WO2008147143A2 - Immunoglobulin fusion proteins - Google Patents
Immunoglobulin fusion proteins Download PDFInfo
- Publication number
- WO2008147143A2 WO2008147143A2 PCT/KR2008/003060 KR2008003060W WO2008147143A2 WO 2008147143 A2 WO2008147143 A2 WO 2008147143A2 KR 2008003060 W KR2008003060 W KR 2008003060W WO 2008147143 A2 WO2008147143 A2 WO 2008147143A2
- Authority
- WO
- WIPO (PCT)
- Prior art keywords
- amino acid
- seq
- acid residues
- positions
- polypeptide
- Prior art date
Links
- 108060003951 Immunoglobulin Proteins 0.000 title claims abstract description 26
- 102000018358 immunoglobulin Human genes 0.000 title claims abstract description 26
- 108020001507 fusion proteins Proteins 0.000 title abstract description 67
- 102000037865 fusion proteins Human genes 0.000 title abstract description 67
- 125000000539 amino acid group Chemical group 0.000 claims description 241
- 108090000765 processed proteins & peptides Proteins 0.000 claims description 202
- 229920001184 polypeptide Polymers 0.000 claims description 183
- 102000004196 processed proteins & peptides Human genes 0.000 claims description 183
- 125000003275 alpha amino acid group Chemical group 0.000 claims description 140
- 108090000623 proteins and genes Proteins 0.000 claims description 93
- 102000004169 proteins and genes Human genes 0.000 claims description 75
- 210000004027 cell Anatomy 0.000 claims description 66
- 210000004899 c-terminal region Anatomy 0.000 claims description 46
- 238000000034 method Methods 0.000 claims description 45
- 108010076504 Protein Sorting Signals Proteins 0.000 claims description 36
- 102000039446 nucleic acids Human genes 0.000 claims description 34
- 108020004707 nucleic acids Proteins 0.000 claims description 34
- 150000007523 nucleic acids Chemical class 0.000 claims description 34
- 239000012634 fragment Substances 0.000 claims description 30
- -1 IL-I Proteins 0.000 claims description 29
- 108010017080 Granulocyte Colony-Stimulating Factor Proteins 0.000 claims description 25
- 102000004269 Granulocyte Colony-Stimulating Factor Human genes 0.000 claims description 25
- 239000013604 expression vector Substances 0.000 claims description 25
- 108020004414 DNA Proteins 0.000 claims description 22
- 239000002773 nucleotide Substances 0.000 claims description 17
- 125000003729 nucleotide group Chemical group 0.000 claims description 17
- 210000004897 n-terminal region Anatomy 0.000 claims description 14
- 125000002924 primary amino group Chemical group [H]N([H])* 0.000 claims description 14
- 108060008683 Tumor Necrosis Factor Receptor Proteins 0.000 claims description 13
- 102000003298 tumor necrosis factor receptor Human genes 0.000 claims description 13
- 102000009027 Albumins Human genes 0.000 claims description 12
- 108010088751 Albumins Proteins 0.000 claims description 12
- 108090000467 Interferon-beta Proteins 0.000 claims description 12
- 241000124008 Mammalia Species 0.000 claims description 10
- 102000004127 Cytokines Human genes 0.000 claims description 9
- 108090000695 Cytokines Proteins 0.000 claims description 9
- 102100026720 Interferon beta Human genes 0.000 claims description 9
- 208000024891 symptom Diseases 0.000 claims description 9
- 230000001965 increasing effect Effects 0.000 claims description 8
- 238000006467 substitution reaction Methods 0.000 claims description 8
- 102100028728 Bone morphogenetic protein 1 Human genes 0.000 claims description 7
- 108090000654 Bone morphogenetic protein 1 Proteins 0.000 claims description 7
- 102000006992 Interferon-alpha Human genes 0.000 claims description 7
- 108010047761 Interferon-alpha Proteins 0.000 claims description 7
- 239000003102 growth factor Substances 0.000 claims description 7
- 102100039620 Granulocyte-macrophage colony-stimulating factor Human genes 0.000 claims description 6
- 239000002253 acid Substances 0.000 claims description 6
- FWMNVWWHGCHHJJ-SKKKGAJSSA-N 4-amino-1-[(2r)-6-amino-2-[[(2r)-2-[[(2r)-2-[[(2r)-2-amino-3-phenylpropanoyl]amino]-3-phenylpropanoyl]amino]-4-methylpentanoyl]amino]hexanoyl]piperidine-4-carboxylic acid Chemical compound C([C@H](C(=O)N[C@H](CC(C)C)C(=O)N[C@H](CCCCN)C(=O)N1CCC(N)(CC1)C(O)=O)NC(=O)[C@H](N)CC=1C=CC=CC=1)C1=CC=CC=C1 FWMNVWWHGCHHJJ-SKKKGAJSSA-N 0.000 claims description 5
- 239000000854 Human Growth Hormone Substances 0.000 claims description 5
- 108010002350 Interleukin-2 Proteins 0.000 claims description 5
- 102000016715 Transforming Growth Factor beta Receptors Human genes 0.000 claims description 5
- 230000002685 pulmonary effect Effects 0.000 claims description 5
- 208000023275 Autoimmune disease Diseases 0.000 claims description 4
- 102100023804 Coagulation factor VII Human genes 0.000 claims description 4
- 102100039498 Cytotoxic T-lymphocyte protein 4 Human genes 0.000 claims description 4
- 108010023321 Factor VII Proteins 0.000 claims description 4
- 101000889276 Homo sapiens Cytotoxic T-lymphocyte protein 4 Proteins 0.000 claims description 4
- 108010002386 Interleukin-3 Proteins 0.000 claims description 4
- 108010002616 Interleukin-5 Proteins 0.000 claims description 4
- 108090001005 Interleukin-6 Proteins 0.000 claims description 4
- 101001032756 Rattus norvegicus Granzyme-like protein 1 Proteins 0.000 claims description 4
- 102000003675 cytokine receptors Human genes 0.000 claims description 4
- 108010057085 cytokine receptors Proteins 0.000 claims description 4
- 201000010099 disease Diseases 0.000 claims description 4
- 208000037265 diseases, disorders, signs and symptoms Diseases 0.000 claims description 4
- 239000002158 endotoxin Substances 0.000 claims description 4
- 229940012413 factor vii Drugs 0.000 claims description 4
- 239000001963 growth medium Substances 0.000 claims description 4
- 238000003306 harvesting Methods 0.000 claims description 4
- 229940088597 hormone Drugs 0.000 claims description 4
- 239000005556 hormone Substances 0.000 claims description 4
- 230000002401 inhibitory effect Effects 0.000 claims description 4
- 208000004235 neutropenia Diseases 0.000 claims description 4
- 230000035939 shock Effects 0.000 claims description 4
- 102000053602 DNA Human genes 0.000 claims description 3
- 102000009465 Growth Factor Receptors Human genes 0.000 claims description 3
- 108010009202 Growth Factor Receptors Proteins 0.000 claims description 3
- 108010000521 Human Growth Hormone Proteins 0.000 claims description 3
- 102000002265 Human Growth Hormone Human genes 0.000 claims description 3
- 108090000978 Interleukin-4 Proteins 0.000 claims description 3
- 102000004388 Interleukin-4 Human genes 0.000 claims description 3
- 108010002586 Interleukin-7 Proteins 0.000 claims description 3
- 108090001007 Interleukin-8 Proteins 0.000 claims description 3
- 108091005735 TGF-beta receptors Proteins 0.000 claims description 3
- 238000002512 chemotherapy Methods 0.000 claims description 3
- 108091008039 hormone receptors Proteins 0.000 claims description 3
- 206010039073 rheumatoid arthritis Diseases 0.000 claims description 3
- 230000004936 stimulating effect Effects 0.000 claims description 3
- 206010000830 Acute leukaemia Diseases 0.000 claims description 2
- 206010002556 Ankylosing Spondylitis Diseases 0.000 claims description 2
- 208000032467 Aplastic anaemia Diseases 0.000 claims description 2
- 206010065553 Bone marrow failure Diseases 0.000 claims description 2
- 201000003793 Myelodysplastic syndrome Diseases 0.000 claims description 2
- 201000004681 Psoriasis Diseases 0.000 claims description 2
- 238000010322 bone marrow transplantation Methods 0.000 claims description 2
- 238000005534 hematocrit Methods 0.000 claims description 2
- 230000002757 inflammatory effect Effects 0.000 claims description 2
- 201000006417 multiple sclerosis Diseases 0.000 claims description 2
- 210000005259 peripheral blood Anatomy 0.000 claims description 2
- 239000011886 peripheral blood Substances 0.000 claims description 2
- 210000000130 stem cell Anatomy 0.000 claims description 2
