=C1C=C[C@]2(C)[C@H]3C(=O)C[C@](C)([C@@](CC4)(O)C(=O)CO)[C@@H]4[C@@H]3CCC2=C1 XOFYZVNMUHMLCC-ZPOLXVRWSA-N 0.000 description 1
- 230000003449 preventive effect Effects 0.000 description 1
- 125000002924 primary amino group Chemical group [H]N([H])* 0.000 description 1
- 238000012545 processing Methods 0.000 description 1
- 210000001236 prokaryotic cell Anatomy 0.000 description 1
- 125000001500 prolyl group Chemical group [H]N1C([H])(C(=O)[*])C([H])([H])C([H])([H])C1([H])[H] 0.000 description 1
- 230000001737 promoting effect Effects 0.000 description 1
- 230000000069 prophylactic effect Effects 0.000 description 1
- 210000002307 prostate Anatomy 0.000 description 1
- 235000019833 protease Nutrition 0.000 description 1
- 230000004952 protein activity Effects 0.000 description 1
- 229940076372 protein antagonist Drugs 0.000 description 1
- 108020001580 protein domains Proteins 0.000 description 1
- 231100000654 protein toxin Toxicity 0.000 description 1
- 201000001474 proteinuria Diseases 0.000 description 1
- 230000006337 proteolytic cleavage Effects 0.000 description 1
- 210000001938 protoplast Anatomy 0.000 description 1
- 239000012264 purified product Substances 0.000 description 1
- 150000003212 purines Chemical class 0.000 description 1
- 150000003230 pyrimidines Chemical class 0.000 description 1
- 229940048084 pyrophosphate Drugs 0.000 description 1
- 238000001959 radiotherapy Methods 0.000 description 1
- 238000002708 random mutagenesis Methods 0.000 description 1
- 238000010188 recombinant method Methods 0.000 description 1
- 210000000664 rectum Anatomy 0.000 description 1
- 230000000306 recurrent effect Effects 0.000 description 1
- 230000001172 regenerating effect Effects 0.000 description 1
- 210000001525 retina Anatomy 0.000 description 1
- 238000004007 reversed phase HPLC Methods 0.000 description 1
- 230000002441 reversible effect Effects 0.000 description 1
- PYWVYCXTNDRMGF-UHFFFAOYSA-N rhodamine B Chemical compound [Cl-].C=12C=CC(=[N+](CC)CC)C=C2OC2=CC(N(CC)CC)=CC=C2C=1C1=CC=CC=C1C(O)=O PYWVYCXTNDRMGF-UHFFFAOYSA-N 0.000 description 1
- 239000002336 ribonucleotide Substances 0.000 description 1
- 125000002652 ribonucleotide group Chemical group 0.000 description 1
- 239000012146 running buffer Substances 0.000 description 1
- 210000003079 salivary gland Anatomy 0.000 description 1
- 238000003118 sandwich ELISA Methods 0.000 description 1
- 201000000306 sarcoidosis Diseases 0.000 description 1
- 230000018448 secretion by cell Effects 0.000 description 1
- 238000004062 sedimentation Methods 0.000 description 1
- 125000003607 serino group Chemical group [H]N([H])[C@]([H])(C(=O)[*])C(O[H])([H])[H] 0.000 description 1
- 239000004017 serum-free culture medium Substances 0.000 description 1
- 230000035938 sexual maturation Effects 0.000 description 1
- 230000019491 signal transduction Effects 0.000 description 1
- 230000011664 signaling Effects 0.000 description 1
- 229910052710 silicon Inorganic materials 0.000 description 1
- 239000010703 silicon Substances 0.000 description 1
- 150000003376 silicon Chemical class 0.000 description 1
- 208000017520 skin disease Diseases 0.000 description 1
- 230000000391 smoking effect Effects 0.000 description 1
- 239000011734 sodium Substances 0.000 description 1
- POECFFCNUXZPJT-UHFFFAOYSA-M sodium;carbonic acid;hydrogen carbonate Chemical compound [Na+].OC(O)=O.OC([O-])=O POECFFCNUXZPJT-UHFFFAOYSA-M 0.000 description 1
- 238000000638 solvent extraction Methods 0.000 description 1
- 230000009870 specific binding Effects 0.000 description 1
- 238000002798 spectrophotometry method Methods 0.000 description 1
- 238000001228 spectrum Methods 0.000 description 1
- 210000004989 spleen cell Anatomy 0.000 description 1
- 230000003393 splenic effect Effects 0.000 description 1
- 201000005671 spondyloarthropathy Diseases 0.000 description 1
- 210000003802 sputum Anatomy 0.000 description 1
- 208000024794 sputum Diseases 0.000 description 1
- 238000011255 standard chemotherapy Methods 0.000 description 1
- 239000007858 starting material Substances 0.000 description 1
- 238000007619 statistical method Methods 0.000 description 1
- 210000000130 stem cell Anatomy 0.000 description 1
- 239000000021 stimulant Substances 0.000 description 1
- 210000002784 stomach Anatomy 0.000 description 1
- 238000003860 storage Methods 0.000 description 1
- 229960005322 streptomycin Drugs 0.000 description 1
- 238000010254 subcutaneous injection Methods 0.000 description 1
- 239000007929 subcutaneous injection Substances 0.000 description 1
- 125000000547 substituted alkyl group Chemical group 0.000 description 1
- 238000001356 surgical procedure Methods 0.000 description 1
- 230000004083 survival effect Effects 0.000 description 1
- 239000000725 suspension Substances 0.000 description 1
- 210000005222 synovial tissue Anatomy 0.000 description 1
- 201000000596 systemic lupus erythematosus Diseases 0.000 description 1
- 238000012353 t test Methods 0.000 description 1
- 230000008685 targeting Effects 0.000 description 1
- 230000002123 temporal effect Effects 0.000 description 1
- 208000012271 tenesmus Diseases 0.000 description 1
- ISXSCDLOGDJUNJ-UHFFFAOYSA-N tert-butyl prop-2-enoate Chemical compound CC(C)(C)OC(=O)C=C ISXSCDLOGDJUNJ-UHFFFAOYSA-N 0.000 description 1
- 210000001550 testis Anatomy 0.000 description 1
- 229960002180 tetracycline Drugs 0.000 description 1
- 229930101283 tetracycline Natural products 0.000 description 1
