TW200911832A - Polypeptides, antibody variable domains & antagonists - Google Patents
Polypeptides, antibody variable domains & antagonists Download PDFInfo
- Publication number
- TW200911832A TW200911832A TW097121295A TW97121295A TW200911832A TW 200911832 A TW200911832 A TW 200911832A TW 097121295 A TW097121295 A TW 097121295A TW 97121295 A TW97121295 A TW 97121295A TW 200911832 A TW200911832 A TW 200911832A
- Authority
- TW
- Taiwan
- Prior art keywords
- dom15
- acid sequence
- amino acid
- variable region
- sequence
- Prior art date
Links
- 108090000765 processed proteins & peptides Proteins 0.000 title claims abstract description 572
- 102000004196 processed proteins & peptides Human genes 0.000 title claims abstract description 416
- 229920001184 polypeptide Polymers 0.000 title claims abstract description 347
- 239000005557 antagonist Substances 0.000 title claims abstract description 191
- 239000004365 Protease Substances 0.000 claims abstract description 300
- 108091005804 Peptidases Proteins 0.000 claims abstract description 295
- 206010028980 Neoplasm Diseases 0.000 claims abstract description 37
- 210000004072 lung Anatomy 0.000 claims abstract description 36
- 238000012384 transportation and delivery Methods 0.000 claims abstract description 22
- 201000011510 cancer Diseases 0.000 claims abstract description 20
- 230000002685 pulmonary effect Effects 0.000 claims abstract description 14
- 208000027866 inflammatory disease Diseases 0.000 claims abstract description 8
- 102000035195 Peptidases Human genes 0.000 claims description 294
- 125000003275 alpha amino acid group Chemical group 0.000 claims description 206
- 239000003446 ligand Substances 0.000 claims description 158
- 102000005789 Vascular Endothelial Growth Factors Human genes 0.000 claims description 155
- 108010019530 Vascular Endothelial Growth Factors Proteins 0.000 claims description 155
- 238000000034 method Methods 0.000 claims description 147
- 230000027455 binding Effects 0.000 claims description 133
- 150000007523 nucleic acids Chemical group 0.000 claims description 116
- 108090000623 proteins and genes Proteins 0.000 claims description 106
- 108060003951 Immunoglobulin Proteins 0.000 claims description 101
- 102000018358 immunoglobulin Human genes 0.000 claims description 101
- 102000004169 proteins and genes Human genes 0.000 claims description 89
- 108020004707 nucleic acids Proteins 0.000 claims description 76
- 102000039446 nucleic acids Human genes 0.000 claims description 76
- 102100035360 Cerebellar degeneration-related antigen 1 Human genes 0.000 claims description 64
- 210000004027 cell Anatomy 0.000 claims description 60
- 108090000631 Trypsin Proteins 0.000 claims description 55
- 102000004142 Trypsin Human genes 0.000 claims description 55
- 239000000203 mixture Substances 0.000 claims description 55
- 239000012588 trypsin Substances 0.000 claims description 54
- ZACLXWTWERGCLX-MDUHGFIHSA-N dom-1 Chemical compound O([C@@H]1C=C(C([C@@H](O)[C@@]11CO)=O)C)[C@@H]2[C@H](O)C[C@@]1(C)C2=C ZACLXWTWERGCLX-MDUHGFIHSA-N 0.000 claims description 51
- 101100279566 Arabidopsis thaliana EMB514 gene Proteins 0.000 claims description 43
- 101100268514 Mus musculus Serpina1a gene Proteins 0.000 claims description 43
- 201000010099 disease Diseases 0.000 claims description 41
- 208000037265 diseases, disorders, signs and symptoms Diseases 0.000 claims description 41
- 102100035361 Cerebellar degeneration-related protein 2 Human genes 0.000 claims description 40
- 101000737793 Homo sapiens Cerebellar degeneration-related antigen 1 Proteins 0.000 claims description 40
- 101000737796 Homo sapiens Cerebellar degeneration-related protein 2 Proteins 0.000 claims description 40
- 101100112922 Candida albicans CDR3 gene Proteins 0.000 claims description 39
- 241000282414 Homo sapiens Species 0.000 claims description 37
- 108091028043 Nucleic acid sequence Proteins 0.000 claims description 36
- 102000016387 Pancreatic elastase Human genes 0.000 claims description 34
- 108010067372 Pancreatic elastase Proteins 0.000 claims description 34
- -1 leucozyme Proteins 0.000 claims description 33
- 239000013598 vector Substances 0.000 claims description 32
- 239000003814 drug Substances 0.000 claims description 30
- 239000002773 nucleotide Substances 0.000 claims description 24
- 125000003729 nucleotide group Chemical group 0.000 claims description 24
- 210000003802 sputum Anatomy 0.000 claims description 23
- 238000011282 treatment Methods 0.000 claims description 23
- 206010036790 Productive cough Diseases 0.000 claims description 22
- 208000024794 sputum Diseases 0.000 claims description 22
- 238000009472 formulation Methods 0.000 claims description 21
- 108090000317 Chymotrypsin Proteins 0.000 claims description 20
- 101000808011 Homo sapiens Vascular endothelial growth factor A Proteins 0.000 claims description 19
- 229960002376 chymotrypsin Drugs 0.000 claims description 19
- 102000058223 human VEGFA Human genes 0.000 claims description 19
- 239000002253 acid Substances 0.000 claims description 17
- 150000001413 amino acids Chemical class 0.000 claims description 16
- 238000004519 manufacturing process Methods 0.000 claims description 16
- 239000000178 monomer Substances 0.000 claims description 16
- 230000002265 prevention Effects 0.000 claims description 14
- 108010028275 Leukocyte Elastase Proteins 0.000 claims description 11
- 206010064930 age-related macular degeneration Diseases 0.000 claims description 11
- 101100372758 Danio rerio vegfaa gene Proteins 0.000 claims description 10
- 206010035664 Pneumonia Diseases 0.000 claims description 10
- 101150030763 Vegfa gene Proteins 0.000 claims description 10
- 238000003556 assay Methods 0.000 claims description 10
- 108020001507 fusion proteins Proteins 0.000 claims description 10
- 102000037865 fusion proteins Human genes 0.000 claims description 10
- 208000002780 macular degeneration Diseases 0.000 claims description 10
- 238000002965 ELISA Methods 0.000 claims description 9
- 102000016799 Leukocyte elastase Human genes 0.000 claims description 9
- 208000006545 Chronic Obstructive Pulmonary Disease Diseases 0.000 claims description 8
- 206010058467 Lung neoplasm malignant Diseases 0.000 claims description 8
- 201000005202 lung cancer Diseases 0.000 claims description 8
- 208000020816 lung neoplasm Diseases 0.000 claims description 8
- 230000001404 mediated effect Effects 0.000 claims description 8
- 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 claims description 7
- 208000023275 Autoimmune disease Diseases 0.000 claims description 7
- 239000007788 liquid Substances 0.000 claims description 7
- 108010026228 mRNA guanylyltransferase Proteins 0.000 claims description 7
- 206010009944 Colon cancer Diseases 0.000 claims description 6
- 206010061902 Pancreatic neoplasm Diseases 0.000 claims description 6
- 150000001412 amines Chemical class 0.000 claims description 6
- 201000010536 head and neck cancer Diseases 0.000 claims description 6
- 208000014829 head and neck neoplasm Diseases 0.000 claims description 6
- 238000011534 incubation Methods 0.000 claims description 6
- 208000015486 malignant pancreatic neoplasm Diseases 0.000 claims description 6
- 201000002528 pancreatic cancer Diseases 0.000 claims description 6
- 208000008443 pancreatic carcinoma Diseases 0.000 claims description 6
- 239000006187 pill Substances 0.000 claims description 6
- 206010006187 Breast cancer Diseases 0.000 claims description 5
- 208000026310 Breast neoplasm Diseases 0.000 claims description 5
- 208000001333 Colorectal Neoplasms Diseases 0.000 claims description 5
- 206010061218 Inflammation Diseases 0.000 claims description 5
- 206010033128 Ovarian cancer Diseases 0.000 claims description 5
- 206010061535 Ovarian neoplasm Diseases 0.000 claims description 5
- 206010006451 bronchitis Diseases 0.000 claims description 5
- 230000004054 inflammatory process Effects 0.000 claims description 5
- 230000003115 biocidal effect Effects 0.000 claims description 4
- 230000008859 change Effects 0.000 claims description 4
- 239000008194 pharmaceutical composition Substances 0.000 claims description 4
- 206010006458 Bronchitis chronic Diseases 0.000 claims description 3
- 206010014561 Emphysema Diseases 0.000 claims description 3
- 208000022559 Inflammatory bowel disease Diseases 0.000 claims description 3
- ROHFNLRQFUQHCH-UHFFFAOYSA-N Leucine Natural products CC(C)CC(N)C(O)=O ROHFNLRQFUQHCH-UHFFFAOYSA-N 0.000 claims description 3
- 208000009956 adenocarcinoma Diseases 0.000 claims description 3
- 239000002775 capsule Substances 0.000 claims description 3
- 208000007451 chronic bronchitis Diseases 0.000 claims description 3
- 239000003085 diluting agent Substances 0.000 claims description 3
- 238000001502 gel electrophoresis Methods 0.000 claims description 3
- 125000001909 leucine group Chemical group [H]N(*)C(C(*)=O)C([H])([H])C(C([H])([H])[H])C([H])([H])[H] 0.000 claims description 3
- 239000000463 material Substances 0.000 claims description 3
- 210000002784 stomach Anatomy 0.000 claims description 3
- 108090000626 DNA-directed RNA polymerases Proteins 0.000 claims description 2
- 102000004163 DNA-directed RNA polymerases Human genes 0.000 claims description 2
- 230000005540 biological transmission Effects 0.000 claims description 2
- 238000012258 culturing Methods 0.000 claims description 2
- 239000003937 drug carrier Substances 0.000 claims description 2
- 239000000710 homodimer Substances 0.000 claims description 2
- 229940099472 immunoglobulin a Drugs 0.000 claims description 2
- 239000000546 pharmaceutical excipient Substances 0.000 claims description 2
- 201000001178 Bacterial Pneumonia Diseases 0.000 claims 4
- 125000003277 amino group Chemical group 0.000 claims 4
- 230000001684 chronic effect Effects 0.000 claims 3
- 208000011231 Crohn disease Diseases 0.000 claims 2
- 206010060862 Prostate cancer Diseases 0.000 claims 2
- 208000000236 Prostatic Neoplasms Diseases 0.000 claims 2
- 206010009900 Colitis ulcerative Diseases 0.000 claims 1
- 241000282324 Felis Species 0.000 claims 1
- 208000005577 Gastroenteritis Diseases 0.000 claims 1
- 206010035734 Pneumonia staphylococcal Diseases 0.000 claims 1
- 208000015634 Rectal Neoplasms Diseases 0.000 claims 1
- 208000025865 Ulcer Diseases 0.000 claims 1
- 201000006704 Ulcerative Colitis Diseases 0.000 claims 1
- KZSNJWFQEVHDMF-UHFFFAOYSA-N Valine Natural products CC(C)C(N)C(O)=O KZSNJWFQEVHDMF-UHFFFAOYSA-N 0.000 claims 1
- 230000000735 allogeneic effect Effects 0.000 claims 1
- 208000029742 colonic neoplasm Diseases 0.000 claims 1
- 230000009137 competitive binding Effects 0.000 claims 1
- 239000007937 lozenge Substances 0.000 claims 1
- 230000003472 neutralizing effect Effects 0.000 claims 1
- 230000000414 obstructive effect Effects 0.000 claims 1
- 206010038038 rectal cancer Diseases 0.000 claims 1
- 201000001275 rectum cancer Diseases 0.000 claims 1
- 208000004048 staphylococcal pneumonia Diseases 0.000 claims 1
- 239000006188 syrup Substances 0.000 claims 1
- 235000020357 syrup Nutrition 0.000 claims 1
- 239000004474 valine Substances 0.000 claims 1
- 125000002987 valine group Chemical group [H]N([H])C([H])(C(*)=O)C([H])(C([H])([H])[H])C([H])([H])[H] 0.000 claims 1
- 230000015556 catabolic process Effects 0.000 abstract description 27
- 238000006731 degradation reaction Methods 0.000 abstract description 27
- 210000001035 gastrointestinal tract Anatomy 0.000 abstract description 8
- 206010003246 arthritis Diseases 0.000 abstract description 3
- 102100037486 Reverse transcriptase/ribonuclease H Human genes 0.000 abstract 1
- 235000019419 proteases Nutrition 0.000 description 238
- 108010073929 Vascular Endothelial Growth Factor A Proteins 0.000 description 141
- 235000018102 proteins Nutrition 0.000 description 85
- 229940088598 enzyme Drugs 0.000 description 77
- 102000004190 Enzymes Human genes 0.000 description 76
- 108090000790 Enzymes Proteins 0.000 description 76
- 229960001322 trypsin Drugs 0.000 description 46
- 239000000427 antigen Substances 0.000 description 34
- 108091007433 antigens Proteins 0.000 description 34
- 102000036639 antigens Human genes 0.000 description 34
- 210000000265 leukocyte Anatomy 0.000 description 33
- 210000001519 tissue Anatomy 0.000 description 29
- 230000000694 effects Effects 0.000 description 27
- 235000001014 amino acid Nutrition 0.000 description 26
- 230000004071 biological effect Effects 0.000 description 26
- 239000003795 chemical substances by application Substances 0.000 description 24
- 235000013601 eggs Nutrition 0.000 description 23
- 239000012634 fragment Substances 0.000 description 23
- 238000002823 phage display Methods 0.000 description 21
- 206010057190 Respiratory tract infections Diseases 0.000 description 20
- 230000000875 corresponding effect Effects 0.000 description 20
- 239000000243 solution Substances 0.000 description 19
- 210000001508 eye Anatomy 0.000 description 16
- 241000894006 Bacteria Species 0.000 description 15
- 240000004808 Saccharomyces cerevisiae Species 0.000 description 15
- 230000006870 function Effects 0.000 description 15
- 235000014680 Saccharomyces cerevisiae Nutrition 0.000 description 14
- 239000013604 expression vector Substances 0.000 description 14
- 239000000284 extract Substances 0.000 description 14
- 229940024606 amino acid Drugs 0.000 description 13
- 239000000137 peptide hydrolase inhibitor Substances 0.000 description 13
- 210000002706 plastid Anatomy 0.000 description 13
- 238000009877 rendering Methods 0.000 description 13
- 238000001727 in vivo Methods 0.000 description 12
- 210000003097 mucus Anatomy 0.000 description 12
- 238000003752 polymerase chain reaction Methods 0.000 description 12
- 210000003979 eosinophil Anatomy 0.000 description 11
- 102000005962 receptors Human genes 0.000 description 11
- 108020003175 receptors Proteins 0.000 description 11
- 102000005600 Cathepsins Human genes 0.000 description 10
- 108010084457 Cathepsins Proteins 0.000 description 10
- 108020004705 Codon Proteins 0.000 description 10
- 241000588724 Escherichia coli Species 0.000 description 10
- 230000001580 bacterial effect Effects 0.000 description 10
- 230000001965 increasing effect Effects 0.000 description 10
- 239000000126 substance Substances 0.000 description 10
- 102000011727 Caspases Human genes 0.000 description 9
- 108010076667 Caspases Proteins 0.000 description 9
- 241000124008 Mammalia Species 0.000 description 9
- 241001465754 Metazoa Species 0.000 description 9
- 238000004091 panning Methods 0.000 description 9
- 230000002797 proteolythic effect Effects 0.000 description 9
- 230000010076 replication Effects 0.000 description 9
- 210000002966 serum Anatomy 0.000 description 9
- 208000024891 symptom Diseases 0.000 description 9
- 102000009027 Albumins Human genes 0.000 description 8
- 108010088751 Albumins Proteins 0.000 description 8
- 102100023701 C-C motif chemokine 18 Human genes 0.000 description 8
- 108010067060 Immunoglobulin Variable Region Proteins 0.000 description 8
- 102000002274 Matrix Metalloproteinases Human genes 0.000 description 8
- 108010000684 Matrix Metalloproteinases Proteins 0.000 description 8
- 108060008682 Tumor Necrosis Factor Proteins 0.000 description 8
- 230000009870 specific binding Effects 0.000 description 8
- 230000001225 therapeutic effect Effects 0.000 description 8
- 108020004414 DNA Proteins 0.000 description 7
- 102000017727 Immunoglobulin Variable Region Human genes 0.000 description 7
- 241000235058 Komagataella pastoris Species 0.000 description 7
- 230000010261 cell growth Effects 0.000 description 7
- 238000010494 dissociation reaction Methods 0.000 description 7
