CA2294782A1 - Vertebrate telomerase genes and proteins and uses thereof - Google Patents
Vertebrate telomerase genes and proteins and uses thereof Download PDFInfo
- Publication number
- CA2294782A1 CA2294782A1 CA002294782A CA2294782A CA2294782A1 CA 2294782 A1 CA2294782 A1 CA 2294782A1 CA 002294782 A CA002294782 A CA 002294782A CA 2294782 A CA2294782 A CA 2294782A CA 2294782 A1 CA2294782 A1 CA 2294782A1
- Authority
- CA
- Canada
- Prior art keywords
- telomerase
- nucleic acid
- acid molecule
- region
- sequence
- 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.)
- Abandoned
Links
- 108010017842 Telomerase Proteins 0.000 title claims abstract description 347
- 108090000623 proteins and genes Proteins 0.000 title claims abstract description 151
- 102000004169 proteins and genes Human genes 0.000 title claims abstract description 105
- 241000251539 Vertebrata <Metazoa> Species 0.000 title claims abstract description 42
- 150000007523 nucleic acids Chemical class 0.000 claims abstract description 112
- 102000039446 nucleic acids Human genes 0.000 claims abstract description 93
- 108020004707 nucleic acids Proteins 0.000 claims abstract description 93
- 230000000694 effects Effects 0.000 claims abstract description 76
- 238000000034 method Methods 0.000 claims abstract description 71
- 239000003112 inhibitor Substances 0.000 claims abstract description 48
- 239000000203 mixture Substances 0.000 claims abstract description 21
- 239000013604 expression vector Substances 0.000 claims abstract description 16
- 210000004027 cell Anatomy 0.000 claims description 157
- 239000013615 primer Substances 0.000 claims description 111
- 108091032973 (ribonucleotides)n+m Proteins 0.000 claims description 70
- 239000013598 vector Substances 0.000 claims description 61
- 239000002299 complementary DNA Substances 0.000 claims description 59
- 230000014509 gene expression Effects 0.000 claims description 57
- 108020004414 DNA Proteins 0.000 claims description 55
- 125000003729 nucleotide group Chemical group 0.000 claims description 50
- 239000002773 nucleotide Substances 0.000 claims description 48
- 108091028043 Nucleic acid sequence Proteins 0.000 claims description 44
- 206010028980 Neoplasm Diseases 0.000 claims description 40
- 150000001413 amino acids Chemical class 0.000 claims description 40
- 238000009396 hybridization Methods 0.000 claims description 40
- 108091034117 Oligonucleotide Proteins 0.000 claims description 36
- 108090000765 processed proteins & peptides Proteins 0.000 claims description 33
- 230000027455 binding Effects 0.000 claims description 32
- 108090000994 Catalytic RNA Proteins 0.000 claims description 29
- 108091092562 ribozyme Proteins 0.000 claims description 28
- 102000053642 Catalytic RNA Human genes 0.000 claims description 27
- 230000000295 complement effect Effects 0.000 claims description 26
- 101100532034 Drosophila melanogaster RTase gene Proteins 0.000 claims description 24
- 125000003275 alpha amino acid group Chemical group 0.000 claims description 24
- 102000004196 processed proteins & peptides Human genes 0.000 claims description 21
- 240000004808 Saccharomyces cerevisiae Species 0.000 claims description 19
- 201000011510 cancer Diseases 0.000 claims description 16
- 210000004899 c-terminal region Anatomy 0.000 claims description 15
- 108010057210 telomerase RNA Proteins 0.000 claims description 15
- 239000012636 effector Substances 0.000 claims description 14
- 230000000692 anti-sense effect Effects 0.000 claims description 12
- 230000001580 bacterial effect Effects 0.000 claims description 12
- 230000003197 catalytic effect Effects 0.000 claims description 12
- 239000008194 pharmaceutical composition Substances 0.000 claims description 11
- 102000004190 Enzymes Human genes 0.000 claims description 10
- 108090000790 Enzymes Proteins 0.000 claims description 10
- 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 claims description 8
- 150000001875 compounds Chemical class 0.000 claims description 7
- 239000003155 DNA primer Substances 0.000 claims description 6
- 210000004408 hybridoma Anatomy 0.000 claims description 6
- 229960002685 biotin Drugs 0.000 claims description 4
- 235000020958 biotin Nutrition 0.000 claims description 4
- 239000011616 biotin Substances 0.000 claims description 4
- 238000003745 diagnosis Methods 0.000 claims description 4
- 239000007850 fluorescent dye Substances 0.000 claims description 4
- 229920001184 polypeptide Polymers 0.000 claims description 4
- 210000005260 human cell Anatomy 0.000 claims description 3
- 230000001177 retroviral effect Effects 0.000 claims description 3
- 241000282693 Cercopithecidae Species 0.000 claims description 2
- 102000053602 DNA Human genes 0.000 claims description 2
- 229940127073 nucleoside analogue Drugs 0.000 claims description 2
- 238000012258 culturing Methods 0.000 claims 1
- 239000003937 drug carrier Substances 0.000 claims 1
- 210000005253 yeast cell Anatomy 0.000 claims 1
- 235000018102 proteins Nutrition 0.000 description 99
- 230000003321 amplification Effects 0.000 description 95
- 238000003199 nucleic acid amplification method Methods 0.000 description 95
- 239000000047 product Substances 0.000 description 65
- 239000012634 fragment Substances 0.000 description 62
- 238000003556 assay Methods 0.000 description 61
- 239000000523 sample Substances 0.000 description 43
- 108020004999 messenger RNA Proteins 0.000 description 39
- 235000001014 amino acid Nutrition 0.000 description 36
- 102100031780 Endonuclease Human genes 0.000 description 23
- 108010092799 RNA-directed DNA polymerase Proteins 0.000 description 22
- 239000013612 plasmid Substances 0.000 description 21
- 235000014680 Saccharomyces cerevisiae Nutrition 0.000 description 18
- 238000003780 insertion Methods 0.000 description 18
- 230000037431 insertion Effects 0.000 description 18
- 108091035539 telomere Proteins 0.000 description 17
- 102000055501 telomere Human genes 0.000 description 17
- 210000001519 tissue Anatomy 0.000 description 17
- 238000012300 Sequence Analysis Methods 0.000 description 16
- 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 16
- 230000006870 function Effects 0.000 description 16
- 230000004927 fusion Effects 0.000 description 16
- 210000003411 telomere Anatomy 0.000 description 16
- 238000013518 transcription Methods 0.000 description 16
- 230000035897 transcription Effects 0.000 description 16
- 108091092195 Intron Proteins 0.000 description 15
- 238000004458 analytical method Methods 0.000 description 15
- 239000012528 membrane Substances 0.000 description 14
- 108020004705 Codon Proteins 0.000 description 13
- 102000006382 Ribonucleases Human genes 0.000 description 13
- 108010083644 Ribonucleases Proteins 0.000 description 13
- 238000001514 detection method Methods 0.000 description 13
- 239000003623 enhancer Substances 0.000 description 13
- 241000894007 species Species 0.000 description 13
- 230000007246 mechanism Effects 0.000 description 12
- 230000010076 replication Effects 0.000 description 12
- 206010025323 Lymphomas Diseases 0.000 description 11
- 208000037265 diseases, disorders, signs and symptoms Diseases 0.000 description 11
- 238000012340 reverse transcriptase PCR Methods 0.000 description 11
- 239000000872 buffer Substances 0.000 description 10
- 238000012216 screening Methods 0.000 description 10
- 210000004881 tumor cell Anatomy 0.000 description 10
- 108091026890 Coding region Proteins 0.000 description 9
- 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 9
- 201000010099 disease Diseases 0.000 description 9
- 239000003814 drug Substances 0.000 description 9
- 229940088598 enzyme Drugs 0.000 description 9
- 230000035755 proliferation Effects 0.000 description 9
- 210000001550 testis Anatomy 0.000 description 9
- 208000026310 Breast neoplasm Diseases 0.000 description 8
- 241000248488 Euplotes Species 0.000 description 8
- 108020005038 Terminator Codon Proteins 0.000 description 8
- 238000006243 chemical reaction Methods 0.000 description 8
- 238000010367 cloning Methods 0.000 description 8
- 238000012217 deletion Methods 0.000 description 8
- 230000037430 deletion Effects 0.000 description 8
- 238000002955 isolation Methods 0.000 description 8
- 239000003550 marker Substances 0.000 description 8
- 201000001441 melanoma Diseases 0.000 description 8
- 238000002360 preparation method Methods 0.000 description 8
- 230000001105 regulatory effect Effects 0.000 description 8
- 206010006187 Breast cancer Diseases 0.000 description 7
- 241000699666 Mus <mouse, genus> Species 0.000 description 7
- 230000033228 biological regulation Effects 0.000 description 7
- 239000006166 lysate Substances 0.000 description 7
- 241000894006 Bacteria Species 0.000 description 6
- LFQSCWFLJHTTHZ-UHFFFAOYSA-N Ethanol Chemical compound CCO LFQSCWFLJHTTHZ-UHFFFAOYSA-N 0.000 description 6
- 206010027476 Metastases Diseases 0.000 description 6
- 241001465754 Metazoa Species 0.000 description 6
- 241000699670 Mus sp. Species 0.000 description 6
- 241000700159 Rattus Species 0.000 description 6
- 102100032938 Telomerase reverse transcriptase Human genes 0.000 description 6
- 239000007983 Tris buffer Substances 0.000 description 6
- 230000015572 biosynthetic process Effects 0.000 description 6
- 210000001072 colon Anatomy 0.000 description 6
- 239000000284 extract Substances 0.000 description 6
- 230000037433 frameshift Effects 0.000 description 6
- 230000001965 increasing effect Effects 0.000 description 6
- 230000009401 metastasis Effects 0.000 description 6