- 235000019364 tetracycline Nutrition 0.000 description 1
- 150000003522 tetracyclines Chemical class 0.000 description 1
- 238000011285 therapeutic regimen Methods 0.000 description 1
- 230000008719 thickening Effects 0.000 description 1
- 125000003396 thiol group Chemical group [H]S* 0.000 description 1
- 229940113082 thymine Drugs 0.000 description 1
- 210000001541 thymus gland Anatomy 0.000 description 1
- 229960002175 thyroglobulin Drugs 0.000 description 1
- 210000001685 thyroid gland Anatomy 0.000 description 1
- 206010043778 thyroiditis Diseases 0.000 description 1
- 210000002105 tongue Anatomy 0.000 description 1
- 230000000699 topical effect Effects 0.000 description 1
- 201000002516 toxic megacolon Diseases 0.000 description 1
- 230000001988 toxicity Effects 0.000 description 1
- 231100000419 toxicity Toxicity 0.000 description 1
- 210000003437 trachea Anatomy 0.000 description 1
- FGMPLJWBKKVCDB-UHFFFAOYSA-N trans-L-hydroxy-proline Natural products ON1CCCC1C(O)=O FGMPLJWBKKVCDB-UHFFFAOYSA-N 0.000 description 1
- 230000005030 transcription termination Effects 0.000 description 1
- 238000010361 transduction Methods 0.000 description 1
- 230000026683 transduction Effects 0.000 description 1
- 238000012546 transfer Methods 0.000 description 1
- 230000001131 transforming effect Effects 0.000 description 1
- 238000003146 transient transfection Methods 0.000 description 1
- QORWJWZARLRLPR-UHFFFAOYSA-H tricalcium bis(phosphate) Chemical compound [Ca+2].[Ca+2].[Ca+2].[O-]P([O-])([O-])=O.[O-]P([O-])([O-])=O QORWJWZARLRLPR-UHFFFAOYSA-H 0.000 description 1
- PIEPQKCYPFFYMG-UHFFFAOYSA-N tris acetate Chemical compound CC(O)=O.OCC(N)(CO)CO PIEPQKCYPFFYMG-UHFFFAOYSA-N 0.000 description 1
- 239000002753 trypsin inhibitor Substances 0.000 description 1
- 231100000588 tumorigenic Toxicity 0.000 description 1
- 230000000381 tumorigenic effect Effects 0.000 description 1
- OUYCCCASQSFEME-UHFFFAOYSA-N tyrosine Natural products OC(=O)C(N)CC1=CC=C(O)C=C1 OUYCCCASQSFEME-UHFFFAOYSA-N 0.000 description 1
- 125000001493 tyrosinyl group Chemical group [H]OC1=C([H])C([H])=C(C([H])=C1[H])C([H])([H])C([H])(N([H])[H])C(*)=O 0.000 description 1
- 238000013060 ultrafiltration and diafiltration Methods 0.000 description 1
- 210000003954 umbilical cord Anatomy 0.000 description 1
- 210000003606 umbilical vein Anatomy 0.000 description 1
- 241000701161 unidentified adenovirus Species 0.000 description 1
- 241000701447 unidentified baculovirus Species 0.000 description 1
- 241001515965 unidentified phage Species 0.000 description 1
- 229940035893 uracil Drugs 0.000 description 1
- 210000000626 ureter Anatomy 0.000 description 1
- 210000003932 urinary bladder Anatomy 0.000 description 1
- 210000004291 uterus Anatomy 0.000 description 1
- 210000001215 vagina Anatomy 0.000 description 1
- 210000001186 vagus nerve Anatomy 0.000 description 1
- 210000003462 vein Anatomy 0.000 description 1
- 230000035899 viability Effects 0.000 description 1
- OGWKCGZFUXNPDA-XQKSVPLYSA-N vincristine Chemical compound C([N@]1C[C@@H](C[C@]2(C(=O)OC)C=3C(=CC4=C([C@]56[C@H]([C@@]([C@H](OC(C)=O)[C@]7(CC)C=CCN([C@H]67)CC5)(O)C(=O)OC)N4C=O)C=3)OC)C[C@@](C1)(O)CC)CC1=C2NC2=CC=CC=C12 OGWKCGZFUXNPDA-XQKSVPLYSA-N 0.000 description 1
- 229960004528 vincristine Drugs 0.000 description 1
- OGWKCGZFUXNPDA-UHFFFAOYSA-N vincristine Natural products C1C(CC)(O)CC(CC2(C(=O)OC)C=3C(=CC4=C(C56C(C(C(OC(C)=O)C7(CC)C=CCN(C67)CC5)(O)C(=O)OC)N4C=O)C=3)OC)CN1CCC1=C2NC2=CC=CC=C12 OGWKCGZFUXNPDA-UHFFFAOYSA-N 0.000 description 1
- 230000009385 viral infection Effects 0.000 description 1
- 230000036642 wellbeing Effects 0.000 description 1
- 229940075420 xanthine Drugs 0.000 description 1
- 238000001086 yeast two-hybrid system Methods 0.000 description 1
Classifications
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K16/00—Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies
- C07K16/18—Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies against material from animals or humans
- C07K16/28—Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies against material from animals or humans against receptors, cell surface antigens or cell surface determinants
- C07K16/2803—Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies against material from animals or humans against receptors, cell surface antigens or cell surface determinants against the immunoglobulin superfamily
- C07K16/2806—Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies against material from animals or humans against receptors, cell surface antigens or cell surface determinants against the immunoglobulin superfamily against CD2
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K16/00—Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61K—PREPARATIONS FOR MEDICAL, DENTAL OR TOILETRY PURPOSES
- A61K45/00—Medicinal preparations containing active ingredients not provided for in groups A61K31/00 - A61K41/00
- A61K45/06—Mixtures of active ingredients without chemical characterisation, e.g. antiphlogistics and cardiaca
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61K—PREPARATIONS FOR MEDICAL, DENTAL OR TOILETRY PURPOSES
- A61K39/00—Medicinal preparations containing antigens or antibodies
- A61K39/395—Antibodies; Immunoglobulins; Immune serum, e.g. antilymphocytic serum
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61K—PREPARATIONS FOR MEDICAL, DENTAL OR TOILETRY PURPOSES
- A61K39/00—Medicinal preparations containing antigens or antibodies