- 230000005593 dissociations Effects 0.000 description 7
- 229940079593 drug Drugs 0.000 description 7
- 239000003112 inhibitor Substances 0.000 description 7
- 238000010187 selection method Methods 0.000 description 7
- 238000012360 testing method Methods 0.000 description 7
- 102100021943 C-C motif chemokine 2 Human genes 0.000 description 6
- 102000008394 Immunoglobulin Fragments Human genes 0.000 description 6
- 108010021625 Immunoglobulin Fragments Proteins 0.000 description 6
- 241000235648 Pichia Species 0.000 description 6
- 102000007562 Serum Albumin Human genes 0.000 description 6
- 108010071390 Serum Albumin Proteins 0.000 description 6
- 102100021669 Stromal cell-derived factor 1 Human genes 0.000 description 6
- 102000000852 Tumor Necrosis Factor-alpha Human genes 0.000 description 6
- 230000003321 amplification Effects 0.000 description 6
- 239000003124 biologic agent Substances 0.000 description 6
- 230000000295 complement effect Effects 0.000 description 6
- 239000000839 emulsion Substances 0.000 description 6
- 239000012530 fluid Substances 0.000 description 6
- 239000003550 marker Substances 0.000 description 6
- 239000011159 matrix material Substances 0.000 description 6
- 230000035772 mutation Effects 0.000 description 6
- 238000003199 nucleic acid amplification method Methods 0.000 description 6
- 229940055729 papain Drugs 0.000 description 6
- 238000002360 preparation method Methods 0.000 description 6
- 230000017854 proteolysis Effects 0.000 description 6
- RXWNCPJZOCPEPQ-NVWDDTSBSA-N puromycin Chemical compound C1=CC(OC)=CC=C1C[C@H](N)C(=O)N[C@H]1[C@@H](O)[C@H](N2C3=NC=NC(=C3N=C2)N(C)C)O[C@@H]1CO RXWNCPJZOCPEPQ-NVWDDTSBSA-N 0.000 description 6
- 239000000523 sample Substances 0.000 description 6
- 231100000617 superantigen Toxicity 0.000 description 6
- 244000099147 Ananas comosus Species 0.000 description 5
- 235000007119 Ananas comosus Nutrition 0.000 description 5
- 241000193830 Bacillus <bacterium> Species 0.000 description 5
- 108090000746 Chymosin Proteins 0.000 description 5
- 102100031107 Disintegrin and metalloproteinase domain-containing protein 11 Human genes 0.000 description 5
- 101710121366 Disintegrin and metalloproteinase domain-containing protein 11 Proteins 0.000 description 5
- 208000019693 Lung disease Diseases 0.000 description 5
- 101000686985 Mouse mammary tumor virus (strain C3H) Protein PR73 Proteins 0.000 description 5
- 108010025020 Nerve Growth Factor Proteins 0.000 description 5
- 108090000526 Papain Proteins 0.000 description 5
- 102100033237 Pro-epidermal growth factor Human genes 0.000 description 5
- 101710098940 Pro-epidermal growth factor Proteins 0.000 description 5
- 102000004338 Transferrin Human genes 0.000 description 5
- 108090000901 Transferrin Proteins 0.000 description 5
- 108010033576 Transferrin Receptors Proteins 0.000 description 5
- 108060008683 Tumor Necrosis Factor Receptor Proteins 0.000 description 5
- 108091008605 VEGF receptors Proteins 0.000 description 5
- 102000009484 Vascular Endothelial Growth Factor Receptors Human genes 0.000 description 5
- 241000700605 Viruses Species 0.000 description 5
- 230000002776 aggregation Effects 0.000 description 5
- 238000004220 aggregation Methods 0.000 description 5
- 238000013103 analytical ultracentrifugation Methods 0.000 description 5
- 208000006673 asthma Diseases 0.000 description 5
- 239000011324 bead Substances 0.000 description 5
- 239000000872 buffer Substances 0.000 description 5
- 230000003399 chemotactic effect Effects 0.000 description 5
- 239000005482 chemotactic factor Substances 0.000 description 5
- 229940080701 chymosin Drugs 0.000 description 5
- 230000006698 induction Effects 0.000 description 5
- 230000002401 inhibitory effect Effects 0.000 description 5
- 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 5
- 210000004962 mammalian cell Anatomy 0.000 description 5
- 239000002609 medium Substances 0.000 description 5
- GNOLWGAJQVLBSM-UHFFFAOYSA-N n,n,5,7-tetramethyl-1,2,3,4-tetrahydronaphthalen-1-amine Chemical compound C1=C(C)C=C2C(N(C)C)CCCC2=C1C GNOLWGAJQVLBSM-UHFFFAOYSA-N 0.000 description 5
- 235000019834 papain Nutrition 0.000 description 5
- 239000000047 product Substances 0.000 description 5
- 241000894007 species Species 0.000 description 5
- 239000012581 transferrin Substances 0.000 description 5
- 102000003298 tumor necrosis factor receptor Human genes 0.000 description 5
- LKDMKWNDBAVNQZ-UHFFFAOYSA-N 4-[[1-[[1-[2-[[1-(4-nitroanilino)-1-oxo-3-phenylpropan-2-yl]carbamoyl]pyrrolidin-1-yl]-1-oxopropan-2-yl]amino]-1-oxopropan-2-yl]amino]-4-oxobutanoic acid Chemical compound OC(=O)CCC(=O)NC(C)C(=O)NC(C)C(=O)N1CCCC1C(=O)NC(C(=O)NC=1C=CC(=CC=1)[N+]([O-])=O)CC1=CC=CC=C1 LKDMKWNDBAVNQZ-UHFFFAOYSA-N 0.000 description 4
- 102100023995 Beta-nerve growth factor Human genes 0.000 description 4
- 102100023698 C-C motif chemokine 17 Human genes 0.000 description 4
- 102100032367 C-C motif chemokine 5 Human genes 0.000 description 4
- 108010029697 CD40 Ligand Proteins 0.000 description 4
- 101150013553 CD40 gene Proteins 0.000 description 4
- 102100032937 CD40 ligand Human genes 0.000 description 4
- 102000004066 Caspase-12 Human genes 0.000 description 4
- 108090000570 Caspase-12 Proteins 0.000 description 4
- 108090000617 Cathepsin G Proteins 0.000 description 4
- 102100025975 Cathepsin G Human genes 0.000 description 4
- 108010055166 Chemokine CCL5 Proteins 0.000 description 4
- 102000008186 Collagen Human genes 0.000 description 4
- 108010035532 Collagen Proteins 0.000 description 4
- 102000005927 Cysteine Proteases Human genes 0.000 description 4
- 108010005843 Cysteine Proteases Proteins 0.000 description 4
- 102000016942 Elastin Human genes 0.000 description 4
- 108010014258 Elastin Proteins 0.000 description 4
- 102000004864 Fibroblast growth factor 10 Human genes 0.000 description 4
- 108090001047 Fibroblast growth factor 10 Proteins 0.000 description 4
- 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 4
- 108010017213 Granulocyte-Macrophage Colony-Stimulating Factor Proteins 0.000 description 4
- 102100039620 Granulocyte-macrophage colony-stimulating factor Human genes 0.000 description 4
- 102100034221 Growth-regulated alpha protein Human genes 0.000 description 4
- ZRALSGWEFCBTJO-UHFFFAOYSA-N Guanidine Chemical compound NC(N)=N ZRALSGWEFCBTJO-UHFFFAOYSA-N 0.000 description 4
- 101000600756 Homo sapiens 3-phosphoinositide-dependent protein kinase 1 Proteins 0.000 description 4
- 101000978362 Homo sapiens C-C motif chemokine 17 Proteins 0.000 description 4
- 101000978371 Homo sapiens C-C motif chemokine 18 Proteins 0.000 description 4
- 101000897480 Homo sapiens C-C motif chemokine 2 Proteins 0.000 description 4
- 101000914324 Homo sapiens Carcinoembryonic antigen-related cell adhesion molecule 5 Proteins 0.000 description 4
- 101000914321 Homo sapiens Carcinoembryonic antigen-related cell adhesion molecule 7 Proteins 0.000 description 4
- 101000577881 Homo sapiens Macrophage metalloelastase Proteins 0.000 description 4
- 101000581981 Homo sapiens Neural cell adhesion molecule 1 Proteins 0.000 description 4
- 101000617725 Homo sapiens Pregnancy-specific beta-1-glycoprotein 2 Proteins 0.000 description 4
- 101000874179 Homo sapiens Syndecan-1 Proteins 0.000 description 4
- 101001117146 Homo sapiens [Pyruvate dehydrogenase (acetyl-transferring)] kinase isozyme 1, mitochondrial Proteins 0.000 description 4
- 102000019223 Interleukin-1 receptor Human genes 0.000 description 4
- 108050006617 Interleukin-1 receptor Proteins 0.000 description 4
- 102000003812 Interleukin-15 Human genes 0.000 description 4
- 108090000172 Interleukin-15 Proteins 0.000 description 4
- 108050003558 Interleukin-17 Proteins 0.000 description 4
- 102000013691 Interleukin-17 Human genes 0.000 description 4
- 102000003810 Interleukin-18 Human genes 0.000 description 4
- 108090000171 Interleukin-18 Proteins 0.000 description 4
- 108010001831 LDL receptors Proteins 0.000 description 4
- 102100024640 Low-density lipoprotein receptor Human genes 0.000 description 4
- 102100027998 Macrophage metalloelastase Human genes 0.000 description 4
- 102100027347 Neural cell adhesion molecule 1 Human genes 0.000 description 4
- 102100022019 Pregnancy-specific beta-1-glycoprotein 2 Human genes 0.000 description 4
- 229940124158 Protease/peptidase inhibitor Drugs 0.000 description 4
- 102000012479 Serine Proteases Human genes 0.000 description 4
- 108010022999 Serine Proteases Proteins 0.000 description 4
- 101710088580 Stromal cell-derived factor 1 Proteins 0.000 description 4
- 102100035721 Syndecan-1 Human genes 0.000 description 4
- 101710097834 Thiol protease Proteins 0.000 description 4
- 108090000190 Thrombin Proteins 0.000 description 4
- 102100026144 Transferrin receptor protein 1 Human genes 0.000 description 4
- 102100040245 Tumor necrosis factor receptor superfamily member 5 Human genes 0.000 description 4
- 102100024148 [Pyruvate dehydrogenase (acetyl-transferring)] kinase isozyme 1, mitochondrial Human genes 0.000 description 4
- 230000008901 benefit Effects 0.000 description 4
- 229920001436 collagen Polymers 0.000 description 4
- 229920002549 elastin Polymers 0.000 description 4
- 239000003889 eye drop Substances 0.000 description 4
- 230000004927 fusion Effects 0.000 description 4
- 239000000499 gel Substances 0.000 description 4
- 210000004602 germ cell Anatomy 0.000 description 4
- 239000011521 glass Substances 0.000 description 4
- 239000003102 growth factor Substances 0.000 description 4
- 229940072221 immunoglobulins Drugs 0.000 description 4
- 239000000893 inhibin Substances 0.000 description 4
- 230000005764 inhibitory process Effects 0.000 description 4
- NOESYZHRGYRDHS-UHFFFAOYSA-N insulin Chemical compound N1C(=O)C(NC(=O)C(CCC(N)=O)NC(=O)C(CCC(O)=O)NC(=O)C(C(C)C)NC(=O)C(NC(=O)CN)C(C)CC)CSSCC(C(NC(CO)C(=O)NC(CC(C)C)C(=O)NC(CC=2C=CC(O)=CC=2)C(=O)NC(CCC(N)=O)C(=O)NC(CC(C)C)C(=O)NC(CCC(O)=O)C(=O)NC(CC(N)=O)C(=O)NC(CC=2C=CC(O)=CC=2)C(=O)NC(CSSCC(NC(=O)C(C(C)C)NC(=O)C(CC(C)C)NC(=O)C(CC=2C=CC(O)=CC=2)NC(=O)C(CC(C)C)NC(=O)C(C)NC(=O)C(CCC(O)=O)NC(=O)C(C(C)C)NC(=O)C(CC(C)C)NC(=O)C(CC=2NC=NC=2)NC(=O)C(CO)NC(=O)CNC2=O)C(=O)NCC(=O)NC(CCC(O)=O)C(=O)NC(CCCNC(N)=N)C(=O)NCC(=O)NC(CC=3C=CC=CC=3)C(=O)NC(CC=3C=CC=CC=3)C(=O)NC(CC=3C=CC(O)=CC=3)C(=O)NC(C(C)O)C(=O)N3C(CCC3)C(=O)NC(CCCCN)C(=O)NC(C)C(O)=O)C(=O)NC(CC(N)=O)C(O)=O)=O)NC(=O)C(C(C)CC)NC(=O)C(CO)NC(=O)C(C(C)O)NC(=O)C1CSSCC2NC(=O)C(CC(C)C)NC(=O)C(NC(=O)C(CCC(N)=O)NC(=O)C(CC(N)=O)NC(=O)C(NC(=O)C(N)CC=1C=CC=CC=1)C(C)C)CC1=CN=CN1 NOESYZHRGYRDHS-UHFFFAOYSA-N 0.000 description 4
- 230000002062 proliferating effect Effects 0.000 description 4
- 230000000069 prophylactic effect Effects 0.000 description 4
- 235000019833 protease Nutrition 0.000 description 4
- 238000011084 recovery Methods 0.000 description 4
- 230000002829 reductive effect Effects 0.000 description 4
- 210000003296 saliva Anatomy 0.000 description 4
- 210000003491 skin Anatomy 0.000 description 4
- 238000003786 synthesis reaction Methods 0.000 description 4
- 210000001138 tear Anatomy 0.000 description 4
- 229960004072 thrombin Drugs 0.000 description 4
- 230000004614 tumor growth Effects 0.000 description 4
- 230000002792 vascular Effects 0.000 description 4
- 229920000936 Agarose Polymers 0.000 description 3
- 102100022712 Alpha-1-antitrypsin Human genes 0.000 description 3
- 101710081722 Antitrypsin Proteins 0.000 description 3
- 101710132601 Capsid protein Proteins 0.000 description 3
- 108010078791 Carrier Proteins Proteins 0.000 description 3
- 102000004046 Caspase-2 Human genes 0.000 description 3
- 108090000552 Caspase-2 Proteins 0.000 description 3
- 102100024539 Chymase Human genes 0.000 description 3
- 108090000227 Chymases Proteins 0.000 description 3
- 101710094648 Coat protein Proteins 0.000 description 3
- 101100539403 Drosophila melanogaster sgl gene Proteins 0.000 description 3
- 102000001301 EGF receptor Human genes 0.000 description 3
- 108060006698 EGF receptor Proteins 0.000 description 3
- 108010013369 Enteropeptidase Proteins 0.000 description 3
- 102100029727 Enteropeptidase Human genes 0.000 description 3
- 108010087819 Fc receptors Proteins 0.000 description 3
- 102000009109 Fc receptors Human genes 0.000 description 3
- 108010049003 Fibrinogen Proteins 0.000 description 3
- 102000008946 Fibrinogen Human genes 0.000 description 3
- 108090001126 Furin Proteins 0.000 description 3
- 102000004961 Furin Human genes 0.000 description 3
- 102000006395 Globulins Human genes 0.000 description 3
- 108010044091 Globulins Proteins 0.000 description 3
- 102100021181 Golgi phosphoprotein 3 Human genes 0.000 description 3
- 241000282412 Homo Species 0.000 description 3
- 101000823116 Homo sapiens Alpha-1-antitrypsin Proteins 0.000 description 3
- 101001010513 Homo sapiens Leukocyte elastase inhibitor Proteins 0.000 description 3
- 102000049772 Interleukin-16 Human genes 0.000 description 3
- 101800003050 Interleukin-16 Proteins 0.000 description 3
- 102000004890 Interleukin-8 Human genes 0.000 description 3
- 108090001007 Interleukin-8 Proteins 0.000 description 3
- 101710125418 Major capsid protein Proteins 0.000 description 3
- 241001529936 Murinae Species 0.000 description 3
- 101710141454 Nucleoprotein Proteins 0.000 description 3
- 108090000284 Pepsin A Proteins 0.000 description 3
- 102000057297 Pepsin A Human genes 0.000 description 3
- 101710083689 Probable capsid protein Proteins 0.000 description 3
- 101710180316 Protease 2 Proteins 0.000 description 3
- 101710180313 Protease 3 Proteins 0.000 description 3
- 241000589516 Pseudomonas Species 0.000 description 3
- 108010025832 RANK Ligand Proteins 0.000 description 3
- 102000014128 RANK Ligand Human genes 0.000 description 3
- 241000235070 Saccharomyces Species 0.000 description 3
- 241000239226 Scorpiones Species 0.000 description 3
- 108090001109 Thermolysin Proteins 0.000 description 3
- 101710120037 Toxin CcdB Proteins 0.000 description 3
- 108090000848 Ubiquitin Proteins 0.000 description 3
- 102000044159 Ubiquitin Human genes 0.000 description 3
- 238000004458 analytical method Methods 0.000 description 3
- 239000003242 anti bacterial agent Substances 0.000 description 3
- 230000001475 anti-trypsic effect Effects 0.000 description 3
- 239000011230 binding agent Substances 0.000 description 3
- 210000004369 blood Anatomy 0.000 description 3
- 239000008280 blood Substances 0.000 description 3
- 239000003153 chemical reaction reagent Substances 0.000 description 3
- 239000008121 dextrose Substances 0.000 description 3
- 238000003745 diagnosis Methods 0.000 description 3
- 239000000539 dimer Substances 0.000 description 3
- 229940012952 fibrinogen Drugs 0.000 description 3
- 230000002496 gastric effect Effects 0.000 description 3
- 210000004051 gastric juice Anatomy 0.000 description 3
- BRZYSWJRSDMWLG-CAXSIQPQSA-N geneticin Natural products O1C[C@@](O)(C)[C@H](NC)[C@@H](O)[C@H]1O[C@@H]1[C@@H](O)[C@H](O[C@@H]2[C@@H]([C@@H](O)[C@H](O)[C@@H](C(C)O)O2)N)[C@@H](N)C[C@H]1N BRZYSWJRSDMWLG-CAXSIQPQSA-N 0.000 description 3
- 230000012010 growth Effects 0.000 description 3
- 235000003642 hunger Nutrition 0.000 description 3
- 230000004968 inflammatory condition Effects 0.000 description 3
- 206010022000 influenza Diseases 0.000 description 3
- 108010044426 integrins Proteins 0.000 description 3
- 102000006495 integrins Human genes 0.000 description 3
- 229940096397 interleukin-8 Drugs 0.000 description 3