- 238000002054 transplantation Methods 0.000 claims description 2
- 206010003645 Atopy Diseases 0.000 claims 1
- 101100120663 Drosophila melanogaster fs(1)h gene Proteins 0.000 claims 1
- 101000746373 Homo sapiens Granulocyte-macrophage colony-stimulating factor Proteins 0.000 claims 1
- 108090000174 Interleukin-10 Proteins 0.000 claims 1
- 208000001132 Osteoporosis Diseases 0.000 claims 1
- 102000004887 Transforming Growth Factor beta Human genes 0.000 claims 1
- 108090001012 Transforming Growth Factor beta Proteins 0.000 claims 1
- 108040006870 interleukin-10 receptor activity proteins Proteins 0.000 claims 1
- 201000008482 osteoarthritis Diseases 0.000 claims 1
- 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 claims 1
- 235000018102 proteins Nutrition 0.000 description 63
- 150000001413 amino acids Chemical class 0.000 description 54
- 235000001014 amino acid Nutrition 0.000 description 44
- 239000003814 drug Substances 0.000 description 34
- 229940079593 drug Drugs 0.000 description 27
- 238000002347 injection Methods 0.000 description 26
- 239000007924 injection Substances 0.000 description 26
- 108010091135 Immunoglobulin Fc Fragments Proteins 0.000 description 23
- 102000018071 Immunoglobulin Fc Fragments Human genes 0.000 description 23
- 108010008165 Etanercept Proteins 0.000 description 22
- 238000007920 subcutaneous administration Methods 0.000 description 22
- 230000004927 fusion Effects 0.000 description 19
- 238000001727 in vivo Methods 0.000 description 19
- 239000013598 vector Substances 0.000 description 19
- 230000014509 gene expression Effects 0.000 description 18
- 238000001990 intravenous administration Methods 0.000 description 18
- 108010019673 Darbepoetin alfa Proteins 0.000 description 16
- 229940027941 immunoglobulin g Drugs 0.000 description 16
- 239000000203 mixture Substances 0.000 description 16
- 229940073621 enbrel Drugs 0.000 description 15
- 238000000338 in vitro Methods 0.000 description 15
- OXCMYAYHXIHQOA-UHFFFAOYSA-N potassium;[2-butyl-5-chloro-3-[[4-[2-(1,2,4-triaza-3-azanidacyclopenta-1,4-dien-5-yl)phenyl]phenyl]methyl]imidazol-4-yl]methanol Chemical compound [K+].CCCCC1=NC(Cl)=C(CO)N1CC1=CC=C(C=2C(=CC=CC=2)C2=N[N-]N=N2)C=C1 OXCMYAYHXIHQOA-UHFFFAOYSA-N 0.000 description 15
- 102000003951 Erythropoietin Human genes 0.000 description 14
- 108090000394 Erythropoietin Proteins 0.000 description 14
- 229940105423 erythropoietin Drugs 0.000 description 14
- 230000028327 secretion Effects 0.000 description 13
- 229940115115 aranesp Drugs 0.000 description 12
- 102000008394 Immunoglobulin Fragments Human genes 0.000 description 11
- 108010021625 Immunoglobulin Fragments Proteins 0.000 description 11
- 230000027455 binding Effects 0.000 description 11
- 210000004369 blood Anatomy 0.000 description 11
- 239000008280 blood Substances 0.000 description 11
- 108091006020 Fc-tagged proteins Proteins 0.000 description 10
- 102000004190 Enzymes Human genes 0.000 description 9
- 108090000790 Enzymes Proteins 0.000 description 9
- 229940088598 enzyme Drugs 0.000 description 9
- 108091033319 polynucleotide Proteins 0.000 description 9
- 102000040430 polynucleotide Human genes 0.000 description 9
- 239000002157 polynucleotide Substances 0.000 description 9
- 239000012091 fetal bovine serum Substances 0.000 description 8
- 238000011534 incubation Methods 0.000 description 8
- 108010002352 Interleukin-1 Proteins 0.000 description 7
- 102000000589 Interleukin-1 Human genes 0.000 description 7
- FAPWRFPIFSIZLT-UHFFFAOYSA-M Sodium chloride Chemical compound [Na+].[Cl-] FAPWRFPIFSIZLT-UHFFFAOYSA-M 0.000 description 7
- 239000003242 anti bacterial agent Substances 0.000 description 7
- 229940088710 antibiotic agent Drugs 0.000 description 7
- 229960000403 etanercept Drugs 0.000 description 7
- 230000006870 function Effects 0.000 description 7
- 210000003714 granulocyte Anatomy 0.000 description 7
- 241000282693 Cercopithecidae Species 0.000 description 6
- 101000694288 Homo sapiens 40S ribosomal protein SA Proteins 0.000 description 6
- 101001090483 Homo sapiens Glutathione S-transferase LANCL1 Proteins 0.000 description 6
- 108091006905 Human Serum Albumin Proteins 0.000 description 6
- 102000008100 Human Serum Albumin Human genes 0.000 description 6
- 241000282567 Macaca fascicularis Species 0.000 description 6
- 239000000427 antigen Substances 0.000 description 6
- 102000036639 antigens Human genes 0.000 description 6
- 108091007433 antigens Proteins 0.000 description 6
- 238000005516 engineering process Methods 0.000 description 6
- 102000005962 receptors Human genes 0.000 description 6
- 108020003175 receptors Proteins 0.000 description 6
- 210000002966 serum Anatomy 0.000 description 6
- 238000012360 testing method Methods 0.000 description 6
- 229940124597 therapeutic agent Drugs 0.000 description 6
- 241000701022 Cytomegalovirus Species 0.000 description 5
- 108010017213 Granulocyte-Macrophage Colony-Stimulating Factor Proteins 0.000 description 5
- 241001529936 Murinae Species 0.000 description 5
- 101150114197 TOP gene Proteins 0.000 description 5
- 239000003795 chemical substances by application Substances 0.000 description 5
- 239000000539 dimer Substances 0.000 description 5
- 230000000694 effects Effects 0.000 description 5
- 210000004408 hybridoma Anatomy 0.000 description 5
- 210000000265 leukocyte Anatomy 0.000 description 5
- 238000004519 manufacturing process Methods 0.000 description 5
- 108010044644 pegfilgrastim Proteins 0.000 description 5
- 239000008194 pharmaceutical composition Substances 0.000 description 5
- 230000006337 proteolytic cleavage Effects 0.000 description 5
- 229960004641 rituximab Drugs 0.000 description 5
- 239000000126 substance Substances 0.000 description 5
- 108091032973 (ribonucleotides)n+m Proteins 0.000 description 4
- 238000012286 ELISA Assay Methods 0.000 description 4
- 238000008157 ELISA kit Methods 0.000 description 4
- 108010029961 Filgrastim Proteins 0.000 description 4
- 102100039619 Granulocyte colony-stimulating factor Human genes 0.000 description 4
- 241000282412 Homo Species 0.000 description 4
- 101000716102 Homo sapiens T-cell surface glycoprotein CD4 Proteins 0.000 description 4
- 238000000134 MTT assay Methods 0.000 description 4
- 231100000002 MTT assay Toxicity 0.000 description 4
- 206010035226 Plasma cell myeloma Diseases 0.000 description 4
- 239000012980 RPMI-1640 medium Substances 0.000 description 4
- 102100036011 T-cell surface glycoprotein CD4 Human genes 0.000 description 4
- 241000700605 Viruses Species 0.000 description 4
- 230000004075 alteration Effects 0.000 description 4
- 230000010056 antibody-dependent cellular cytotoxicity Effects 0.000 description 4
- 230000004071 biological effect Effects 0.000 description 4
- 238000004113 cell culture Methods 0.000 description 4
- 230000010261 cell growth Effects 0.000 description 4
- 238000005119 centrifugation Methods 0.000 description 4
- 210000004978 chinese hamster ovary cell Anatomy 0.000 description 4
- 238000003776 cleavage reaction Methods 0.000 description 4
- 230000000295 complement effect Effects 0.000 description 4
- 230000004540 complement-dependent cytotoxicity Effects 0.000 description 4
- 230000008878 coupling Effects 0.000 description 4
- 238000010168 coupling process Methods 0.000 description 4
- 238000005859 coupling reaction Methods 0.000 description 4
- 229960005029 darbepoetin alfa Drugs 0.000 description 4
- 239000012636 effector Substances 0.000 description 4
- 229960004177 filgrastim Drugs 0.000 description 4
- 238000009396 hybridization Methods 0.000 description 4
- 230000002209 hydrophobic effect Effects 0.000 description 4
- 239000002609 medium Substances 0.000 description 4
- 201000000050 myeloid neoplasm Diseases 0.000 description 4
- 238000010899 nucleation Methods 0.000 description 4
- 108091008146 restriction endonucleases Proteins 0.000 description 4
- 230000007017 scission Effects 0.000 description 4