- A61K39/395—Antibodies; Immunoglobulins; Immune serum, e.g. antilymphocytic serum
- A61K39/39533—Antibodies; Immunoglobulins; Immune serum, e.g. antilymphocytic serum against materials from animals
- A61K39/39558—Antibodies; Immunoglobulins; Immune serum, e.g. antilymphocytic serum against materials from animals against tumor tissues, cells, antigens
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P1/00—Drugs for disorders of the alimentary tract or the digestive system
- A61P1/04—Drugs for disorders of the alimentary tract or the digestive system for ulcers, gastritis or reflux esophagitis, e.g. antacids, inhibitors of acid secretion, mucosal protectants
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P35/00—Antineoplastic agents
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P35/00—Antineoplastic agents
- A61P35/02—Antineoplastic agents specific for leukemia
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P37/00—Drugs for immunological or allergic disorders
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P43/00—Drugs for specific purposes, not provided for in groups A61P1/00-A61P41/00
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K14/00—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof
- C07K14/435—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from animals; from humans
- C07K14/705—Receptors; Cell surface antigens; Cell surface determinants
- C07K14/70503—Immunoglobulin superfamily
- C07K14/70507—CD2
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K16/00—Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies
- C07K16/18—Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies against material from animals or humans
- C07K16/28—Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies against material from animals or humans against receptors, cell surface antigens or cell surface determinants
- C07K16/2803—Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies against material from animals or humans against receptors, cell surface antigens or cell surface determinants against the immunoglobulin superfamily
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61K—PREPARATIONS FOR MEDICAL, DENTAL OR TOILETRY PURPOSES
- A61K39/00—Medicinal preparations containing antigens or antibodies
- A61K2039/505—Medicinal preparations containing antigens or antibodies comprising antibodies
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K2317/00—Immunoglobulins specific features
- C07K2317/20—Immunoglobulins specific features characterized by taxonomic origin
- C07K2317/24—Immunoglobulins specific features characterized by taxonomic origin containing regions, domains or residues from different species, e.g. chimeric, humanized or veneered
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K2317/00—Immunoglobulins specific features
- C07K2317/40—Immunoglobulins specific features characterized by post-translational modification
- C07K2317/41—Glycosylation, sialylation, or fucosylation
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K2317/00—Immunoglobulins specific features
- C07K2317/50—Immunoglobulins specific features characterized by immunoglobulin fragments
- C07K2317/56—Immunoglobulins specific features characterized by immunoglobulin fragments variable (Fv) region, i.e. VH and/or VL
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K2317/00—Immunoglobulins specific features
- C07K2317/50—Immunoglobulins specific features characterized by immunoglobulin fragments
- C07K2317/56—Immunoglobulins specific features characterized by immunoglobulin fragments variable (Fv) region, i.e. VH and/or VL
- C07K2317/565—Complementarity determining region [CDR]
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K2317/00—Immunoglobulins specific features
- C07K2317/70—Immunoglobulins specific features characterized by effect upon binding to a cell or to an antigen
- C07K2317/73—Inducing cell death, e.g. apoptosis, necrosis or inhibition of cell proliferation
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K2317/00—Immunoglobulins specific features
- C07K2317/70—Immunoglobulins specific features characterized by effect upon binding to a cell or to an antigen
- C07K2317/73—Inducing cell death, e.g. apoptosis, necrosis or inhibition of cell proliferation
- C07K2317/732—Antibody-dependent cellular cytotoxicity [ADCC]
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K2317/00—Immunoglobulins specific features
- C07K2317/70—Immunoglobulins specific features characterized by effect upon binding to a cell or to an antigen
- C07K2317/76—Antagonist effect on antigen, e.g. neutralization or inhibition of binding
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K2317/00—Immunoglobulins specific features
- C07K2317/90—Immunoglobulins specific features characterized by (pharmaco)kinetic aspects or by stability of the immunoglobulin
- C07K2317/92—Affinity (KD), association rate (Ka), dissociation rate (Kd) or EC50 value
Landscapes
- Health & Medical Sciences (AREA)
- Chemical & Material Sciences (AREA)
- Life Sciences & Earth Sciences (AREA)
- Immunology (AREA)
- Medicinal Chemistry (AREA)
- Organic Chemistry (AREA)
- General Health & Medical Sciences (AREA)
- Public Health (AREA)
- Veterinary Medicine (AREA)
- Pharmacology & Pharmacy (AREA)
- Animal Behavior & Ethology (AREA)
- Biophysics (AREA)
- Biochemistry (AREA)
- Proteomics, Peptides & Aminoacids (AREA)
- Molecular Biology (AREA)
- Genetics & Genomics (AREA)
- Engineering & Computer Science (AREA)