- XKTZWUACRZHVAN-VADRZIEHSA-N interleukin-8 Chemical compound C([C@H](NC(=O)[C@H](CC(O)=O)NC(=O)[C@H](CC=1C2=CC=CC=C2NC=1)NC(=O)[C@@H](NC(C)=O)CCSC)C(=O)N[C@@H](CC(O)=O)C(=O)N[C@@H](CC(O)=O)C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](CC(N)=O)C(=O)N[C@@H](CC=1C=CC=CC=1)C(=O)N[C@@H]([C@@H](C)O)C(=O)NCC(=O)N[C@@H](CCSC)C(=O)N1[C@H](CCC1)C(=O)N1[C@H](CCC1)C(=O)N[C@@H](C)C(=O)N[C@H](CC(O)=O)C(=O)N[C@H](CCC(O)=O)C(=O)N[C@H](CC(O)=O)C(=O)N[C@H](CC=1C=CC(O)=CC=1)C(=O)N[C@H](CO)C(=O)N1[C@H](CCC1)C(N)=O)C1=CC=CC=C1 XKTZWUACRZHVAN-VADRZIEHSA-N 0.000 description 3
- 238000007918 intramuscular administration Methods 0.000 description 3
- 238000001990 intravenous administration Methods 0.000 description 3
- 210000001616 monocyte Anatomy 0.000 description 3
- 231100000350 mutagenesis Toxicity 0.000 description 3
- 239000006199 nebulizer Substances 0.000 description 3
- 235000015097 nutrients Nutrition 0.000 description 3
- 150000002923 oximes Chemical class 0.000 description 3
- 239000005022 packaging material Substances 0.000 description 3
- 229940062190 pancreas extract Drugs 0.000 description 3
- 229940111202 pepsin Drugs 0.000 description 3
- 229920001223 polyethylene glycol Polymers 0.000 description 3
- 230000008569 process Effects 0.000 description 3
- 210000001236 prokaryotic cell Anatomy 0.000 description 3
- 229950010131 puromycin Drugs 0.000 description 3
- 208000023504 respiratory system disease Diseases 0.000 description 3
- 108091000053 retinol binding Proteins 0.000 description 3
- 102000029752 retinol binding Human genes 0.000 description 3
- 239000007787 solid Substances 0.000 description 3
- 238000001228 spectrum Methods 0.000 description 3
- 239000007921 spray Substances 0.000 description 3
- 238000010561 standard procedure Methods 0.000 description 3
- 210000000130 stem cell Anatomy 0.000 description 3
- 230000008685 targeting Effects 0.000 description 3
- 238000013518 transcription Methods 0.000 description 3
- 230000035897 transcription Effects 0.000 description 3
- 238000013519 translation Methods 0.000 description 3
- 239000002753 trypsin inhibitor Substances 0.000 description 3
- 241001515965 unidentified phage Species 0.000 description 3
- 230000003612 virological effect Effects 0.000 description 3
- 108091032973 (ribonucleotides)n+m Proteins 0.000 description 2
- 102100023990 60S ribosomal protein L17 Human genes 0.000 description 2
- 102100031585 ADP-ribosyl cyclase/cyclic ADP-ribose hydrolase 1 Human genes 0.000 description 2
- 108091005508 Acid proteases Proteins 0.000 description 2
- 235000009434 Actinidia chinensis Nutrition 0.000 description 2
- 235000009436 Actinidia deliciosa Nutrition 0.000 description 2
- ORILYTVJVMAKLC-UHFFFAOYSA-N Adamantane Natural products C1C(C2)CC3CC1CC2C3 ORILYTVJVMAKLC-UHFFFAOYSA-N 0.000 description 2
- 101000716807 Arabidopsis thaliana Protein SCO1 homolog 1, mitochondrial 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
- 108010017640 Aspartic Acid Proteases Proteins 0.000 description 2
- 102000004580 Aspartic Acid Proteases Human genes 0.000 description 2
- 201000002909 Aspergillosis Diseases 0.000 description 2
- 208000036641 Aspergillus infections Diseases 0.000 description 2
- 108010081589 Becaplermin Proteins 0.000 description 2
- 102000004506 Blood Proteins Human genes 0.000 description 2
- 108010017384 Blood Proteins Proteins 0.000 description 2
- 101001069913 Bos taurus Growth-regulated protein homolog beta Proteins 0.000 description 2
- 101001069912 Bos taurus Growth-regulated protein homolog gamma Proteins 0.000 description 2
- 108090000715 Brain-derived neurotrophic factor Proteins 0.000 description 2
- 102000004219 Brain-derived neurotrophic factor Human genes 0.000 description 2
- 102100031151 C-C chemokine receptor type 2 Human genes 0.000 description 2
- 101710149815 C-C chemokine receptor type 2 Proteins 0.000 description 2
- 102100024167 C-C chemokine receptor type 3 Human genes 0.000 description 2
- 101710149862 C-C chemokine receptor type 3 Proteins 0.000 description 2
- 101710149863 C-C chemokine receptor type 4 Proteins 0.000 description 2
- 102100035875 C-C chemokine receptor type 5 Human genes 0.000 description 2
- 101710149870 C-C chemokine receptor type 5 Proteins 0.000 description 2
- 102100036301 C-C chemokine receptor type 7 Human genes 0.000 description 2
- 102100036305 C-C chemokine receptor type 8 Human genes 0.000 description 2
- 102100023702 C-C motif chemokine 13 Human genes 0.000 description 2
- 101710112613 C-C motif chemokine 13 Proteins 0.000 description 2
- 101710155857 C-C motif chemokine 2 Proteins 0.000 description 2
- 102100036846 C-C motif chemokine 21 Human genes 0.000 description 2
- 102100032366 C-C motif chemokine 7 Human genes 0.000 description 2
- 101710155834 C-C motif chemokine 7 Proteins 0.000 description 2
- 102100034871 C-C motif chemokine 8 Human genes 0.000 description 2
- 101710155833 C-C motif chemokine 8 Proteins 0.000 description 2
- 102100025248 C-X-C motif chemokine 10 Human genes 0.000 description 2
- 102100039398 C-X-C motif chemokine 2 Human genes 0.000 description 2
- 102100036189 C-X-C motif chemokine 3 Human genes 0.000 description 2
- 102100036153 C-X-C motif chemokine 6 Human genes 0.000 description 2
- 101710085504 C-X-C motif chemokine 6 Proteins 0.000 description 2
- 102100032528 C-type lectin domain family 11 member A Human genes 0.000 description 2
- 102100031168 CCN family member 2 Human genes 0.000 description 2
- 102100032976 CCR4-NOT transcription complex subunit 6 Human genes 0.000 description 2
- 102100027207 CD27 antigen Human genes 0.000 description 2
- 101150093802 CXCL1 gene Proteins 0.000 description 2
- 101100123850 Caenorhabditis elegans her-1 gene Proteins 0.000 description 2
- 101100369802 Caenorhabditis elegans tim-1 gene Proteins 0.000 description 2
- 101100314454 Caenorhabditis elegans tra-1 gene Proteins 0.000 description 2
- 108010006303 Carboxypeptidases Proteins 0.000 description 2
- 102000005367 Carboxypeptidases Human genes 0.000 description 2
- 102100025597 Caspase-4 Human genes 0.000 description 2
- 101710090338 Caspase-4 Proteins 0.000 description 2
- 102100038916 Caspase-5 Human genes 0.000 description 2
- 101710090333 Caspase-5 Proteins 0.000 description 2
- 102000004039 Caspase-9 Human genes 0.000 description 2
- 108090000566 Caspase-9 Proteins 0.000 description 2
- 108010082155 Chemokine CCL18 Proteins 0.000 description 2
- 108010082161 Chemokine CCL19 Proteins 0.000 description 2
- 102000003805 Chemokine CCL19 Human genes 0.000 description 2
- 108010083702 Chemokine CCL21 Proteins 0.000 description 2
- 102000015833 Cystatin Human genes 0.000 description 2
- 108010002069 Defensins Proteins 0.000 description 2
- 102000000541 Defensins Human genes 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
- 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 2
- 108010000912 Egg Proteins Proteins 0.000 description 2
- 102000002322 Egg Proteins Human genes 0.000 description 2
- 102400000686 Endothelin-1 Human genes 0.000 description 2
- 101800004490 Endothelin-1 Proteins 0.000 description 2
- 208000009386 Experimental Arthritis Diseases 0.000 description 2
- 101150021185 FGF gene Proteins 0.000 description 2
- 108010014173 Factor X Proteins 0.000 description 2
- 102000008857 Ferritin Human genes 0.000 description 2
- 108050000784 Ferritin Proteins 0.000 description 2
- 238000008416 Ferritin Methods 0.000 description 2
- 108010073385 Fibrin Proteins 0.000 description 2
- 102000009123 Fibrin Human genes 0.000 description 2
- BWGVNKXGVNDBDI-UHFFFAOYSA-N Fibrin monomer Chemical compound CNC(=O)CNC(=O)CN BWGVNKXGVNDBDI-UHFFFAOYSA-N 0.000 description 2
- 108010088842 Fibrinolysin Proteins 0.000 description 2
- 108090000385 Fibroblast growth factor 7 Proteins 0.000 description 2
- 102100037362 Fibronectin Human genes 0.000 description 2
- 108010067306 Fibronectins Proteins 0.000 description 2
- 108090000270 Ficain Proteins 0.000 description 2
- 101710115997 Gamma-tubulin complex component 2 Proteins 0.000 description 2
- 102000034615 Glial cell line-derived neurotrophic factor Human genes 0.000 description 2
- 108091010837 Glial cell line-derived neurotrophic factor Proteins 0.000 description 2
- 108010017080 Granulocyte Colony-Stimulating Factor Proteins 0.000 description 2
- 102100039619 Granulocyte colony-stimulating factor Human genes 0.000 description 2
- 101000777636 Homo sapiens ADP-ribosyl cyclase/cyclic ADP-ribose hydrolase 1 Proteins 0.000 description 2
- 101000716065 Homo sapiens C-C chemokine receptor type 7 Proteins 0.000 description 2
- 101000716063 Homo sapiens C-C chemokine receptor type 8 Proteins 0.000 description 2
- 101000947193 Homo sapiens C-X-C motif chemokine 3 Proteins 0.000 description 2
- 101000942297 Homo sapiens C-type lectin domain family 11 member A Proteins 0.000 description 2
- 101100382881 Homo sapiens CCL18 gene Proteins 0.000 description 2
- 101000777550 Homo sapiens CCN family member 2 Proteins 0.000 description 2
- 101000914511 Homo sapiens CD27 antigen Proteins 0.000 description 2
- 101000856395 Homo sapiens Cullin-9 Proteins 0.000 description 2
- 101001069921 Homo sapiens Growth-regulated alpha protein Proteins 0.000 description 2
- 101001057504 Homo sapiens Interferon-stimulated gene 20 kDa protein Proteins 0.000 description 2
- 101000960954 Homo sapiens Interleukin-18 Proteins 0.000 description 2
- 101001055144 Homo sapiens Interleukin-2 receptor subunit alpha Proteins 0.000 description 2
- 101000853002 Homo sapiens Interleukin-25 Proteins 0.000 description 2
- 101000878605 Homo sapiens Low affinity immunoglobulin epsilon Fc receptor Proteins 0.000 description 2
- 101001128431 Homo sapiens Myeloid-derived growth factor Proteins 0.000 description 2
- 101000973997 Homo sapiens Nucleosome assembly protein 1-like 4 Proteins 0.000 description 2
- 101000947178 Homo sapiens Platelet basic protein Proteins 0.000 description 2
- 101001076715 Homo sapiens RNA-binding protein 39 Proteins 0.000 description 2
- 101000863884 Homo sapiens Sialic acid-binding Ig-like lectin 8 Proteins 0.000 description 2
- 101000617130 Homo sapiens Stromal cell-derived factor 1 Proteins 0.000 description 2
- 101000914514 Homo sapiens T-cell-specific surface glycoprotein CD28 Proteins 0.000 description 2
- 101000851376 Homo sapiens Tumor necrosis factor receptor superfamily member 8 Proteins 0.000 description 2
- 101000851007 Homo sapiens Vascular endothelial growth factor receptor 2 Proteins 0.000 description 2
- 101000851030 Homo sapiens Vascular endothelial growth factor receptor 3 Proteins 0.000 description 2
- 108090001061 Insulin Proteins 0.000 description 2
- 102000004877 Insulin Human genes 0.000 description 2
- 108090000723 Insulin-Like Growth Factor I Proteins 0.000 description 2
- 102000004218 Insulin-Like Growth Factor I Human genes 0.000 description 2
- 108010008212 Integrin alpha4beta1 Proteins 0.000 description 2
- 108010064593 Intercellular Adhesion Molecule-1 Proteins 0.000 description 2
- 102100037877 Intercellular adhesion molecule 1 Human genes 0.000 description 2
- 102100027268 Interferon-stimulated gene 20 kDa protein Human genes 0.000 description 2
- 108090000174 Interleukin-10 Proteins 0.000 description 2
- 108090000177 Interleukin-11 Proteins 0.000 description 2
- 102000003815 Interleukin-11 Human genes 0.000 description 2
- 108010065805 Interleukin-12 Proteins 0.000 description 2
- 108090000176 Interleukin-13 Proteins 0.000 description 2
- 102100039898 Interleukin-18 Human genes 0.000 description 2
- 108010002350 Interleukin-2 Proteins 0.000 description 2
- 102000013264 Interleukin-23 Human genes 0.000 description 2
- 108010065637 Interleukin-23 Proteins 0.000 description 2
- 102100036672 Interleukin-23 receptor Human genes 0.000 description 2
- 108090000978 Interleukin-4 Proteins 0.000 description 2
- 108090001005 Interleukin-6 Proteins 0.000 description 2
- 108010002586 Interleukin-7 Proteins 0.000 description 2
- 108010002335 Interleukin-9 Proteins 0.000 description 2
- XEEYBQQBJWHFJM-UHFFFAOYSA-N Iron Chemical compound [Fe] XEEYBQQBJWHFJM-UHFFFAOYSA-N 0.000 description 2
- 108010092694 L-Selectin Proteins 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
- FBOZXECLQNJBKD-ZDUSSCGKSA-N L-methotrexate Chemical compound C=1N=C2N=C(N)N=C(N)C2=NC=1CN(C)C1=CC=C(C(=O)N[C@@H](CCC(O)=O)C(O)=O)C=C1 FBOZXECLQNJBKD-ZDUSSCGKSA-N 0.000 description 2
- 102100033467 L-selectin Human genes 0.000 description 2
- 108090000581 Leukemia inhibitory factor Proteins 0.000 description 2
- 102100038007 Low affinity immunoglobulin epsilon Fc receptor Human genes 0.000 description 2
- 102000004083 Lymphotoxin-alpha Human genes 0.000 description 2
- 108090000542 Lymphotoxin-alpha Proteins 0.000 description 2
- KDXKERNSBIXSRK-UHFFFAOYSA-N Lysine Natural products NCCCCC(N)C(O)=O KDXKERNSBIXSRK-UHFFFAOYSA-N 0.000 description 2
- 102000034655 MIF Human genes 0.000 description 2
- 108060004872 MIF Proteins 0.000 description 2
- 108010046938 Macrophage Colony-Stimulating Factor Proteins 0.000 description 2
- 102000007651 Macrophage Colony-Stimulating Factor Human genes 0.000 description 2
- 102000005741 Metalloproteases Human genes 0.000 description 2
- 108010006035 Metalloproteases Proteins 0.000 description 2
- 102000016943 Muramidase Human genes 0.000 description 2
- 108010014251 Muramidase Proteins 0.000 description 2
- 108010062010 N-Acetylmuramoyl-L-alanine Amidase Proteins 0.000 description 2
- CHJJGSNFBQVOTG-UHFFFAOYSA-N N-methyl-guanidine Natural products CNC(N)=N CHJJGSNFBQVOTG-UHFFFAOYSA-N 0.000 description 2
- 229930193140 Neomycin Natural products 0.000 description 2
- 102000007072 Nerve Growth Factors Human genes 0.000 description 2
- 108090000742 Neurotrophin 3 Proteins 0.000 description 2
- 102100029268 Neurotrophin-3 Human genes 0.000 description 2
- 102000003683 Neurotrophin-4 Human genes 0.000 description 2
- 108090000099 Neurotrophin-4 Proteins 0.000 description 2
- 102100033174 Neutrophil elastase Human genes 0.000 description 2
- 108091034117 Oligonucleotide Proteins 0.000 description 2
- 102000004264 Osteopontin Human genes 0.000 description 2
- 108010081689 Osteopontin Proteins 0.000 description 2
- 102100036154 Platelet basic protein Human genes 0.000 description 2
- 108090000778 Platelet factor 4 Proteins 0.000 description 2
- 101710089372 Programmed cell death protein 1 Proteins 0.000 description 2
- 108010076504 Protein Sorting Signals Proteins 0.000 description 2
- 101710123874 Protein-glutamine gamma-glutamyltransferase Proteins 0.000 description 2
- 241000589540 Pseudomonas fluorescens Species 0.000 description 2
- KJTLSVCANCCWHF-UHFFFAOYSA-N Ruthenium Chemical compound [Ru] KJTLSVCANCCWHF-UHFFFAOYSA-N 0.000 description 2
- 102100023361 SAP domain-containing ribonucleoprotein Human genes 0.000 description 2
- 206010039491 Sarcoma Diseases 0.000 description 2
- 102100029964 Sialic acid-binding Ig-like lectin 8 Human genes 0.000 description 2
- CDBYLPFSWZWCQE-UHFFFAOYSA-L Sodium Carbonate Chemical compound [Na+].[Na+].[O-]C([O-])=O CDBYLPFSWZWCQE-UHFFFAOYSA-L 0.000 description 2
- 102100025237 T-cell surface antigen CD2 Human genes 0.000 description 2
- 102100036011 T-cell surface glycoprotein CD4 Human genes 0.000 description 2
- 102100027213 T-cell-specific surface glycoprotein CD28 Human genes 0.000 description 2
- 239000004098 Tetracycline Substances 0.000 description 2
- 102100027188 Thyroid peroxidase Human genes 0.000 description 2
- 101710113649 Thyroid peroxidase Proteins 0.000 description 2
- 102000004887 Transforming Growth Factor beta Human genes 0.000 description 2
- 108090001012 Transforming Growth Factor beta Proteins 0.000 description 2
- 108010009583 Transforming Growth Factors Proteins 0.000 description 2
- 102000009618 Transforming Growth Factors Human genes 0.000 description 2