- 102000040430 polynucleotide Human genes 0.000 description 6
- 108091033319 polynucleotide Proteins 0.000 description 6
- 239000002157 polynucleotide Substances 0.000 description 6
- 238000006467 substitution reaction Methods 0.000 description 6
- LENZDBCJOHFCAS-UHFFFAOYSA-N tris Chemical compound OCC(N)(CO)CO LENZDBCJOHFCAS-UHFFFAOYSA-N 0.000 description 6
- 102000040650 (ribonucleotides)n+m Human genes 0.000 description 5
- 241000588724 Escherichia coli Species 0.000 description 5
- 239000004677 Nylon Substances 0.000 description 5
- 108700026244 Open Reading Frames Proteins 0.000 description 5
- 108010029485 Protein Isoforms Proteins 0.000 description 5
- 102000001708 Protein Isoforms Human genes 0.000 description 5
- 239000002253 acid Substances 0.000 description 5
- 239000002671 adjuvant Substances 0.000 description 5
- 238000005119 centrifugation Methods 0.000 description 5
- 239000003153 chemical reaction reagent Substances 0.000 description 5
- 210000000349 chromosome Anatomy 0.000 description 5
- 238000011161 development Methods 0.000 description 5
- 230000018109 developmental process Effects 0.000 description 5
- 210000002950 fibroblast Anatomy 0.000 description 5
- 108020001507 fusion proteins Proteins 0.000 description 5
- 102000037865 fusion proteins Human genes 0.000 description 5
- 238000001727 in vivo Methods 0.000 description 5
- 230000001293 nucleolytic effect Effects 0.000 description 5
- 229920001778 nylon Polymers 0.000 description 5
- 230000036961 partial effect Effects 0.000 description 5
- 230000028327 secretion Effects 0.000 description 5
- 239000000243 solution Substances 0.000 description 5
- 210000000130 stem cell Anatomy 0.000 description 5
- XSYUPRQVAHJETO-WPMUBMLPSA-N (2s)-2-[[(2s)-2-[[(2s)-2-[[(2s)-2-[[(2s)-2-[[(2s)-2-amino-3-(1h-imidazol-5-yl)propanoyl]amino]-3-(1h-imidazol-5-yl)propanoyl]amino]-3-(1h-imidazol-5-yl)propanoyl]amino]-3-(1h-imidazol-5-yl)propanoyl]amino]-3-(1h-imidazol-5-yl)propanoyl]amino]-3-(1h-imidaz Chemical compound C([C@H](N)C(=O)N[C@@H](CC=1NC=NC=1)C(=O)N[C@@H](CC=1NC=NC=1)C(=O)N[C@@H](CC=1NC=NC=1)C(=O)N[C@@H](CC=1NC=NC=1)C(=O)N[C@@H](CC=1NC=NC=1)C(O)=O)C1=CN=CN1 XSYUPRQVAHJETO-WPMUBMLPSA-N 0.000 description 4
- 206010009944 Colon cancer Diseases 0.000 description 4
- 108020004635 Complementary DNA Proteins 0.000 description 4
- 241000206602 Eukaryota Species 0.000 description 4
- 241000282412 Homo Species 0.000 description 4
- 206010058467 Lung neoplasm malignant Diseases 0.000 description 4
- 108020004511 Recombinant DNA Proteins 0.000 description 4
- 241000251131 Sphyrna Species 0.000 description 4
- 150000007513 acids Chemical class 0.000 description 4
- 238000007792 addition Methods 0.000 description 4
- 201000008275 breast carcinoma Diseases 0.000 description 4
- 239000003085 diluting agent Substances 0.000 description 4
- 208000037765 diseases and disorders Diseases 0.000 description 4
- 210000003527 eukaryotic cell Anatomy 0.000 description 4
- 238000001502 gel electrophoresis Methods 0.000 description 4
- RWSXRVCMGQZWBV-WDSKDSINSA-N glutathione Chemical compound OC(=O)[C@@H](N)CCC(=O)N[C@@H](CS)C(=O)NCC(O)=O RWSXRVCMGQZWBV-WDSKDSINSA-N 0.000 description 4
- 230000012010 growth Effects 0.000 description 4
- 230000002401 inhibitory effect Effects 0.000 description 4
- 239000003446 ligand Substances 0.000 description 4
- 201000005296 lung carcinoma Diseases 0.000 description 4
- 230000001404 mediated effect Effects 0.000 description 4
- 230000035772 mutation Effects 0.000 description 4
- 239000000546 pharmaceutical excipient Substances 0.000 description 4
- 230000000644 propagated effect Effects 0.000 description 4
- 230000035945 sensitivity Effects 0.000 description 4
- 238000010186 staining Methods 0.000 description 4
- 238000003786 synthesis reaction Methods 0.000 description 4
- 230000001225 therapeutic effect Effects 0.000 description 4
- 230000014616 translation Effects 0.000 description 4
- 230000029663 wound healing Effects 0.000 description 4
- 238000002965 ELISA Methods 0.000 description 3
- 241000238631 Hexapoda Species 0.000 description 3
- 101000655352 Homo sapiens Telomerase reverse transcriptase Proteins 0.000 description 3
- 206010035226 Plasma cell myeloma Diseases 0.000 description 3
- 108010076504 Protein Sorting Signals Proteins 0.000 description 3
- 229920002684 Sepharose Polymers 0.000 description 3
- HEMHJVSKTPXQMS-UHFFFAOYSA-M Sodium hydroxide Chemical compound [OH-].[Na+] HEMHJVSKTPXQMS-UHFFFAOYSA-M 0.000 description 3
- 241000223892 Tetrahymena Species 0.000 description 3
- 239000011543 agarose gel Substances 0.000 description 3
- 230000004075 alteration Effects 0.000 description 3
- 229960000723 ampicillin Drugs 0.000 description 3
- 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 3
- 230000008901 benefit Effects 0.000 description 3
- 238000013461 design Methods 0.000 description 3
- 238000010586 diagram Methods 0.000 description 3
- 239000000539 dimer Substances 0.000 description 3
- 229940079593 drug Drugs 0.000 description 3
- 230000002255 enzymatic effect Effects 0.000 description 3
- 210000003811 finger Anatomy 0.000 description 3
- 210000004602 germ cell Anatomy 0.000 description 3
- 238000004128 high performance liquid chromatography Methods 0.000 description 3
- 238000007901 in situ hybridization Methods 0.000 description 3
- 238000000099 in vitro assay Methods 0.000 description 3
- 230000001939 inductive effect Effects 0.000 description 3
- 230000005764 inhibitory process Effects 0.000 description 3
- BPHPUYQFMNQIOC-NXRLNHOXSA-N isopropyl beta-D-thiogalactopyranoside Chemical compound CC(C)S[C@@H]1O[C@H](CO)[C@H](O)[C@H](O)[C@H]1O BPHPUYQFMNQIOC-NXRLNHOXSA-N 0.000 description 3
- 210000004185 liver Anatomy 0.000 description 3
- 210000004698 lymphocyte Anatomy 0.000 description 3
- 239000011159 matrix material Substances 0.000 description 3
- 238000010369 molecular cloning Methods 0.000 description 3
- 201000000050 myeloid neoplasm Diseases 0.000 description 3
- 230000008488 polyadenylation Effects 0.000 description 3
- 102000054765 polymorphisms of proteins Human genes 0.000 description 3
- 230000002062 proliferating effect Effects 0.000 description 3
- 238000000746 purification Methods 0.000 description 3
- 230000000717 retained effect Effects 0.000 description 3
- 230000002441 reversible effect Effects 0.000 description 3
- 230000009758 senescence Effects 0.000 description 3
- 239000006228 supernatant Substances 0.000 description 3
- 238000012360 testing method Methods 0.000 description 3
- 238000002560 therapeutic procedure Methods 0.000 description 3
- 238000013519 translation Methods 0.000 description 3
- 239000013603 viral vector Substances 0.000 description 3
- 230000003612 virological effect Effects 0.000 description 3
- 238000001262 western blot Methods 0.000 description 3
- 102000000872 ATM Human genes 0.000 description 2
- 108700028369 Alleles Proteins 0.000 description 2
- 108010039627 Aprotinin Proteins 0.000 description 2
- CIWBSHSKHKDKBQ-JLAZNSOCSA-N Ascorbic acid Chemical compound OC[C@H](O)[C@H]1OC(=O)C(O)=C1O CIWBSHSKHKDKBQ-JLAZNSOCSA-N 0.000 description 2
- 241000271566 Aves Species 0.000 description 2
- 241000282472 Canis lupus familiaris Species 0.000 description 2
- 208000005623 Carcinogenesis Diseases 0.000 description 2
- 241001227713 Chiron Species 0.000 description 2
- 108090000626 DNA-directed RNA polymerases Proteins 0.000 description 2
- 102000004163 DNA-directed RNA polymerases Human genes 0.000 description 2
- 108010054576 Deoxyribonuclease EcoRI Proteins 0.000 description 2
- 241000248499 Euplotes aediculatus Species 0.000 description 2
- 108700024394 Exon Proteins 0.000 description 2
- 102100039556 Galectin-4 Human genes 0.000 description 2
- 108700039691 Genetic Promoter Regions Proteins 0.000 description 2
- 208000032612 Glial tumor Diseases 0.000 description 2
- 206010018338 Glioma Diseases 0.000 description 2
- 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 2
- 108010024636 Glutathione Proteins 0.000 description 2
- DHMQDGOQFOQNFH-UHFFFAOYSA-N Glycine Chemical compound NCC(O)=O DHMQDGOQFOQNFH-UHFFFAOYSA-N 0.000 description 2
- 101000608765 Homo sapiens Galectin-4 Proteins 0.000 description 2
- 108010054477 Immunoglobulin Fab Fragments Proteins 0.000 description 2
- 102000001706 Immunoglobulin Fab Fragments Human genes 0.000 description 2
- 108010021625 Immunoglobulin Fragments Proteins 0.000 description 2
- 102000008394 Immunoglobulin Fragments Human genes 0.000 description 2
- GDBQQVLCIARPGH-UHFFFAOYSA-N Leupeptin Natural products CC(C)CC(NC(C)=O)C(=O)NC(CC(C)C)C(=O)NC(C=O)CCCN=C(N)N GDBQQVLCIARPGH-UHFFFAOYSA-N 0.000 description 2
- 241000124008 Mammalia Species 0.000 description 2
- YXOLAZRVSSWPPT-UHFFFAOYSA-N Morin Chemical compound OC1=CC(O)=CC=C1C1=C(O)C(=O)C2=C(O)C=C(O)C=C2O1 YXOLAZRVSSWPPT-UHFFFAOYSA-N 0.000 description 2
- 241001529936 Murinae Species 0.000 description 2
- 241000699660 Mus musculus Species 0.000 description 2
- OKIZCWYLBDKLSU-UHFFFAOYSA-M N,N,N-Trimethylmethanaminium chloride Chemical compound [Cl-].C[N+](C)(C)C OKIZCWYLBDKLSU-UHFFFAOYSA-M 0.000 description 2
- PXHVJJICTQNCMI-UHFFFAOYSA-N Nickel Chemical compound [Ni] PXHVJJICTQNCMI-UHFFFAOYSA-N 0.000 description 2
- 239000000020 Nitrocellulose Substances 0.000 description 2
- 108020004711 Nucleic Acid Probes Proteins 0.000 description 2
- ISWSIDIOOBJBQZ-UHFFFAOYSA-N Phenol Chemical compound OC1=CC=CC=C1 ISWSIDIOOBJBQZ-UHFFFAOYSA-N 0.000 description 2
- 108010039918 Polylysine Proteins 0.000 description 2