- Bioinformatics & Cheminformatics (AREA)
- General Chemical & Material Sciences (AREA)
- Chemical Kinetics & Catalysis (AREA)
- Nuclear Medicine, Radiotherapy & Molecular Imaging (AREA)
- Epidemiology (AREA)
- Oncology (AREA)
- Mycology (AREA)
- Microbiology (AREA)
- Zoology (AREA)
- Toxicology (AREA)
- Gastroenterology & Hepatology (AREA)
- Cell Biology (AREA)
- Biomedical Technology (AREA)
- Hematology (AREA)
- Medicines Containing Antibodies Or Antigens For Use As Internal Diagnostic Agents (AREA)
- Peptides Or Proteins (AREA)
- Medicines That Contain Protein Lipid Enzymes And Other Medicines (AREA)
- Preparation Of Compounds By Using Micro-Organisms (AREA)
- Pharmaceuticals Containing Other Organic And Inorganic Compounds (AREA)
- Medicinal Preparation (AREA)
- Micro-Organisms Or Cultivation Processes Thereof (AREA)
- Luminescent Compositions (AREA)
- Glass Compositions (AREA)
Applications Claiming Priority (9)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| US46921103P | 2003-05-08 | 2003-05-08 | |
| US60/469,211 | 2003-05-08 | ||
| US55762104P | 2004-03-29 | 2004-03-29 | |
| US55762004P | 2004-03-29 | 2004-03-29 | |
| US55762204P | 2004-03-29 | 2004-03-29 | |
| US60/557,622 | 2004-03-29 | ||
| US60/557,621 | 2004-03-29 | ||
| US60/557,620 | 2004-03-29 | ||
| PCT/US2004/014866 WO2004100898A2 (en) | 2003-05-08 | 2004-05-10 | Therapeutic use of anti-cs1 antibodies |
Publications (2)
| Publication Number | Publication Date |
|---|---|
| CA2523001A1 CA2523001A1 (en) | 2004-11-25 |
| CA2523001C true CA2523001C (en) | 2013-12-31 |
Family
ID=33459144
Family Applications (1)
| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| CA2523001A Expired - Lifetime CA2523001C (en) | 2003-05-08 | 2004-05-10 | Therapeutic use of anti-cs1 antibodies |
Country Status (25)
| Country | Link |
|---|---|
| US (8) | US20050025763A1 (enExample) |
| EP (4) | EP2371391B1 (enExample) |
| JP (4) | JP4887152B2 (enExample) |
| KR (1) | KR101268707B1 (enExample) |
| CN (1) | CN1805755B (enExample) |
| AT (1) | ATE506076T1 (enExample) |
| AU (2) | AU2004238363B2 (enExample) |
| BE (1) | BE2016C056I2 (enExample) |
| BR (1) | BRPI0410129B8 (enExample) |
| CA (1) | CA2523001C (enExample) |
| CY (4) | CY1111958T1 (enExample) |
| DE (1) | DE602004032328D1 (enExample) |
| DK (3) | DK2371391T3 (enExample) |
| ES (2) | ES2516840T3 (enExample) |
| FR (1) | FR16C1012I2 (enExample) |
| HK (1) | HK1208815A1 (enExample) |
| HU (2) | HUE034908T2 (enExample) |
| LT (1) | LT2853272T (enExample) |
| LU (1) | LU93274I2 (enExample) |
| MX (1) | MXPA05012011A (enExample) |
| NL (1) | NL300838I2 (enExample) |
| PL (3) | PL1624892T3 (enExample) |
| PT (3) | PT1624892E (enExample) |
| SI (3) | SI2371391T1 (enExample) |
| WO (1) | WO2004100898A2 (enExample) |
Families Citing this family (86)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| US20050025763A1 (en) | 2003-05-08 | 2005-02-03 | Protein Design Laboratories, Inc. | Therapeutic use of anti-CS1 antibodies |
| US7709610B2 (en) | 2003-05-08 | 2010-05-04 | Facet Biotech Corporation | Therapeutic use of anti-CS1 antibodies |
| MX2009001440A (es) * | 2006-08-07 | 2009-04-15 | Pdl Biopharma Inc | Composiciones y metodos que utilizan anticuerpos anti-cs1 para tratar mieloma multiple. |
| WO2008019379A2 (en) * | 2006-08-07 | 2008-02-14 | Pdl Biopharma, Inc. | Use of allogeneic effector cells and anti-cs1 antibodies for selective killing of multiple myeloma cells |
| PT2641601T (pt) | 2006-08-07 | 2016-10-14 | Dana Farber Cancer Inst Inc | Métodos de tratamento de mieloma múltiplo utilizando terapias de combinação baseadas em huluc63 com bortezomib |
| US9096681B2 (en) * | 2008-06-02 | 2015-08-04 | Dana-Farber Cancer Institute, Inc. | XBP1, CD138, and CS1 peptides |
| EP2361263A1 (en) * | 2008-10-31 | 2011-08-31 | Abbott Biotherapeutics Corp. | Use of anti-cs1 antibodies for treatment of rare lymphomas |
| WO2010080910A1 (en) * | 2009-01-08 | 2010-07-15 | Bio-Rad Laboratories, Inc. | Methods and compositions for improving efficiency of nucleic acids amplification reactions |
| US20120269814A1 (en) * | 2009-11-10 | 2012-10-25 | Amgen Inc. | Anti-c mpl antibodies |
| BR112012018914A2 (pt) | 2010-01-28 | 2017-07-25 | Glaxo Group Ltd | "anticorpo humanizado, proteína de ligação de antígeno, molécula de ácido nucleico, vetor de expressão, célula hospedeira recombinante, proteína de ligação de anticorpo ou de antígeno, métodos para a produção de uma proteína de ligação de antígeno e para tratar um sujeito afetado por uma doença autoimune ou inflamatória, e, composição farmacêutica." |
| EP3196212B1 (en) | 2010-02-24 | 2020-06-03 | ImmunoGen, Inc. | Immunoconjugates comprising a folate receptor 1 antibody |
| UA113403C2 (xx) | 2011-04-01 | 2017-01-25 | Спосіб підвищення ефективності folr1 терапії раку | |
| SMT202000158T1 (it) | 2012-08-31 | 2020-05-08 | Immunogen Inc | Saggi e kit diagnostici per il rilevamento del recettore dei folati 1 |
| JP6374392B2 (ja) | 2012-11-05 | 2018-08-15 | デイナ ファーバー キャンサー インスティチュート，インコーポレイテッド | Ｘｂｐ１、ｃｄ１３８およびｃｓ１ペプチド、該ペプチドを含有する薬学的組成物、ならびにかかるペプチドおよび組成物を使用する方法 |
| AU2014233528B2 (en) * | 2013-03-15 | 2019-02-28 | Abbvie Biotherapeutics Inc. | Fc variants |
| CA2904532A1 (en) * | 2013-03-15 | 2014-09-18 | Abbvie Biotechnology Ltd. | Anti-cd25 antibodies and their uses |
| US10358494B2 (en) * | 2013-05-03 | 2019-07-23 | Ohio State Innovation Foundation | CS1-specific chimeric antigen receptor engineered immune effector cells |