- 238000013207 serial dilution Methods 0.000 description 4
- 239000011780 sodium chloride Substances 0.000 description 4
- 235000002639 sodium chloride Nutrition 0.000 description 4
- 239000000243 solution Substances 0.000 description 4
- 239000013589 supplement Substances 0.000 description 4
- 125000001433 C-terminal amino-acid group Chemical group 0.000 description 3
- 108091026890 Coding region Proteins 0.000 description 3
- 102000003996 Interferon-beta Human genes 0.000 description 3
- 241001465754 Metazoa Species 0.000 description 3
- 241000699666 Mus <mouse, genus> Species 0.000 description 3
- 108010025020 Nerve Growth Factor Proteins 0.000 description 3
- 108091028043 Nucleic acid sequence Proteins 0.000 description 3
- 102000035195 Peptidases Human genes 0.000 description 3
- 108091005804 Peptidases Proteins 0.000 description 3
- 108090000373 Tissue Plasminogen Activator Proteins 0.000 description 3
- 102000003978 Tissue Plasminogen Activator Human genes 0.000 description 3
- 102100040247 Tumor necrosis factor Human genes 0.000 description 3
- 230000003213 activating effect Effects 0.000 description 3
- 238000007398 colorimetric assay Methods 0.000 description 3
- 230000021615 conjugation Effects 0.000 description 3
- 239000003937 drug carrier Substances 0.000 description 3
- 150000002148 esters Chemical class 0.000 description 3
- 239000012530 fluid Substances 0.000 description 3
- 230000028993 immune response Effects 0.000 description 3
- 230000001976 improved effect Effects 0.000 description 3
- 230000001939 inductive effect Effects 0.000 description 3
- 239000003112 inhibitor Substances 0.000 description 3
- 210000004698 lymphocyte Anatomy 0.000 description 3
- 210000004962 mammalian cell Anatomy 0.000 description 3
- 239000012528 membrane Substances 0.000 description 3
- 239000000178 monomer Substances 0.000 description 3
- 229940071846 neulasta Drugs 0.000 description 3
- 238000002360 preparation method Methods 0.000 description 3
- 238000000746 purification Methods 0.000 description 3
- 238000011002 quantification Methods 0.000 description 3
- 230000002829 reductive effect Effects 0.000 description 3
- 239000001509 sodium citrate Substances 0.000 description 3
- NLJMYIDDQXHKNR-UHFFFAOYSA-K sodium citrate Chemical compound O.O.[Na+].[Na+].[Na+].[O-]C(=O)CC(O)(CC([O-])=O)C([O-])=O NLJMYIDDQXHKNR-UHFFFAOYSA-K 0.000 description 3
- 238000013222 sprague-dawley male rat Methods 0.000 description 3
- 238000012453 sprague-dawley rat model Methods 0.000 description 3
- 239000000758 substrate Substances 0.000 description 3
- 230000001225 therapeutic effect Effects 0.000 description 3
- 229960000187 tissue plasminogen activator Drugs 0.000 description 3
- 238000013518 transcription Methods 0.000 description 3
- 230000035897 transcription Effects 0.000 description 3
- 238000001890 transfection Methods 0.000 description 3
- 239000013603 viral vector Substances 0.000 description 3
- 239000011534 wash buffer Substances 0.000 description 3
- 238000005406 washing Methods 0.000 description 3
- 102400001242 Betacellulin Human genes 0.000 description 2
- 101800001382 Betacellulin Proteins 0.000 description 2
- 108091003079 Bovine Serum Albumin Proteins 0.000 description 2
- 108050005493 CD3 protein, epsilon/gamma/delta subunit Proteins 0.000 description 2
- 102000017420 CD3 protein, epsilon/gamma/delta subunit Human genes 0.000 description 2
- 102000014914 Carrier Proteins Human genes 0.000 description 2
- 102000000844 Cell Surface Receptors Human genes 0.000 description 2
- 108010001857 Cell Surface Receptors Proteins 0.000 description 2
- 239000006144 Dulbecco’s modified Eagle's medium Substances 0.000 description 2
- 101000987586 Homo sapiens Eosinophil peroxidase Proteins 0.000 description 2
- 101000746367 Homo sapiens Granulocyte colony-stimulating factor Proteins 0.000 description 2
- 101000611183 Homo sapiens Tumor necrosis factor Proteins 0.000 description 2
- 101000798130 Homo sapiens Tumor necrosis factor receptor superfamily member 11B Proteins 0.000 description 2
- 101000801232 Homo sapiens Tumor necrosis factor receptor superfamily member 1B Proteins 0.000 description 2
- 102000003864 Human Follicle Stimulating Hormone Human genes 0.000 description 2
- 108010082302 Human Follicle Stimulating Hormone Proteins 0.000 description 2
- 108010054477 Immunoglobulin Fab Fragments Proteins 0.000 description 2
- 102000001706 Immunoglobulin Fab Fragments Human genes 0.000 description 2
- 108090000723 Insulin-Like Growth Factor I Proteins 0.000 description 2
- 102000014150 Interferons Human genes 0.000 description 2
- 108010050904 Interferons Proteins 0.000 description 2
- 102000004560 Interleukin-12 Receptors Human genes 0.000 description 2
- 108010017515 Interleukin-12 Receptors Proteins 0.000 description 2
- 102000004554 Interleukin-17 Receptors Human genes 0.000 description 2
- 108010017525 Interleukin-17 Receptors Proteins 0.000 description 2
- 102000015696 Interleukins Human genes 0.000 description 2
- 108010063738 Interleukins Proteins 0.000 description 2
- 102100033342 Lysosomal acid glucosylceramidase Human genes 0.000 description 2
- 125000000729 N-terminal amino-acid group Chemical group 0.000 description 2
- 102000007072 Nerve Growth Factors Human genes 0.000 description 2
- 108700026244 Open Reading Frames Proteins 0.000 description 2
- 102000003992 Peroxidases Human genes 0.000 description 2
- 244000046052 Phaseolus vulgaris Species 0.000 description 2
- 235000010627 Phaseolus vulgaris Nutrition 0.000 description 2
- 239000004698 Polyethylene Substances 0.000 description 2
- WCUXLLCKKVVCTQ-UHFFFAOYSA-M Potassium chloride Chemical compound [Cl-].[K+] WCUXLLCKKVVCTQ-UHFFFAOYSA-M 0.000 description 2
- 108020004511 Recombinant DNA Proteins 0.000 description 2
- 240000004808 Saccharomyces cerevisiae Species 0.000 description 2
- 102000013275 Somatomedins Human genes 0.000 description 2
- 108010022394 Threonine synthase Proteins 0.000 description 2
- 108010092867 Transforming Growth Factor beta Receptors Proteins 0.000 description 2
- 108060008682 Tumor Necrosis Factor Proteins 0.000 description 2
- 238000003556 assay Methods 0.000 description 2
- 230000001580 bacterial effect Effects 0.000 description 2
- 238000002869 basic local alignment search tool Methods 0.000 description 2
- 238000004166 bioassay Methods 0.000 description 2
- 230000000903 blocking effect Effects 0.000 description 2
- 108010006025 bovine growth hormone Proteins 0.000 description 2
- 239000006172 buffering agent Substances 0.000 description 2
- 230000024245 cell differentiation Effects 0.000 description 2
- 238000006243 chemical reaction Methods 0.000 description 2
- 239000002299 complementary DNA Substances 0.000 description 2
- 238000004590 computer program Methods 0.000 description 2
- 239000003636 conditioned culture medium Substances 0.000 description 2
- 238000010276 construction Methods 0.000 description 2
- 239000007822 coupling agent Substances 0.000 description 2
- 125000000151 cysteine group Chemical group N[C@@H](CS)C(=O)* 0.000 description 2
- 230000000120 cytopathologic effect Effects 0.000 description 2
- 238000012217 deletion Methods 0.000 description 2
- 230000037430 deletion Effects 0.000 description 2
- 238000011161 development Methods 0.000 description 2
- 230000018109 developmental process Effects 0.000 description 2
- 102000004419 dihydrofolate reductase Human genes 0.000 description 2
- 210000002472 endoplasmic reticulum Anatomy 0.000 description 2
- 238000001943 fluorescence-activated cell sorting Methods 0.000 description 2
- 238000009472 formulation Methods 0.000 description 2
- 238000010353 genetic engineering Methods 0.000 description 2
- 238000002873 global sequence alignment Methods 0.000 description 2
- 210000003958 hematopoietic stem cell Anatomy 0.000 description 2
- 102000044890 human EPO Human genes 0.000 description 2
- 229940072221 immunoglobulins Drugs 0.000 description 2