- 102100040247 Tumor necrosis factor Human genes 0.000 description 2
- 102100036857 Tumor necrosis factor receptor superfamily member 8 Human genes 0.000 description 2
- XSQUKJJJFZCRTK-UHFFFAOYSA-N Urea Chemical compound NC(N)=O XSQUKJJJFZCRTK-UHFFFAOYSA-N 0.000 description 2
- 102000009524 Vascular Endothelial Growth Factor A Human genes 0.000 description 2
- 102100033177 Vascular endothelial growth factor receptor 2 Human genes 0.000 description 2
- 102100033179 Vascular endothelial growth factor receptor 3 Human genes 0.000 description 2
- 230000003213 activating effect Effects 0.000 description 2
- 230000004913 activation Effects 0.000 description 2
- 230000001154 acute effect Effects 0.000 description 2
- 230000000172 allergic effect Effects 0.000 description 2
- 125000000539 amino acid group Chemical group 0.000 description 2
- 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 2
- 229960000723 ampicillin Drugs 0.000 description 2
- 229940088710 antibiotic agent Drugs 0.000 description 2
- 239000004019 antithrombin Substances 0.000 description 2
- 238000003491 array Methods 0.000 description 2
- 208000010668 atopic eczema Diseases 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
- 230000015572 biosynthetic process Effects 0.000 description 2
- 210000000988 bone and bone Anatomy 0.000 description 2
- 125000003178 carboxy group Chemical group [H]OC(*)=O 0.000 description 2
- 239000000969 carrier Substances 0.000 description 2
- 108010018550 caspase 13 Proteins 0.000 description 2
- 230000003197 catalytic effect Effects 0.000 description 2
- 210000000349 chromosome Anatomy 0.000 description 2
- 150000001875 compounds Chemical class 0.000 description 2
- 108050004038 cystatin Proteins 0.000 description 2
- 238000000354 decomposition reaction Methods 0.000 description 2
- SWSQBOPZIKWTGO-UHFFFAOYSA-N dimethylaminoamidine Natural products CN(C)C(N)=N SWSQBOPZIKWTGO-UHFFFAOYSA-N 0.000 description 2
- 229940042399 direct acting antivirals protease inhibitors Drugs 0.000 description 2
- 239000002532 enzyme inhibitor Substances 0.000 description 2
- 210000002744 extracellular matrix Anatomy 0.000 description 2
- 238000000605 extraction Methods 0.000 description 2
- 229940012356 eye drops Drugs 0.000 description 2
- 229950003499 fibrin Drugs 0.000 description 2
- 235000019836 ficin Nutrition 0.000 description 2
- 108700014844 flt3 ligand Proteins 0.000 description 2
- PCHJSUWPFVWCPO-UHFFFAOYSA-N gold Chemical compound [Au] PCHJSUWPFVWCPO-UHFFFAOYSA-N 0.000 description 2
- 229910052737 gold Inorganic materials 0.000 description 2
- 239000010931 gold Substances 0.000 description 2
- 239000001963 growth medium Substances 0.000 description 2
- 230000036541 health Effects 0.000 description 2
- 229940088597 hormone Drugs 0.000 description 2
- 239000005556 hormone Substances 0.000 description 2
- 230000001900 immune effect Effects 0.000 description 2
- 210000000987 immune system Anatomy 0.000 description 2
- 238000000338 in vitro Methods 0.000 description 2
- 208000015181 infectious disease Diseases 0.000 description 2
- 230000002757 inflammatory effect Effects 0.000 description 2
- 238000002347 injection Methods 0.000 description 2
- 239000007924 injection Substances 0.000 description 2
- 229940125396 insulin Drugs 0.000 description 2
- 102000008616 interleukin-15 receptor activity proteins Human genes 0.000 description 2
- 108040002039 interleukin-15 receptor activity proteins Proteins 0.000 description 2
- 102000053460 interleukin-17 receptor activity proteins Human genes 0.000 description 2
- 108040001304 interleukin-17 receptor activity proteins Proteins 0.000 description 2
- 102000008625 interleukin-18 receptor activity proteins Human genes 0.000 description 2
- 108040002014 interleukin-18 receptor activity proteins Proteins 0.000 description 2
- 108040001844 interleukin-23 receptor activity proteins Proteins 0.000 description 2
- 238000007912 intraperitoneal administration Methods 0.000 description 2
- 238000002955 isolation Methods 0.000 description 2
- 210000002429 large intestine Anatomy 0.000 description 2
- 210000004185 liver Anatomy 0.000 description 2
- 108010019677 lymphotactin Proteins 0.000 description 2
- 229960000274 lysozyme Drugs 0.000 description 2
- 239000004325 lysozyme Substances 0.000 description 2
- 235000010335 lysozyme Nutrition 0.000 description 2
- AEUKDPKXTPNBNY-XEYRWQBLSA-N mcp 2 Chemical compound C([C@@H](C(=O)N[C@@H](CS)C(=O)N[C@@H](CCCNC(N)=N)C(=O)N[C@@H]([C@@H](C)CC)C(=O)N[C@@H](CCCNC(N)=N)C(=O)NCC(=O)N[C@@H](CCCNC(N)=N)C(=O)N[C@@H]([C@@H](C)CC)C(=O)N[C@@H](CC=1NC=NC=1)C(=O)N1[C@@H](CCC1)C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](CS)C(=O)N[C@@H](CS)C(=O)N[C@@H](CCCNC(N)=N)C(=O)N[C@@H](CCCNC(N)=N)C(O)=O)NC(=O)CNC(=O)[C@H](C)NC(=O)[C@H](CCCNC(N)=N)NC(=O)[C@H](CCCNC(N)=N)NC(=O)[C@H](CCC(O)=O)NC(=O)[C@H](CC(C)C)NC(=O)[C@H]1N(CCC1)C(=O)[C@H](CC(C)C)NC(=O)[C@H](CS)NC(=O)[C@H](CC(C)C)NC(=O)[C@H](C)NC(=O)[C@H](CCCNC(N)=N)NC(=O)[C@H](CCCNC(N)=N)NC(=O)[C@H](CS)NC(=O)[C@H](C)NC(=O)[C@H](CS)NC(=O)[C@@H](NC(=O)[C@@H](N)C(C)C)C(C)C)C1=CC=CC=C1 AEUKDPKXTPNBNY-XEYRWQBLSA-N 0.000 description 2
- 238000002844 melting Methods 0.000 description 2
- 230000008018 melting Effects 0.000 description 2
- 229960000485 methotrexate Drugs 0.000 description 2
- 238000012544 monitoring process Methods 0.000 description 2
- 210000000214 mouth Anatomy 0.000 description 2
- 229960004927 neomycin Drugs 0.000 description 2
- 229940053128 nerve growth factor Drugs 0.000 description 2
- 239000003900 neurotrophic factor Substances 0.000 description 2
- 210000000056 organ Anatomy 0.000 description 2
- 239000002245 particle Substances 0.000 description 2
- 230000007170 pathology Effects 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
- 229940012957 plasmin Drugs 0.000 description 2
- 239000004033 plastic Substances 0.000 description 2
- 229920003023 plastic Polymers 0.000 description 2
- 108010017843 platelet-derived growth factor A Proteins 0.000 description 2
- 108010000685 platelet-derived growth factor AB Proteins 0.000 description 2
- 102000054765 polymorphisms of proteins Human genes 0.000 description 2
- 230000006337 proteolytic cleavage Effects 0.000 description 2
- 230000003362 replicative effect Effects 0.000 description 2
- 229910052707 ruthenium Inorganic materials 0.000 description 2
- QZAYGJVTTNCVMB-UHFFFAOYSA-N serotonin Chemical class C1=C(O)C=C2C(CCN)=CNC2=C1 QZAYGJVTTNCVMB-UHFFFAOYSA-N 0.000 description 2
- 230000001568 sexual effect Effects 0.000 description 2
- 230000019491 signal transduction Effects 0.000 description 2
- 238000005507 spraying Methods 0.000 description 2
- 239000000725 suspension Substances 0.000 description 2
- 229960002180 tetracycline Drugs 0.000 description 2
- 229930101283 tetracycline Natural products 0.000 description 2
- 235000019364 tetracycline Nutrition 0.000 description 2
- 150000003522 tetracyclines Chemical class 0.000 description 2
- ZRKFYGHZFMAOKI-QMGMOQQFSA-N tgfbeta Chemical compound C([C@H](NC(=O)[C@H](C(C)C)NC(=O)CNC(=O)[C@H](CCC(O)=O)NC(=O)[C@H](CCCNC(N)=N)NC(=O)[C@H](CC(N)=O)NC(=O)[C@H](CC(C)C)NC(=O)[C@H]([C@@H](C)O)NC(=O)[C@H](CCC(O)=O)NC(=O)[C@H]([C@@H](C)O)NC(=O)[C@H](CC(C)C)NC(=O)CNC(=O)[C@H](C)NC(=O)[C@H](CO)NC(=O)[C@H](CCC(N)=O)NC(=O)[C@@H](NC(=O)[C@H](C)NC(=O)[C@H](C)NC(=O)[C@@H](NC(=O)[C@H](CC(C)C)NC(=O)[C@@H](N)CCSC)C(C)C)[C@@H](C)CC)C(=O)N[C@@H]([C@@H](C)O)C(=O)N[C@@H](C(C)C)C(=O)N[C@@H](CC=1C=CC=CC=1)C(=O)N[C@@H](C)C(=O)N1[C@@H](CCC1)C(=O)N[C@@H]([C@@H](C)O)C(=O)N[C@@H](CC(N)=O)C(=O)N[C@@H](CCC(O)=O)C(=O)N[C@@H](C)C(=O)N[C@@H](CC=1C=CC=CC=1)C(=O)N[C@@H](CCCNC(N)=N)C(=O)N[C@@H](C)C(=O)N[C@@H](CC(C)C)C(=O)N1[C@@H](CCC1)C(=O)N1[C@@H](CCC1)C(=O)N[C@@H](CCCNC(N)=N)C(=O)N[C@@H](CCC(O)=O)C(=O)N[C@@H](CCCNC(N)=N)C(=O)N[C@@H](CO)C(=O)N[C@@H](CCCNC(N)=N)C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](CC(C)C)C(O)=O)C1=CC=C(O)C=C1 ZRKFYGHZFMAOKI-QMGMOQQFSA-N 0.000 description 2
- 229940124597 therapeutic agent Drugs 0.000 description 2
- 210000003437 trachea Anatomy 0.000 description 2
- 238000001890 transfection Methods 0.000 description 2
- APJYDQYYACXCRM-UHFFFAOYSA-N tryptamine Chemical compound C1=CC=C2C(CCN)=CNC2=C1 APJYDQYYACXCRM-UHFFFAOYSA-N 0.000 description 2
- 230000005747 tumor angiogenesis Effects 0.000 description 2
- 241000701161 unidentified adenovirus Species 0.000 description 2
- 239000003981 vehicle Substances 0.000 description 2
- 238000003260 vortexing Methods 0.000 description 2
- XLYOFNOQVPJJNP-UHFFFAOYSA-N water Substances O XLYOFNOQVPJJNP-UHFFFAOYSA-N 0.000 description 2
- IJWCGVPEDDQUDE-YGJAXBLXSA-N (2s)-2-[[(1s)-2-[[(2s)-5-amino-1,5-dioxo-1-[[(2s)-1-oxopropan-2-yl]amino]pentan-2-yl]amino]-1-[(6s)-2-amino-1,4,5,6-tetrahydropyrimidin-6-yl]-2-oxoethyl]carbamoylamino]-4-methylpentanoic acid Chemical compound O=C[C@H](C)NC(=O)[C@H](CCC(N)=O)NC(=O)[C@@H](NC(=O)N[C@@H](CC(C)C)C(O)=O)[C@@H]1CCN=C(N)N1 IJWCGVPEDDQUDE-YGJAXBLXSA-N 0.000 description 1
- FHVDTGUDJYJELY-UHFFFAOYSA-N 6-{[2-carboxy-4,5-dihydroxy-6-(phosphanyloxy)oxan-3-yl]oxy}-4,5-dihydroxy-3-phosphanyloxane-2-carboxylic acid Chemical compound O1C(C(O)=O)C(P)C(O)C(O)C1OC1C(C(O)=O)OC(OP)C(O)C1O FHVDTGUDJYJELY-UHFFFAOYSA-N 0.000 description 1
- 244000298715 Actinidia chinensis Species 0.000 description 1
- 244000298697 Actinidia deliciosa Species 0.000 description 1
- 241000186361 Actinobacteria <class> Species 0.000 description 1
- 241000251468 Actinopterygii Species 0.000 description 1
- 102000007698 Alcohol dehydrogenase Human genes 0.000 description 1
- 108010021809 Alcohol dehydrogenase Proteins 0.000 description 1
- 102000002260 Alkaline Phosphatase Human genes 0.000 description 1
- 108020004774 Alkaline Phosphatase Proteins 0.000 description 1
- 102100033312 Alpha-2-macroglobulin Human genes 0.000 description 1
- 102100034452 Alternative prion protein Human genes 0.000 description 1
- 206010001881 Alveolar proteinosis Diseases 0.000 description 1
- 108010043324 Amyloid Precursor Protein Secretases Proteins 0.000 description 1
- 102000002659 Amyloid Precursor Protein Secretases Human genes 0.000 description 1
- 108010005853 Anti-Mullerian Hormone Proteins 0.000 description 1
- 108010087765 Antipain Proteins 0.000 description 1
- 102100040214 Apolipoprotein(a) Human genes 0.000 description 1
- 108010025628 Apolipoproteins E Proteins 0.000 description 1
- 102000013918 Apolipoproteins E Human genes 0.000 description 1
- 108010039627 Aprotinin Proteins 0.000 description 1
- 208000033116 Asbestos intoxication Diseases 0.000 description 1
- 108010011485 Aspartame Proteins 0.000 description 1
- 201000001320 Atherosclerosis Diseases 0.000 description 1
- 108090001008 Avidin Proteins 0.000 description 1
- 235000017166 Bambusa arundinacea Nutrition 0.000 description 1
- 235000017491 Bambusa tulda Nutrition 0.000 description 1
- VGGGPCQERPFHOB-MCIONIFRSA-N Bestatin Chemical compound CC(C)C[C@H](C(O)=O)NC(=O)[C@@H](O)[C@H](N)CC1=CC=CC=C1 VGGGPCQERPFHOB-MCIONIFRSA-N 0.000 description 1
- VGGGPCQERPFHOB-UHFFFAOYSA-N Bestatin Natural products CC(C)CC(C(O)=O)NC(=O)C(O)C(N)CC1=CC=CC=C1 VGGGPCQERPFHOB-UHFFFAOYSA-N 0.000 description 1
- 101710129634 Beta-nerve growth factor Proteins 0.000 description 1
- 108010074051 C-Reactive Protein Proteins 0.000 description 1
- 102100036150 C-X-C motif chemokine 5 Human genes 0.000 description 1
- 102100032752 C-reactive protein Human genes 0.000 description 1
- 108010021064 CTLA-4 Antigen Proteins 0.000 description 1
- 229940045513 CTLA4 antagonist Drugs 0.000 description 1
- 101100510617 Caenorhabditis elegans sel-8 gene Proteins 0.000 description 1
- 108010032088 Calpain Proteins 0.000 description 1
- 102000007590 Calpain Human genes 0.000 description 1
- 102000003900 Calpain-2 Human genes 0.000 description 1
- 108090000232 Calpain-2 Proteins 0.000 description 1
- 229920002134 Carboxymethyl cellulose Polymers 0.000 description 1
- 102000000496 Carboxypeptidases A Human genes 0.000 description 1
- 108010080937 Carboxypeptidases A Proteins 0.000 description 1
- 102100035904 Caspase-1 Human genes 0.000 description 1
- 108090000426 Caspase-1 Proteins 0.000 description 1
- 108010075016 Ceruloplasmin Proteins 0.000 description 1
- 102100023321 Ceruloplasmin Human genes 0.000 description 1
- 102000019034 Chemokines Human genes 0.000 description 1
- 108010012236 Chemokines Proteins 0.000 description 1
- 241000193403 Clostridium Species 0.000 description 1
- 102100029117 Coagulation factor X Human genes 0.000 description 1
- 108091026890 Coding region Proteins 0.000 description 1
- 102000012422 Collagen Type I Human genes 0.000 description 1
- 108010022452 Collagen Type I Proteins 0.000 description 1
- 102000000503 Collagen Type II Human genes 0.000 description 1
- 108010041390 Collagen Type II Proteins 0.000 description 1
- 102000004266 Collagen Type IV Human genes 0.000 description 1
- 108010042086 Collagen Type IV Proteins 0.000 description 1
- 108700040183 Complement C1 Inhibitor Proteins 0.000 description 1
- 102000055157 Complement C1 Inhibitor Human genes 0.000 description 1
- 206010056370 Congestive cardiomyopathy Diseases 0.000 description 1
- RYGMFSIKBFXOCR-UHFFFAOYSA-N Copper Chemical compound [Cu] RYGMFSIKBFXOCR-UHFFFAOYSA-N 0.000 description 1
- 241000195493 Cryptophyta Species 0.000 description 1
- PMATZTZNYRCHOR-CGLBZJNRSA-N Cyclosporin A Chemical compound CC[C@@H]1NC(=O)[C@H]([C@H](O)[C@H](C)C\C=C\C)N(C)C(=O)[C@H](C(C)C)N(C)C(=O)[C@H](CC(C)C)N(C)C(=O)[C@H](CC(C)C)N(C)C(=O)[C@@H](C)NC(=O)[C@H](C)NC(=O)[C@H](CC(C)C)N(C)C(=O)[C@H](C(C)C)NC(=O)[C@H](CC(C)C)N(C)C(=O)CN(C)C1=O PMATZTZNYRCHOR-CGLBZJNRSA-N 0.000 description 1
- 108010036949 Cyclosporine Proteins 0.000 description 1
- 201000003883 Cystic fibrosis Diseases 0.000 description 1
- 102000004127 Cytokines Human genes 0.000 description 1
- 108090000695 Cytokines Proteins 0.000 description 1
- 102100039498 Cytotoxic T-lymphocyte protein 4 Human genes 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
- 102000053602 DNA Human genes 0.000 description 1
- 102000052510 DNA-Binding Proteins Human genes 0.000 description 1
- 108700020911 DNA-Binding Proteins Proteins 0.000 description 1
- 238000009007 Diagnostic Kit Methods 0.000 description 1
- 201000010046 Dilated cardiomyopathy Diseases 0.000 description 1
- 101800001224 Disintegrin Proteins 0.000 description 1
- 241000255581 Drosophila <fruit fly, genus> Species 0.000 description 1
- 101100379225 Drosophila melanogaster cass gene Proteins 0.000 description 1
- 206010059866 Drug resistance Diseases 0.000 description 1
- 229940122858 Elastase inhibitor Drugs 0.000 description 1
- IJWCGVPEDDQUDE-UHFFFAOYSA-N Elastatinal Natural products O=CC(C)NC(=O)C(CCC(N)=O)NC(=O)C(NC(=O)NC(CC(C)C)C(O)=O)C1CCN=C(N)N1 IJWCGVPEDDQUDE-UHFFFAOYSA-N 0.000 description 1
- 241000196324 Embryophyta Species 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
- 102000010834 Extracellular Matrix Proteins Human genes 0.000 description 1
- 108010037362 Extracellular Matrix Proteins Proteins 0.000 description 1
- 208000004248 Familial Primary Pulmonary Hypertension Diseases 0.000 description 1
- 102000003971 Fibroblast Growth Factor 1 Human genes 0.000 description 1
- 108090000386 Fibroblast Growth Factor 1 Proteins 0.000 description 1
- 241000724791 Filamentous phage Species 0.000 description 1
- 108010010803 Gelatin Proteins 0.000 description 1
- 108700028146 Genetic Enhancer Elements Proteins 0.000 description 1
- 241000251152 Ginglymostoma cirratum Species 0.000 description 1
- 102000003886 Glycoproteins Human genes 0.000 description 1
- 108090000288 Glycoproteins Proteins 0.000 description 1
- 208000009329 Graft vs Host Disease Diseases 0.000 description 1