| WO2015013508A2 (en) * | 2013-07-24 | 2015-01-29 | The General Hospital Corporation | Methods for diagnosing and treating immune disease |
| CA2921975C (en) | 2013-08-30 | 2024-02-13 | Immunogen, Inc. | Antibodies and assays for detection of folate receptor 1 |
| US9482289B2 (en) | 2013-10-14 | 2016-11-01 | Club Car, Llc | Self-preloading shift lever |
| EP3066127A1 (en) | 2013-11-06 | 2016-09-14 | Bristol-Myers Squibb Company | Immunotherapeutic dosing regimens and combinations thereof |
| WO2015069785A1 (en) | 2013-11-06 | 2015-05-14 | Bristol-Myers Squibb Company | Combination of anti-kir and anti-cs1 antibodies to treat multiple myeloma |
| JP2017518071A (ja) * | 2014-05-02 | 2017-07-06 | セレクティスＣｅｌｌｅｃｔｉｓ | Ｃｓ１特異的多重鎖キメラ抗原受容体 |
| RS60061B1 (sr) * | 2014-06-17 | 2020-04-30 | Medimmune Ltd | Unapređena alfa-v beta-8 antitela |
| KR20170032406A (ko) | 2014-07-15 | 2017-03-22 | 주노 쎄러퓨티크스 인코퍼레이티드 | 입양 세포 치료를 위한 조작된 세포 |
| WO2016049022A1 (en) * | 2014-09-23 | 2016-03-31 | Board Of Trustees Of Michigan State University | Compositions and methods for modulating an immune response |
| AU2015339012B2 (en) * | 2014-10-31 | 2020-11-05 | Abbvie Biotherapeutics Inc. | Anti-CS1 antibodies and antibody drug conjugates |
| EA201791049A1 (ru) | 2014-12-04 | 2017-10-31 | Бристол-Майерс Сквибб Компани | Комбинация анти-cs1 и анти-pd1 антител для лечения рака (миеломы) |
| DE102015102183B4 (de) * | 2015-02-16 | 2018-03-01 | Robert Bosch Automotive Steering Gmbh | Lenkzwischenwelle für ein Kraftfahrzeug und Verfahren zum Betreiben einer Lenkzwischenwelle für ein Kraftfahrzeug |
| JP2018510623A (ja) | 2015-02-20 | 2018-04-19 | オハイオ・ステイト・イノベーション・ファウンデーション | Ｎｋｇ２ｄ及び腫瘍関連抗原に対する二価抗体 |
| WO2016168766A1 (en) * | 2015-04-15 | 2016-10-20 | The California Institute For Biomedical Research | Optimized chimeric receptor t cell switches and uses thereof |
| CN107949425A (zh) | 2015-06-29 | 2018-04-20 | 百时美施贵宝公司 | 用于治疗癌症的包含泊马度胺和抗cs1抗体的免疫治疗给药方案 |
| MA42895A (fr) | 2015-07-15 | 2018-05-23 | Juno Therapeutics Inc | Cellules modifiées pour thérapie cellulaire adoptive |
| US10172875B2 (en) | 2015-09-17 | 2019-01-08 | Immunogen, Inc. | Therapeutic combinations comprising anti-FOLR1 immunoconjugates |
| HUE057837T2 (hu) | 2015-11-03 | 2022-06-28 | Janssen Biotech Inc | PD-1-et specifikusan kötõ ellenanyagok és alkalmazásaik |
| IL269318B2 (en) | 2017-03-13 | 2024-10-01 | Intrinsic Lifesciences Llc | ANTIBODIES TO HUMAN ERYTHROFERRONE AND USES THEREOF |
| US11124579B2 (en) | 2017-03-29 | 2021-09-21 | Agency For Science, Technology And Research | Anti oligosaccharide antibody |
| HUE053760T2 (hu) | 2017-06-20 | 2021-07-28 | Inst Curie | SUV39h1-deficiens immunsejtek |
| WO2019030223A1 (en) | 2017-08-07 | 2019-02-14 | Nbe-Therapeutics Ag | ANTHRACYCLINE ANTIBODY-MEDICINAL CONJUGATES HAVING HIGH IN VIVO TOLERABILITY |
| US20210254000A1 (en) | 2017-11-01 | 2021-08-19 | Juno Therapeutics, Inc. | Process for producing a t cell composition |
| MA50855A (fr) | 2017-11-01 | 2020-09-09 | Juno Therapeutics Inc | Procédé de génération de compositions thérapeutiques de cellules modifiées |
| US12031975B2 (en) | 2017-11-01 | 2024-07-09 | Juno Therapeutics, Inc. | Methods of assessing or monitoring a response to a cell therapy |
| MX2020004243A (es) | 2017-11-01 | 2020-09-25 | Juno Therapeutics Inc | Receptores de anticuerpos y de antigenos quimericos especificos para el antigeno de maduracion de celulas b. |
| WO2019089848A1 (en) | 2017-11-01 | 2019-05-09 | Juno Therapeutics, Inc. | Methods associated with tumor burden for assessing response to a cell therapy |
| PE20200850A1 (es) | 2017-11-01 | 2020-08-20 | Juno Therapeutics Inc | Receptores de antigenos quimericos especificos para el antigeno de maduracion de celulas b y polinucleotidos que codifican los mismos |
| KR102862251B1 (ko) | 2017-12-08 | 2025-09-22 | 주노 쎄러퓨티크스 인코퍼레이티드 | 세포 요법을 위한 표현형 마커 및 관련 방법 |
| JP2021505168A (ja) | 2017-12-08 | 2021-02-18 | ジュノー セラピューティクス インコーポレイテッド | 操作されたｔ細胞の組成物を製造するための方法 |
| CN112041430A (zh) | 2017-12-08 | 2020-12-04 | 朱诺治疗学股份有限公司 | 用于培养细胞的无血清培养基配制品及其使用方法 |
| US10537585B2 (en) | 2017-12-18 | 2020-01-21 | Dexcel Pharma Technologies Ltd. | Compositions comprising dexamethasone |
| US12398209B2 (en) | 2018-01-22 | 2025-08-26 | Janssen Biotech, Inc. | Methods of treating cancers with antagonistic anti-PD-1 antibodies |
| US10633435B2 (en) | 2018-03-05 | 2020-04-28 | Janssen Pharmaceutica Nv | Anti-PHF-tau antibodies and uses thereof |
| US11629179B2 (en) | 2018-06-29 | 2023-04-18 | Stichting Het Nederlands Kanker Instituut—Antoni van Leeuwenhoek Ziekenhuis | TWEAK-receptor agonists for use in combination with immunotherapy of a cancer |
| MX2021001519A (es) | 2018-08-09 | 2021-05-27 | Juno Therapeutics Inc | Metodos para valorar acidos nucleicos integrados. |
| CN109406798A (zh) * | 2018-10-29 | 2019-03-01 | 美康生物科技股份有限公司 | 肌酐酶法检测试剂盒 |
| SG11202104188VA (en) | 2018-11-01 | 2021-05-28 | Juno Therapeutics Inc | Methods for treatment using chimeric antigen receptors specific for b-cell maturation antigen |
| PE20211058A1 (es) | 2018-11-01 | 2021-06-07 | Juno Therapeutics Inc | Receptores de antigenos quimericos especificos para el miembro d del grupo 5 de la clase c del receptor acoplado a proteina g (gprc5d) |
| IL263394A (en) * | 2018-11-29 | 2020-05-31 | Amit Ido | Methods of activating dysfunctional immune cells and treatment of cancer |
| WO2020223535A1 (en) | 2019-05-01 | 2020-11-05 | Juno Therapeutics, Inc. | Cells expressing a recombinant receptor from a modified tgfbr2 locus, related polynucleotides and methods |