- 230000005764 inhibitory process Effects 0.000 description 2
- 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 2
- 229960001388 interferon-beta Drugs 0.000 description 2
- 229940047124 interferons Drugs 0.000 description 2
- 238000007912 intraperitoneal administration Methods 0.000 description 2
- 210000003734 kidney Anatomy 0.000 description 2
- 210000002540 macrophage Anatomy 0.000 description 2
- 238000005259 measurement Methods 0.000 description 2
- 108020004999 messenger RNA Proteins 0.000 description 2
- 210000000822 natural killer cell Anatomy 0.000 description 2
- 101800000857 p40 protein Proteins 0.000 description 2
- 230000036961 partial effect Effects 0.000 description 2
- HQQSBEDKMRHYME-UHFFFAOYSA-N pefloxacin mesylate Chemical compound [H+].CS([O-])(=O)=O.C1=C2N(CC)C=C(C(O)=O)C(=O)C2=CC(F)=C1N1CCN(C)CC1 HQQSBEDKMRHYME-UHFFFAOYSA-N 0.000 description 2
- 229960001373 pegfilgrastim Drugs 0.000 description 2
- 210000003819 peripheral blood mononuclear cell Anatomy 0.000 description 2
- 108040007629 peroxidase activity proteins Proteins 0.000 description 2
- 239000013612 plasmid Substances 0.000 description 2
- 229920000573 polyethylene Polymers 0.000 description 2
- 230000035755 proliferation Effects 0.000 description 2
- 229940024999 proteolytic enzymes for treatment of wounds and ulcers Drugs 0.000 description 2
- 230000004044 response Effects 0.000 description 2
- 210000001995 reticulocyte Anatomy 0.000 description 2
- 239000006228 supernatant Substances 0.000 description 2
- 238000013519 translation Methods 0.000 description 2
- 230000032258 transport Effects 0.000 description 2
- 108010087967 type I signal peptidase Proteins 0.000 description 2
- 241000701161 unidentified adenovirus Species 0.000 description 2
- 241001430294 unidentified retrovirus Species 0.000 description 2
- 229960005486 vaccine Drugs 0.000 description 2
- FHZSIZRTNHGLSX-FLMSMKGQSA-N (2s)-1-[(2s)-4-amino-2-[[(2s)-2-[[(2s)-2-[[(2s)-2-[[(2s)-2-[[(2s)-2-amino-3-hydroxypropanoyl]amino]-3-phenylpropanoyl]amino]-4-methylpentanoyl]amino]-4-methylpentanoyl]amino]-5-(diaminomethylideneamino)pentanoyl]amino]-4-oxobutanoyl]pyrrolidine-2-carboxyl Chemical compound C([C@@H](C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](CCCN=C(N)N)C(=O)N[C@@H](CC(N)=O)C(=O)N1[C@@H](CCC1)C(O)=O)NC(=O)[C@@H](N)CO)C1=CC=CC=C1 FHZSIZRTNHGLSX-FLMSMKGQSA-N 0.000 description 1
- DDYAPMZTJAYBOF-ZMYDTDHYSA-N (3S)-4-[[(2S)-1-[[(2S)-1-[[(2S)-5-amino-1-[[(2S)-1-[[(2S)-1-[[(2S)-1-[[(2S)-4-amino-1-[[(2S,3R)-1-[[(2S)-6-amino-1-[[(2S)-1-[[(2S)-4-amino-1-[[(2S)-1-[[(2S)-4-amino-1-[[(2S)-4-amino-1-[[(2S,3S)-1-[[(1S)-1-carboxyethyl]amino]-3-methyl-1-oxopentan-2-yl]amino]-1,4-dioxobutan-2-yl]amino]-1,4-dioxobutan-2-yl]amino]-5-carbamimidamido-1-oxopentan-2-yl]amino]-1,4-dioxobutan-2-yl]amino]-5-carbamimidamido-1-oxopentan-2-yl]amino]-1-oxohexan-2-yl]amino]-3-hydroxy-1-oxobutan-2-yl]amino]-1,4-dioxobutan-2-yl]amino]-4-methylsulfanyl-1-oxobutan-2-yl]amino]-4-methyl-1-oxopentan-2-yl]amino]-3-(1H-indol-3-yl)-1-oxopropan-2-yl]amino]-1,5-dioxopentan-2-yl]amino]-3-methyl-1-oxobutan-2-yl]amino]-1-oxo-3-phenylpropan-2-yl]amino]-3-[[(2S)-5-amino-2-[[(2S)-2-[[(2S)-2-[[(2S)-2-[[(2S)-2-[[(2S)-2-[[(2S)-2-[[(2S)-2-[[(2S)-6-amino-2-[[(2S)-2-[[(2S)-2-[[(2S)-2-[[(2S)-2-[[(2S,3R)-2-[[(2S)-2-[[(2S,3R)-2-[[2-[[(2S)-5-amino-2-[[(2S)-2-[[(2S)-2-amino-3-(1H-imidazol-4-yl)propanoyl]amino]-3-hydroxypropanoyl]amino]-5-oxopentanoyl]amino]acetyl]amino]-3-hydroxybutanoyl]amino]-3-phenylpropanoyl]amino]-3-hydroxybutanoyl]amino]-3-hydroxypropanoyl]amino]-3-carboxypropanoyl]amino]-3-(4-hydroxyphenyl)propanoyl]amino]-3-hydroxypropanoyl]amino]hexanoyl]amino]-3-(4-hydroxyphenyl)propanoyl]amino]-4-methylpentanoyl]amino]-3-carboxypropanoyl]amino]-3-hydroxypropanoyl]amino]-5-carbamimidamidopentanoyl]amino]-5-carbamimidamidopentanoyl]amino]propanoyl]amino]-5-oxopentanoyl]amino]-4-oxobutanoic acid Chemical class [H]N[C@@H](CC1=CNC=N1)C(=O)N[C@@H](CO)C(=O)N[C@@H](CCC(N)=O)C(=O)NCC(=O)N[C@@H]([C@@H](C)O)C(=O)N[C@@H](CC1=CC=CC=C1)C(=O)N[C@@H]([C@@H](C)O)C(=O)N[C@@H](CO)C(=O)N[C@@H](CC(O)=O)C(=O)N[C@@H](CC1=CC=C(O)C=C1)C(=O)N[C@@H](CO)C(=O)N[C@@H](CCCCN)C(=O)N[C@@H](CC1=CC=C(O)C=C1)C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](CC(O)=O)C(=O)N[C@@H](CO)C(=O)N[C@@H](CCCNC(N)=N)C(=O)N[C@@H](CCCNC(N)=N)C(=O)N[C@@H](C)C(=O)N[C@@H](CCC(N)=O)C(=O)N[C@@H](CC(O)=O)C(=O)N[C@@H](CC1=CC=CC=C1)C(=O)N[C@@H](C(C)C)C(=O)N[C@@H](CCC(N)=O)C(=O)N[C@@H](CC1=CNC2=C1C=CC=C2)C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](CCSC)C(=O)N[C@@H](CC(N)=O)C(=O)N[C@@H]([C@@H](C)O)C(=O)N[C@@H](CCCCN)C(=O)N[C@@H](CCCNC(N)=N)C(=O)N[C@@H](CC(N)=O)C(=O)N[C@@H](CCCNC(N)=N)C(=O)N[C@@H](CC(N)=O)C(=O)N[C@@H](CC(N)=O)C(=O)N[C@@H]([C@@H](C)CC)C(=O)N[C@@H](C)C(O)=O DDYAPMZTJAYBOF-ZMYDTDHYSA-N 0.000 description 1
- NFGXHKASABOEEW-UHFFFAOYSA-N 1-methylethyl 11-methoxy-3,7,11-trimethyl-2,4-dodecadienoate Chemical compound COC(C)(C)CCCC(C)CC=CC(C)=CC(=O)OC(C)C NFGXHKASABOEEW-UHFFFAOYSA-N 0.000 description 1
- 150000003923 2,5-pyrrolediones Chemical class 0.000 description 1
- JVJUWEFOGFCHKR-UHFFFAOYSA-N 2-(diethylamino)ethyl 1-(3,4-dimethylphenyl)cyclopentane-1-carboxylate;hydrochloride Chemical compound Cl.C=1C=C(C)C(C)=CC=1C1(C(=O)OCCN(CC)CC)CCCC1 JVJUWEFOGFCHKR-UHFFFAOYSA-N 0.000 description 1
- BIGBDMFRWJRLGJ-UHFFFAOYSA-N 3-benzyl-1,5-didiazoniopenta-1,4-diene-2,4-diolate Chemical compound [N-]=[N+]=CC(=O)C(C(=O)C=[N+]=[N-])CC1=CC=CC=C1 BIGBDMFRWJRLGJ-UHFFFAOYSA-N 0.000 description 1
- CYDQOEWLBCCFJZ-UHFFFAOYSA-N 4-(4-fluorophenyl)oxane-4-carboxylic acid Chemical compound C=1C=C(F)C=CC=1C1(C(=O)O)CCOCC1 CYDQOEWLBCCFJZ-UHFFFAOYSA-N 0.000 description 1
- NLPWSMKACWGINL-UHFFFAOYSA-N 4-azido-2-hydroxybenzoic acid Chemical compound OC(=O)C1=CC=C(N=[N+]=[N-])C=C1O NLPWSMKACWGINL-UHFFFAOYSA-N 0.000 description 1
- HFDKKNHCYWNNNQ-YOGANYHLSA-N 75976-10-2 Chemical compound C([C@@H](C(=O)N[C@@H]([C@@H](C)CC)C(=O)N[C@@H](CC(N)=O)C(=O)N[C@@H](CCSC)C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H]([C@@H](C)O)C(=O)N[C@@H](CCCNC(N)=N)C(=O)N1[C@@H](CCC1)C(=O)N[C@@H](CCCNC(N)=N)C(=O)N[C@@H](CC=1C=CC(O)=CC=1)C(N)=O)NC(=O)[C@H](CCCNC(N)=N)NC(=O)[C@H](CCCNC(N)=N)NC(=O)[C@H](CC(C)C)NC(=O)[C@H](CC(O)=O)NC(=O)[C@H](C)NC(=O)[C@H](C)NC(=O)[C@H](CC=1C=CC(O)=CC=1)NC(=O)[C@H](CCC(N)=O)NC(=O)[C@H](C)NC(=O)[C@H](CCSC)NC(=O)[C@H](CCC(N)=O)NC(=O)[C@H](CCC(O)=O)NC(=O)[C@H]1N(CCC1)C(=O)[C@@H](NC(=O)[C@H](C)NC(=O)[C@H](CC(N)=O)NC(=O)[C@H](CC(O)=O)NC(=O)CNC(=O)[C@H]1N(CCC1)C(=O)[C@H](CC=1C=CC(O)=CC=1)NC(=O)[C@@H](NC(=O)[C@H]1N(CCC1)C(=O)[C@H](CCC(O)=O)NC(=O)[C@H](CC(C)C)NC(=O)[C@H]1N(CCC1)C(=O)[C@H](C)N)C(C)C)[C@@H](C)O)C1=CC=C(O)C=C1 HFDKKNHCYWNNNQ-YOGANYHLSA-N 0.000 description 1
- IPWKGIFRRBGCJO-IMJSIDKUSA-N Ala-Ser Chemical compound C[C@H]([NH3+])C(=O)N[C@@H](CO)C([O-])=O IPWKGIFRRBGCJO-IMJSIDKUSA-N 0.000 description 1
- 102100026277 Alpha-galactosidase A Human genes 0.000 description 1
- 102000009840 Angiopoietins Human genes 0.000 description 1
- 108010009906 Angiopoietins Proteins 0.000 description 1
- 102400000068 Angiostatin Human genes 0.000 description 1
- 108010079709 Angiostatins Proteins 0.000 description 1
- 108010064733 Angiotensins Proteins 0.000 description 1
- 102000015427 Angiotensins Human genes 0.000 description 1
- 102100029470 Apolipoprotein E Human genes 0.000 description 1
- 101710095339 Apolipoprotein E Proteins 0.000 description 1
- 102100033367 Appetite-regulating hormone Human genes 0.000 description 1
- 108010024976 Asparaginase Proteins 0.000 description 1
- 102000002723 Atrial Natriuretic Factor Human genes 0.000 description 1
- 101800001288 Atrial natriuretic factor Proteins 0.000 description 1
- 108010046304 B-Cell Activation Factor Receptor Proteins 0.000 description 1
- 102000007536 B-Cell Activation Factor Receptor Human genes 0.000 description 1
- 102100022005 B-lymphocyte antigen CD20 Human genes 0.000 description 1
- 241000894006 Bacteria Species 0.000 description 1