- 108010045292 Proto-Oncogene Proteins c-abl Proteins 0.000 description 2
- 102000005663 Proto-Oncogene Proteins c-abl Human genes 0.000 description 2
- 239000013614 RNA sample Substances 0.000 description 2
- 230000004570 RNA-binding Effects 0.000 description 2
- 108010081734 Ribonucleoproteins Proteins 0.000 description 2
- 102000004389 Ribonucleoproteins Human genes 0.000 description 2
- 102000000395 SH3 domains Human genes 0.000 description 2
- 108050008861 SH3 domains Proteins 0.000 description 2
- XUIMIQQOPSSXEZ-UHFFFAOYSA-N Silicon Chemical compound [Si] XUIMIQQOPSSXEZ-UHFFFAOYSA-N 0.000 description 2
- FAPWRFPIFSIZLT-UHFFFAOYSA-M Sodium chloride Chemical compound [Na+].[Cl-] FAPWRFPIFSIZLT-UHFFFAOYSA-M 0.000 description 2
- CZMRCDWAGMRECN-UGDNZRGBSA-N Sucrose Chemical compound O[C@H]1[C@H](O)[C@@H](CO)O[C@@]1(CO)O[C@@H]1[C@H](O)[C@@H](O)[C@H](O)[C@@H](CO)O1 CZMRCDWAGMRECN-UGDNZRGBSA-N 0.000 description 2
- 229930006000 Sucrose Natural products 0.000 description 2
- 108010006785 Taq Polymerase Proteins 0.000 description 2
- 102000010823 Telomere-Binding Proteins Human genes 0.000 description 2
- 108010038599 Telomere-Binding Proteins Proteins 0.000 description 2
- 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 2
- 241000700605 Viruses Species 0.000 description 2
- 208000027418 Wounds and injury Diseases 0.000 description 2
- 230000004913 activation Effects 0.000 description 2
- 239000000654 additive Substances 0.000 description 2
- 239000003963 antioxidant agent Substances 0.000 description 2
- 235000006708 antioxidants Nutrition 0.000 description 2
- 229960004405 aprotinin Drugs 0.000 description 2
- 239000013602 bacteriophage vector Substances 0.000 description 2
- 239000011324 bead Substances 0.000 description 2
- 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 2
- 239000007975 buffered saline Substances 0.000 description 2
- 230000036952 cancer formation Effects 0.000 description 2
- 150000001720 carbohydrates Chemical class 0.000 description 2
- 235000014633 carbohydrates Nutrition 0.000 description 2
- 231100000504 carcinogenesis Toxicity 0.000 description 2
- 239000000969 carrier Substances 0.000 description 2
- 230000010261 cell growth Effects 0.000 description 2
- 230000004663 cell proliferation Effects 0.000 description 2
- 238000012512 characterization method Methods 0.000 description 2
- 239000002738 chelating agent Substances 0.000 description 2
- 238000004587 chromatography analysis Methods 0.000 description 2
- 230000002759 chromosomal effect Effects 0.000 description 2
- 208000029742 colonic neoplasm Diseases 0.000 description 2
- 230000006378 damage Effects 0.000 description 2
- 230000003247 decreasing effect Effects 0.000 description 2
- 238000004925 denaturation Methods 0.000 description 2
- 230000036425 denaturation Effects 0.000 description 2
- 239000003599 detergent Substances 0.000 description 2
- 230000004069 differentiation Effects 0.000 description 2
- 238000010790 dilution Methods 0.000 description 2
- 239000012895 dilution Substances 0.000 description 2
- 208000035475 disorder Diseases 0.000 description 2
- 238000005516 engineering process Methods 0.000 description 2
- 239000000499 gel Substances 0.000 description 2
- 239000011521 glass Substances 0.000 description 2
- 239000008103 glucose Substances 0.000 description 2
- 229960003180 glutathione Drugs 0.000 description 2
- 210000003958 hematopoietic stem cell Anatomy 0.000 description 2
- FDGQSTZJBFJUBT-UHFFFAOYSA-N hypoxanthine Chemical compound O=C1NC=NC2=C1NC=N2 FDGQSTZJBFJUBT-UHFFFAOYSA-N 0.000 description 2
- 238000001114 immunoprecipitation Methods 0.000 description 2
- 238000011065 in-situ storage Methods 0.000 description 2
- 230000006698 induction Effects 0.000 description 2
- ZPNFWUPYTFPOJU-LPYSRVMUSA-N iniprol Chemical compound C([C@H]1C(=O)NCC(=O)NCC(=O)N[C@H]2CSSC[C@H]3C(=O)N[C@@H](CCCCN)C(=O)N[C@@H](C)C(=O)N[C@@H](CCCNC(N)=N)C(=O)N[C@H](C(N[C@H](C(=O)N[C@@H](CCCNC(N)=N)C(=O)N[C@@H](CC=4C=CC(O)=CC=4)C(=O)N[C@@H](CC=4C=CC=CC=4)C(=O)N[C@@H](CC=4C=CC(O)=CC=4)C(=O)N[C@@H](CC(N)=O)C(=O)N[C@@H](C)C(=O)N[C@@H](CCCCN)C(=O)N[C@@H](C)C(=O)NCC(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](CSSC[C@H](NC(=O)[C@H](CC(O)=O)NC(=O)[C@H](CCC(O)=O)NC(=O)[C@H](C)NC(=O)[C@H](CO)NC(=O)[C@H](CCCCN)NC(=O)[C@H](CC=4C=CC=CC=4)NC(=O)[C@H](CC(N)=O)NC(=O)[C@H](CC(N)=O)NC(=O)[C@H](CCCNC(N)=N)NC(=O)[C@H](CCCCN)NC(=O)[C@H](C)NC(=O)[C@H](CCCNC(N)=N)NC2=O)C(=O)N[C@@H](CCSC)C(=O)N[C@@H](CCCNC(N)=N)C(=O)N[C@@H]([C@@H](C)O)C(=O)N[C@@H](CSSC[C@H](NC(=O)[C@H](CC=2C=CC=CC=2)NC(=O)[C@H](CC(O)=O)NC(=O)[C@H]2N(CCC2)C(=O)[C@@H](N)CCCNC(N)=N)C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](CCC(O)=O)C(=O)N2[C@@H](CCC2)C(=O)N2[C@@H](CCC2)C(=O)N[C@@H](CC=2C=CC(O)=CC=2)C(=O)N[C@@H]([C@@H](C)O)C(=O)NCC(=O)N2[C@@H](CCC2)C(=O)N3)C(=O)NCC(=O)NCC(=O)N[C@@H](C)C(O)=O)C(=O)N[C@@H](CCC(N)=O)C(=O)N[C@H](C(=O)N[C@@H](CC=2C=CC=CC=2)C(=O)N[C@H](C(=O)N1)C(C)C)[C@@H](C)O)[C@@H](C)CC)=O)[C@@H](C)CC)C1=CC=C(O)C=C1 ZPNFWUPYTFPOJU-LPYSRVMUSA-N 0.000 description 2
- 208000014674 injury Diseases 0.000 description 2
- 230000003993 interaction Effects 0.000 description 2
- 238000007918 intramuscular administration Methods 0.000 description 2
- 238000007912 intraperitoneal administration Methods 0.000 description 2
- 229940065638 intron a Drugs 0.000 description 2
- 229930027917 kanamycin Natural products 0.000 description 2
- 229960000318 kanamycin Drugs 0.000 description 2
- 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 2
- 229930182823 kanamycin A Natural products 0.000 description 2
- 101150109249 lacI gene Proteins 0.000 description 2
- GDBQQVLCIARPGH-ULQDDVLXSA-N leupeptin Chemical compound CC(C)C[C@H](NC(C)=O)C(=O)N[C@@H](CC(C)C)C(=O)N[C@H](C=O)CCCN=C(N)N GDBQQVLCIARPGH-ULQDDVLXSA-N 0.000 description 2
- 108010052968 leupeptin Proteins 0.000 description 2
- 230000000670 limiting effect Effects 0.000 description 2
- 239000002502 liposome Substances 0.000 description 2
- 238000011068 loading method Methods 0.000 description 2
- 210000004072 lung Anatomy 0.000 description 2
- 239000012139 lysis buffer Substances 0.000 description 2
- 210000004962 mammalian cell Anatomy 0.000 description 2
- 238000005259 measurement Methods 0.000 description 2
- 239000002609 medium Substances 0.000 description 2
- 229910021645 metal ion Inorganic materials 0.000 description 2
- 230000004048 modification Effects 0.000 description 2
- 238000012986 modification Methods 0.000 description 2
- UXOUKMQIEVGVLY-UHFFFAOYSA-N morin Natural products OC1=CC(O)=CC(C2=C(C(=O)C3=C(O)C=C(O)C=C3O2)O)=C1 UXOUKMQIEVGVLY-UHFFFAOYSA-N 0.000 description 2
- 235000007708 morin Nutrition 0.000 description 2
- 230000007935 neutral effect Effects 0.000 description 2
- 238000006386 neutralization reaction Methods 0.000 description 2
- 229920001220 nitrocellulos Polymers 0.000 description 2
- 231100000252 nontoxic Toxicity 0.000 description 2
- 230000003000 nontoxic effect Effects 0.000 description 2
- 238000007899 nucleic acid hybridization Methods 0.000 description 2
- 239000002853 nucleic acid probe Substances 0.000 description 2
- 229950000964 pepstatin Drugs 0.000 description 2
- 108010091212 pepstatin Proteins 0.000 description 2
- FAXGPCHRFPCXOO-LXTPJMTPSA-N pepstatin A Chemical compound OC(=O)C[C@H](O)[C@H](CC(C)C)NC(=O)[C@H](C)NC(=O)C[C@H](O)[C@H](CC(C)C)NC(=O)[C@H](C(C)C)NC(=O)[C@H](C(C)C)NC(=O)CC(C)C FAXGPCHRFPCXOO-LXTPJMTPSA-N 0.000 description 2
- 210000003819 peripheral blood mononuclear cell Anatomy 0.000 description 2
- YBYRMVIVWMBXKQ-UHFFFAOYSA-N phenylmethanesulfonyl fluoride Chemical compound FS(=O)(=O)CC1=CC=CC=C1 YBYRMVIVWMBXKQ-UHFFFAOYSA-N 0.000 description 2
- 239000002953 phosphate buffered saline Substances 0.000 description 2
- 230000026731 phosphorylation Effects 0.000 description 2
- 238000006366 phosphorylation reaction Methods 0.000 description 2
- 230000004962 physiological condition Effects 0.000 description 2
- 229920000656 polylysine Polymers 0.000 description 2
- 239000002987 primer (paints) Substances 0.000 description 2
- 235000004252 protein component Nutrition 0.000 description 2
- 238000000164 protein isolation Methods 0.000 description 2
- ZCCUUQDIBDJBTK-UHFFFAOYSA-N psoralen Chemical compound C1=C2OC(=O)C=CC2=CC2=C1OC=C2 ZCCUUQDIBDJBTK-UHFFFAOYSA-N 0.000 description 2
- 230000006798 recombination Effects 0.000 description 2
- -1 reeF Proteins 0.000 description 2
- 108091008146 restriction endonucleases Proteins 0.000 description 2
- 108020004418 ribosomal RNA Proteins 0.000 description 2
- 238000004904 shortening Methods 0.000 description 2
- 229910052710 silicon Inorganic materials 0.000 description 2
- 239000010703 silicon Substances 0.000 description 2
- 239000002002 slurry Substances 0.000 description 2
- 150000003384 small molecules Chemical class 0.000 description 2
- 239000011780 sodium chloride Substances 0.000 description 2
- 238000002415 sodium dodecyl sulfate polyacrylamide gel electrophoresis Methods 0.000 description 2
- 239000007787 solid Substances 0.000 description 2
- 210000001082 somatic cell Anatomy 0.000 description 2
- 210000000952 spleen Anatomy 0.000 description 2
- 238000007920 subcutaneous administration Methods 0.000 description 2
- 239000000126 substance Substances 0.000 description 2
- 239000000758 substrate Substances 0.000 description 2
- 239000005720 sucrose Substances 0.000 description 2
- 229940124597 therapeutic agent Drugs 0.000 description 2
- 210000003813 thumb Anatomy 0.000 description 2
- 238000011830 transgenic mouse model Methods 0.000 description 2