| BR112021021200A2 (pt) | 2019-05-01 | 2021-12-21 | Juno Therapeutics Inc | Células expressando um receptor quimérico de um locus cd247 modificado, polinucleotídeos relacionados e métodos |
| JP7735249B2 (ja) | 2019-07-23 | 2025-09-08 | ムネモ・セラピューティクス | Ｓｕｖ３９ｈ１欠損免疫細胞 |
| KR20220092578A (ko) | 2019-11-05 | 2022-07-01 | 브리스톨-마이어스 스큅 컴퍼니 | M-단백질 검정 및 이의 용도 |
| CA3169809A1 (en) * | 2020-02-05 | 2021-08-12 | Navaux, Inc. | Anti-hepsin antibodies and uses thereof |
| KR20230009386A (ko) | 2020-04-10 | 2023-01-17 | 주노 쎄러퓨티크스 인코퍼레이티드 | Ｂ-세포 성숙 항원을 표적화하는 키메라 항원 수용체로 조작된 세포 요법 관련 방법 및 용도 |
| CN115803824A (zh) | 2020-05-13 | 2023-03-14 | 朱诺治疗学股份有限公司 | 鉴定与临床反应相关的特征的方法及其用途 |
| CN116234558A (zh) | 2020-06-26 | 2023-06-06 | 朱诺治疗学有限公司 | 条件性地表达重组受体的工程化t细胞、相关多核苷酸和方法 |
| CA3190266A1 (en) | 2020-07-30 | 2022-02-03 | Institut Curie | Immune cells defective for socs1 |
| US20230295331A1 (en) * | 2020-08-06 | 2023-09-21 | Promab Biotechnologies, Inc. | Cs1- antibody and anti-cs1-car-t cells |
| JP2023549780A (ja) | 2020-11-04 | 2023-11-29 | ジュノー セラピューティクス インコーポレイテッド | 改変されたインバリアントｃｄ３免疫グロブリンスーパーファミリー鎖遺伝子座からキメラ受容体を発現する細胞ならびに関連するポリヌクレオチドおよび方法 |
| JP2024509853A (ja) | 2021-03-03 | 2024-03-05 | ジュノー セラピューティクス インコーポレイテッド | Ｔ細胞療法およびｄｇｋ阻害剤の組合せ |
| US20250283037A1 (en) | 2021-05-06 | 2025-09-11 | Juno Therapeutics Gmbh | Methods for stimulating and transducing t cells |
| WO2022238386A1 (en) | 2021-05-10 | 2022-11-17 | Institut Curie | Methods for the treatment of cancer, inflammatory diseases and autoimmune diseases |
| WO2022248602A1 (en) | 2021-05-25 | 2022-12-01 | Institut Curie | Myeloid cells overexpressing bcl2 |
| EP4456910A1 (en) | 2021-12-28 | 2024-11-06 | Mnemo Therapeutics | Immune cells with inactivated suv39h1 and modified tcr |
| JP2025504002A (ja) | 2022-01-28 | 2025-02-06 | ジュノー セラピューティクス インコーポレイテッド | 細胞組成物を製造する方法 |
| CN119095874A (zh) | 2022-02-18 | 2024-12-06 | 乐天医药生技股份有限公司 | 抗程序性死亡配体1(pd-l1)抗体分子、编码多核苷酸及使用方法 |
| EP4499677A1 (en) | 2022-03-31 | 2025-02-05 | Institut Curie | Modified rela protein for inducing interferon expression and engineered immune cells with improved interferon expression |
| WO2023213969A1 (en) | 2022-05-05 | 2023-11-09 | Juno Therapeutics Gmbh | Viral-binding protein and related reagents, articles, and methods of use |
| WO2023220655A1 (en) | 2022-05-11 | 2023-11-16 | Celgene Corporation | Methods to overcome drug resistance by re-sensitizing cancer cells to treatment with a prior therapy via treatment with a t cell therapy |
| EP4532695A1 (en) | 2022-05-25 | 2025-04-09 | Celgene Corporation | Methods of manufacturing t cell therapies |
| WO2023230548A1 (en) | 2022-05-25 | 2023-11-30 | Celgene Corporation | Method for predicting response to a t cell therapy |
| JP2025531850A (ja) | 2022-09-08 | 2025-09-25 | ジュノー セラピューティクス インコーポレイテッド | Ｔ細胞療法および継続的または間欠的ｄｇｋ阻害剤投薬の組合せ |
| WO2024100604A1 (en) | 2022-11-09 | 2024-05-16 | Juno Therapeutics Gmbh | Methods for manufacturing engineered immune cells |
| CN120344563A (zh) * | 2022-12-02 | 2025-07-18 | 广州荔泰生物科技有限公司 | 人cs1 car-t细胞 |
| EP4630782A1 (en) | 2022-12-09 | 2025-10-15 | Juno Therapeutics, Inc. | Machine learning methods for predicting cell phenotype using holographic imaging |
| AU2024214593A1 (en) | 2023-02-03 | 2025-08-07 | C3S2 Gmbh | Methods for non-viral manufacturing of engineered immune cells |
| WO2026006370A1 (en) | 2024-06-28 | 2026-01-02 | Immunitybio, Inc. | Anti-slamf7 antibodies and therapeutics |
Family Cites Families (65)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| US4179337A (en) | 1973-07-20 | 1979-12-18 | Davis Frank F | Non-immunogenic polypeptides |
| JPS6023084B2 (ja) | 1979-07-11 | 1985-06-05 | 味の素株式会社 | 代用血液 |
| US4469863A (en) | 1980-11-12 | 1984-09-04 | Ts O Paul O P | Nonionic nucleic acid alkyl and aryl phosphonates and processes for manufacture and use thereof |
| US4640835A (en) | 1981-10-30 | 1987-02-03 | Nippon Chemiphar Company, Ltd. | Plasminogen activator derivatives |
| CH652145A5 (de) | 1982-01-22 | 1985-10-31 | Sandoz Ag | Verfahren zur in vitro-herstellung von hybridomen welche humane monoklonale antikoerper erzeugen. |
| US4496689A (en) | 1983-12-27 | 1985-01-29 | Miles Laboratories, Inc. | Covalently attached complex of alpha-1-proteinase inhibitor with a water soluble polymer |
| US4634666A (en) | 1984-01-06 | 1987-01-06 | The Board Of Trustees Of The Leland Stanford Junior University | Human-murine hybridoma fusion partner |
| US5235033A (en) | 1985-03-15 | 1993-08-10 | Anti-Gene Development Group | Alpha-morpholino ribonucleoside derivatives and polymers thereof |
| US5034506A (en) | 1985-03-15 | 1991-07-23 | Anti-Gene Development Group | Uncharged morpholino-based polymers having achiral intersubunit linkages |
| DE3675588D1 (de) | 1985-06-19 | 1990-12-20 | Ajinomoto Kk | Haemoglobin, das an ein poly(alkenylenoxid) gebunden ist. |
| WO1987005330A1 (en) | 1986-03-07 | 1987-09-11 | Michel Louis Eugene Bergh | Method for enhancing glycoprotein stability |
| US4791192A (en) | 1986-06-26 | 1988-12-13 | Takeda Chemical Industries, Ltd. | Chemically modified protein with polyethyleneglycol |
| US4946778A (en) | 1987-09-21 | 1990-08-07 | Genex Corporation | Single polypeptide chain binding molecules |
| IL85035A0 (en) | 1987-01-08 | 1988-06-30 | Int Genetic Eng | Polynucleotide molecule,a chimeric antibody with specificity for human b cell surface antigen,a process for the preparation and methods utilizing the same |