- 102400000667 Brain natriuretic peptide 32 Human genes 0.000 description 1
- 101800000407 Brain natriuretic peptide 32 Proteins 0.000 description 1
- 101800002247 Brain natriuretic peptide 45 Proteins 0.000 description 1
- 108010074051 C-Reactive Protein Proteins 0.000 description 1
- 102100032752 C-reactive protein Human genes 0.000 description 1
- 101150013553 CD40 gene Proteins 0.000 description 1
- 108060001064 Calcitonin Proteins 0.000 description 1
- 102000055006 Calcitonin Human genes 0.000 description 1
- UXVMQQNJUSDDNG-UHFFFAOYSA-L Calcium chloride Chemical compound [Cl-].[Cl-].[Ca+2] UXVMQQNJUSDDNG-UHFFFAOYSA-L 0.000 description 1
- 108010078791 Carrier Proteins Proteins 0.000 description 1
- 108010012236 Chemokines Proteins 0.000 description 1
- 102000019034 Chemokines Human genes 0.000 description 1
- 102000012286 Chitinases Human genes 0.000 description 1
- 108010022172 Chitinases Proteins 0.000 description 1
- 101800001982 Cholecystokinin Proteins 0.000 description 1
- 102100025841 Cholecystokinin Human genes 0.000 description 1
- 108010005939 Ciliary Neurotrophic Factor Proteins 0.000 description 1
- 102100031614 Ciliary neurotrophic factor Human genes 0.000 description 1
- 102100022641 Coagulation factor IX Human genes 0.000 description 1
- 108010022152 Corticotropin-Releasing Hormone Proteins 0.000 description 1
- 239000000055 Corticotropin-Releasing Hormone Substances 0.000 description 1
- 102000012289 Corticotropin-Releasing Hormone Human genes 0.000 description 1
- 102100025012 Dipeptidyl peptidase 4 Human genes 0.000 description 1
- 108010024212 E-Selectin Proteins 0.000 description 1
- 102100023471 E-selectin Human genes 0.000 description 1
- 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 1
- 102100021977 Ectonucleotide pyrophosphatase/phosphodiesterase family member 2 Human genes 0.000 description 1
- 108050004000 Ectonucleotide pyrophosphatase/phosphodiesterase family member 2 Proteins 0.000 description 1
- 108010013369 Enteropeptidase Proteins 0.000 description 1
- 102100029727 Enteropeptidase Human genes 0.000 description 1
- 102000009024 Epidermal Growth Factor Human genes 0.000 description 1
- 101800003838 Epidermal growth factor Proteins 0.000 description 1
- 241000588724 Escherichia coli Species 0.000 description 1
- LFQSCWFLJHTTHZ-UHFFFAOYSA-N Ethanol Chemical compound CCO LFQSCWFLJHTTHZ-UHFFFAOYSA-N 0.000 description 1
- 108010076282 Factor IX Proteins 0.000 description 1
- 108010054218 Factor VIII Proteins 0.000 description 1
- 102000001690 Factor VIII Human genes 0.000 description 1
- 108010071289 Factor XIII Proteins 0.000 description 1
- 102000009109 Fc receptors Human genes 0.000 description 1
- 108010087819 Fc receptors Proteins 0.000 description 1
- 108010008177 Fd immunoglobulins Proteins 0.000 description 1
- 102000009123 Fibrin Human genes 0.000 description 1
- 108010073385 Fibrin Proteins 0.000 description 1
- BWGVNKXGVNDBDI-UHFFFAOYSA-N Fibrin monomer Chemical compound CNC(=O)CNC(=O)CN BWGVNKXGVNDBDI-UHFFFAOYSA-N 0.000 description 1
- 108010088842 Fibrinolysin Proteins 0.000 description 1
- 238000012413 Fluorescence activated cell sorting analysis Methods 0.000 description 1
- 108010079345 Follicle Stimulating Hormone Proteins 0.000 description 1
- 102000012673 Follicle Stimulating Hormone Human genes 0.000 description 1
- 108090000045 G-Protein-Coupled Receptors Proteins 0.000 description 1
- 102000003688 G-Protein-Coupled Receptors Human genes 0.000 description 1
- 108700012941 GNRH1 Proteins 0.000 description 1
- 102000004862 Gastrin releasing peptide Human genes 0.000 description 1
- 108090001053 Gastrin releasing peptide Proteins 0.000 description 1
- 108700039691 Genetic Promoter Regions Proteins 0.000 description 1
- 206010056740 Genital discharge Diseases 0.000 description 1
- 102000034615 Glial cell line-derived neurotrophic factor Human genes 0.000 description 1
- 108091010837 Glial cell line-derived neurotrophic factor Proteins 0.000 description 1
- 102400000321 Glucagon Human genes 0.000 description 1
- 108060003199 Glucagon Proteins 0.000 description 1
- 108010088406 Glucagon-Like Peptides Proteins 0.000 description 1
- 108010017544 Glucosylceramidase Proteins 0.000 description 1
- 102000008214 Glutamate decarboxylase Human genes 0.000 description 1
- 108091022930 Glutamate decarboxylase Proteins 0.000 description 1
- 102000003886 Glycoproteins Human genes 0.000 description 1
- 108090000288 Glycoproteins Proteins 0.000 description 1
- 239000000579 Gonadotropin-Releasing Hormone Substances 0.000 description 1
- 239000000095 Growth Hormone-Releasing Hormone Substances 0.000 description 1
- 102100021519 Hemoglobin subunit beta Human genes 0.000 description 1
- 108091005904 Hemoglobin subunit beta Proteins 0.000 description 1
- 108010054147 Hemoglobins Proteins 0.000 description 1
- 102000001554 Hemoglobins Human genes 0.000 description 1
- 102100021866 Hepatocyte growth factor Human genes 0.000 description 1
- 241000238631 Hexapoda Species 0.000 description 1
- 102000007625 Hirudins Human genes 0.000 description 1
- 108010007267 Hirudins Proteins 0.000 description 1
- 101000897405 Homo sapiens B-lymphocyte antigen CD20 Proteins 0.000 description 1
- 101000777314 Homo sapiens Choline kinase alpha Proteins 0.000 description 1
- 101000777313 Homo sapiens Choline/ethanolamine kinase Proteins 0.000 description 1
- 101000908391 Homo sapiens Dipeptidyl peptidase 4 Proteins 0.000 description 1
- 101000898034 Homo sapiens Hepatocyte growth factor Proteins 0.000 description 1
- 101000599951 Homo sapiens Insulin-like growth factor I Proteins 0.000 description 1
- 101001054334 Homo sapiens Interferon beta Proteins 0.000 description 1
- 101001057504 Homo sapiens Interferon-stimulated gene 20 kDa protein Proteins 0.000 description 1
- 101001055144 Homo sapiens Interleukin-2 receptor subunit alpha Proteins 0.000 description 1
- 101001076408 Homo sapiens Interleukin-6 Proteins 0.000 description 1
- 101000651236 Homo sapiens NCK-interacting protein with SH3 domain Proteins 0.000 description 1
- 101000868152 Homo sapiens Son of sevenless homolog 1 Proteins 0.000 description 1
- 101000946843 Homo sapiens T-cell surface glycoprotein CD8 alpha chain Proteins 0.000 description 1
- 241000700588 Human alphaherpesvirus 1 Species 0.000 description 1
- 241000701024 Human betaherpesvirus 5 Species 0.000 description 1
- 206010020751 Hypersensitivity Diseases 0.000 description 1
- 102100029199 Iduronate 2-sulfatase Human genes 0.000 description 1
- 101710096421 Iduronate 2-sulfatase Proteins 0.000 description 1
- 102000004627 Iduronidase Human genes 0.000 description 1
- 108010003381 Iduronidase Proteins 0.000 description 1
- 102000009438 IgE Receptors Human genes 0.000 description 1
- 108010073816 IgE Receptors Proteins 0.000 description 1
- 102000009786 Immunoglobulin Constant Regions Human genes 0.000 description 1
- 108010009817 Immunoglobulin Constant Regions Proteins 0.000 description 1
- 108010065825 Immunoglobulin Light Chains Proteins 0.000 description 1
- 102000012745 Immunoglobulin Subunits Human genes 0.000 description 1
- 108010079585 Immunoglobulin Subunits Proteins 0.000 description 1
- 206010061218 Inflammation Diseases 0.000 description 1
- 102000004877 Insulin Human genes 0.000 description 1
- 108090001061 Insulin Proteins 0.000 description 1
- 102100037852 Insulin-like growth factor I Human genes 0.000 description 1
- 102000001617 Interferon Receptors Human genes 0.000 description 1
- 108010054267 Interferon Receptors Proteins 0.000 description 1
- 102000007438 Interferon alpha-beta Receptor Human genes 0.000 description 1
- 108010086140 Interferon alpha-beta Receptor Proteins 0.000 description 1
- 108010074328 Interferon-gamma Proteins 0.000 description 1
- 102000008070 Interferon-gamma Human genes 0.000 description 1
- 102100027268 Interferon-stimulated gene 20 kDa protein Human genes 0.000 description 1