- 241000701161 unidentified adenovirus Species 0.000 description 2
- 241000701447 unidentified baculovirus Species 0.000 description 2
- 238000005406 washing Methods 0.000 description 2
- DIGQNXIGRZPYDK-WKSCXVIASA-N (2R)-6-amino-2-[[2-[[(2S)-2-[[2-[[(2R)-2-[[(2S)-2-[[(2R,3S)-2-[[2-[[(2S)-2-[[2-[[(2S)-2-[[(2S)-2-[[(2R)-2-[[(2S,3S)-2-[[(2R)-2-[[(2S)-2-[[(2S)-2-[[(2S)-2-[[2-[[(2S)-2-[[(2R)-2-[[2-[[2-[[2-[(2-amino-1-hydroxyethylidene)amino]-3-carboxy-1-hydroxypropylidene]amino]-1-hydroxy-3-sulfanylpropylidene]amino]-1-hydroxyethylidene]amino]-1-hydroxy-3-sulfanylpropylidene]amino]-1,3-dihydroxypropylidene]amino]-1-hydroxyethylidene]amino]-1-hydroxypropylidene]amino]-1,3-dihydroxypropylidene]amino]-1,3-dihydroxypropylidene]amino]-1-hydroxy-3-sulfanylpropylidene]amino]-1,3-dihydroxybutylidene]amino]-1-hydroxy-3-sulfanylpropylidene]amino]-1-hydroxypropylidene]amino]-1,3-dihydroxypropylidene]amino]-1-hydroxyethylidene]amino]-1,5-dihydroxy-5-iminopentylidene]amino]-1-hydroxy-3-sulfanylpropylidene]amino]-1,3-dihydroxybutylidene]amino]-1-hydroxy-3-sulfanylpropylidene]amino]-1,3-dihydroxypropylidene]amino]-1-hydroxyethylidene]amino]-1-hydroxy-3-sulfanylpropylidene]amino]-1-hydroxyethylidene]amino]hexanoic acid Chemical compound C[C@@H]([C@@H](C(=N[C@@H](CS)C(=N[C@@H](C)C(=N[C@@H](CO)C(=NCC(=N[C@@H](CCC(=N)O)C(=NC(CS)C(=N[C@H]([C@H](C)O)C(=N[C@H](CS)C(=N[C@H](CO)C(=NCC(=N[C@H](CS)C(=NCC(=N[C@H](CCCCN)C(=O)O)O)O)O)O)O)O)O)O)O)O)O)O)O)N=C([C@H](CS)N=C([C@H](CO)N=C([C@H](CO)N=C([C@H](C)N=C(CN=C([C@H](CO)N=C([C@H](CS)N=C(CN=C(C(CS)N=C(C(CC(=O)O)N=C(CN)O)O)O)O)O)O)O)O)O)O)O)O DIGQNXIGRZPYDK-WKSCXVIASA-N 0.000 description 1
- 101150084750 1 gene Proteins 0.000 description 1
- VXGRJERITKFWPL-UHFFFAOYSA-N 4',5'-Dihydropsoralen Natural products C1=C2OC(=O)C=CC2=CC2=C1OCC2 VXGRJERITKFWPL-UHFFFAOYSA-N 0.000 description 1
- QFVHZQCOUORWEI-UHFFFAOYSA-N 4-[(4-anilino-5-sulfonaphthalen-1-yl)diazenyl]-5-hydroxynaphthalene-2,7-disulfonic acid Chemical compound C=12C(O)=CC(S(O)(=O)=O)=CC2=CC(S(O)(=O)=O)=CC=1N=NC(C1=CC=CC(=C11)S(O)(=O)=O)=CC=C1NC1=CC=CC=C1 QFVHZQCOUORWEI-UHFFFAOYSA-N 0.000 description 1
- 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 1
- 101100295756 Acinetobacter baumannii (strain ATCC 19606 / DSM 30007 / JCM 6841 / CCUG 19606 / CIP 70.34 / NBRC 109757 / NCIMB 12457 / NCTC 12156 / 81) omp38 gene Proteins 0.000 description 1
- 102000002260 Alkaline Phosphatase Human genes 0.000 description 1
- 108020004774 Alkaline Phosphatase Proteins 0.000 description 1
- 108091093088 Amplicon Proteins 0.000 description 1
- 108020004491 Antisense DNA Proteins 0.000 description 1
- 108020005544 Antisense RNA Proteins 0.000 description 1
- 101100136076 Aspergillus oryzae (strain ATCC 42149 / RIB 40) pel1 gene Proteins 0.000 description 1
- 206010003594 Ataxia telangiectasia Diseases 0.000 description 1
- 101150065175 Atm gene Proteins 0.000 description 1
- 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 1
- 102100021935 C-C motif chemokine 26 Human genes 0.000 description 1
- 102000014914 Carrier Proteins Human genes 0.000 description 1
- 108010078791 Carrier Proteins Proteins 0.000 description 1
- 108010001857 Cell Surface Receptors Proteins 0.000 description 1
- 101100499417 Chlamydia pneumoniae dnaA1 gene Proteins 0.000 description 1
- 208000037088 Chromosome Breakage Diseases 0.000 description 1
- 108010047041 Complementarity Determining Regions Proteins 0.000 description 1
- 108091035707 Consensus sequence Proteins 0.000 description 1
- FBPFZTCFMRRESA-KVTDHHQDSA-N D-Mannitol Chemical compound OC[C@@H](O)[C@@H](O)[C@H](O)[C@H](O)CO FBPFZTCFMRRESA-KVTDHHQDSA-N 0.000 description 1
- MNQZXJOMYWMBOU-VKHMYHEASA-N D-glyceraldehyde Chemical compound OC[C@@H](O)C=O MNQZXJOMYWMBOU-VKHMYHEASA-N 0.000 description 1
- WQZGKKKJIJFFOK-QTVWNMPRSA-N D-mannopyranose Chemical compound OC[C@H]1OC(O)[C@@H](O)[C@@H](O)[C@@H]1O WQZGKKKJIJFFOK-QTVWNMPRSA-N 0.000 description 1
- 230000004568 DNA-binding Effects 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
- 241001533413 Deltavirus Species 0.000 description 1
- 229920002307 Dextran Polymers 0.000 description 1
- 239000004375 Dextrin Substances 0.000 description 1
- 229920001353 Dextrin Polymers 0.000 description 1
- 108090000204 Dipeptidase 1 Proteins 0.000 description 1
- 108010016626 Dipeptides Proteins 0.000 description 1
- 241000255581 Drosophila <fruit fly, genus> Species 0.000 description 1
- 241000196324 Embryophyta Species 0.000 description 1
- 108010042407 Endonucleases Proteins 0.000 description 1
- 108010067770 Endopeptidase K Proteins 0.000 description 1
- YQYJSBFKSSDGFO-UHFFFAOYSA-N Epihygromycin Natural products OC1C(O)C(C(=O)C)OC1OC(C(=C1)O)=CC=C1C=C(C)C(=O)NC1C(O)C(O)C2OCOC2C1O YQYJSBFKSSDGFO-UHFFFAOYSA-N 0.000 description 1
- 101710104359 F protein Proteins 0.000 description 1
- 241000233866 Fungi Species 0.000 description 1
- 102100040004 Gamma-glutamylcyclotransferase Human genes 0.000 description 1
- 101150112014 Gapdh gene Proteins 0.000 description 1
- 108700028146 Genetic Enhancer Elements Proteins 0.000 description 1
- 108700007698 Genetic Terminator Regions Proteins 0.000 description 1
- KOSRFJWDECSPRO-WDSKDSINSA-N Glu-Glu Chemical compound OC(=O)CC[C@H](N)C(=O)N[C@@H](CCC(O)=O)C(O)=O KOSRFJWDECSPRO-WDSKDSINSA-N 0.000 description 1
- 102000005720 Glutathione transferase Human genes 0.000 description 1
- 108010070675 Glutathione transferase Proteins 0.000 description 1
- 239000004471 Glycine Substances 0.000 description 1
- 108010043121 Green Fluorescent Proteins Proteins 0.000 description 1
- 102000004144 Green Fluorescent Proteins Human genes 0.000 description 1
- 108090001102 Hammerhead ribozyme Proteins 0.000 description 1
- 208000005331 Hepatitis D Diseases 0.000 description 1
- 208000037262 Hepatitis delta Diseases 0.000 description 1
- 241000724709 Hepatitis delta virus Species 0.000 description 1
- 241000175212 Herpesvirales Species 0.000 description 1
- 101710121996 Hexon protein p72 Proteins 0.000 description 1
- 101000897493 Homo sapiens C-C motif chemokine 26 Proteins 0.000 description 1
- 101000886680 Homo sapiens Gamma-glutamylcyclotransferase Proteins 0.000 description 1
- 101000785063 Homo sapiens Serine-protein kinase ATM Proteins 0.000 description 1
- 108090000144 Human Proteins Proteins 0.000 description 1
- 102000003839 Human Proteins Human genes 0.000 description 1
- 241000701044 Human gammaherpesvirus 4 Species 0.000 description 1
- UGQMRVRMYYASKQ-UHFFFAOYSA-N Hypoxanthine nucleoside Natural products OC1C(O)C(CO)OC1N1C(NC=NC2=O)=C2N=C1 UGQMRVRMYYASKQ-UHFFFAOYSA-N 0.000 description 1
- 108060003951 Immunoglobulin Proteins 0.000 description 1
- 108010067060 Immunoglobulin Variable Region Proteins 0.000 description 1
- 102000017727 Immunoglobulin Variable Region Human genes 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
- QNAYBMKLOCPYGJ-REOHCLBHSA-N L-alanine Chemical compound C[C@H](N)C(O)=O QNAYBMKLOCPYGJ-REOHCLBHSA-N 0.000 description 1
- 102000003960 Ligases Human genes 0.000 description 1
- 108090000364 Ligases Proteins 0.000 description 1
- 208000007433 Lymphatic Metastasis Diseases 0.000 description 1
- 241000282553 Macaca Species 0.000 description 1
- 101710125418 Major capsid protein Proteins 0.000 description 1
- 229930195725 Mannitol Natural products 0.000 description 1
- 208000000172 Medulloblastoma Diseases 0.000 description 1
- 102000003792 Metallothionein Human genes 0.000 description 1
- 108090000157 Metallothionein Proteins 0.000 description 1
- 108060004795 Methyltransferase Proteins 0.000 description 1
- 241000713333 Mouse mammary tumor virus Species 0.000 description 1
- 102000016943 Muramidase Human genes 0.000 description 1
- 108010014251 Muramidase Proteins 0.000 description 1
- 241000711408 Murine respirovirus Species 0.000 description 1
- 108010021466 Mutant Proteins Proteins 0.000 description 1
- 102000008300 Mutant Proteins Human genes 0.000 description 1
- 108010062010 N-Acetylmuramoyl-L-alanine Amidase Proteins 0.000 description 1
- 125000001429 N-terminal alpha-amino-acid group Chemical group 0.000 description 1
- 206010029260 Neuroblastoma Diseases 0.000 description 1
- 238000000636 Northern blotting Methods 0.000 description 1
- 101710163270 Nuclease Proteins 0.000 description 1
- 108700020796 Oncogene Proteins 0.000 description 1
- 241000283973 Oryctolagus cuniculus Species 0.000 description 1
- 241000248501 Oxytricha Species 0.000 description 1
- 238000002944 PCR assay Methods 0.000 description 1
- 229910019142 PO4 Inorganic materials 0.000 description 1
- 241000282520 Papio Species 0.000 description 1
- OAICVXFJPJFONN-UHFFFAOYSA-N Phosphorus Chemical compound [P] OAICVXFJPJFONN-UHFFFAOYSA-N 0.000 description 1
- 108091000080 Phosphotransferase Proteins 0.000 description 1
- 239000002202 Polyethylene glycol Substances 0.000 description 1
- 241000288906 Primates Species 0.000 description 1
- 102000006478 Protein Phosphatase 2 Human genes 0.000 description 1
- 108010058956 Protein Phosphatase 2 Proteins 0.000 description 1
- 101710188306 Protein Y Proteins 0.000 description 1
- 101100084022 Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1) lapA gene Proteins 0.000 description 1
- 108091034057 RNA (poly(A)) Proteins 0.000 description 1
- 238000002123 RNA extraction Methods 0.000 description 1
- 238000010240 RT-PCR analysis Methods 0.000 description 1
- 108091081062 Repeated sequence (DNA) Proteins 0.000 description 1
- 108700008625 Reporter Genes Proteins 0.000 description 1
- 102000009661 Repressor Proteins Human genes 0.000 description 1