| US5004692A (en) | 1987-12-15 | 1991-04-02 | Protein Design Labs, Inc. | Cloning and expression of phosopholipase C genes |
| US5700637A (en) | 1988-05-03 | 1997-12-23 | Isis Innovation Limited | Apparatus and method for analyzing polynucleotide sequences and method of generating oligonucleotide arrays |
| US5216141A (en) | 1988-06-06 | 1993-06-01 | Benner Steven A | Oligonucleotide analogs containing sulfur linkages |
| US5530101A (en) | 1988-12-28 | 1996-06-25 | Protein Design Labs, Inc. | Humanized immunoglobulins |
| US5143854A (en) | 1989-06-07 | 1992-09-01 | Affymax Technologies N.V. | Large scale photolithographic solid phase synthesis of polypeptides and receptor binding screening thereof |
| US6329508B1 (en) | 1989-09-07 | 2001-12-11 | Alkermes, Inc. | Transferrin receptor reactive chimeric antibodies |
| KR0162259B1 (ko) | 1989-12-05 | 1998-12-01 | 아미 펙터 | 감염성 병변 및 염증성 병변을 검출 및 치료하기 위한 키메라 항체 |
| US20020099179A1 (en) * | 1989-12-21 | 2002-07-25 | Linda K. Jolliffe | Cdr-grafted antibodies |
| EP1690935A3 (en) | 1990-01-12 | 2008-07-30 | Abgenix, Inc. | Generation of xenogeneic antibodies |
| US6150584A (en) | 1990-01-12 | 2000-11-21 | Abgenix, Inc. | Human antibodies derived from immunized xenomice |
| US5427908A (en) | 1990-05-01 | 1995-06-27 | Affymax Technologies N.V. | Recombinant library screening methods |
| GB9015198D0 (en) | 1990-07-10 | 1990-08-29 | Brien Caroline J O | Binding substance |
| US5386023A (en) | 1990-07-27 | 1995-01-31 | Isis Pharmaceuticals | Backbone modified oligonucleotide analogs and preparation thereof through reductive coupling |
| US5602240A (en) | 1990-07-27 | 1997-02-11 | Ciba Geigy Ag. | Backbone modified oligonucleotide analogs |
| US5545806A (en) | 1990-08-29 | 1996-08-13 | Genpharm International, Inc. | Ransgenic non-human animals for producing heterologous antibodies |
| EP0746609A4 (en) | 1991-12-17 | 1997-12-17 | Genpharm Int | NON-HUMAN TRANSGENIC ANIMALS CAPABLE OF PRODUCING HETEROLOGOUS ANTIBODIES |
| US5644048A (en) | 1992-01-10 | 1997-07-01 | Isis Pharmaceuticals, Inc. | Process for preparing phosphorothioate oligonucleotides |
| JPH07101999A (ja) * | 1993-10-06 | 1995-04-18 | Hagiwara Yoshihide | 抗癌ヒトモノクローナル抗体に対する抗イデイオタイプ抗体のアミノ酸配列およびそれをコードするｄｎａ塩基配列 |
| US5637684A (en) | 1994-02-23 | 1997-06-10 | Isis Pharmaceuticals, Inc. | Phosphoramidate and phosphorothioamidate oligomeric compounds |
| US6015880A (en) | 1994-03-16 | 2000-01-18 | California Institute Of Technology | Method and substrate for performing multiple sequential reactions on a matrix |
| US5807522A (en) | 1994-06-17 | 1998-09-15 | The Board Of Trustees Of The Leland Stanford Junior University | Methods for fabricating microarrays of biological samples |
| AU6094696A (en) | 1995-06-05 | 1996-12-24 | Bionebraska, Inc. | Lead binding polypeptides and nucleotides coding therefor |
| US6607898B1 (en) * | 1996-03-26 | 2003-08-19 | Oncomedx, Inc. | Method for detection of hTR and hTERT telomerase-associated RNA in plasma or serum |
| WO1999063088A2 (en) | 1998-06-02 | 1999-12-09 | Genentech, Inc. | Membrane-bound proteins and nucleic acids encoding the same |
| WO2000047602A1 (en) | 1999-02-10 | 2000-08-17 | Human Genome Sciences, Inc. | 33 human secreted proteins |
| WO2003004622A2 (en) | 2001-03-21 | 2003-01-16 | Human Genome Sciences, Inc. | Human secreted proteins |
| JP2001522239A (ja) | 1997-03-21 | 2001-11-13 | ヒューマン ジノーム サイエンシーズ，インコーポレイテッド | ８７個のヒト分泌タンパク質 |
| WO2000011150A1 (en) | 1998-08-25 | 2000-03-02 | Incyte Pharmaceuticals, Inc. | Cell surface immunomodulators |
| CA2296792A1 (en) | 1999-02-26 | 2000-08-26 | Genset S.A. | Expressed sequence tags and encoded human proteins |
| US7465785B2 (en) * | 1999-03-08 | 2008-12-16 | Genentech, Inc. | Polypeptide encoded by a nucleic acid over-expressed in melanoma |
| WO2000055627A1 (en) | 1999-03-15 | 2000-09-21 | Eos Biotechnology, Inc. | Reusable low fluorescent plastic biochip |
| AU3774300A (en) | 1999-06-02 | 2000-12-18 | Genentech Inc. | Secreted and transmembrane polypeptides and nucleic acids encoding the same |
| EP1208202A2 (en) | 1999-09-01 | 2002-05-29 | Genentech, Inc. | Secreted and transmembrane polypeptides and nucleic acids encoding the same |
| AU2911601A (en) * | 1999-12-23 | 2001-07-03 | Bristol-Myers Squibb Company | Novel immunoglobulin superfamily members apex-1, apex-2 and apex-3 and uses thereof |
| AU6802801A (en) | 2000-03-01 | 2001-09-24 | Genentech Inc | Secreted and transmembrane polypeptides and nucleic acids encoding the same |
| WO2001071005A2 (en) * | 2000-03-24 | 2001-09-27 | Micromet Ag | Multifunctional polypeptides comprising a binding site to an epitope of the nkg2d receptor complex |
| EP1283721A4 (en) | 2000-05-26 | 2004-07-07 | Smithkline Beecham Corp | ANTI-RANK-LIGAND-BINDING MONOCLONAL ANTIBODIES USEFUL FOR TREATING DISEASES CAUSED BY THE RANK-LIGANDS |
| US6410271B1 (en) | 2000-06-23 | 2002-06-25 | Genetastix Corporation | Generation of highly diverse library of expression vectors via homologous recombination in yeast |
| CN1494553A (zh) * | 2001-01-29 | 2004-05-05 | IDECҩ�﹫˾ | 改变的抗体及其使用方法 |
| US20030099974A1 (en) * | 2001-07-18 | 2003-05-29 | Millennium Pharmaceuticals, Inc. | Novel genes, compositions, kits and methods for identification, assessment, prevention, and therapy of breast cancer |
| WO2003018621A2 (en) | 2001-08-23 | 2003-03-06 | Oxford Biomedica (Uk) Limited | Genes |