- 102000010787 Interleukin-4 Receptors Human genes 0.000 description 1
- 108010038486 Interleukin-4 Receptors Proteins 0.000 description 1
- 108091092195 Intron Proteins 0.000 description 1
- 108010092694 L-Selectin Proteins 0.000 description 1
- LEVWYRKDKASIDU-IMJSIDKUSA-N L-cystine Chemical compound [O-]C(=O)[C@@H]([NH3+])CSSC[C@H]([NH3+])C([O-])=O LEVWYRKDKASIDU-IMJSIDKUSA-N 0.000 description 1
- 102100033467 L-selectin Human genes 0.000 description 1
- 102000004407 Lactalbumin Human genes 0.000 description 1
- 108090000942 Lactalbumin Proteins 0.000 description 1
- 108010063045 Lactoferrin Proteins 0.000 description 1
- 102000010445 Lactoferrin Human genes 0.000 description 1
- 108010092277 Leptin Proteins 0.000 description 1
- 102000016267 Leptin Human genes 0.000 description 1
- 102000004882 Lipase Human genes 0.000 description 1
- 108090001060 Lipase Proteins 0.000 description 1
- 239000004367 Lipase Substances 0.000 description 1
- 239000000232 Lipid Bilayer Substances 0.000 description 1
- 108010073521 Luteinizing Hormone Proteins 0.000 description 1
- 102000009151 Luteinizing Hormone Human genes 0.000 description 1
- 108090000542 Lymphotoxin-alpha Proteins 0.000 description 1
- 102000004083 Lymphotoxin-alpha Human genes 0.000 description 1
- 206010027476 Metastases Diseases 0.000 description 1
- 101000966481 Mus musculus Dihydrofolate reductase Proteins 0.000 description 1
- 101001033276 Mus musculus Interleukin-3 Proteins 0.000 description 1
- 241000699670 Mus sp. Species 0.000 description 1
- 102400000569 Myeloperoxidase Human genes 0.000 description 1
- 108090000235 Myeloperoxidases Proteins 0.000 description 1
- 101001055320 Myxine glutinosa Insulin-like growth factor Proteins 0.000 description 1
- 206010028851 Necrosis Diseases 0.000 description 1
- 206010028980 Neoplasm Diseases 0.000 description 1
- 102000003729 Neprilysin Human genes 0.000 description 1
- 108090000028 Neprilysin Proteins 0.000 description 1
- 102000015336 Nerve Growth Factor Human genes 0.000 description 1
- 102000010803 Netrins Human genes 0.000 description 1
- 108010063605 Netrins Proteins 0.000 description 1
- 241000283973 Oryctolagus cuniculus Species 0.000 description 1
- 108010035766 P-Selectin Proteins 0.000 description 1
- 102100023472 P-selectin Human genes 0.000 description 1
- 102000018886 Pancreatic Polypeptide Human genes 0.000 description 1
- 102000003982 Parathyroid hormone Human genes 0.000 description 1
- 108090000445 Parathyroid hormone Proteins 0.000 description 1
- 108010067902 Peptide Library Proteins 0.000 description 1
- 102100037765 Periostin Human genes 0.000 description 1
- 101710199268 Periostin Proteins 0.000 description 1
- 102100031538 Phosphatidylcholine-sterol acyltransferase Human genes 0.000 description 1
- 102000013566 Plasminogen Human genes 0.000 description 1
- 108010051456 Plasminogen Proteins 0.000 description 1
- 102000010780 Platelet-Derived Growth Factor Human genes 0.000 description 1
- 108010038512 Platelet-Derived Growth Factor Proteins 0.000 description 1
- 102100033237 Pro-epidermal growth factor Human genes 0.000 description 1
- 101800004937 Protein C Proteins 0.000 description 1
- 102000017975 Protein C Human genes 0.000 description 1
- 101710149951 Protein Tat Proteins 0.000 description 1
- 108091034057 RNA (poly(A)) Proteins 0.000 description 1
- 241000700159 Rattus Species 0.000 description 1
- 108010008281 Recombinant Fusion Proteins Proteins 0.000 description 1
- 102000007056 Recombinant Fusion Proteins Human genes 0.000 description 1
- 102000003743 Relaxin Human genes 0.000 description 1
- 108090000103 Relaxin Proteins 0.000 description 1
- 101710102802 Runt-related transcription factor 2 Proteins 0.000 description 1
- 101800001700 Saposin-D Proteins 0.000 description 1
- 102100037505 Secretin Human genes 0.000 description 1
- 108010086019 Secretin Proteins 0.000 description 1
- VMHLLURERBWHNL-UHFFFAOYSA-M Sodium acetate Chemical compound [Na+].CC([O-])=O VMHLLURERBWHNL-UHFFFAOYSA-M 0.000 description 1
- 101710142969 Somatoliberin Proteins 0.000 description 1
- 102100022831 Somatoliberin Human genes 0.000 description 1
- 108010023197 Streptokinase Proteins 0.000 description 1
- QAOWNCQODCNURD-UHFFFAOYSA-N Sulfuric acid Chemical compound OS(O)(=O)=O QAOWNCQODCNURD-UHFFFAOYSA-N 0.000 description 1
- 102000019197 Superoxide Dismutase Human genes 0.000 description 1
- 108010012715 Superoxide dismutase Proteins 0.000 description 1
- 101000983124 Sus scrofa Pancreatic prohormone precursor Proteins 0.000 description 1
- 102100034922 T-cell surface glycoprotein CD8 alpha chain Human genes 0.000 description 1
- 210000001744 T-lymphocyte Anatomy 0.000 description 1
- 102000000479 TCF Transcription Factors Human genes 0.000 description 1
- 108010016283 TCF Transcription Factors Proteins 0.000 description 1
- 108020005038 Terminator Codon Proteins 0.000 description 1
- 108090000190 Thrombin Proteins 0.000 description 1
- 102000003790 Thrombin receptors Human genes 0.000 description 1
- 108010079274 Thrombomodulin Proteins 0.000 description 1
- 102100026966 Thrombomodulin Human genes 0.000 description 1
- 102000011923 Thyrotropin Human genes 0.000 description 1
- 108010061174 Thyrotropin Proteins 0.000 description 1
- 102100030951 Tissue factor pathway inhibitor Human genes 0.000 description 1
- 108090000631 Trypsin Proteins 0.000 description 1
- 102000004142 Trypsin Human genes 0.000 description 1
- 102100040245 Tumor necrosis factor receptor superfamily member 5 Human genes 0.000 description 1
- 108010092464 Urate Oxidase Proteins 0.000 description 1
- 108090000435 Urokinase-type plasminogen activator Proteins 0.000 description 1
- 102000003990 Urokinase-type plasminogen activator Human genes 0.000 description 1
- 108091008605 VEGF receptors Proteins 0.000 description 1
- 102000009484 Vascular Endothelial Growth Factor Receptors Human genes 0.000 description 1
- 238000002835 absorbance Methods 0.000 description 1
- 230000009471 action Effects 0.000 description 1
- 238000007792 addition Methods 0.000 description 1
- 239000002671 adjuvant Substances 0.000 description 1
- 239000003470 adrenal cortex hormone Substances 0.000 description 1
- 230000002411 adverse Effects 0.000 description 1
- 239000000443 aerosol Substances 0.000 description 1
- 208000026935 allergic disease Diseases 0.000 description 1
- 230000007815 allergy Effects 0.000 description 1
- 108010050122 alpha 1-Antitrypsin Proteins 0.000 description 1
- 102000015395 alpha 1-Antitrypsin Human genes 0.000 description 1
- 229940024142 alpha 1-antitrypsin Drugs 0.000 description 1
- 108010030291 alpha-Galactosidase Proteins 0.000 description 1
- 238000004458 analytical method Methods 0.000 description 1
- 210000000628 antibody-producing cell Anatomy 0.000 description 1
- 238000013459 approach Methods 0.000 description 1
- FZCSTZYAHCUGEM-UHFFFAOYSA-N aspergillomarasmine B Natural products OC(=O)CNC(C(O)=O)CNC(C(O)=O)CC(O)=O FZCSTZYAHCUGEM-UHFFFAOYSA-N 0.000 description 1
- 238000003149 assay kit Methods 0.000 description 1
- 210000003719 b-lymphocyte Anatomy 0.000 description 1
- 230000001588 bifunctional effect Effects 0.000 description 1
- 108091008324 binding proteins Proteins 0.000 description 1
- 210000000601 blood cell Anatomy 0.000 description 1
- 210000000988 bone and bone Anatomy 0.000 description 1
- 230000008468 bone growth Effects 0.000 description 1
- 239000000872 buffer Substances 0.000 description 1
- 229960004015 calcitonin Drugs 0.000 description 1
- BBBFJLBPOGFECG-VJVYQDLKSA-N calcitonin Chemical compound N([C@H](C(=O)N[C@@H](CC(C)C)C(=O)NCC(=O)N[C@@H](CCCCN)C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](CO)C(=O)N[C@@H](CCC(N)=O)C(=O)N[C@@H](CCC(O)=O)C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](CC=1NC=NC=1)C(=O)N[C@@H](CCCCN)C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](CCC(N)=O)C(=O)N[C@@H]([C@@H](C)O)C(=O)N[C@@H](CC=1C=CC(O)=CC=1)C(=O)N1[C@@H](CCC1)C(=O)N[C@@H](CCCNC(N)=N)C(=O)N[C@@H]([C@@H](C)O)C(=O)N[C@@H](CC(N)=O)C(=O)N[C@@H]([C@@H](C)O)C(=O)NCC(=O)N[C@@H](CO)C(=O)NCC(=O)N[C@@H]([C@@H](C)O)C(=O)N1[C@@H](CCC1)C(N)=O)C(C)C)C(=O)[C@@H]1CSSC[C@H](N)C(=O)N[C@@H](CO)C(=O)N[C@@H](CC(N)=O)C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](CO)C(=O)N[C@@H]([C@@H](C)O)C(=O)N1 BBBFJLBPOGFECG-VJVYQDLKSA-N 0.000 description 1