- 108010034634 Repressor Proteins Proteins 0.000 description 1
- 208000005074 Retroviridae Infections Diseases 0.000 description 1
- 108090000621 Ribonuclease P Proteins 0.000 description 1
- 102000004167 Ribonuclease P Human genes 0.000 description 1
- 241000283984 Rodentia Species 0.000 description 1
- 241000235070 Saccharomyces Species 0.000 description 1
- 102000007562 Serum Albumin Human genes 0.000 description 1
- 108010071390 Serum Albumin Proteins 0.000 description 1
- 108020004682 Single-Stranded DNA Proteins 0.000 description 1
- 208000000453 Skin Neoplasms Diseases 0.000 description 1
- 102220497176 Small vasohibin-binding protein_T47D_mutation Human genes 0.000 description 1
- 241000256251 Spodoptera frugiperda Species 0.000 description 1
- 208000037065 Subacute sclerosing leukoencephalitis Diseases 0.000 description 1
- 206010042297 Subacute sclerosing panencephalitis Diseases 0.000 description 1
- 108700026226 TATA Box Proteins 0.000 description 1
- 239000004098 Tetracycline Substances 0.000 description 1
- 102000006601 Thymidine Kinase Human genes 0.000 description 1
- 108020004440 Thymidine kinase Proteins 0.000 description 1
- RTAQQCXQSZGOHL-UHFFFAOYSA-N Titanium Chemical compound [Ti] RTAQQCXQSZGOHL-UHFFFAOYSA-N 0.000 description 1
- 101710120037 Toxin CcdB Proteins 0.000 description 1
- 108700009124 Transcription Initiation Site Proteins 0.000 description 1
- 229920004890 Triton X-100 Polymers 0.000 description 1
- 239000013504 Triton X-100 Substances 0.000 description 1
- 108091023045 Untranslated Region Proteins 0.000 description 1
- 208000008383 Wilms tumor Diseases 0.000 description 1
- 238000002441 X-ray diffraction Methods 0.000 description 1
- 239000004480 active ingredient Substances 0.000 description 1
- 238000001042 affinity chromatography Methods 0.000 description 1
- 230000032683 aging Effects 0.000 description 1
- 238000013019 agitation Methods 0.000 description 1
- 239000000556 agonist Substances 0.000 description 1
- 235000004279 alanine Nutrition 0.000 description 1
- KOSRFJWDECSPRO-UHFFFAOYSA-N alpha-L-glutamyl-L-glutamic acid Natural products OC(=O)CCC(N)C(=O)NC(CCC(O)=O)C(O)=O KOSRFJWDECSPRO-UHFFFAOYSA-N 0.000 description 1
- WNROFYMDJYEPJX-UHFFFAOYSA-K aluminium hydroxide Chemical compound [OH-].[OH-].[OH-].[Al+3] WNROFYMDJYEPJX-UHFFFAOYSA-K 0.000 description 1
- 125000000539 amino acid group Chemical group 0.000 description 1
- 229960003896 aminopterin Drugs 0.000 description 1
- 210000004102 animal cell Anatomy 0.000 description 1
- 210000003423 ankle Anatomy 0.000 description 1
- 238000000137 annealing Methods 0.000 description 1
- 239000005557 antagonist Substances 0.000 description 1
- 239000003816 antisense DNA Substances 0.000 description 1
- 239000000074 antisense oligonucleotide Substances 0.000 description 1
- 238000012230 antisense oligonucleotides Methods 0.000 description 1
- 238000013459 approach Methods 0.000 description 1
- 101150042295 arfA gene Proteins 0.000 description 1
- 210000001106 artificial yeast chromosome Anatomy 0.000 description 1
- 125000003118 aryl group Chemical group 0.000 description 1
- 235000010323 ascorbic acid Nutrition 0.000 description 1
- 229960005070 ascorbic acid Drugs 0.000 description 1
- 239000011668 ascorbic acid Substances 0.000 description 1
- CKLJMWTZIZZHCS-REOHCLBHSA-N aspartic acid group Chemical group N[C@@H](CC(=O)O)C(=O)O CKLJMWTZIZZHCS-REOHCLBHSA-N 0.000 description 1
- 230000002238 attenuated effect Effects 0.000 description 1
- MHMUIIBVMBOAON-UHFFFAOYSA-N azane;2,2,2-trichloroacetic acid Chemical compound [NH4+].[O-]C(=O)C(Cl)(Cl)Cl MHMUIIBVMBOAON-UHFFFAOYSA-N 0.000 description 1
- 210000003719 b-lymphocyte Anatomy 0.000 description 1
- 230000009286 beneficial effect Effects 0.000 description 1
- IQFYYKKMVGJFEH-UHFFFAOYSA-N beta-L-thymidine Natural products O=C1NC(=O)C(C)=CN1C1OC(CO)C(O)C1 IQFYYKKMVGJFEH-UHFFFAOYSA-N 0.000 description 1
- 102000006635 beta-lactamase Human genes 0.000 description 1
- 230000000903 blocking effect Effects 0.000 description 1
- 210000004369 blood Anatomy 0.000 description 1
- 239000008280 blood Substances 0.000 description 1
- 210000001185 bone marrow Anatomy 0.000 description 1
- 238000010322 bone marrow transplantation Methods 0.000 description 1
- 108010006025 bovine growth hormone Proteins 0.000 description 1
- 210000004556 brain Anatomy 0.000 description 1
- 210000004958 brain cell Anatomy 0.000 description 1
- 239000008366 buffered solution Substances 0.000 description 1
- 239000006227 byproduct Substances 0.000 description 1
- 238000010804 cDNA synthesis Methods 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
- 239000012830 cancer therapeutic Substances 0.000 description 1
- 238000006555 catalytic reaction Methods 0.000 description 1
- 238000004113 cell culture Methods 0.000 description 1
- 230000022131 cell cycle Effects 0.000 description 1
- 230000025084 cell cycle arrest Effects 0.000 description 1
- 230000032823 cell division Effects 0.000 description 1
- 230000036978 cell physiology Effects 0.000 description 1
- 230000003833 cell viability Effects 0.000 description 1
- 210000002421 cell wall Anatomy 0.000 description 1
- 108091092328 cellular RNA Proteins 0.000 description 1
- 230000010094 cellular senescence Effects 0.000 description 1
- 239000001913 cellulose Substances 0.000 description 1
- 229920002678 cellulose Polymers 0.000 description 1
- 230000002490 cerebral effect Effects 0.000 description 1
- 230000008859 change Effects 0.000 description 1
- 230000003196 chaotropic effect Effects 0.000 description 1
- 239000003795 chemical substances by application Substances 0.000 description 1
- 239000013611 chromosomal DNA Substances 0.000 description 1
- 238000003776 cleavage reaction Methods 0.000 description 1
- 238000000749 co-immunoprecipitation Methods 0.000 description 1
- 230000000112 colonic effect Effects 0.000 description 1
- 239000003184 complementary RNA Substances 0.000 description 1
- 238000012790 confirmation Methods 0.000 description 1
- 238000010276 construction Methods 0.000 description 1
- 230000001276 controlling effect Effects 0.000 description 1
- 238000007796 conventional method Methods 0.000 description 1
- 239000013078 crystal Substances 0.000 description 1
- 238000002425 crystallisation Methods 0.000 description 1
- 230000008025 crystallization Effects 0.000 description 1
- 230000001351 cycling effect Effects 0.000 description 1
- 230000007812 deficiency Effects 0.000 description 1
- 230000002950 deficient Effects 0.000 description 1
- 230000001419 dependent effect Effects 0.000 description 1
- 238000006209 dephosphorylation reaction Methods 0.000 description 1
- 235000019425 dextrin Nutrition 0.000 description 1
- 230000029087 digestion Effects 0.000 description 1
- 230000003292 diminished effect Effects 0.000 description 1
- LOKCTEFSRHRXRJ-UHFFFAOYSA-I dipotassium trisodium dihydrogen phosphate hydrogen phosphate dichloride Chemical compound P(=O)(O)(O)[O-].[K+].P(=O)(O)([O-])[O-].[Na+].[Na+].[Cl-].[K+].[Cl-].[Na+] LOKCTEFSRHRXRJ-UHFFFAOYSA-I 0.000 description 1
- 238000010494 dissociation reaction Methods 0.000 description 1
- 230000005593 dissociations Effects 0.000 description 1
- 238000009826 distribution Methods 0.000 description 1
- 101150020338 dnaA gene Proteins 0.000 description 1
- 230000005684 electric field Effects 0.000 description 1
- 238000001962 electrophoresis Methods 0.000 description 1
- 238000004520 electroporation Methods 0.000 description 1
- 239000000839 emulsion Substances 0.000 description 1
- 230000002708 enhancing effect Effects 0.000 description 1
- 230000006862 enzymatic digestion Effects 0.000 description 1
- 230000009088 enzymatic function Effects 0.000 description 1
- 239000006167 equilibration buffer Substances 0.000 description 1
- DEFVIWRASFVYLL-UHFFFAOYSA-N ethylene glycol bis(2-aminoethyl)tetraacetic acid Chemical compound OC(=O)CN(CC(O)=O)CCOCCOCCN(CC(O)=O)CC(O)=O DEFVIWRASFVYLL-UHFFFAOYSA-N 0.000 description 1
- 230000005713 exacerbation Effects 0.000 description 1
- 238000002474 experimental method Methods 0.000 description 1
- 238000000605 extraction Methods 0.000 description 1
- 238000000855 fermentation Methods 0.000 description 1
- 230000004151 fermentation Effects 0.000 description 1
- 230000001605 fetal effect Effects 0.000 description 1
- 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 1
- 238000002825 functional assay Methods 0.000 description 1
- 238000010363 gene targeting Methods 0.000 description 1
- 238000001415 gene therapy Methods 0.000 description 1
- 108010055341 glutamyl-glutamic acid Proteins 0.000 description 1
- 239000005090 green fluorescent protein Substances 0.000 description 1
- 239000001963 growth medium Substances 0.000 description 1
- 230000003779 hair growth Effects 0.000 description 1
- 108090001052 hairpin ribozyme Proteins 0.000 description 1
- 230000035876 healing Effects 0.000 description 1
- 210000002216 heart Anatomy 0.000 description 1
- 208000029570 hepatitis D virus infection Diseases 0.000 description 1
- 210000001320 hippocampus Anatomy 0.000 description 1
- 238000000265 homogenisation Methods 0.000 description 1
- 230000006801 homologous recombination Effects 0.000 description 1
- 238000002744 homologous recombination Methods 0.000 description 1
- 206010020718 hyperplasia Diseases 0.000 description 1
- 230000003463 hyperproliferative effect Effects 0.000 description 1
- 230000028993 immune response Effects 0.000 description 1
- 238000002649 immunization Methods 0.000 description 1