- 102000009465 Growth Factor Receptors Human genes 0.000 description 1
- 108010009202 Growth Factor Receptors Proteins 0.000 description 1
- 101150009006 HIS3 gene Proteins 0.000 description 1
- 102000001554 Hemoglobins Human genes 0.000 description 1
- 108010054147 Hemoglobins Proteins 0.000 description 1
- HTTJABKRGRZYRN-UHFFFAOYSA-N Heparin Chemical compound OC1C(NC(=O)C)C(O)OC(COS(O)(=O)=O)C1OC1C(OS(O)(=O)=O)C(O)C(OC2C(C(OS(O)(=O)=O)C(OC3C(C(O)C(O)C(O3)C(O)=O)OS(O)(=O)=O)C(CO)O2)NS(O)(=O)=O)C(C(O)=O)O1 HTTJABKRGRZYRN-UHFFFAOYSA-N 0.000 description 1
- 102000009824 Hepatocyte Nuclear Factor 1-alpha Human genes 0.000 description 1
- 108010020382 Hepatocyte Nuclear Factor 1-alpha Proteins 0.000 description 1
- 241000238631 Hexapoda Species 0.000 description 1
- 101000947186 Homo sapiens C-X-C motif chemokine 5 Proteins 0.000 description 1
- 101001076292 Homo sapiens Insulin-like growth factor II Proteins 0.000 description 1
- 101000891579 Homo sapiens Microtubule-associated protein tau Proteins 0.000 description 1
- 101000797623 Homo sapiens Protein AMBP Proteins 0.000 description 1
- 101000934346 Homo sapiens T-cell surface antigen CD2 Proteins 0.000 description 1
- 101000716102 Homo sapiens T-cell surface glycoprotein CD4 Proteins 0.000 description 1
- 102000008100 Human Serum Albumin Human genes 0.000 description 1
- 108091006905 Human Serum Albumin Proteins 0.000 description 1
- 206010020751 Hypersensitivity Diseases 0.000 description 1
- 101150088952 IGF1 gene Proteins 0.000 description 1
- DGAQECJNVWCQMB-PUAWFVPOSA-M Ilexoside XXIX Chemical compound C[C@@H]1CC[C@@]2(CC[C@@]3(C(=CC[C@H]4[C@]3(CC[C@@H]5[C@@]4(CC[C@@H](C5(C)C)OS(=O)(=O)[O-])C)C)[C@@H]2[C@]1(C)O)C)C(=O)O[C@H]6[C@@H]([C@H]([C@@H]([C@H](O6)CO)O)O)O.[Na+] DGAQECJNVWCQMB-PUAWFVPOSA-M 0.000 description 1
- 102000001706 Immunoglobulin Fab Fragments Human genes 0.000 description 1
- 108010054477 Immunoglobulin Fab Fragments Proteins 0.000 description 1
- 102000013463 Immunoglobulin Light Chains Human genes 0.000 description 1
- 108010065825 Immunoglobulin Light Chains Proteins 0.000 description 1
- 206010062717 Increased upper airway secretion Diseases 0.000 description 1
- 102000048143 Insulin-Like Growth Factor II Human genes 0.000 description 1
- 108090001117 Insulin-Like Growth Factor II Proteins 0.000 description 1
- 102100025947 Insulin-like growth factor II Human genes 0.000 description 1
- 102100037850 Interferon gamma Human genes 0.000 description 1
- 108010074328 Interferon-gamma Proteins 0.000 description 1
- 108010002386 Interleukin-3 Proteins 0.000 description 1
- 102000000646 Interleukin-3 Human genes 0.000 description 1
- 108010002616 Interleukin-5 Proteins 0.000 description 1
- 108010076876 Keratins Proteins 0.000 description 1
- 102000011782 Keratins Human genes 0.000 description 1
- KDXKERNSBIXSRK-YFKPBYRVSA-N L-lysine Chemical compound NCCCC[C@H](N)C(O)=O KDXKERNSBIXSRK-YFKPBYRVSA-N 0.000 description 1
- GUBGYTABKSRVRQ-QKKXKWKRSA-N Lactose Natural products OC[C@H]1O[C@@H](O[C@H]2[C@H](O)[C@@H](O)C(O)O[C@@H]2CO)[C@H](O)[C@@H](O)[C@H]1O GUBGYTABKSRVRQ-QKKXKWKRSA-N 0.000 description 1
- 102000007547 Laminin Human genes 0.000 description 1
- 108010085895 Laminin Proteins 0.000 description 1
- 108010092277 Leptin Proteins 0.000 description 1
- 102000016267 Leptin Human genes 0.000 description 1
- 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 1
- 102000019298 Lipocalin Human genes 0.000 description 1
- 108050006654 Lipocalin Proteins 0.000 description 1
- 108010033266 Lipoprotein(a) Proteins 0.000 description 1
- 206010025102 Lung infiltration Diseases 0.000 description 1
- 101710126949 Lysin Proteins 0.000 description 1
- 239000004472 Lysine Substances 0.000 description 1
- 208000029001 Mediastinal disease Diseases 0.000 description 1
- 206010027406 Mesothelioma Diseases 0.000 description 1
- 206010027476 Metastases Diseases 0.000 description 1
- 101100165554 Mus musculus Bmp5 gene Proteins 0.000 description 1
- 108010083674 Myelin Proteins Proteins 0.000 description 1
- 102000006386 Myelin Proteins Human genes 0.000 description 1
- 102100031789 Myeloid-derived growth factor Human genes 0.000 description 1
- 102100030856 Myoglobin Human genes 0.000 description 1
- 108010062374 Myoglobin Proteins 0.000 description 1
- GHAZCVNUKKZTLG-UHFFFAOYSA-N N-ethyl-succinimide Natural products CCN1C(=O)CCC1=O GHAZCVNUKKZTLG-UHFFFAOYSA-N 0.000 description 1
- HDFGOPSGAURCEO-UHFFFAOYSA-N N-ethylmaleimide Chemical compound CCN1C(=O)C=CC1=O HDFGOPSGAURCEO-UHFFFAOYSA-N 0.000 description 1
- MQUQNUAYKLCRME-INIZCTEOSA-N N-tosyl-L-phenylalanyl chloromethyl ketone Chemical compound C1=CC(C)=CC=C1S(=O)(=O)N[C@H](C(=O)CCl)CC1=CC=CC=C1 MQUQNUAYKLCRME-INIZCTEOSA-N 0.000 description 1
- 101710117081 Neutrophil defensin 1 Proteins 0.000 description 1
- 102100029494 Neutrophil defensin 1 Human genes 0.000 description 1
- 102400001060 Neutrophil defensin 2 Human genes 0.000 description 1
- 101710117153 Neutrophil defensin 2 Proteins 0.000 description 1
- 102100024761 Neutrophil defensin 3 Human genes 0.000 description 1
- 101710117152 Neutrophil defensin 3 Proteins 0.000 description 1
- 206010029443 Nocardia Infections Diseases 0.000 description 1
- 102000007990 Organic Anion Transporters Human genes 0.000 description 1
- 108010089503 Organic Anion Transporters Proteins 0.000 description 1
- 102000008108 Osteoprotegerin Human genes 0.000 description 1
- 108010035042 Osteoprotegerin Proteins 0.000 description 1
- 101710126321 Pancreatic trypsin inhibitor Proteins 0.000 description 1
- 206010033892 Paraplegia Diseases 0.000 description 1
- 241001494479 Pecora Species 0.000 description 1
- 239000001888 Peptone Substances 0.000 description 1
- 108010080698 Peptones Proteins 0.000 description 1
- 241000286209 Phasianidae Species 0.000 description 1
- 244000082204 Phyllostachys viridis Species 0.000 description 1
- 235000015334 Phyllostachys viridis Nutrition 0.000 description 1
- 108010051456 Plasminogen Proteins 0.000 description 1
- 102100038124 Plasminogen Human genes 0.000 description 1
- 208000002151 Pleural effusion Diseases 0.000 description 1
- 208000035109 Pneumococcal Infections Diseases 0.000 description 1
- 239000002202 Polyethylene glycol Substances 0.000 description 1
- 102000007584 Prealbumin Human genes 0.000 description 1
- 108010071690 Prealbumin Proteins 0.000 description 1
- 108010015078 Pregnancy-Associated alpha 2-Macroglobulins Proteins 0.000 description 1
- 108091000054 Prion Proteins 0.000 description 1
- 108010059712 Pronase Proteins 0.000 description 1
- 102100032859 Protein AMBP Human genes 0.000 description 1
- 108010029485 Protein Isoforms Proteins 0.000 description 1
- 102000001708 Protein Isoforms Human genes 0.000 description 1
- 101710098761 Protein alpha-1 Proteins 0.000 description 1
- 101710150593 Protein beta Proteins 0.000 description 1
- 208000010378 Pulmonary Embolism Diseases 0.000 description 1
- 206010064911 Pulmonary arterial hypertension Diseases 0.000 description 1
- 206010037423 Pulmonary oedema Diseases 0.000 description 1
- 108020004511 Recombinant DNA Proteins 0.000 description 1
- 108020005091 Replication Origin Proteins 0.000 description 1
- 206010039085 Rhinitis allergic Diseases 0.000 description 1
- 101100394989 Rhodopseudomonas palustris (strain ATCC BAA-98 / CGA009) hisI gene Proteins 0.000 description 1
- 241000283984 Rodentia Species 0.000 description 1
- 102400001107 Secretory component Human genes 0.000 description 1
- 229940122055 Serine protease inhibitor Drugs 0.000 description 1
- 101710102218 Serine protease inhibitor Proteins 0.000 description 1
- 108700028909 Serum Amyloid A Proteins 0.000 description 1
- 102000054727 Serum Amyloid A Human genes 0.000 description 1
- 108020004682 Single-Stranded DNA Proteins 0.000 description 1
- 238000003723 Smelting Methods 0.000 description 1
- 229920002472 Starch Polymers 0.000 description 1
- 108010090804 Streptavidin Proteins 0.000 description 1
- 210000001744 T-lymphocyte Anatomy 0.000 description 1
- 108010022394 Threonine synthase Proteins 0.000 description 1
- 102000007238 Transferrin Receptors Human genes 0.000 description 1
- 206010052779 Transplant rejections Diseases 0.000 description 1
- 108060005989 Tryptase Proteins 0.000 description 1
- 102000001400 Tryptase Human genes 0.000 description 1
- 229910052770 Uranium Inorganic materials 0.000 description 1
- GXBMIBRIOWHPDT-UHFFFAOYSA-N Vasopressin Natural products N1C(=O)C(CC=2C=C(O)C=CC=2)NC(=O)C(N)CSSCC(C(=O)N2C(CCC2)C(=O)NC(CCCN=C(N)N)C(=O)NCC(N)=O)NC(=O)C(CC(N)=O)NC(=O)C(CCC(N)=O)NC(=O)C1CC1=CC=CC=C1 GXBMIBRIOWHPDT-UHFFFAOYSA-N 0.000 description 1
- 108010004977 Vasopressins Proteins 0.000 description 1
- 102000002852 Vasopressins Human genes 0.000 description 1
- 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 1
- 239000012190 activator Substances 0.000 description 1
- 239000013543 active substance Substances 0.000 description 1
- 239000000654 additive Substances 0.000 description 1
- 239000002671 adjuvant Substances 0.000 description 1
- MGSKVZWGBWPBTF-UHFFFAOYSA-N aebsf Chemical compound NCCC1=CC=C(S(F)(=O)=O)C=C1 MGSKVZWGBWPBTF-UHFFFAOYSA-N 0.000 description 1
- 230000009824 affinity maturation Effects 0.000 description 1
- 230000001476 alcoholic effect Effects 0.000 description 1
- 229940072056 alginate Drugs 0.000 description 1
- 235000010443 alginic acid Nutrition 0.000 description 1
- 229920000615 alginic acid Polymers 0.000 description 1
- 201000009961 allergic asthma Diseases 0.000 description 1
- 201000010105 allergic rhinitis Diseases 0.000 description 1
- 230000007815 allergy Effects 0.000 description 1
- 230000033115 angiogenesis Effects 0.000 description 1
- 239000002870 angiogenesis inducing agent Substances 0.000 description 1
- 238000010171 animal model Methods 0.000 description 1
- 235000021120 animal protein Nutrition 0.000 description 1
- 230000003042 antagnostic effect Effects 0.000 description 1
- 230000008485 antagonism Effects 0.000 description 1
- 230000002744 anti-aggregatory effect Effects 0.000 description 1
- 229940121363 anti-inflammatory agent Drugs 0.000 description 1
- 239000002260 anti-inflammatory agent Substances 0.000 description 1
- 239000000868 anti-mullerian hormone Substances 0.000 description 1
- 230000000890 antigenic effect Effects 0.000 description 1
- 239000003963 antioxidant agent Substances 0.000 description 1
- 235000006708 antioxidants Nutrition 0.000 description 1
- SDNYTAYICBFYFH-TUFLPTIASA-N antipain Chemical compound NC(N)=NCCC[C@@H](C=O)NC(=O)[C@H](C(C)C)NC(=O)[C@H](CCCN=C(N)N)NC(=O)N[C@H](C(O)=O)CC1=CC=CC=C1 SDNYTAYICBFYFH-TUFLPTIASA-N 0.000 description 1
- 108010026054 apolipoprotein SAA Proteins 0.000 description 1
- 238000013459 approach Methods 0.000 description 1
- 229960004405 aprotinin Drugs 0.000 description 1
- 239000007864 aqueous solution Substances 0.000 description 1
- KBZOIRJILGZLEJ-LGYYRGKSSA-N argipressin Chemical compound C([C@H]1C(=O)N[C@@H](CCC(N)=O)C(=O)N[C@@H](CC(N)=O)C(=O)N[C@@H](CSSC[C@@H](C(N[C@@H](CC=2C=CC(O)=CC=2)C(=O)N1)=O)N)C(=O)N1[C@@H](CCC1)C(=O)N[C@@H](CCCN=C(N)N)C(=O)NCC(N)=O)C1=CC=CC=C1 KBZOIRJILGZLEJ-LGYYRGKSSA-N 0.000 description 1
- 230000002917 arthritic effect Effects 0.000 description 1
- 210000004507 artificial chromosome Anatomy 0.000 description 1
- 206010003441 asbestosis Diseases 0.000 description 1
- 229940072107 ascorbate Drugs 0.000 description 1
- 235000010323 ascorbic acid Nutrition 0.000 description 1
- 239000011668 ascorbic acid Substances 0.000 description 1
- IAOZJIPTCAWIRG-QWRGUYRKSA-N aspartame Chemical compound OC(=O)C[C@H](N)C(=O)N[C@H](C(=O)OC)CC1=CC=CC=C1 IAOZJIPTCAWIRG-QWRGUYRKSA-N 0.000 description 1
- 239000000605 aspartame Substances 0.000 description 1
- 235000010357 aspartame Nutrition 0.000 description 1
- 229960003438 aspartame Drugs 0.000 description 1
- 229940009098 aspartate Drugs 0.000 description 1
- 235000003704 aspartic acid Nutrition 0.000 description 1
- 239000005667 attractant Substances 0.000 description 1
- 229940120638 avastin Drugs 0.000 description 1
- 238000002819 bacterial display Methods 0.000 description 1
- 239000013602 bacteriophage vector Substances 0.000 description 1
- 241000385736 bacterium B Species 0.000 description 1
- 239000011425 bamboo Substances 0.000 description 1
- 230000009286 beneficial effect Effects 0.000 description 1
- 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 1
- 102000012265 beta-defensin Human genes 0.000 description 1
- 108050002883 beta-defensin Proteins 0.000 description 1
- 229960000397 bevacizumab Drugs 0.000 description 1
- 238000002306 biochemical method Methods 0.000 description 1
- 230000000903 blocking effect Effects 0.000 description 1
- 230000008499 blood brain barrier function Effects 0.000 description 1
- 230000017531 blood circulation Effects 0.000 description 1
- 210000004204 blood vessel Anatomy 0.000 description 1
- 210000001218 blood-brain barrier Anatomy 0.000 description 1
- 230000037396 body weight Effects 0.000 description 1
- 210000004781 brain capillary Anatomy 0.000 description 1
- GEHJBWKLJVFKPS-UHFFFAOYSA-N bromochloroacetic acid Chemical compound OC(=O)C(Cl)Br GEHJBWKLJVFKPS-UHFFFAOYSA-N 0.000 description 1
- 201000009267 bronchiectasis Diseases 0.000 description 1
- 230000003139 buffering effect Effects 0.000 description 1
- 238000004422 calculation algorithm Methods 0.000 description 1
- 239000004202 carbamide Substances 0.000 description 1
- 150000001720 carbohydrates Chemical class 0.000 description 1
- 235000014633 carbohydrates Nutrition 0.000 description 1
- 239000001768 carboxy methyl cellulose Substances 0.000 description 1
- 235000010948 carboxy methyl cellulose Nutrition 0.000 description 1
- 239000008112 carboxymethyl-cellulose Substances 0.000 description 1
- 230000000747 cardiac effect Effects 0.000 description 1
- 210000000845 cartilage Anatomy 0.000 description 1
- 238000006555 catalytic reaction Methods 0.000 description 1
- 238000000423 cell based assay Methods 0.000 description 1
- 238000004113 cell culture Methods 0.000 description 1
- 230000001413 cellular effect Effects 0.000 description 1
- 238000005119 centrifugation Methods 0.000 description 1
- 239000003610 charcoal Substances 0.000 description 1
- 239000002738 chelating agent Substances 0.000 description 1
- SFZULDYEOVSIKM-UHFFFAOYSA-N chembl321317 Chemical compound C1=CC(C(=N)NO)=CC=C1C1=CC=C(C=2C=CC(=CC=2)C(=N)NO)O1 SFZULDYEOVSIKM-UHFFFAOYSA-N 0.000 description 1
- 239000002975 chemoattractant Substances 0.000 description 1
- 230000031902 chemoattractant activity Effects 0.000 description 1
- 208000037976 chronic inflammation Diseases 0.000 description 1
- 208000037893 chronic inflammatory disorder Diseases 0.000 description 1
- 229960001265 ciclosporin Drugs 0.000 description 1
- 230000004087 circulation Effects 0.000 description 1
- DQLATGHUWYMOKM-UHFFFAOYSA-L cisplatin Chemical compound N[Pt](N)(Cl)Cl DQLATGHUWYMOKM-UHFFFAOYSA-L 0.000 description 1
- 229960004316 cisplatin Drugs 0.000 description 1
- 230000015271 coagulation Effects 0.000 description 1
- 238000005345 coagulation Methods 0.000 description 1
- 229940105756 coagulation factor x Drugs 0.000 description 1
- 230000002860 competitive effect Effects 0.000 description 1
- 239000002299 complementary DNA Substances 0.000 description 1
- 230000000536 complexating effect Effects 0.000 description 1
- 230000001276 controlling effect Effects 0.000 description 1
- 229910052802 copper Inorganic materials 0.000 description 1
- 239000010949 copper Substances 0.000 description 1
- 210000004087 cornea Anatomy 0.000 description 1
- 238000012937 correction Methods 0.000 description 1