- 239000001110 calcium chloride Substances 0.000 description 1
- 229910001628 calcium chloride Inorganic materials 0.000 description 1
- 235000011148 calcium chloride Nutrition 0.000 description 1
- 125000003178 carboxy group Chemical group [H]OC(*)=O 0.000 description 1
- 229950008486 carperitide Drugs 0.000 description 1
- NSQLIUXCMFBZME-MPVJKSABSA-N carperitide Chemical compound C([C@H]1C(=O)NCC(=O)NCC(=O)N[C@@H](CCCNC(N)=N)C(=O)N[C@@H](CCSC)C(=O)N[C@@H](CC(O)=O)C(=O)N[C@@H](CCCNC(N)=N)C(=O)N[C@H](C(NCC(=O)N[C@@H](C)C(=O)N[C@@H](CCC(N)=O)C(=O)N[C@@H](CO)C(=O)NCC(=O)N[C@@H](CC(C)C)C(=O)NCC(=O)N[C@@H](CSSC[C@@H](C(=O)N1)NC(=O)[C@H](CO)NC(=O)[C@H](CO)NC(=O)[C@H](CCCNC(N)=N)NC(=O)[C@H](CCCNC(N)=N)NC(=O)[C@H](CC(C)C)NC(=O)[C@@H](N)CO)C(=O)N[C@@H](CC(N)=O)C(=O)N[C@@H](CO)C(=O)N[C@@H](CC=1C=CC=CC=1)C(=O)N[C@@H](CCCNC(N)=N)C(=O)N[C@@H](CC=1C=CC(O)=CC=1)C(O)=O)=O)[C@@H](C)CC)C1=CC=CC=C1 NSQLIUXCMFBZME-MPVJKSABSA-N 0.000 description 1
- 210000000845 cartilage Anatomy 0.000 description 1
- 230000015556 catabolic process Effects 0.000 description 1
- 230000020411 cell activation Effects 0.000 description 1
- 230000022534 cell killing Effects 0.000 description 1
- 239000013592 cell lysate Substances 0.000 description 1
- 210000000170 cell membrane Anatomy 0.000 description 1
- 230000001413 cellular effect Effects 0.000 description 1
- 230000036755 cellular response Effects 0.000 description 1
- 230000008859 change Effects 0.000 description 1
- DDPFHDCZUJFNAT-PZPWKVFESA-N chembl2104402 Chemical compound N([C@H](C(=O)N[C@@H](CC(C)C)C(=O)NCC(=O)N[C@@H](CCCCN)C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](CO)C(=O)N[C@@H](CCC(N)=O)C(=O)N[C@@H](CCC(O)=O)C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](CC=1N=CNC=1)C(=O)N[C@@H](CCCCN)C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](CCC(N)=O)C(=O)N[C@@H]([C@@H](C)O)C(=O)N[C@@H](CC=1C=CC(O)=CC=1)C(=O)N1[C@@H](CCC1)C(=O)N[C@@H](CCCNC(N)=N)C(=O)N[C@@H]([C@@H](C)O)C(=O)N[C@@H](CC(O)=O)C(=O)N[C@@H](C(C)C)C(=O)NCC(=O)N[C@@H](C)C(=O)NCC(=O)N[C@@H]([C@@H](C)O)C(=O)N1[C@@H](CCC1)C(N)=O)C(C)C)C(=O)[C@@H]1CCCCCC(=O)N[C@@H](CO)C(=O)N[C@@H](CC(N)=O)C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](CO)C(=O)N[C@@H]([C@@H](C)O)C(=O)N1 DDPFHDCZUJFNAT-PZPWKVFESA-N 0.000 description 1
- 229940107137 cholecystokinin Drugs 0.000 description 1
- 238000004440 column chromatography Methods 0.000 description 1
- 150000001875 compounds Chemical class 0.000 description 1
- 210000002808 connective tissue Anatomy 0.000 description 1
- 238000012258 culturing Methods 0.000 description 1
- 102000026898 cytokine binding proteins Human genes 0.000 description 1
- 108091008470 cytokine binding proteins Proteins 0.000 description 1
- 230000003247 decreasing effect Effects 0.000 description 1
- 238000006731 degradation reaction Methods 0.000 description 1
- 238000001514 detection method Methods 0.000 description 1
- 238000010586 diagram Methods 0.000 description 1
- 238000000502 dialysis Methods 0.000 description 1
- 230000004069 differentiation Effects 0.000 description 1
- 230000029087 digestion Effects 0.000 description 1
- 238000010790 dilution Methods 0.000 description 1
- 239000012895 dilution Substances 0.000 description 1
- 230000006806 disease prevention Effects 0.000 description 1
- 239000002270 dispersing agent Substances 0.000 description 1
- 230000006334 disulfide bridging Effects 0.000 description 1
- 231100000673 dose–response relationship Toxicity 0.000 description 1
- 239000013583 drug formulation Substances 0.000 description 1
- 108700032313 elcatonin Proteins 0.000 description 1
- 229960000756 elcatonin Drugs 0.000 description 1
- 239000003792 electrolyte Substances 0.000 description 1
- 238000004520 electroporation Methods 0.000 description 1
- 238000006911 enzymatic reaction Methods 0.000 description 1
- 239000002532 enzyme inhibitor Substances 0.000 description 1
- 229940116977 epidermal growth factor Drugs 0.000 description 1
- 230000008472 epithelial growth Effects 0.000 description 1
- 210000003743 erythrocyte Anatomy 0.000 description 1
- 125000001495 ethyl group Chemical group [H]C([H])([H])C([H])([H])* 0.000 description 1
- 210000003527 eukaryotic cell Anatomy 0.000 description 1
- 230000001747 exhibiting effect Effects 0.000 description 1
- 238000002474 experimental method Methods 0.000 description 1
- 239000000284 extract Substances 0.000 description 1
- 229960004222 factor ix Drugs 0.000 description 1
- 229960000301 factor viii Drugs 0.000 description 1
- 229940012444 factor xiii Drugs 0.000 description 1
- 239000003925 fat Substances 0.000 description 1
- 229950003499 fibrin Drugs 0.000 description 1
- 229940028334 follicle stimulating hormone Drugs 0.000 description 1
- 239000012737 fresh medium Substances 0.000 description 1
- 108010077689 gamma-aminobutyryl-2-methyltryptophyl-2-methyltryptophyl-2-methyltryptophyl-lysinamide Proteins 0.000 description 1
- PUBCCFNQJQKCNC-XKNFJVFFSA-N gastrin-releasingpeptide Chemical compound C([C@@H](C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](CCSC)C(N)=O)NC(=O)CNC(=O)[C@@H](NC(=O)[C@H](C)NC(=O)[C@H](CC=1C2=CC=CC=C2NC=1)NC(=O)[C@H](CC=1N=CNC=1)NC(=O)[C@H](CC(N)=O)NC(=O)CNC(=O)[C@H](CCCN=C(N)N)NC(=O)[C@H]1N(CCC1)C(=O)[C@H](CC=1C=CC(O)=CC=1)NC(=O)[C@H](CCSC)NC(=O)[C@H](CCCCN)NC(=O)[C@@H](NC(=O)[C@H](CC(C)C)NC(=O)[C@@H](NC(=O)[C@@H](NC(=O)CNC(=O)CNC(=O)CNC(=O)[C@H](C)NC(=O)[C@H]1N(CCC1)C(=O)[C@H](CC(C)C)NC(=O)[C@H]1N(CCC1)C(=O)[C@@H](N)C(C)C)[C@@H](C)O)C(C)C)[C@@H](C)O)C(C)C)C1=CNC=N1 PUBCCFNQJQKCNC-XKNFJVFFSA-N 0.000 description 1
- 238000001415 gene therapy Methods 0.000 description 1
- 230000002068 genetic effect Effects 0.000 description 1
- 102000018146 globin Human genes 0.000 description 1
- 108060003196 globin Proteins 0.000 description 1
- 229960004666 glucagon Drugs 0.000 description 1
- MASNOZXLGMXCHN-ZLPAWPGGSA-N glucagon Chemical compound C([C@@H](C(=O)N[C@H](C(=O)N[C@@H](CCC(N)=O)C(=O)N[C@@H](CC=1C2=CC=CC=C2NC=1)C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](CCSC)C(=O)N[C@@H](CC(N)=O)C(=O)N[C@@H]([C@@H](C)O)C(O)=O)C(C)C)NC(=O)[C@H](CC(O)=O)NC(=O)[C@H](CCC(N)=O)NC(=O)[C@H](C)NC(=O)[C@H](CCCNC(N)=N)NC(=O)[C@H](CCCNC(N)=N)NC(=O)[C@H](CO)NC(=O)[C@H](CC(O)=O)NC(=O)[C@H](CC(C)C)NC(=O)[C@H](CC=1C=CC(O)=CC=1)NC(=O)[C@H](CCCCN)NC(=O)[C@H](CO)NC(=O)[C@H](CC=1C=CC(O)=CC=1)NC(=O)[C@H](CC(O)=O)NC(=O)[C@H](CO)NC(=O)[C@@H](NC(=O)[C@H](CC=1C=CC=CC=1)NC(=O)[C@@H](NC(=O)CNC(=O)[C@H](CCC(N)=O)NC(=O)[C@H](CO)NC(=O)[C@@H](N)CC=1NC=NC=1)[C@@H](C)O)[C@@H](C)O)C1=CC=CC=C1 MASNOZXLGMXCHN-ZLPAWPGGSA-N 0.000 description 1
- 239000008187 granular material Substances 0.000 description 1
- 230000012010 growth Effects 0.000 description 1
- 239000000122 growth hormone Substances 0.000 description 1
- 230000036541 health Effects 0.000 description 1
- 210000002443 helper t lymphocyte Anatomy 0.000 description 1
- 229940006607 hirudin Drugs 0.000 description 1
- WQPDUTSPKFMPDP-OUMQNGNKSA-N hirudin Chemical compound C([C@@H](C(=O)N[C@@H](CCC(O)=O)C(=O)N[C@@H](CCC(O)=O)C(=O)N[C@@H]([C@@H](C)CC)C(=O)N1[C@@H](CCC1)C(=O)N[C@@H](CCC(O)=O)C(=O)N[C@@H](CCC(O)=O)C(=O)N[C@@H](CC=1C=CC(OS(O)(=O)=O)=CC=1)C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](CCC(N)=O)C(O)=O)NC(=O)[C@H](CC(O)=O)NC(=O)CNC(=O)[C@H](CC(O)=O)NC(=O)[C@H](CC(N)=O)NC(=O)[C@H](CC=1NC=NC=1)NC(=O)[C@H](CO)NC(=O)[C@H](CCC(N)=O)NC(=O)[C@H]1N(CCC1)C(=O)[C@H](CCCCN)NC(=O)[C@H]1N(CCC1)C(=O)[C@@H](NC(=O)CNC(=O)[C@H](CCC(O)=O)NC(=O)CNC(=O)[C@@H](NC(=O)[C@@H](NC(=O)[C@H]1NC(=O)[C@H](CCC(N)=O)NC(=O)[C@H](CC(N)=O)NC(=O)[C@H](CCCCN)NC(=O)[C@H](CCC(O)=O)NC(=O)CNC(=O)[C@H](CC(O)=O)NC(=O)[C@H](CO)NC(=O)CNC(=O)[C@H](CC(C)C)NC(=O)[C@H]([C@@H](C)CC)NC(=O)[C@@H]2CSSC[C@@H](C(=O)N[C@@H](CCC(O)=O)C(=O)NCC(=O)N[C@@H](CO)C(=O)N[C@@H](CC(N)=O)C(=O)N[C@H](C(=O)N[C@H](C(NCC(=O)N[C@@H](CCC(N)=O)C(=O)NCC(=O)N[C@@H](CC(N)=O)C(=O)N[C@@H](CCCCN)C(=O)N2)=O)CSSC1)C(C)C)NC(=O)[C@H](CC(C)C)NC(=O)[C@H]1NC(=O)[C@H](CC(C)C)NC(=O)[C@H](CC(N)=O)NC(=O)[C@H](CCC(N)=O)NC(=O)CNC(=O)[C@H](CO)NC(=O)[C@H](CCC(O)=O)NC(=O)[C@H]([C@@H](C)O)NC(=O)[C@@H](NC(=O)[C@H](CC(O)=O)NC(=O)[C@@H](NC(=O)[C@H](CC=2C=CC(O)=CC=2)NC(=O)[C@@H](NC(=O)[C@@H](N)C(C)C)C(C)C)[C@@H](C)O)CSSC1)C(C)C)[C@@H](C)O)[C@@H](C)O)C1=CC=CC=C1 WQPDUTSPKFMPDP-OUMQNGNKSA-N 0.000 description 1