- 230000003053 immunization Effects 0.000 description 1
- 238000000760 immunoelectrophoresis Methods 0.000 description 1
- 102000018358 immunoglobulin Human genes 0.000 description 1
- 239000007943 implant Substances 0.000 description 1
- 238000000338 in vitro Methods 0.000 description 1
- 238000012603 in vitro chemosensitivity assay Methods 0.000 description 1
- 239000000411 inducer Substances 0.000 description 1
- 208000015181 infectious disease Diseases 0.000 description 1
- 239000004615 ingredient Substances 0.000 description 1
- 238000007917 intracranial administration Methods 0.000 description 1
- 238000004255 ion exchange chromatography Methods 0.000 description 1
- 108010045069 keyhole-limpet hemocyanin Proteins 0.000 description 1
- 238000011813 knockout mouse model Methods 0.000 description 1
- 208000032839 leukemia Diseases 0.000 description 1
- 239000007788 liquid Substances 0.000 description 1
- 230000033001 locomotion Effects 0.000 description 1
- 210000001165 lymph node Anatomy 0.000 description 1
- 229960000274 lysozyme Drugs 0.000 description 1
- 239000004325 lysozyme Substances 0.000 description 1
- 235000010335 lysozyme Nutrition 0.000 description 1
- 230000002101 lytic effect Effects 0.000 description 1
- 235000010355 mannitol Nutrition 0.000 description 1
- 239000000594 mannitol Substances 0.000 description 1
- 238000013507 mapping Methods 0.000 description 1
- 102000006240 membrane receptors Human genes 0.000 description 1
- 229910052751 metal Inorganic materials 0.000 description 1
- 239000002184 metal Substances 0.000 description 1
- 238000000520 microinjection Methods 0.000 description 1
- 238000012544 monitoring process Methods 0.000 description 1
- 238000002887 multiple sequence alignment Methods 0.000 description 1
- 210000002569 neuron Anatomy 0.000 description 1
- 230000009689 neuronal regeneration Effects 0.000 description 1
- 229910052759 nickel Inorganic materials 0.000 description 1
- 101150087557 omcB gene Proteins 0.000 description 1
- 101150115693 ompA gene Proteins 0.000 description 1
- 101150110245 ompC gene Proteins 0.000 description 1
- 101150073640 ompF gene Proteins 0.000 description 1
- 101150093139 ompT gene Proteins 0.000 description 1
- 210000000056 organ Anatomy 0.000 description 1
- 230000033667 organ regeneration Effects 0.000 description 1
- 201000008968 osteosarcoma Diseases 0.000 description 1
- 230000002018 overexpression Effects 0.000 description 1
- 239000005022 packaging material Substances 0.000 description 1
- 210000000496 pancreas Anatomy 0.000 description 1
- 244000045947 parasite Species 0.000 description 1
- LCCNCVORNKJIRZ-UHFFFAOYSA-N parathion Chemical compound CCOP(=S)(OCC)OC1=CC=C([N+]([O-])=O)C=C1 LCCNCVORNKJIRZ-UHFFFAOYSA-N 0.000 description 1
- 101150040383 pel2 gene Proteins 0.000 description 1
- 101150050446 pelB gene Proteins 0.000 description 1
- 239000008188 pellet Substances 0.000 description 1
- 210000005105 peripheral blood lymphocyte Anatomy 0.000 description 1
- 230000002093 peripheral effect Effects 0.000 description 1
- 210000001322 periplasm Anatomy 0.000 description 1
- 208000028591 pheochromocytoma Diseases 0.000 description 1
- 101150009573 phoA gene Proteins 0.000 description 1
- NBIIXXVUZAFLBC-UHFFFAOYSA-K phosphate Chemical compound [O-]P([O-])([O-])=O NBIIXXVUZAFLBC-UHFFFAOYSA-K 0.000 description 1
- 239000010452 phosphate Substances 0.000 description 1
- 102000020233 phosphotransferase Human genes 0.000 description 1
- 238000000053 physical method Methods 0.000 description 1
- 239000013600 plasmid vector Substances 0.000 description 1
- 229920001223 polyethylene glycol Polymers 0.000 description 1
- 239000013641 positive control Substances 0.000 description 1
- 238000001556 precipitation Methods 0.000 description 1
- 239000002243 precursor Substances 0.000 description 1
- 239000003755 preservative agent Substances 0.000 description 1
- 125000002924 primary amino group Chemical group [H]N([H])* 0.000 description 1
- 230000037452 priming Effects 0.000 description 1
- 230000008569 process Effects 0.000 description 1
- 230000001915 proofreading effect Effects 0.000 description 1
- 230000004952 protein activity Effects 0.000 description 1
- 230000009822 protein phosphorylation Effects 0.000 description 1
- 230000004850 protein–protein interaction Effects 0.000 description 1
- 238000012205 qualitative assay Methods 0.000 description 1
- 230000002285 radioactive effect Effects 0.000 description 1
- 238000003127 radioimmunoassay Methods 0.000 description 1
- 238000003156 radioimmunoprecipitation Methods 0.000 description 1
- 230000009257 reactivity Effects 0.000 description 1
- 238000003753 real-time PCR Methods 0.000 description 1
- 230000008707 rearrangement Effects 0.000 description 1
- 101150079601 recA gene Proteins 0.000 description 1
- 102000005962 receptors Human genes 0.000 description 1
- 108020003175 receptors Proteins 0.000 description 1
- 238000010188 recombinant method Methods 0.000 description 1
- 238000005215 recombination Methods 0.000 description 1
- 230000009467 reduction Effects 0.000 description 1
- 230000001172 regenerating effect Effects 0.000 description 1
- 230000022983 regulation of cell cycle Effects 0.000 description 1
- 230000022532 regulation of transcription, DNA-dependent Effects 0.000 description 1
- 230000003362 replicative effect Effects 0.000 description 1
- 239000011347 resin Substances 0.000 description 1
- 229920005989 resin Polymers 0.000 description 1
- 230000004044 response Effects 0.000 description 1
- 230000008458 response to injury Effects 0.000 description 1
- 238000004007 reversed phase HPLC Methods 0.000 description 1
- YVSWPCCVTYEEHG-UHFFFAOYSA-N rhodamine B 5-isothiocyanate Chemical compound [Cl-].C=12C=CC(=[N+](CC)CC)C=C2OC2=CC(N(CC)CC)=CC=C2C=1C1=CC=C(N=C=S)C=C1C(O)=O YVSWPCCVTYEEHG-UHFFFAOYSA-N 0.000 description 1
- 239000012723 sample buffer Substances 0.000 description 1
- 230000007017 scission Effects 0.000 description 1
- 238000007423 screening assay Methods 0.000 description 1
- 238000001542 size-exclusion chromatography Methods 0.000 description 1
- 230000008470 skin growth Effects 0.000 description 1
- 210000000329 smooth muscle myocyte Anatomy 0.000 description 1
- 230000000392 somatic effect Effects 0.000 description 1
- 230000009870 specific binding Effects 0.000 description 1
- 239000003381 stabilizer Substances 0.000 description 1
- 238000003153 stable transfection Methods 0.000 description 1
- 238000012289 standard assay Methods 0.000 description 1
- 238000010561 standard procedure Methods 0.000 description 1
- 230000004960 subcellular localization Effects 0.000 description 1
- 239000007929 subcutaneous injection Substances 0.000 description 1
- 238000010254 subcutaneous injection Methods 0.000 description 1
- 238000013268 sustained release Methods 0.000 description 1
- 239000012730 sustained-release form Substances 0.000 description 1
- 208000024891 symptom Diseases 0.000 description 1
- 230000008685 targeting Effects 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
- MPLHNVLQVRSVEE-UHFFFAOYSA-N texas red Chemical compound [O-]S(=O)(=O)C1=CC(S(Cl)(=O)=O)=CC=C1C(C1=CC=2CCCN3CCCC(C=23)=C1O1)=C2C1=C(CCC1)C3=[N+]1CCCC3=C2 MPLHNVLQVRSVEE-UHFFFAOYSA-N 0.000 description 1
- 229940104230 thymidine Drugs 0.000 description 1
- 230000005030 transcription termination Effects 0.000 description 1
- 230000002103 transcriptional effect Effects 0.000 description 1
- 238000010361 transduction Methods 0.000 description 1
- 230000026683 transduction Effects 0.000 description 1
- 238000001890 transfection Methods 0.000 description 1
- 230000009466 transformation Effects 0.000 description 1
- 230000009261 transgenic effect Effects 0.000 description 1
- 230000001052 transient effect Effects 0.000 description 1
- 230000007704 transition Effects 0.000 description 1
- 230000014621 translational initiation Effects 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
- 230000005748 tumor development Effects 0.000 description 1
- 238000010396 two-hybrid screening Methods 0.000 description 1
- 239000003981 vehicle Substances 0.000 description 1
- 238000012795 verification Methods 0.000 description 1
- 238000003260 vortexing Methods 0.000 description 1
- XLYOFNOQVPJJNP-UHFFFAOYSA-N water Substances O XLYOFNOQVPJJNP-UHFFFAOYSA-N 0.000 description 1
- 238000002424 x-ray crystallography Methods 0.000 description 1
- 238000001086 yeast two-hybrid system Methods 0.000 description 1
Classifications
-
- C—CHEMISTRY; METALLURGY
- C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
- C12N—MICROORGANISMS OR ENZYMES; COMPOSITIONS THEREOF; PROPAGATING, PRESERVING, OR MAINTAINING MICROORGANISMS; MUTATION OR GENETIC ENGINEERING; CULTURE MEDIA
- C12N15/00—Mutation or genetic engineering; DNA or RNA concerning genetic engineering, vectors, e.g. plasmids, or their isolation, preparation or purification; Use of hosts therefor
- C12N15/09—Recombinant DNA-technology
- C12N15/11—DNA or RNA fragments; Modified forms thereof; Non-coding nucleic acids having a biological activity
- C12N15/52—Genes encoding for enzymes or proenzymes
-
- C—CHEMISTRY; METALLURGY
- C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
- C12N—MICROORGANISMS OR ENZYMES; COMPOSITIONS THEREOF; PROPAGATING, PRESERVING, OR MAINTAINING MICROORGANISMS; MUTATION OR GENETIC ENGINEERING; CULTURE MEDIA
- C12N9/00—Enzymes; Proenzymes; Compositions thereof; Processes for preparing, activating, inhibiting, separating or purifying enzymes
- C12N9/10—Transferases (2.)