- 239000003246 corticosteroid Substances 0.000 description 1
- 229960001334 corticosteroids Drugs 0.000 description 1
- 238000004132 cross linking Methods 0.000 description 1
- 229930182912 cyclosporin Natural products 0.000 description 1
- 102000003675 cytokine receptors Human genes 0.000 description 1
- 108010057085 cytokine receptors Proteins 0.000 description 1
- 230000001086 cytosolic effect Effects 0.000 description 1
- 231100000433 cytotoxic Toxicity 0.000 description 1
- 230000001472 cytotoxic effect Effects 0.000 description 1
- 230000007547 defect Effects 0.000 description 1
- 230000003111 delayed effect Effects 0.000 description 1
- 238000001514 detection method Methods 0.000 description 1
- 238000011161 development Methods 0.000 description 1
- 239000000032 diagnostic agent Substances 0.000 description 1
- 229940039227 diagnostic agent Drugs 0.000 description 1
- 208000012059 diaphragm disease Diseases 0.000 description 1
- 235000015872 dietary supplement Nutrition 0.000 description 1
- 238000009792 diffusion process Methods 0.000 description 1
- 102000004419 dihydrofolate reductase Human genes 0.000 description 1
- MUCZHBLJLSDCSD-UHFFFAOYSA-N diisopropyl fluorophosphate Chemical compound CC(C)OP(F)(=O)OC(C)C MUCZHBLJLSDCSD-UHFFFAOYSA-N 0.000 description 1
- 230000006806 disease prevention Effects 0.000 description 1
- 238000004090 dissolution Methods 0.000 description 1
- 229960004679 doxorubicin Drugs 0.000 description 1
- 239000006196 drop Substances 0.000 description 1
- 210000002969 egg yolk Anatomy 0.000 description 1
- 235000013345 egg yolk Nutrition 0.000 description 1
- 239000003602 elastase inhibitor Substances 0.000 description 1
- 108010039262 elastatinal Proteins 0.000 description 1
- 239000003792 electrolyte Substances 0.000 description 1
- 238000004520 electroporation Methods 0.000 description 1
- 210000002889 endothelial cell Anatomy 0.000 description 1
- 239000003623 enhancer Substances 0.000 description 1
- 231100000655 enterotoxin Toxicity 0.000 description 1
- 230000007613 environmental effect Effects 0.000 description 1
- 230000002255 enzymatic effect Effects 0.000 description 1
- 229940125532 enzyme inhibitor Drugs 0.000 description 1
- 210000000222 eosinocyte Anatomy 0.000 description 1
- 230000002327 eosinophilic effect Effects 0.000 description 1
- 201000009580 eosinophilic pneumonia Diseases 0.000 description 1
- 102000052116 epidermal growth factor receptor activity proteins Human genes 0.000 description 1
- 108700015053 epidermal growth factor receptor activity proteins Proteins 0.000 description 1
- 102000015694 estrogen receptors Human genes 0.000 description 1
- 108010038795 estrogen receptors Proteins 0.000 description 1
- 210000003527 eukaryotic cell Anatomy 0.000 description 1
- 238000011156 evaluation Methods 0.000 description 1
- 229940014425 exodus Drugs 0.000 description 1
- 238000002474 experimental method Methods 0.000 description 1
- 208000030533 eye disease Diseases 0.000 description 1
- 239000000835 fiber Substances 0.000 description 1
- 229940029303 fibroblast growth factor-1 Drugs 0.000 description 1
- POTUGHMKJGOKRI-UHFFFAOYSA-N ficin Chemical compound FI=CI=N POTUGHMKJGOKRI-UHFFFAOYSA-N 0.000 description 1
- 230000005714 functional activity Effects 0.000 description 1
- 238000002825 functional assay Methods 0.000 description 1
- 125000000524 functional group Chemical group 0.000 description 1
- BTCSSZJGUNDROE-UHFFFAOYSA-N gamma-aminobutyric acid Chemical compound NCCCC(O)=O BTCSSZJGUNDROE-UHFFFAOYSA-N 0.000 description 1
- 239000007789 gas Substances 0.000 description 1
- 238000001641 gel filtration chromatography Methods 0.000 description 1
- 239000008273 gelatin Substances 0.000 description 1
- 229920000159 gelatin Polymers 0.000 description 1
- 235000019322 gelatine Nutrition 0.000 description 1
- 235000011852 gelatine desserts Nutrition 0.000 description 1
- 238000002523 gelfiltration Methods 0.000 description 1
- 230000002068 genetic effect Effects 0.000 description 1
- 210000004907 gland Anatomy 0.000 description 1
- 239000008103 glucose Substances 0.000 description 1
- 229920000550 glycopolymer Polymers 0.000 description 1
- 208000024908 graft versus host disease Diseases 0.000 description 1
- 239000001307 helium Substances 0.000 description 1
- 229910052734 helium Inorganic materials 0.000 description 1
- SWQJXJOGLNCZEY-UHFFFAOYSA-N helium atom Chemical compound [He] SWQJXJOGLNCZEY-UHFFFAOYSA-N 0.000 description 1
- 229960002897 heparin Drugs 0.000 description 1
- 229920000669 heparin Polymers 0.000 description 1
- 230000006801 homologous recombination Effects 0.000 description 1
- 238000002744 homologous recombination Methods 0.000 description 1
- 102000054037 human AFG3L2 Human genes 0.000 description 1
- 102000057063 human MAPT Human genes 0.000 description 1
- 238000009396 hybridization Methods 0.000 description 1
- 230000002209 hydrophobic effect Effects 0.000 description 1
- 206010020718 hyperplasia Diseases 0.000 description 1
- 208000000122 hyperventilation Diseases 0.000 description 1
- 230000000870 hyperventilation Effects 0.000 description 1
- 230000002163 immunogen Effects 0.000 description 1
- 230000001024 immunotherapeutic effect Effects 0.000 description 1
- 238000009169 immunotherapy Methods 0.000 description 1
- 230000002637 immunotoxin Effects 0.000 description 1
- 239000002596 immunotoxin Substances 0.000 description 1
- 231100000608 immunotoxin Toxicity 0.000 description 1
- 229940051026 immunotoxin Drugs 0.000 description 1
- 239000007943 implant Substances 0.000 description 1
- 230000002779 inactivation Effects 0.000 description 1
- 238000010348 incorporation Methods 0.000 description 1
- 239000000411 inducer Substances 0.000 description 1
- 230000001939 inductive effect Effects 0.000 description 1
- 239000011261 inert gas Substances 0.000 description 1
- 230000002458 infectious effect Effects 0.000 description 1
- 238000001802 infusion Methods 0.000 description 1
- 230000003993 interaction Effects 0.000 description 1
- 229940076264 interleukin-3 Drugs 0.000 description 1
- 210000000936 intestine Anatomy 0.000 description 1
- 235000000396 iron Nutrition 0.000 description 1
- 229910052742 iron Inorganic materials 0.000 description 1
- 230000002262 irrigation Effects 0.000 description 1
- 238000003973 irrigation Methods 0.000 description 1
- 210000003734 kidney Anatomy 0.000 description 1
- 230000002147 killing effect Effects 0.000 description 1
- 239000008101 lactose Substances 0.000 description 1
- NRYBAZVQPHGZNS-ZSOCWYAHSA-N leptin Chemical compound O=C([C@H](CO)NC(=O)[C@H](CC(C)C)NC(=O)[C@H](CC(O)=O)NC(=O)[C@H](CC(C)C)NC(=O)[C@H](CCC(N)=O)NC(=O)[C@H](CC=1C2=CC=CC=C2NC=1)NC(=O)[C@H](CC(C)C)NC(=O)[C@@H](NC(=O)[C@H](CC(O)=O)NC(=O)[C@H](CCC(N)=O)NC(=O)[C@H](CC(C)C)NC(=O)[C@H](CO)NC(=O)CNC(=O)[C@H](CCC(N)=O)NC(=O)[C@@H](N)CC(C)C)CCSC)N1CCC[C@H]1C(=O)NCC(=O)N[C@@H](CS)C(O)=O NRYBAZVQPHGZNS-ZSOCWYAHSA-N 0.000 description 1
- 229940039781 leptin Drugs 0.000 description 1
- 208000032839 leukemia Diseases 0.000 description 1
- 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 1
- 108010052968 leupeptin Proteins 0.000 description 1
- 150000002632 lipids Chemical class 0.000 description 1
- 230000004807 localization Effects 0.000 description 1
- 230000007774 longterm Effects 0.000 description 1
- 210000003750 lower gastrointestinal tract Anatomy 0.000 description 1
- 210000004698 lymphocyte Anatomy 0.000 description 1
- 125000003588 lysine group Chemical group [H]N([H])C([H])([H])C([H])([H])C([H])([H])C([H])([H])C([H])(N([H])[H])C(*)=O 0.000 description 1
- 230000002101 lytic effect Effects 0.000 description 1
- 230000014759 maintenance of location Effects 0.000 description 1
- 235000013372 meat Nutrition 0.000 description 1
- 230000007246 mechanism Effects 0.000 description 1
- 239000012528 membrane Substances 0.000 description 1
- 239000002207 metabolite Substances 0.000 description 1
- 230000009401 metastasis Effects 0.000 description 1
- 229940071648 metered dose inhaler Drugs 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
- 235000013336 milk Nutrition 0.000 description 1
- 239000008267 milk Substances 0.000 description 1
- 210000004080 milk Anatomy 0.000 description 1
- 238000010369 molecular cloning Methods 0.000 description 1
- 230000000877 morphologic effect Effects 0.000 description 1
- 201000006417 multiple sclerosis Diseases 0.000 description 1
- 210000003205 muscle Anatomy 0.000 description 1
- 239000003471 mutagenic agent Substances 0.000 description 1
- 208000027531 mycobacterial infectious disease Diseases 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
- 210000005012 myelin Anatomy 0.000 description 1
- YFCUZWYIPBUQBD-ZOWNYOTGSA-N n-[(3s)-7-amino-1-chloro-2-oxoheptan-3-yl]-4-methylbenzenesulfonamide;hydron;chloride Chemical compound Cl.CC1=CC=C(S(=O)(=O)N[C@@H](CCCCN)C(=O)CCl)C=C1 YFCUZWYIPBUQBD-ZOWNYOTGSA-N 0.000 description 1
- YOHYSYJDKVYCJI-UHFFFAOYSA-N n-[3-[[6-[3-(trifluoromethyl)anilino]pyrimidin-4-yl]amino]phenyl]cyclopropanecarboxamide Chemical compound FC(F)(F)C1=CC=CC(NC=2N=CN=C(NC=3C=C(NC(=O)C4CC4)C=CC=3)C=2)=C1 YOHYSYJDKVYCJI-UHFFFAOYSA-N 0.000 description 1
- 230000010807 negative regulation of binding Effects 0.000 description 1
- 230000009826 neoplastic cell growth Effects 0.000 description 1
- 230000001537 neural effect Effects 0.000 description 1
- 210000003458 notochord Anatomy 0.000 description 1
- 239000002777 nucleoside Substances 0.000 description 1
- 125000003835 nucleoside group Chemical group 0.000 description 1
- 210000004940 nucleus Anatomy 0.000 description 1
- 235000016709 nutrition Nutrition 0.000 description 1
- XXUPLYBCNPLTIW-UHFFFAOYSA-N octadec-7-ynoic acid Chemical compound CCCCCCCCCCC#CCCCCCC(O)=O XXUPLYBCNPLTIW-UHFFFAOYSA-N 0.000 description 1
- 238000005457 optimization Methods 0.000 description 1
- 230000011164 ossification Effects 0.000 description 1
- 230000002188 osteogenic effect Effects 0.000 description 1
- 239000006174 pH buffer Substances 0.000 description 1
- 210000000496 pancreas Anatomy 0.000 description 1
- 230000036961 partial effect Effects 0.000 description 1
- 230000001717 pathogenic effect Effects 0.000 description 1
- 230000001575 pathological effect Effects 0.000 description 1
- 230000037361 pathway Effects 0.000 description 1
- 239000008188 pellet Substances 0.000 description 1
- 229950000964 pepstatin Drugs 0.000 description 1
- 108010091212 pepstatin Proteins 0.000 description 1
- 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 1
- 235000019319 peptone Nutrition 0.000 description 1
- 108700010839 phage proteins Proteins 0.000 description 1
- 210000000680 phagosome Anatomy 0.000 description 1
- 208000026435 phlegm Diseases 0.000 description 1
- 230000004962 physiological condition Effects 0.000 description 1
- 239000002504 physiological saline solution Substances 0.000 description 1
- 239000013612 plasmid Substances 0.000 description 1
- 206010035653 pneumoconiosis Diseases 0.000 description 1
- 229920000642 polymer Polymers 0.000 description 1
- 210000004896 polypeptide structure Anatomy 0.000 description 1
- 239000001267 polyvinylpyrrolidone Substances 0.000 description 1
- 229920000036 polyvinylpyrrolidone Polymers 0.000 description 1
- 235000013855 polyvinylpyrrolidone Nutrition 0.000 description 1
- 230000003389 potentiating effect Effects 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
- 201000008312 primary pulmonary hypertension Diseases 0.000 description 1
- 238000012545 processing Methods 0.000 description 1
- 230000002035 prolonged effect Effects 0.000 description 1
- 238000000159 protein binding assay Methods 0.000 description 1
- 208000005333 pulmonary edema Diseases 0.000 description 1
- 201000009732 pulmonary eosinophilia Diseases 0.000 description 1
- 208000005069 pulmonary fibrosis Diseases 0.000 description 1
- 208000002815 pulmonary hypertension Diseases 0.000 description 1
- 208000008128 pulmonary tuberculosis Diseases 0.000 description 1
- 238000005215 recombination Methods 0.000 description 1
- 230000006798 recombination Effects 0.000 description 1
- 238000004064 recycling Methods 0.000 description 1
- 230000022532 regulation of transcription, DNA-dependent Effects 0.000 description 1
- 230000000241 respiratory effect Effects 0.000 description 1
- 108091008146 restriction endonucleases Proteins 0.000 description 1
- 230000001177 retroviral effect Effects 0.000 description 1
- 206010039073 rheumatoid arthritis Diseases 0.000 description 1
- 208000021569 rheumatoid lung disease Diseases 0.000 description 1
- 150000003839 salts Chemical class 0.000 description 1
- 239000004576 sand Substances 0.000 description 1
- 238000007790 scraping Methods 0.000 description 1
- 239000006152 selective media Substances 0.000 description 1
- 238000002864 sequence alignment Methods 0.000 description 1
- 238000012163 sequencing technique Methods 0.000 description 1
- 230000009919 sequestration Effects 0.000 description 1
- UQDJGEHQDNVPGU-UHFFFAOYSA-N serine phosphoethanolamine Chemical compound [NH3+]CCOP([O-])(=O)OCC([NH3+])C([O-])=O UQDJGEHQDNVPGU-UHFFFAOYSA-N 0.000 description 1
- 239000003001 serine protease inhibitor Substances 0.000 description 1
- 229940076279 serotonin Drugs 0.000 description 1
- 208000015891 sexual disease Diseases 0.000 description 1
- 238000010008 shearing Methods 0.000 description 1
- 238000004088 simulation Methods 0.000 description 1
- 201000002859 sleep apnea Diseases 0.000 description 1
- 210000000813 small intestine Anatomy 0.000 description 1
- CBXWGGFGZDVPNV-UHFFFAOYSA-N so4-so4 Chemical compound OS(O)(=O)=O.OS(O)(=O)=O CBXWGGFGZDVPNV-UHFFFAOYSA-N 0.000 description 1
- 229910052708 sodium Inorganic materials 0.000 description 1
- 239000011734 sodium Substances 0.000 description 1
- 229910000029 sodium carbonate Inorganic materials 0.000 description 1
- 238000002415 sodium dodecyl sulfate polyacrylamide gel electrophoresis Methods 0.000 description 1
- 210000000952 spleen Anatomy 0.000 description 1
- 239000008107 starch Substances 0.000 description 1
- 235000019698 starch Nutrition 0.000 description 1
- 230000003637 steroidlike Effects 0.000 description 1
- 238000003860 storage Methods 0.000 description 1
- 238000007920 subcutaneous administration Methods 0.000 description 1
- 239000000758 substrate Substances 0.000 description 1
- 235000000346 sugar Nutrition 0.000 description 1
- 230000001629 suppression Effects 0.000 description 1
- 208000011580 syndromic disease Diseases 0.000 description 1
- 210000005222 synovial tissue Anatomy 0.000 description 1
- 230000001839 systemic circulation Effects 0.000 description 1
- 238000012385 systemic delivery Methods 0.000 description 1
- 230000009885 systemic effect Effects 0.000 description 1
- 239000003826 tablet Substances 0.000 description 1
- 101150118377 tet gene Proteins 0.000 description 1
- 239000004753 textile Substances 0.000 description 1
- 238000002560 therapeutic procedure Methods 0.000 description 1
- 230000008646 thermal stress Effects 0.000 description 1
- 239000002562 thickening agent Substances 0.000 description 1
- 230000000699 topical effect Effects 0.000 description 1
- 231100000331 toxic Toxicity 0.000 description 1
- 230000002588 toxic effect Effects 0.000 description 1
- 239000003053 toxin Substances 0.000 description 1
- 231100000765 toxin Toxicity 0.000 description 1
- 108700012359 toxins Proteins 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
- 230000009466 transformation Effects 0.000 description 1
- 239000013638 trimer Substances 0.000 description 1
- 230000005740 tumor formation Effects 0.000 description 1
- 229950009811 ubenimex Drugs 0.000 description 1