| US20040038877A1 (en) | 2001-10-02 | 2004-02-26 | Alsobrook John P. | Therapeutic polypeptides, nucleic acids encoding same, and methods of use |
| US7521053B2 (en) * | 2001-10-11 | 2009-04-21 | Amgen Inc. | Angiopoietin-2 specific binding agents |
| US6478825B1 (en) * | 2001-11-28 | 2002-11-12 | Osteotech, Inc. | Implant, method of making same and use of the implant for the treatment of bone defects |
| US7041499B2 (en) * | 2001-12-12 | 2006-05-09 | University Of North Texas Health Science Center | Immuno activation of CS1 receptor in natural killer cells to inhibit tumor cell growth |
| CN101987871A (zh) | 2002-09-27 | 2011-03-23 | 赞科股份有限公司 | 优化的Fc变体及其产生方法 |
| US7709610B2 (en) | 2003-05-08 | 2010-05-04 | Facet Biotech Corporation | Therapeutic use of anti-CS1 antibodies |
| US20050025763A1 (en) | 2003-05-08 | 2005-02-03 | Protein Design Laboratories, Inc. | Therapeutic use of anti-CS1 antibodies |
| EP2361263A1 (en) | 2008-10-31 | 2011-08-31 | Abbott Biotherapeutics Corp. | Use of anti-cs1 antibodies for treatment of rare lymphomas |
| CN104010774B (zh) | 2011-09-15 | 2017-10-13 | 康富真信息技术股份有限公司 | 用于自动生成机器人程序的系统和方法 |
| WO2013123099A1 (en) | 2012-02-13 | 2013-08-22 | Radius Engineering Inc. | Reusable cartridge for injection molding |
-
2004
- 2004-05-07 US US10/842,011 patent/US20050025763A1/en not_active Abandoned
- 2004-05-10 CA CA2523001A patent/CA2523001C/en not_active Expired - Lifetime
- 2004-05-10 AU AU2004238363A patent/AU2004238363B2/en not_active Expired
- 2004-05-10 PL PL04760993T patent/PL1624892T3/pl unknown
- 2004-05-10 ES ES10183377.0T patent/ES2516840T3/es not_active Expired - Lifetime
- 2004-05-10 PL PL10183377T patent/PL2371391T3/pl unknown
- 2004-05-10 SI SI200432193T patent/SI2371391T1/sl unknown
- 2004-05-10 PT PT04760993T patent/PT1624892E/pt unknown
- 2004-05-10 DK DK10183377.0T patent/DK2371391T3/da active
- 2004-05-10 AT AT04760993T patent/ATE506076T1/de active
- 2004-05-10 DK DK04760993.8T patent/DK1624892T3/da active
- 2004-05-10 JP JP2006532992A patent/JP4887152B2/ja not_active Expired - Lifetime
- 2004-05-10 EP EP10183377.0A patent/EP2371391B1/en not_active Expired - Lifetime
- 2004-05-10 DK DK14178061.9T patent/DK2853272T3/da active
- 2004-05-10 SI SI200432408T patent/SI2853272T1/sl unknown
- 2004-05-10 WO PCT/US2004/014866 patent/WO2004100898A2/en not_active Ceased
- 2004-05-10 PL PL14178061T patent/PL2853272T3/pl unknown
- 2004-05-10 MX MXPA05012011A patent/MXPA05012011A/es active IP Right Grant
- 2004-05-10 CN CN2004800164542A patent/CN1805755B/zh not_active Expired - Lifetime
- 2004-05-10 EP EP04760993A patent/EP1624892B1/en not_active Expired - Lifetime
- 2004-05-10 PT PT101833770T patent/PT2371391E/pt unknown
- 2004-05-10 PT PT141780619T patent/PT2853272T/pt unknown
- 2004-05-10 LT LTEP14178061.9T patent/LT2853272T/lt unknown
- 2004-05-10 ES ES14178061.9T patent/ES2643289T3/es not_active Expired - Lifetime
- 2004-05-10 EP EP17176948.2A patent/EP3275463A1/en not_active Withdrawn
- 2004-05-10 DE DE602004032328T patent/DE602004032328D1/de not_active Expired - Lifetime
- 2004-05-10 HU HUE14178061A patent/HUE034908T2/hu unknown
- 2004-05-10 SI SI200431707T patent/SI1624892T1/sl unknown
- 2004-05-10 BR BRPI0410129A patent/BRPI0410129B8/pt active IP Right Grant
- 2004-05-10 EP EP14178061.9A patent/EP2853272B1/en not_active Expired - Lifetime
-
2005
- 2005-11-07 KR KR1020057021141A patent/KR101268707B1/ko not_active Expired - Lifetime
-
2009
- 2009-03-10 US US12/401,513 patent/US8133981B2/en not_active Expired - Lifetime
- 2009-03-10 US US12/401,531 patent/US20090238827A1/en not_active Abandoned
- 2009-11-02 US US12/610,899 patent/US8008450B2/en not_active Expired - Lifetime
-
2010
- 2010-08-25 AU AU2010214661A patent/AU2010214661B2/en not_active Expired
-
2011
- 2011-06-30 US US13/174,134 patent/US8445646B2/en not_active Expired - Fee Related
- 2011-07-14 CY CY20111100687T patent/CY1111958T1/el unknown
- 2011-09-22 JP JP2011207654A patent/JP5976288B2/ja not_active Expired - Lifetime
-
2013
- 2013-05-15 US US13/894,857 patent/US9175081B2/en not_active Expired - Lifetime
-
2014
- 2014-02-20 JP JP2014030549A patent/JP6042834B2/ja not_active Expired - Lifetime
- 2014-10-23 CY CY20141100872T patent/CY1115671T1/el unknown
-
2015
- 2015-09-22 US US14/860,906 patent/US10442859B2/en not_active Expired - Lifetime
- 2015-09-29 HK HK15109572.0A patent/HK1208815A1/en unknown
-
2016
- 2016-07-20 JP JP2016142300A patent/JP2017019795A/ja active Pending
- 2016-10-20 HU HUS1600042C patent/HUS1600042I1/hu unknown
- 2016-10-24 LU LU93274C patent/LU93274I2/fr unknown
- 2016-10-24 BE BE2016C056C patent/BE2016C056I2/fr unknown
- 2016-10-25 NL NL300838C patent/NL300838I2/nl unknown
- 2016-10-26 CY CY2016035C patent/CY2016035I2/el unknown
- 2016-10-27 FR FR16C1012C patent/FR16C1012I2/fr active Active
-
2017
- 2017-09-15 CY CY20171100980T patent/CY1119353T1/el unknown
-
2019
- 2019-10-10 US US16/599,035 patent/US20200031929A1/en not_active Abandoned
Also Published As
Similar Documents
| Publication | Publication Date | Title |
|---|---|---|
| CA2523001C (en) | Therapeutic use of anti-cs1 antibodies | |
| US8444980B2 (en) | Therapeutic use of anti-CS1 antibodies | |
| AU2015213401B2 (en) | Therapeutic use of anti-CS1 antibodies | |
| AU2012216291B2 (en) | Therapeutic use of anti-CS1 antibodies | |
| HK1155670A1 (en) | Therapeutic use of anti-cs1 antibodies | |
| HK1155670B (en) | Therapeutic use of anti-cs1 antibodies |
Legal Events
| Date | Code | Title | Description |
|---|---|---|---|
| EEER | Examination request |