- C12N9/12—Transferases (2.) transferring phosphorus containing groups, e.g. kinases (2.7)
- C12N9/1241—Nucleotidyltransferases (2.7.7)
-
- C—CHEMISTRY; METALLURGY
- C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
- C12N—MICROORGANISMS OR ENZYMES; COMPOSITIONS THEREOF; PROPAGATING, PRESERVING, OR MAINTAINING MICROORGANISMS; MUTATION OR GENETIC ENGINEERING; CULTURE MEDIA
- C12N15/00—Mutation or genetic engineering; DNA or RNA concerning genetic engineering, vectors, e.g. plasmids, or their isolation, preparation or purification; Use of hosts therefor
- C12N15/09—Recombinant DNA-technology
- C12N15/63—Introduction of foreign genetic material using vectors; Vectors; Use of hosts therefor; Regulation of expression
-
- C—CHEMISTRY; METALLURGY
- C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
- C12Q—MEASURING OR TESTING PROCESSES INVOLVING ENZYMES, NUCLEIC ACIDS OR MICROORGANISMS; COMPOSITIONS OR TEST PAPERS THEREFOR; PROCESSES OF PREPARING SUCH COMPOSITIONS; CONDITION-RESPONSIVE CONTROL IN MICROBIOLOGICAL OR ENZYMOLOGICAL PROCESSES
- C12Q1/00—Measuring or testing processes involving enzymes, nucleic acids or microorganisms; Compositions therefor; Processes of preparing such compositions
- C12Q1/68—Measuring or testing processes involving enzymes, nucleic acids or microorganisms; Compositions therefor; Processes of preparing such compositions involving nucleic acids
-
- A—HUMAN NECESSITIES
- A01—AGRICULTURE; FORESTRY; ANIMAL HUSBANDRY; HUNTING; TRAPPING; FISHING
- A01K—ANIMAL HUSBANDRY; AVICULTURE; APICULTURE; PISCICULTURE; FISHING; REARING OR BREEDING ANIMALS, NOT OTHERWISE PROVIDED FOR; NEW BREEDS OF ANIMALS
- A01K2217/00—Genetically modified animals
- A01K2217/05—Animals comprising random inserted nucleic acids (transgenic)
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61K—PREPARATIONS FOR MEDICAL, DENTAL OR TOILETRY PURPOSES
- A61K38/00—Medicinal preparations containing peptides
Landscapes
- Health & Medical Sciences (AREA)
- Life Sciences & Earth Sciences (AREA)
- Genetics & Genomics (AREA)
- Chemical & Material Sciences (AREA)
- Engineering & Computer Science (AREA)
- Organic Chemistry (AREA)
- Zoology (AREA)
- Wood Science & Technology (AREA)
- Bioinformatics & Cheminformatics (AREA)
- General Engineering & Computer Science (AREA)
- Biotechnology (AREA)
- Biomedical Technology (AREA)
- Molecular Biology (AREA)
- Biochemistry (AREA)
- General Health & Medical Sciences (AREA)
- Microbiology (AREA)
- Biophysics (AREA)
- Physics & Mathematics (AREA)
- Plant Pathology (AREA)
- Proteomics, Peptides & Aminoacids (AREA)
- Medicinal Chemistry (AREA)
- Analytical Chemistry (AREA)
- Immunology (AREA)
- Enzymes And Modification Thereof (AREA)
- Measuring Or Testing Involving Enzymes Or Micro-Organisms (AREA)
- Medicines That Contain Protein Lipid Enzymes And Other Medicines (AREA)
- Micro-Organisms Or Cultivation Processes Thereof (AREA)
- Peptides Or Proteins (AREA)
Applications Claiming Priority (11)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| US5141097P | 1997-07-01 | 1997-07-01 | |
| US60/051,410 | 1997-07-01 | ||
| US5301897P | 1997-07-21 | 1997-07-21 | |
| US5332997P | 1997-07-21 | 1997-07-21 | |
| US60/053,018 | 1997-07-21 | ||
| US60/053,329 | 1997-07-21 | ||
| US5464297P | 1997-08-04 | 1997-08-04 | |
| US60/054,642 | 1997-08-04 | ||
| US5828797P | 1997-09-09 | 1997-09-09 | |
| US60/058,287 | 1997-09-09 | ||
| PCT/US1998/013835 WO1999001560A1 (en) | 1997-07-01 | 1998-07-01 | Vertebrate telomerase genes and proteins and uses thereof |
Publications (1)
| Publication Number | Publication Date |
|---|---|
| CA2294782A1 true CA2294782A1 (en) | 1999-01-14 |
Family
ID=27535157
Family Applications (1)
| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| CA002294782A Abandoned CA2294782A1 (en) | 1997-07-01 | 1998-07-01 | Vertebrate telomerase genes and proteins and uses thereof |
Country Status (9)
| Country | Link |
|---|---|
| US (3) | US6916642B1 (enExample) |
| EP (1) | EP0917579A1 (enExample) |
| JP (1) | JP2002514928A (enExample) |
| KR (1) | KR100581990B1 (enExample) |
| CN (1) | CN1270634A (enExample) |
| AU (1) | AU748442B2 (enExample) |
| CA (1) | CA2294782A1 (enExample) |
| IL (1) | IL133830A0 (enExample) |
| WO (1) | WO1999001560A1 (enExample) |
Families Citing this family (53)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| US6261836B1 (en) | 1996-10-01 | 2001-07-17 | Geron Corporation | Telomerase |
| US6808880B2 (en) | 1996-10-01 | 2004-10-26 | Geron Corporation | Method for detecting polynucleotides encoding telomerase |
| US6777203B1 (en) | 1997-11-19 | 2004-08-17 | Geron Corporation | Telomerase promoter driving expression of therapeutic gene sequences |
| FI990655A7 (fi) * | 1996-10-01 | 1999-06-01 | Geron Corp | Ihmistelomeraasin katalyyttinen alayksikkö |
| US6610839B1 (en) | 1997-08-14 | 2003-08-26 | Geron Corporation | Promoter for telomerase reverse transcriptase |
| US6475789B1 (en) | 1996-10-01 | 2002-11-05 | University Technology Corporation | Human telomerase catalytic subunit: diagnostic and therapeutic methods |
| US7585622B1 (en) | 1996-10-01 | 2009-09-08 | Geron Corporation | Increasing the proliferative capacity of cells using telomerase reverse transcriptase |
| US6093809A (en) | 1996-10-01 | 2000-07-25 | University Technology Corporation | Telomerase |
| US7622549B2 (en) | 1997-04-18 | 2009-11-24 | Geron Corporation | Human telomerase reverse transcriptase polypeptides |
| CA2294782A1 (en) * | 1997-07-01 | 1999-01-14 | Cambia Biosystems Llc | Vertebrate telomerase genes and proteins and uses thereof |
| US7378244B2 (en) | 1997-10-01 | 2008-05-27 | Geron Corporation | Telomerase promoters sequences for screening telomerase modulators |
| WO1999027113A1 (en) * | 1997-11-26 | 1999-06-03 | Geron Corporation | Mouse telomerase reverse transcriptase |
| EP1045027B1 (en) * | 1998-01-08 | 2006-05-31 | Chugai Seiyaku Kabushiki Kaisha | Novel gene having reverse transcriptase motif |
| CA2347067C (en) | 1998-03-31 | 2013-09-17 | Geron Corporation | Dendritic cell vaccine containing telomerase reverse transcriptase for the treatment of cancer |
| US7402307B2 (en) | 1998-03-31 | 2008-07-22 | Geron Corporation | Method for identifying and killing cancer cells |
| US6337200B1 (en) | 1998-03-31 | 2002-01-08 | Geron Corporation | Human telomerase catalytic subunit variants |
| DE19916929A1 (de) * | 1999-04-15 | 2000-10-19 | Bayer Ag | Ein automatisierbarer Schnelltest zum Nachweis von Krebserkrankungen auf der Basis von Telomerase(hTC) mRNA mit spezifischen Primern und Sonden |
| US6912492B1 (en) | 1999-05-25 | 2005-06-28 | University Of Medicine & Dentistry Of New Jersey | Methods for diagnosing, preventing, and treating developmental disorders due to a combination of genetic and environmental factors |
| US6210950B1 (en) * | 1999-05-25 | 2001-04-03 | University Of Medicine And Dentistry Of New Jersey | Methods for diagnosing, preventing, and treating developmental disorders due to a combination of genetic and environmental factors |
| US6664046B1 (en) | 1999-12-16 | 2003-12-16 | Roche Molecular Systems, Inc. | Quantitation of hTERT mRNA expression |
| KR20010096991A (ko) * | 2000-04-19 | 2001-11-08 | 임정빈 | 텔로머레이즈의 프로모터에 특정하게 결합하는더블유티이1 절편, 그 유전자, 발현벡터 및 그것을 이용한세포성장 억제 방법 |
| AUPQ923400A0 (en) * | 2000-08-07 | 2000-08-31 | Children's Medical Research Institute | Assays for alternative lengthening of telomeres |
| US7078491B1 (en) | 2000-09-21 | 2006-07-18 | Amgen Inc. | Selective binding agents of telomerase |
| GB0031430D0 (en) * | 2000-12-22 | 2001-02-07 | Norsk Hydro As | Polypeptides |
| GB0112342D0 (en) * | 2001-05-21 | 2001-07-11 | Norsk Hydro As | Polypeptides |
| EP1440085B8 (de) * | 2001-10-18 | 2010-08-04 | Medicyte GmbH | Transiente immortalisierung von zellen durch onkogenproteine oder telomerproteine |
| US20060127909A1 (en) * | 2002-12-06 | 2006-06-15 | Bernd Schwenzer | Polynucleotides targeted against hter and use thereof |
| EP1748067A1 (en) * | 2005-07-29 | 2007-01-31 | Institut Pasteur | Polynucleotides encoding MHC class I-restricted hTERT epitopes, analogues thereof or polyepitopes |
| KR101710981B1 (ko) * | 2006-07-28 | 2017-02-28 | 더 트러스티스 오브 더 유니버시티 오브 펜실바니아 | 개선된 백신 및 이의 사용 방법 |
| EP1994942A1 (en) * | 2007-05-25 | 2008-11-26 | INSERM (Institut National de la Santé et de la Recherche Médicale) | Pharmaceutical compositions comprising telomerase, and uses thereof |