- 241000701447 unidentified baculovirus Species 0.000 description 1
- 210000002438 upper gastrointestinal tract Anatomy 0.000 description 1
- 230000003827 upregulation Effects 0.000 description 1
- 238000011144 upstream manufacturing Methods 0.000 description 1
- 229960003726 vasopressin Drugs 0.000 description 1
- 238000009423 ventilation Methods 0.000 description 1
- 108700026220 vif Genes Proteins 0.000 description 1
- 239000000052 vinegar Substances 0.000 description 1
- 235000021419 vinegar Nutrition 0.000 description 1
- 210000002845 virion Anatomy 0.000 description 1
- 230000009278 visceral effect Effects 0.000 description 1
- 210000004127 vitreous body Anatomy 0.000 description 1
- 238000012447 xenograft mouse model Methods 0.000 description 1
- 235000013618 yogurt Nutrition 0.000 description 1
- 101150069452 z gene Proteins 0.000 description 1
Classifications
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K16/00—Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies
- C07K16/005—Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies constructed by phage libraries
-
- 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
- C07K16/2878—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 NGF-receptor/TNF-receptor superfamily, e.g. CD27, CD30, CD40, CD95
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61K—PREPARATIONS FOR MEDICAL, DENTAL OR TOILETRY PURPOSES
- A61K9/00—Medicinal preparations characterised by special physical form
- A61K9/0012—Galenical forms characterised by the site of application
- A61K9/007—Pulmonary tract; Aromatherapy
- A61K9/0073—Sprays or powders for inhalation; Aerolised or nebulised preparations generated by other means than thermal energy
- A61K9/0078—Sprays or powders for inhalation; Aerolised or nebulised preparations generated by other means than thermal energy for inhalation via a nebulizer such as a jet nebulizer, ultrasonic nebulizer, e.g. in the form of aqueous drug solutions or dispersions
-
- 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
-
- 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
- A61P1/00—Drugs for disorders of the alimentary tract or the digestive system
- A61P1/06—Anti-spasmodics, e.g. drugs for colics, esophagic dyskinesia
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P11/00—Drugs for disorders of the respiratory system
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P11/00—Drugs for disorders of the respiratory system
- A61P11/02—Nasal agents, e.g. decongestants
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P11/00—Drugs for disorders of the respiratory system
- A61P11/06—Antiasthmatics
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P19/00—Drugs for skeletal disorders
- A61P19/02—Drugs for skeletal disorders for joint disorders, e.g. arthritis, arthrosis
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P25/00—Drugs for disorders of the nervous system
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P27/00—Drugs for disorders of the senses
- A61P27/02—Ophthalmic agents
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P27/00—Drugs for disorders of the senses
- A61P27/02—Ophthalmic agents
- A61P27/04—Artificial tears; Irrigation solutions
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P27/00—Drugs for disorders of the senses
- A61P27/02—Ophthalmic agents
- A61P27/06—Antiglaucoma agents or miotics
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P29/00—Non-central analgesic, antipyretic or antiinflammatory agents, e.g. antirheumatic agents; Non-steroidal antiinflammatory drugs [NSAID]
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P31/00—Antiinfectives, i.e. antibiotics, antiseptics, chemotherapeutics
- A61P31/04—Antibacterial agents
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P31/00—Antiinfectives, i.e. antibiotics, antiseptics, chemotherapeutics
- A61P31/04—Antibacterial agents
- A61P31/06—Antibacterial agents for tuberculosis
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P31/00—Antiinfectives, i.e. antibiotics, antiseptics, chemotherapeutics
- A61P31/12—Antivirals
- A61P31/14—Antivirals for RNA viruses
- A61P31/16—Antivirals for RNA viruses for influenza or rhinoviruses
-
- 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
- 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
- A61P37/00—Drugs for immunological or allergic disorders
- A61P37/02—Immunomodulators
-
- 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
- A61P37/02—Immunomodulators
- A61P37/06—Immunosuppressants, e.g. drugs for graft rejection
-
- 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
- A61P37/08—Antiallergic agents
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P39/00—General protective or antinoxious agents
-
- 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
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P7/00—Drugs for disorders of the blood or the extracellular fluid
- A61P7/02—Antithrombotic agents; Anticoagulants; Platelet aggregation inhibitors
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P9/00—Drugs for disorders of the cardiovascular system
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P9/00—Drugs for disorders of the cardiovascular system
- A61P9/12—Antihypertensives
-
- 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
- C07K16/22—Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies against material from animals or humans against growth factors ; against growth regulators
-
- 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
- C07K16/2866—Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies against material from animals or humans against receptors, cell surface antigens or cell surface determinants against receptors for cytokines, lymphokines, interferons
-
- 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
- A61K2039/54—Medicinal preparations containing antigens or antibodies characterised by the route of administration
- A61K2039/541—Mucosal route
- A61K2039/543—Mucosal route intranasal
-
- 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
- A61K2039/54—Medicinal preparations containing antigens or antibodies characterised by the route of administration
- A61K2039/541—Mucosal route
- A61K2039/544—Mucosal route to the airways
-
- 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
- C07K2317/50—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
- C07K2317/567—Framework region [FR]
-
- 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
- C07K2317/569—Single domain, e.g. dAb, sdAb, VHH, VNAR or nanobody®
-
- 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
- C07K2317/76—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
-
- 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
-
- 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
- C07K2317/94—Stability, e.g. half-life, pH, temperature or enzyme-resistance
Landscapes
- Health & Medical Sciences (AREA)
- Chemical & Material Sciences (AREA)
- Organic Chemistry (AREA)
- Life Sciences & Earth Sciences (AREA)
- Medicinal Chemistry (AREA)
- General Health & Medical Sciences (AREA)
- Pharmacology & Pharmacy (AREA)
- Animal Behavior & Ethology (AREA)
- Public Health (AREA)
- Veterinary Medicine (AREA)
- Chemical Kinetics & Catalysis (AREA)
- General Chemical & Material Sciences (AREA)
- Nuclear Medicine, Radiotherapy & Molecular Imaging (AREA)
- Immunology (AREA)
- Bioinformatics & Cheminformatics (AREA)
- Engineering & Computer Science (AREA)
- Molecular Biology (AREA)
- Biochemistry (AREA)
- Proteomics, Peptides & Aminoacids (AREA)
- Genetics & Genomics (AREA)
- Biophysics (AREA)
- Pulmonology (AREA)
- Virology (AREA)
- Ophthalmology & Optometry (AREA)
- Communicable Diseases (AREA)
- Oncology (AREA)
- Otolaryngology (AREA)
- Rheumatology (AREA)
- Heart & Thoracic Surgery (AREA)
- Epidemiology (AREA)
- Dispersion Chemistry (AREA)
- Cardiology (AREA)
- Toxicology (AREA)
- Neurosurgery (AREA)
- Orthopedic Medicine & Surgery (AREA)
- Physical Education & Sports Medicine (AREA)
- Transplantation (AREA)
- Diabetes (AREA)
- Hematology (AREA)
- Pain & Pain Management (AREA)
Applications Claiming Priority (2)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| US93363207P | 2007-06-06 | 2007-06-06 | |
| GBGB0724331.4A GB0724331D0 (en) | 2007-12-13 | 2007-12-13 | Compositions for pulmonary delivery |
Publications (1)
| Publication Number | Publication Date |
|---|---|
| TW200911832A true TW200911832A (en) | 2009-03-16 |
Family
ID=39791116
Family Applications (6)
| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| TW097121295A TW200911832A (en) | 2007-06-06 | 2008-06-06 | Polypeptides, antibody variable domains & antagonists |
| TW097121301A TW200918088A (en) | 2007-06-06 | 2008-06-06 | Polypeptides, antibody variable domains & antagonists |
| TW097121265A TW200911834A (en) | 2007-06-06 | 2008-06-06 | Polypeptides, antibody variable domains & antagonists |
| TW097121268A TW200911831A (en) | 2007-06-06 | 2008-06-06 | Polypeptides, antibody variable domains & antagonists |
| TW097121280A TW200907128A (en) | 2007-06-06 | 2008-06-06 | Methods for selecting protease resistant polypeptides |
| TW097121296A TW200902551A (en) | 2007-06-06 | 2008-06-06 | Polypeptides, antibody variable domains & antagonists |
Family Applications After (5)
| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| TW097121301A TW200918088A (en) | 2007-06-06 | 2008-06-06 | Polypeptides, antibody variable domains & antagonists |
| TW097121265A TW200911834A (en) | 2007-06-06 | 2008-06-06 | Polypeptides, antibody variable domains & antagonists |
| TW097121268A TW200911831A (en) | 2007-06-06 | 2008-06-06 | Polypeptides, antibody variable domains & antagonists |
| TW097121280A TW200907128A (en) | 2007-06-06 | 2008-06-06 | Methods for selecting protease resistant polypeptides |
| TW097121296A TW200902551A (en) | 2007-06-06 | 2008-06-06 | Polypeptides, antibody variable domains & antagonists |
Country Status (31)
Families Citing this family (66)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| JP2005289809A (ja) | 2001-10-24 | 2005-10-20 | Vlaams Interuniversitair Inst Voor Biotechnologie Vzw (Vib Vzw) | 突然変異重鎖抗体 |
| DK1888641T3 (da) | 2005-05-18 | 2012-04-23 | Ablynx Nv | Serumalbuminbindende proteiner |
| DE102005023617A1 (de) | 2005-05-21 | 2006-11-23 | Aspre Ag | Verfahren zum Mischen von Farben in einem Display |
| GB0724331D0 (en) | 2007-12-13 | 2008-01-23 | Domantis Ltd | Compositions for pulmonary delivery |
| JP2010528647A (ja) * | 2007-06-06 | 2010-08-26 | ドマンティス リミテッド | ポリペプチド、抗体可変ドメインおよびアンタゴニスト |
| CA2688434A1 (en) | 2007-06-06 | 2008-12-11 | Domantis Limited | Polypeptides, antibody variable domains and antagonists |
| TW200938222A (en) * | 2007-12-13 | 2009-09-16 | Glaxo Group Ltd | Compositions for pulmonary delivery |
| JP2011516603A (ja) | 2008-04-17 | 2011-05-26 | アブリンクス エン.ヴェー. | 血清タンパク質と結合することが可能なペプチド、並びにこれを含む化合物、構築物及びポリペプチド |
| SI3722310T1 (sl) | 2008-06-25 | 2025-01-31 | Novartis Ag | Stabilna in topna protitelesa, ki zavirajo vegf |
| US8268314B2 (en) | 2008-10-08 | 2012-09-18 | Hoffmann-La Roche Inc. | Bispecific anti-VEGF/anti-ANG-2 antibodies |
| CA2744055A1 (en) * | 2008-11-26 | 2010-06-03 | Glaxo Group Limited | Polypeptides, antibody variable domains & antagonists |
| WO2010081787A1 (en) | 2009-01-14 | 2010-07-22 | Domantis Limited | IMPROVED TNFα ANTAGONISM, PROPHYLAXIS & THERAPY WITH REDUCED ORGAN NECROSIS |
| ES2654929T3 (es) * | 2009-02-19 | 2018-02-15 | Glaxo Group Limited | Variantes de unión de anti-albúmina de suero mejoradas |
| CA2750477A1 (en) | 2009-02-19 | 2010-08-26 | Stephen Duffield | Improved anti-tnfr1 polypeptides, antibody variable domains & antagonists |
| EA028178B1 (ru) * | 2009-02-19 | 2017-10-31 | Глэксо Груп Лимитед | Улучшенные связывающие сывороточный альбумин варианты |
| EP2401298A1 (en) | 2009-02-24 | 2012-01-04 | Glaxo Group Limited | Antigen-binding constructs |
| US20120107330A1 (en) * | 2009-07-16 | 2012-05-03 | Adriaan Allart Stoop | Antagonists, uses & methods for partially inhibiting tnfr1 |
| BR112012001681A2 (pt) | 2009-07-16 | 2019-09-24 | Graxo Group Ltd | domínios variáveis de ligação de anti-albumina sérica aperfeiçoados |
| US20110223149A1 (en) * | 2009-10-14 | 2011-09-15 | Aileron Therapeutics, Inc. | Peptidomimetic macrocycles |
| AU2010311640B2 (en) | 2009-10-27 | 2015-01-29 | Glaxo Group Limited | Stable anti-TNFR1 polypeptides, antibody variable domains & antagonists |
| WO2011095545A1 (en) | 2010-02-05 | 2011-08-11 | Ablynx Nv | Peptides capable of binding to serum albumin and compounds, constructs and polypeptides comprising the same |
| WO2011144751A1 (en) | 2010-05-20 | 2011-11-24 | Glaxo Group Limited | Improved anti-serum albumin binding variants |
| WO2012020143A1 (en) | 2010-08-13 | 2012-02-16 | Glaxo Group Limited | Improved anti-serum albumin binding variants |
| EP2606065A2 (en) * | 2010-08-20 | 2013-06-26 | GlaxoSmithKline Intellectual Property Development Limited | Improved anti-serum albumin binding variants |
| ES2618586T3 (es) | 2010-09-16 | 2017-06-21 | Baliopharm Ag | Anticuerpo anti-huTNFR1 |
| US20130266567A1 (en) | 2010-12-01 | 2013-10-10 | Haren Arulanantham | Anti-serum albumin binding single variable domains |
| WO2012104227A1 (en) | 2011-02-02 | 2012-08-09 | Glaxo Group Limited | Novel antigen binding proteins |
| US9527925B2 (en) | 2011-04-01 | 2016-12-27 | Boehringer Ingelheim International Gmbh | Bispecific binding molecules binding to VEGF and ANG2 |
| EP3569243A1 (en) * | 2011-06-28 | 2019-11-20 | Inhibrx, LP | Serpin fusion polypeptides and methods of use thereof |
| US10400029B2 (en) | 2011-06-28 | 2019-09-03 | Inhibrx, Lp | Serpin fusion polypeptides and methods of use thereof |
| KR101632620B1 (ko) * | 2011-07-27 | 2016-06-23 | 글락소 그룹 리미티드 | Fc 도메인에 융합된 항vegf 단일 가변 도메인 |
| KR102162413B1 (ko) * | 2011-08-17 | 2020-10-07 | 글락소 그룹 리미티드 | 변형된 단백질 및 펩티드 |
| GB2497138A (en) * | 2011-12-02 | 2013-06-05 | Randox Lab Ltd | Biomarkers for stroke and stroke subtype diagnosis. |
| RS57704B1 (sr) | 2012-07-13 | 2018-12-31 | Roche Glycart Ag | Bispecifična anti-vegf/anti-ang-2 antitela i njihova primena u lečenju vaskularnih bolesti oka |
| WO2014111550A1 (en) | 2013-01-17 | 2014-07-24 | Glaxosmithkline Intellectual Property Development Limited | Modified anti-serum albumin binding proteins |
| CA2897345A1 (en) | 2013-01-31 | 2014-08-07 | Glaxo Group Limited | Method of producing a protein |
| US9840553B2 (en) | 2014-06-28 | 2017-12-12 | Kodiak Sciences Inc. | Dual PDGF/VEGF antagonists |
| AR103173A1 (es) | 2014-12-22 | 2017-04-19 | Novarits Ag | Productos farmacéuticos y composiciones líquidas estables de anticuerpos il-17 |
| MA41374A (fr) | 2015-01-20 | 2017-11-28 | Cytomx Therapeutics Inc | Substrats clivables par métalloprotéase matricielle et clivables par sérine protéase et procédés d'utilisation de ceux-ci |
| AU2016381964B2 (en) | 2015-12-30 | 2024-02-15 | Kodiak Sciences Inc. | Antibodies and conjugates thereof |
| GB201617622D0 (en) * | 2016-10-18 | 2016-11-30 | VIB VZW and Universiteit Gent | Means and methods to treat inflammation |
| RU2625010C1 (ru) * | 2016-11-10 | 2017-07-11 | Илья Петрович Приколаб | Экспрессионный плазмидный вектор для экспрессии активной формы TNFR1-Fc и способ получения рекомбинантного белка |
| TW202323287A (zh) | 2016-11-28 | 2023-06-16 | 日商中外製藥股份有限公司 | 包含抗原結合域與運送部分的多胜肽 |
| KR20230073346A (ko) | 2016-11-28 | 2023-05-25 | 추가이 세이야쿠 가부시키가이샤 | 리간드 결합 활성을 조정 가능한 리간드 결합 분자 |
| UY37651A (es) * | 2017-03-31 | 2018-10-31 | Swedish Orphan Biovitrum Ab Publ | Polipéptido de unión al il-1r-i |
| AU2018359532C9 (en) * | 2017-11-01 | 2025-02-13 | Allogene Therapeutics, Inc. | Modified caspase-9 polypeptides and methods of use thereof |
| TW202348632A (zh) | 2017-11-28 | 2023-12-16 | 日商中外製藥股份有限公司 | 含有抗原結合域及運輸部分之多胜肽 |
| BR112020010248A2 (pt) | 2017-11-28 | 2020-11-10 | Chugai Seiyaku Kabushiki Kaisha | molécula de ligação do ligante tendo atividade de ligação do ligante ajustável |
| WO2019169341A1 (en) | 2018-03-02 | 2019-09-06 | Kodiak Sciences Inc. | Il-6 antibodies and fusion constructs and conjugates thereof |
| EP3807312A4 (en) | 2018-05-30 | 2022-07-20 | Chugai Seiyaku Kabushiki Kaisha | POLYPEPTIDE COMPRISING AN AGGREECAN-BINDING DOMAIN AND A TRANSPORT FRACTION |
| JP7428661B2 (ja) * | 2018-05-30 | 2024-02-06 | 中外製薬株式会社 | Il-1r1結合ドメインおよび運搬部分を含むポリペプチド |
| EP3623798B1 (de) * | 2018-09-13 | 2021-11-03 | Euroimmun Medizinische Labordiagnostika AG | Verfahren und vorrichtung zum erfassen und darstellen eines immunfluoreszenzbildes einer biologischen probe |
| JP2022512798A (ja) * | 2018-10-25 | 2022-02-07 | エフ.ホフマン-ラ ロシュ アーゲー | 抗体FcRn結合の改変 |
| EP3890764A2 (en) | 2018-12-06 | 2021-10-13 | CytomX Therapeutics, Inc. | Matrix metalloprotease-cleavable and serine or cysteine protease-cleavable substrates and methods of use thereof |
| CN111454366B (zh) * | 2019-01-21 | 2023-06-16 | 中国科学院深圳先进技术研究院 | 一种融合蛋白及其应用 |
| JP7315967B2 (ja) * | 2019-01-31 | 2023-07-27 | 積水メディカル株式会社 | 生物学的試料中の遊離aimの免疫学的分析方法及び測定キット |
| CN114786731A (zh) | 2019-10-10 | 2022-07-22 | 科达制药股份有限公司 | 治疗眼部病症的方法 |
| JP7473398B2 (ja) * | 2020-05-28 | 2024-04-23 | シスメックス株式会社 | キャリブレータ、複合体、及びIgA凝集体を測定する方法 |
| CN116847887A (zh) | 2020-08-27 | 2023-10-03 | 伊诺西治疗公司 | 治疗自身免疫性疾病和癌症的方法和组合物 |
| WO2022117569A1 (en) | 2020-12-02 | 2022-06-09 | Oncurious Nv | A ccr8 antagonist antibody in combination with a lymphotoxin beta receptor agonist antibody in therapy against cancer |
| CN115181751A (zh) * | 2021-04-02 | 2022-10-14 | 苏州博腾生物制药有限公司 | 靶向白蛋白的嵌合抗原受体及其使用方法 |
| CN114657162B (zh) * | 2022-03-04 | 2023-06-16 | 华南理工大学 | 一种具有血管内皮细胞保护功能的抗氧化五肽及其应用 |
| CN115112704B (zh) * | 2022-06-21 | 2025-07-15 | 中特检验集团有限公司 | 一种光热发电有机热载体热稳定性检测方法 |
| AR129879A1 (es) | 2022-07-08 | 2024-10-09 | Novo Nordisk As | Compuestos de isvd altamente potentes capaces de sustituir al fviii(a) |
| WO2025049818A1 (en) | 2023-08-29 | 2025-03-06 | Enosi Therapeutics Corporation | Tnfr1 antagonists lacking agonist activity and uses thereof |
| CN119909772B (zh) * | 2025-04-01 | 2025-06-20 | 安徽一帆新材料科技有限公司 | 用于净水的再生阴树脂及其制备方法 |
Family Cites Families (54)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| GB2148299B (en) | 1983-09-01 | 1988-01-06 | Hybritech Inc | Antibody compositions of therapeutic agents having an extended serum half-life |
| DE3883899T3 (de) | 1987-03-18 | 1999-04-22 | Sb2, Inc., Danville, Calif. | Geänderte antikörper. |
| GB8725529D0 (en) | 1987-10-30 | 1987-12-02 | Delta Biotechnology Ltd | Polypeptides |
| JP3095168B2 (ja) | 1988-02-05 | 2000-10-03 | エル. モリソン,シェリー | ドメイン‐変性不変部を有する抗体 |
| DE68927933T2 (de) | 1988-09-02 | 1997-08-14 | Dyax Corp | Herstellung und auswahl von rekombinantproteinen mit verschiedenen bindestellen |
| ATE102631T1 (de) | 1988-11-11 | 1994-03-15 | Medical Res Council | Klonierung von immunglobulin sequenzen aus den variabelen domaenen. |
| ATE92107T1 (de) | 1989-04-29 | 1993-08-15 | Delta Biotechnology Ltd | N-terminale fragmente von menschliches serumalbumin enthaltenden fusionsproteinen. |
| CA2016842A1 (en) | 1989-05-16 | 1990-11-16 | Richard A. Lerner | Method for tapping the immunological repertoire |
| 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 |
| US5977307A (en) | 1989-09-07 | 1999-11-02 | Alkermes, Inc. | Transferrin receptor specific ligand-neuropharmaceutical agent fusion proteins |
| GB9015198D0 (en) | 1990-07-10 | 1990-08-29 | Brien Caroline J O | Binding substance |
| US6172197B1 (en) | 1991-07-10 | 2001-01-09 | Medical Research Council | Methods for producing members of specific binding pairs |
| EP0585287B1 (en) | 1990-07-10 | 1999-10-13 | Cambridge Antibody Technology Limited | Methods for producing members of specific binding pairs |
| AU8507191A (en) | 1990-08-29 | 1992-03-30 | Genpharm International, Inc. | Transgenic non-human animals capable of producing heterologous antibodies |
| EP1046421B8 (en) | 1990-12-06 | 2006-01-11 | Affymetrix, Inc. (a Delaware Corporation) | Methods and reagents for very large scale immobilized polymer synthesis |
| WO1993011236A1 (en) | 1991-12-02 | 1993-06-10 | Medical Research Council | Production of anti-self antibodies from antibody segment repertoires and displayed on phage |
| US5733743A (en) | 1992-03-24 | 1998-03-31 | Cambridge Antibody Technology Limited | Methods for producing members of specific binding pairs |
| CA2163345A1 (en) | 1993-06-16 | 1994-12-22 | Susan Adrienne Morgan | Antibodies |
| US5702892A (en) | 1995-05-09 | 1997-12-30 | The United States Of America As Represented By The Department Of Health And Human Services | Phage-display of immunoglobulin heavy chain libraries |
| EP0859841B1 (en) | 1995-08-18 | 2002-06-19 | MorphoSys AG | Protein/(poly)peptide libraries |
| WO1997029131A1 (en) * | 1996-02-09 | 1997-08-14 | Basf Aktiengesellschaft | HUMAN ANTIBODIES THAT BIND HUMAN TNF$g(a) |
| EP1019496B1 (en) | 1997-07-07 | 2004-09-29 | Medical Research Council | In vitro sorting method |
| GB9722131D0 (en) | 1997-10-20 | 1997-12-17 | Medical Res Council | Method |
| GB2361237A (en) | 1998-05-13 | 2001-10-17 | Diversys Ltd | Selection system |
| IL127127A0 (en) | 1998-11-18 | 1999-09-22 | Peptor Ltd | Small functional units of antibody heavy chain variable regions |
| WO2002043660A2 (en) | 2000-11-28 | 2002-06-06 | Mediummune, Inc | Methods of administering/dosing anti-rsv antibodies for prophylaxis and treatment |
| GB2375112A (en) | 2000-02-03 | 2002-11-06 | Domantis Ltd | Combinatorial protein domains |
| EP1263788A2 (en) | 2000-02-11 | 2002-12-11 | THE GOVERNMENT OF THE UNITED STATES OF AMERICA, as represented by THE SECRETARY, DEPARTMENT OF HEALTH AND HUMAN SERVICES | Identification of a domain in the tumor necrosis factor receptor family that mediates pre-ligand receptor assembly and function |
| US7115415B2 (en) * | 2000-09-15 | 2006-10-03 | Genentech, Inc. | PRO9821 nucleic acids |
| DK1399484T3 (da) | 2001-06-28 | 2010-11-08 | Domantis Ltd | Dobbelt-specifik ligand og anvendelse af denne |
| US20060073141A1 (en) * | 2001-06-28 | 2006-04-06 | Domantis Limited | Compositions and methods for treating inflammatory disorders |
| GB0118689D0 (en) * | 2001-08-01 | 2001-09-19 | Psimedica Ltd | Pharmaceutical formulation |
| US20080108560A1 (en) | 2002-03-05 | 2008-05-08 | Eli Lilly And Company | Heterologous G-Csf Fusion Proteins |
| US7696320B2 (en) * | 2004-08-24 | 2010-04-13 | Domantis Limited | Ligands that have binding specificity for VEGF and/or EGFR and methods of use therefor |
| EP2135879A3 (en) * | 2002-06-28 | 2010-06-23 | Domantis Limited | Ligand |
| US20060002935A1 (en) * | 2002-06-28 | 2006-01-05 | Domantis Limited | Tumor Necrosis Factor Receptor 1 antagonists and methods of use therefor |
| ES2614274T3 (es) | 2002-09-06 | 2017-05-30 | Alexion Pharmaceuticals, Inc. | Procedimiento de tratamiento de asma usando anticuerpos frente al componente de complemento C5 |
| JP4317817B2 (ja) | 2002-09-06 | 2009-08-19 | アムジェン インコーポレイテッド | 治療用ヒト抗il−1r1モノクローナル抗体 |
| CA2505326A1 (en) | 2002-11-08 | 2004-05-21 | Ablynx N.V. | Camelidae antibodies against immunoglobulin e and use thereof for the treatment of allergic disorders |
| EP1578801A2 (en) | 2002-12-27 | 2005-09-28 | Domantis Limited | Dual specific single domain antibodies specific for a ligand and for the receptor of the ligand |
| GB0230203D0 (en) * | 2002-12-27 | 2003-02-05 | Domantis Ltd | Fc fusion |
| US20060104968A1 (en) * | 2003-03-05 | 2006-05-18 | Halozyme, Inc. | Soluble glycosaminoglycanases and methods of preparing and using soluble glycosaminogly ycanases |
| DE602004017726D1 (de) | 2003-06-30 | 2008-12-24 | Domantis Ltd | Pegylierte Single-domain-antikörper (dAb) |
| AU2005211725B2 (en) | 2004-02-09 | 2010-07-15 | Human Genome Sciences, Inc. | Albumin fusion proteins |
| DK1737962T3 (da) | 2004-03-24 | 2010-12-13 | Domantis Ltd | GAS1-universel leder |
| EP2324848A3 (en) * | 2004-10-21 | 2011-09-14 | Genentech, Inc. | Method for treating intraocular neovascular diseases |
| GB0521621D0 (en) * | 2005-10-24 | 2005-11-30 | Domantis Ltd | Tumor necrosis factor receptor 1 antagonists for treating respiratory diseases |
| US20090191217A1 (en) * | 2004-12-02 | 2009-07-30 | De Wildt Ruud M | Anti-IL-1R1 Single Domain Antibodies And Therapeutic Uses |
| TW200730539A (en) * | 2005-12-01 | 2007-08-16 | Domantis Ltd | Noncompetitive domain antibody formats that bind interleukin 1 receptor type 1 |
| AU2006321367B2 (en) | 2005-12-01 | 2011-11-03 | Domantis Limited | Competitive domain antibody formats that bind Interleukin 1 Receptor type 1 |
| HUE048024T2 (hu) | 2006-08-10 | 2020-05-28 | Roy C Levitt | Anakinra bronchiolitis obliterans szindróma kezelésében való alkalmazásra |
| JP2010507624A (ja) * | 2006-10-27 | 2010-03-11 | アブリンクス エン.ヴェー. | ポリペプチド及びタンパク質の鼻内送達 |
| CA2688434A1 (en) | 2007-06-06 | 2008-12-11 | Domantis Limited | Polypeptides, antibody variable domains and antagonists |
| JP2010528647A (ja) | 2007-06-06 | 2010-08-26 | ドマンティス リミテッド | ポリペプチド、抗体可変ドメインおよびアンタゴニスト |
-
2008
- 2008-06-03 CA CA002688434A patent/CA2688434A1/en not_active Abandoned
- 2008-06-03 AU AU2008259590A patent/AU2008259590A1/en not_active Abandoned
- 2008-06-03 CA CA002683791A patent/CA2683791A1/en not_active Abandoned
- 2008-06-03 EA EA200901494A patent/EA200901494A1/ru unknown
- 2008-06-03 CA CA002688433A patent/CA2688433A1/en not_active Abandoned
- 2008-06-03 KR KR1020107000188A patent/KR20100018040A/ko not_active Withdrawn
- 2008-06-03 MX MX2009013137A patent/MX2009013137A/es not_active Application Discontinuation
- 2008-06-04 EA EA200901495A patent/EA018723B1/ru not_active IP Right Cessation
- 2008-06-04 WO PCT/GB2008/050407 patent/WO2008149150A2/en not_active Ceased
- 2008-06-04 AR ARP080102363A patent/AR066848A1/es not_active Application Discontinuation
- 2008-06-04 PE PE2008000944A patent/PE20090323A1/es not_active Application Discontinuation
- 2008-06-04 EA EA200901491A patent/EA018129B1/ru not_active IP Right Cessation
- 2008-06-04 WO PCT/GB2008/050405 patent/WO2008149148A2/en not_active Ceased
- 2008-06-04 AR ARP080102365A patent/AR066850A1/es not_active Application Discontinuation
- 2008-06-04 PE PE2008000940A patent/PE20090322A1/es not_active Application Discontinuation
- 2008-06-04 CA CA002683823A patent/CA2683823A1/en not_active Abandoned
- 2008-06-04 BR BRPI0812268A patent/BRPI0812268A2/pt not_active IP Right Cessation
- 2008-06-04 BR BRPI0813899A patent/BRPI0813899A2/pt not_active IP Right Cessation
- 2008-06-04 SI SI200831508T patent/SI2162467T1/sl unknown
- 2008-06-04 JP JP2010510887A patent/JP5444215B2/ja active Active
- 2008-06-04 SG SG2012040275A patent/SG182151A1/en unknown
- 2008-06-04 PL PL08750800T patent/PL2162467T3/pl unknown
- 2008-06-04 EP EP13184209.8A patent/EP2746290B1/en active Active
- 2008-06-04 KR KR1020107000212A patent/KR101604274B1/ko not_active Expired - Fee Related
- 2008-06-04 EP EP08750801A patent/EP2164867A2/en not_active Withdrawn
- 2008-06-04 CA CA002688456A patent/CA2688456A1/en not_active Abandoned
- 2008-06-04 HR HRP20151024TT patent/HRP20151024T1/hr unknown
- 2008-06-04 AU AU2008259515A patent/AU2008259515A1/en not_active Abandoned
- 2008-06-04 MX MX2009012967A patent/MX2009012967A/es not_active Application Discontinuation
- 2008-06-04 AU AU2008259516A patent/AU2008259516A1/en not_active Abandoned
- 2008-06-04 EP EP13184211.4A patent/EP2746291B1/en active Active
- 2008-06-04 CN CN200880019060A patent/CN101802004A/zh active Pending
- 2008-06-04 WO PCT/GB2008/050406 patent/WO2008149149A2/en not_active Ceased
- 2008-06-04 MX MX2009013138A patent/MX2009013138A/es active IP Right Grant
- 2008-06-04 CA CA2688447A patent/CA2688447C/en active Active
- 2008-06-04 DK DK08750800.8T patent/DK2162467T3/en active
- 2008-06-04 EP EP08750802A patent/EP2162468A2/en not_active Withdrawn
- 2008-06-04 AU AU2008259514A patent/AU2008259514B2/en not_active Ceased
- 2008-06-04 KR KR1020107000213A patent/KR20100041746A/ko not_active Withdrawn
- 2008-06-04 PE PE2008000943A patent/PE20090763A1/es not_active Application Discontinuation
- 2008-06-04 EP EP08750800.8A patent/EP2162467B1/en active Active
- 2008-06-04 CN CN2008801020043A patent/CN101883788A/zh active Pending
- 2008-06-04 CN CN200880102207.2A patent/CN101778865B/zh not_active Expired - Fee Related
- 2008-06-04 EA EA200901300A patent/EA200901300A1/ru unknown
- 2008-06-04 JP JP2010510888A patent/JP2010530364A/ja active Pending
- 2008-06-04 ES ES08750800.8T patent/ES2546943T3/es active Active
- 2008-06-04 AR ARP080102362A patent/AR066847A1/es unknown
- 2008-06-04 HU HUE08750800A patent/HUE025899T2/en unknown
- 2008-06-04 MX MX2009013211A patent/MX2009013211A/es active IP Right Grant
- 2008-06-04 JP JP2010510886A patent/JP5325211B2/ja not_active Expired - Fee Related
- 2008-06-04 US US12/663,502 patent/US8398979B2/en not_active Expired - Fee Related
- 2008-06-04 BR BRPI0812795A patent/BRPI0812795C1/pt not_active IP Right Cessation
- 2008-06-04 US US12/663,506 patent/US20100247515A1/en not_active Abandoned
- 2008-06-04 SG SG2012039541A patent/SG182141A1/en unknown
- 2008-06-04 CN CN201410440384.9A patent/CN104311663B/zh not_active Expired - Fee Related
- 2008-06-04 PT PT87508008T patent/PT2162467E/pt unknown
- 2008-06-04 KR KR1020107000223A patent/KR20100040841A/ko not_active Withdrawn
- 2008-06-04 NZ NZ581372A patent/NZ581372A/en not_active IP Right Cessation
- 2008-06-06 TW TW097121295A patent/TW200911832A/zh unknown
- 2008-06-06 TW TW097121301A patent/TW200918088A/zh unknown
- 2008-06-06 CL CL2008001673A patent/CL2008001673A1/es unknown
- 2008-06-06 CL CL2008001674A patent/CL2008001674A1/es unknown
- 2008-06-06 TW TW097121265A patent/TW200911834A/zh unknown
- 2008-06-06 TW TW097121268A patent/TW200911831A/zh unknown
- 2008-06-06 TW TW097121280A patent/TW200907128A/zh unknown
- 2008-06-06 TW TW097121296A patent/TW200902551A/zh unknown
- 2008-06-06 CL CL2008001676A patent/CL2008001676A1/es unknown
- 2008-11-26 US US12/323,632 patent/US20090148437A1/en not_active Abandoned
-
2009
- 2009-10-11 IL IL201398A patent/IL201398A0/en unknown
- 2009-11-04 US US13/130,656 patent/US20110256122A1/en not_active Abandoned
- 2009-11-04 EA EA201100546A patent/EA201100546A1/ru unknown
- 2009-11-18 IL IL202204A patent/IL202204A0/en unknown
- 2009-11-27 DO DO2009000268A patent/DOP2009000268A/es unknown
- 2009-11-30 MA MA32388A patent/MA31403B1/fr unknown
- 2009-11-30 ZA ZA2009/08470A patent/ZA200908470B/en unknown
- 2009-12-14 CO CO09142782A patent/CO6251322A2/es not_active Application Discontinuation
- 2009-12-14 CO CO09142781A patent/CO6251321A2/es not_active Application Discontinuation
-
2010
- 2010-01-04 MA MA32475A patent/MA31668B1/fr unknown
- 2010-01-06 CR CR11195A patent/CR11195A/es unknown
- 2010-01-06 CR CR11194A patent/CR11194A/es not_active Application Discontinuation
-
2011
- 2011-11-17 US US13/299,030 patent/US20120134982A1/en not_active Abandoned
-
2015
- 2015-10-06 CY CY20151100886T patent/CY1116762T1/el unknown
Also Published As
Similar Documents
| Publication | Publication Date | Title |
|---|---|---|
| TW200911832A (en) | Polypeptides, antibody variable domains & antagonists | |
| TW200906853A (en) | Polypeptides, antibody variable domains & antagonists | |
| JP2010529840A (ja) | ポリペプチド、抗体可変ドメインおよびアンタゴニスト | |
| TW201125877A (en) | Stable anti-TNFR1 polypeptides, antibody variable domains & and antagonists |