| US9657068B2 (en) | 2010-02-16 | 2017-05-23 | Ultimovacs As | Telomerase polypeptide vaccine for treating cancer |
| RU2468030C2 (ru) | 2010-04-09 | 2012-11-27 | Государственное учебно-научное учреждение Химический факультет Московского государственного университета им. М.В. Ломоносова | Ингибиторы теломеразы и способ их получения |
| CN108841802B (zh) | 2012-05-11 | 2023-06-09 | 珍白斯凯尔有限公司 | 抗炎性肽及包含其的组合物 |
| KR101873773B1 (ko) | 2012-05-11 | 2018-08-02 | 주식회사 젬백스앤카엘 | 류마티즘 관절염 예방 또는 치료 조성물 |
| JP6272853B2 (ja) | 2012-07-11 | 2018-01-31 | ジェムバックス アンド カエル カンパニー，リミティド | 細胞透過性ペプチド、それを含んだコンジュゲート、及びそれを含んだ組成物 |
| US20150125438A1 (en) * | 2012-07-20 | 2015-05-07 | Sang Jae Kim | Anti-Inflammatory Peptides and Composition Comprising the Same |
| JP6517692B2 (ja) * | 2012-09-19 | 2019-05-22 | ジェムバックス アンド カエル カンパニー，リミティド | 細胞透過性ペプチド、それを含んだコンジュゲート、及びそれを含んだ組成物 |
| EP2970990B1 (en) * | 2013-03-15 | 2018-07-18 | Monsanto Technology LLC | Compositions and methods for the production and delivery of rna |
| WO2014171792A1 (ko) * | 2013-04-19 | 2014-10-23 | 주식회사 카엘젬백스 | 허혈성 손상 치료 및 예방용 조성물 |
| EP4063863A1 (en) | 2013-06-07 | 2022-09-28 | Gemvax & Kael Co., Ltd. | Gv1001, gemcitabine and capecitabine for use in the treatment of pancreatic cancer in high eotaxin baseline level patients |
| CN105324123B (zh) | 2013-06-21 | 2022-02-08 | 珍白斯凯尔有限公司 | 激素分泌调节剂、包含该调节剂的组合物、和利用其控制激素分泌的方法 |
| US9757473B2 (en) * | 2013-07-12 | 2017-09-12 | Gemvax & Kael Co., Ltd. | Cell-penetrating peptide and conjugate comprising same |
| CN110755599A (zh) | 2013-10-23 | 2020-02-07 | 珍白斯凯尔有限公司 | 用于治疗和预防良性前列腺增生的组合物 |
| EP3072519B1 (en) | 2013-11-22 | 2020-08-19 | Gemvax & Kael Co., Ltd. | Peptide having angiogenesis inhibitory activity and composition containing same |
| US11058744B2 (en) | 2013-12-17 | 2021-07-13 | Gemvax & Kael Co., Ltd. | Composition for treating prostate cancer |
| ES2908096T3 (es) | 2014-04-11 | 2022-04-27 | Gemvax & Kael Co Ltd | Péptido con actividad inhibidora de la fibrosis y composición que lo contiene |
| WO2015167067A1 (ko) | 2014-04-30 | 2015-11-05 | 주식회사 카엘젬백스 | 장기, 조직 또는 세포 이식용 조성물, 키트 및 이식 방법 |
| KR102413243B1 (ko) | 2014-12-23 | 2022-06-27 | 주식회사 젬백스앤카엘 | 안질환 치료 펩티드 및 이를 포함하는 안질환 치료용 조성물 |
| CN107405380B (zh) | 2015-02-27 | 2021-04-20 | 珍白斯凯尔有限公司 | 用于预防听觉损伤的肽及其包含该肽的组合物 |
| JP6923453B2 (ja) | 2015-07-02 | 2021-08-18 | ジェムバックス アンド カエル カンパニー，リミティド | 抗ウイルス活性効能を有するペプチド及びこれを含む組成物 |
| WO2017070237A1 (en) * | 2015-10-19 | 2017-04-27 | University Of Maryland, Baltimore | Methods for generating engineered human primary blood dendritic cell lines |
| WO2017176087A1 (ko) | 2016-04-07 | 2017-10-12 | 주식회사 젬백스앤카엘 | 텔로머라제 활성 증가 및 텔로미어 연장 효능을 가지는 펩티드 및 이를 포함하는 조성물 |
| CN110117644A (zh) * | 2019-04-18 | 2019-08-13 | 王金固 | 一种用于生物样本中rna的基因检测方法 |
Family Cites Families (15)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| US5639613A (en) | 1992-05-13 | 1997-06-17 | Board Of Regents, University Of Texas System | Methods for cancer diagnosis and prognosis |
| US5489508A (en) | 1992-05-13 | 1996-02-06 | University Of Texas System Board Of Regents | Therapy and diagnosis of conditions related to telomere length and/or telomerase activity |
| US5645986A (en) | 1992-05-13 | 1997-07-08 | Board Of Reagents, The University Of Texas System | Therapy and diagnosis of conditions related to telomere length and/or telomerase activity |
| WO1995013382A1 (en) * | 1993-11-12 | 1995-05-18 | Geron Corporation | Therapy and diagnosis of conditions related to telomere length and/or telomerase activity |
| US5972605A (en) | 1994-07-07 | 1999-10-26 | Geron Corporation | Assays for regulators of mammalian telomerase expression |
| ATE308554T1 (de) * | 1994-07-07 | 2005-11-15 | Geron Corp | Säugetier-telomerase |
| WO1996019580A2 (en) * | 1994-12-19 | 1996-06-27 | Cold Spring Harbor Laboratory | Telomerase protein component |
| US5770422A (en) | 1996-07-08 | 1998-06-23 | The Regents Of The University Of California | Human telomerase |
| US6261836B1 (en) | 1996-10-01 | 2001-07-17 | Geron Corporation | Telomerase |
| US6093809A (en) * | 1996-10-01 | 2000-07-25 | University Technology Corporation | Telomerase |
| FI990655A7 (fi) * | 1996-10-01 | 1999-06-01 | Geron Corp | Ihmistelomeraasin katalyyttinen alayksikkö |
| US5919656A (en) | 1996-11-15 | 1999-07-06 | Amgen Canada Inc. | Genes encoding telomerase protein 1 |
| US7390891B1 (en) * | 1996-11-15 | 2008-06-24 | Amgen Inc. | Polynucleotides encoding a telomerase component TP2 |
| WO1998037181A2 (en) * | 1997-02-20 | 1998-08-27 | Whitehead Institute For Biomedical Research | Telomerase catalytic subunit gene and encoded protein |
| CA2294782A1 (en) * | 1997-07-01 | 1999-01-14 | Cambia Biosystems Llc | Vertebrate telomerase genes and proteins and uses thereof |
-
1998
- 1998-07-01 CA CA002294782A patent/CA2294782A1/en not_active Abandoned
- 1998-07-01 IL IL13383098A patent/IL133830A0/xx unknown
- 1998-07-01 AU AU82854/98A patent/AU748442B2/en not_active Ceased
- 1998-07-01 WO PCT/US1998/013835 patent/WO1999001560A1/en not_active Ceased
- 1998-07-01 EP EP98933117A patent/EP0917579A1/en not_active Withdrawn
- 1998-07-01 KR KR1019997012595A patent/KR100581990B1/ko not_active Expired - Fee Related
- 1998-07-01 CN CN98808383A patent/CN1270634A/zh active Pending
- 1998-07-01 JP JP50877199A patent/JP2002514928A/ja not_active Ceased
-
2000
- 2000-02-11 US US09/502,424 patent/US6916642B1/en not_active Expired - Fee Related
- 2000-02-11 US US09/502,498 patent/US6846662B1/en not_active Expired - Fee Related
-
2004
- 2004-07-27 US US10/900,231 patent/US20050176022A1/en not_active Abandoned
Also Published As
| Publication number | Publication date |
|---|---|
| US20050176022A1 (en) | 2005-08-11 |
| KR100581990B1 (ko) | 2006-05-23 |
| AU748442B2 (en) | 2002-06-06 |
| WO1999001560A1 (en) | 1999-01-14 |
| EP0917579A1 (en) | 1999-05-26 |
| JP2002514928A (ja) | 2002-05-21 |
| IL133830A0 (en) | 2001-04-30 |
| AU8285498A (en) | 1999-01-25 |
| CN1270634A (zh) | 2000-10-18 |
| US6916642B1 (en) | 2005-07-12 |
| KR20010020601A (ko) | 2001-03-15 |
| US6846662B1 (en) | 2005-01-25 |
Similar Documents
| Publication | Publication Date | Title |
|---|---|---|
| AU748442B2 (en) | Vertebrate telomerase genes and proteins and uses thereof | |
| US6043083A (en) | Inhibitors of the JNK signal transduction pathway and methods of use | |
| Kermouni et al. | The IL-9 receptor gene (IL9R): genomic structure, chromosomal localization in the pseudoautosomal region of the long arm of the sex chromosomes, and identification of IL9R pseudogenes at 9qter, 10pter, 16pter, and 18pter | |
| Laverty et al. | Murine CASK is disrupted in a sex-linked cleft palate mouse mutant | |
| KR20000048820A (ko) | 텔로머라제 역전사 효소 | |
| JP2002272489A (ja) | 哺乳動物のテロメラーゼ | |
| AU745420B2 (en) | Human catalytic telomerase sub-unit and its diagnostic and therapeutic use | |
| US6300110B1 (en) | Peptides related to TPC2 and TPC3, two proteins that are coexpressed with telomerase activity | |
| US6277979B1 (en) | KIAA0551 polynucleotides and polypeptides use | |
| US6297356B1 (en) | Telomere repeat binding factors and diagnostic and therapeutic use thereof | |
| US20040142357A1 (en) | Novel telomerase inhibitors and uses therefor | |
| Shirsat et al. | Structure of the murine lactotransferrin gene is similar to the structure of other transferrin-encoding genes and shares a putative regulatory region with the murine myeloperoxidase gene | |
| US6599728B2 (en) | Second mammalian tankyrase | |
| Lee et al. | Molecular analysis of the cDNA and genomic DNA encoding mouse RNA helicase A | |
| EP1571215A2 (en) | Vertebrate telomerase genes and proteins and uses thereof | |
| US6379887B1 (en) | Gene for inhibiting melanin biosynthesis | |
| US6815532B2 (en) | ATR-2 cell cycle checkpoint | |
| MXPA00000196A (en) | Vertebrate telomerase genes and proteins and uses thereof | |
| EP1364025B1 (en) | A novel gene bno1 mapping to chromosome 16q24.3 | |
| JP2001500379A (ja) | テロメア長およびテロメア活性を調節するための方法および試薬 | |
| HK1032074A (en) | Vertebrate telomerase genes and proteins and uses thereof | |
| EP0972011A1 (en) | Cyclin-dependent protein kinase | |
| CA2261297A1 (en) | A novel maturation-inhibited protein kinase | |
| Moncrieff | Cloning and characterisation of a novel DMPK-related gene: CDC42BPB | |
| US20040086857A1 (en) | Proliferative glomerular nephritis-associated gene |
Legal Events
| Date | Code | Title | Description |
|---|---|---|---|
| EEER | Examination request | ||
| FZDE | Discontinued |