- 102000051179 human NCKIPSD Human genes 0.000 description 1
- 102000057041 human TNF Human genes 0.000 description 1
- 229940098197 human immunoglobulin g Drugs 0.000 description 1
- 125000001165 hydrophobic group Chemical group 0.000 description 1
- 108010039650 imiglucerase Proteins 0.000 description 1
- 229960002127 imiglucerase Drugs 0.000 description 1
- 230000001900 immune effect Effects 0.000 description 1
- 230000008105 immune reaction Effects 0.000 description 1
- 238000003018 immunoassay Methods 0.000 description 1
- 230000036046 immunoreaction Effects 0.000 description 1
- 230000002637 immunotoxin Effects 0.000 description 1
- 239000002596 immunotoxin Substances 0.000 description 1
- 229940051026 immunotoxin Drugs 0.000 description 1
- 231100000608 immunotoxin Toxicity 0.000 description 1
- 239000007943 implant Substances 0.000 description 1
- 238000002513 implantation Methods 0.000 description 1
- 208000015181 infectious disease Diseases 0.000 description 1
- 230000004054 inflammatory process Effects 0.000 description 1
- 230000000977 initiatory effect Effects 0.000 description 1
- 238000003780 insertion Methods 0.000 description 1
- 230000037431 insertion Effects 0.000 description 1
- 229940125396 insulin Drugs 0.000 description 1
- 230000003993 interaction Effects 0.000 description 1
- 108010093036 interleukin receptors Proteins 0.000 description 1
- 102000002467 interleukin receptors Human genes 0.000 description 1
- 229940047122 interleukins Drugs 0.000 description 1
- 238000007917 intracranial administration Methods 0.000 description 1
- 238000007918 intramuscular administration Methods 0.000 description 1
- 238000007913 intrathecal administration Methods 0.000 description 1
- 238000007914 intraventricular administration Methods 0.000 description 1
- 238000005304 joining Methods 0.000 description 1
- CSSYQJWUGATIHM-IKGCZBKSSA-N l-phenylalanyl-l-lysyl-l-cysteinyl-l-arginyl-l-arginyl-l-tryptophyl-l-glutaminyl-l-tryptophyl-l-arginyl-l-methionyl-l-lysyl-l-lysyl-l-leucylglycyl-l-alanyl-l-prolyl-l-seryl-l-isoleucyl-l-threonyl-l-cysteinyl-l-valyl-l-arginyl-l-arginyl-l-alanyl-l-phenylal Chemical compound C([C@H](N)C(=O)N[C@@H](CCCCN)C(=O)N[C@@H](CS)C(=O)N[C@@H](CCCNC(N)=N)C(=O)N[C@@H](CCCNC(N)=N)C(=O)N[C@@H](CC=1C2=CC=CC=C2NC=1)C(=O)N[C@@H](CCC(N)=O)C(=O)N[C@@H](CC=1C2=CC=CC=C2NC=1)C(=O)N[C@@H](CCCNC(N)=N)C(=O)N[C@@H](CCSC)C(=O)N[C@@H](CCCCN)C(=O)N[C@@H](CCCCN)C(=O)N[C@@H](CC(C)C)C(=O)NCC(=O)N[C@@H](C)C(=O)N1CCC[C@H]1C(=O)N[C@@H](CO)C(=O)N[C@@H]([C@@H](C)CC)C(=O)N[C@@H]([C@@H](C)O)C(=O)N[C@@H](CS)C(=O)N[C@@H](C(C)C)C(=O)N[C@@H](CCCNC(N)=N)C(=O)N[C@@H](CCCNC(N)=N)C(=O)N[C@@H](C)C(=O)N[C@@H](CC=1C=CC=CC=1)C(O)=O)C1=CC=CC=C1 CSSYQJWUGATIHM-IKGCZBKSSA-N 0.000 description 1
- 229940078795 lactoferrin Drugs 0.000 description 1
- 235000021242 lactoferrin Nutrition 0.000 description 1
- 229940039781 leptin Drugs 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
- 239000003446 ligand Substances 0.000 description 1
- 230000000670 limiting effect Effects 0.000 description 1
- 235000019421 lipase Nutrition 0.000 description 1
- 108010013555 lipoprotein-associated coagulation inhibitor Proteins 0.000 description 1
- 210000004185 liver Anatomy 0.000 description 1
- 229940040129 luteinizing hormone Drugs 0.000 description 1
- 239000012139 lysis buffer Substances 0.000 description 1
- 239000011159 matrix material Substances 0.000 description 1
- 230000009401 metastasis Effects 0.000 description 1
- MYWUZJCMWCOHBA-VIFPVBQESA-N methamphetamine Chemical compound CN[C@@H](C)CC1=CC=CC=C1 MYWUZJCMWCOHBA-VIFPVBQESA-N 0.000 description 1
- 230000000813 microbial effect Effects 0.000 description 1
- 244000005700 microbiome Species 0.000 description 1
- 230000004048 modification Effects 0.000 description 1
- 238000012986 modification Methods 0.000 description 1
- 238000001823 molecular biology technique Methods 0.000 description 1
- OHDXDNUPVVYWOV-UHFFFAOYSA-N n-methyl-1-(2-naphthalen-1-ylsulfanylphenyl)methanamine Chemical compound CNCC1=CC=CC=C1SC1=CC=CC2=CC=CC=C12 OHDXDNUPVVYWOV-UHFFFAOYSA-N 0.000 description 1
- 230000017074 necrotic cell death Effects 0.000 description 1
- 229940053128 nerve growth factor Drugs 0.000 description 1
- HPNRHPKXQZSDFX-OAQDCNSJSA-N nesiritide Chemical compound C([C@H]1C(=O)NCC(=O)N[C@@H](CCCNC(N)=N)C(=O)N[C@@H](CCCCN)C(=O)N[C@@H](CCSC)C(=O)N[C@@H](CC(O)=O)C(=O)N[C@@H](CCCNC(N)=N)C(=O)N[C@H](C(N[C@@H](CO)C(=O)N[C@@H](CO)C(=O)N[C@@H](CO)C(=O)N[C@@H](CO)C(=O)NCC(=O)N[C@@H](CC(C)C)C(=O)NCC(=O)N[C@@H](CSSC[C@@H](C(=O)N1)NC(=O)CNC(=O)[C@H](CO)NC(=O)CNC(=O)[C@H](CCC(N)=O)NC(=O)[C@@H](NC(=O)[C@H](CCSC)NC(=O)[C@H](CCCCN)NC(=O)[C@H]1N(CCC1)C(=O)[C@@H](N)CO)C(C)C)C(=O)N[C@@H](CCCCN)C(=O)N[C@@H](C(C)C)C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](CCCNC(N)=N)C(=O)N[C@@H](CCCNC(N)=N)C(=O)N[C@@H](CC=1N=CNC=1)C(O)=O)=O)[C@@H](C)CC)C1=CC=CC=C1 HPNRHPKXQZSDFX-OAQDCNSJSA-N 0.000 description 1
- 239000003900 neurotrophic factor Substances 0.000 description 1
- 230000007935 neutral effect Effects 0.000 description 1
- 210000000440 neutrophil Anatomy 0.000 description 1
- 231100000252 nontoxic Toxicity 0.000 description 1
- 230000003000 nontoxic effect Effects 0.000 description 1
- 229940043515 other immunoglobulins in atc Drugs 0.000 description 1
- 239000003002 pH adjusting agent Substances 0.000 description 1
- 239000000199 parathyroid hormone Substances 0.000 description 1
- 229960001319 parathyroid hormone Drugs 0.000 description 1
- 230000000737 periodic effect Effects 0.000 description 1
- 238000002823 phage display Methods 0.000 description 1
- 230000004962 physiological condition Effects 0.000 description 1
- 230000001766 physiological effect Effects 0.000 description 1
- 230000035790 physiological processes and functions Effects 0.000 description 1
- 229940012957 plasmin Drugs 0.000 description 1
- 238000007747 plating Methods 0.000 description 1
- 230000010287 polarization Effects 0.000 description 1
- 230000008488 polyadenylation Effects 0.000 description 1
- 229920000136 polysorbate Polymers 0.000 description 1
- 239000001103 potassium chloride Substances 0.000 description 1
- 235000011164 potassium chloride Nutrition 0.000 description 1
- 230000002265 prevention Effects 0.000 description 1
- 230000008569 process Effects 0.000 description 1
- 239000000047 product Substances 0.000 description 1
- 230000009696 proliferative response Effects 0.000 description 1
- 230000002035 prolonged effect Effects 0.000 description 1
- 125000001500 prolyl group Chemical group [H]N1C([H])(C(=O)[*])C([H])([H])C([H])([H])C1([H])[H] 0.000 description 1
- 238000000159 protein binding assay Methods 0.000 description 1
- 229960000856 protein c Drugs 0.000 description 1
- 239000002464 receptor antagonist Substances 0.000 description 1
- 229940044551 receptor antagonist Drugs 0.000 description 1
- 239000002461 renin inhibitor Substances 0.000 description 1
- 229940086526 renin-inhibitors Drugs 0.000 description 1
- 238000011160 research Methods 0.000 description 1
- 238000012216 screening Methods 0.000 description 1
- 229960002101 secretin Drugs 0.000 description 1
- OWMZNFCDEHGFEP-NFBCVYDUSA-N secretin human Chemical compound C([C@@H](C(=O)N[C@H](C(=O)N[C@@H](CO)C(=O)N[C@@H](CCC(O)=O)C(=O)N[C@@H](CC(C)C)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](CCCNC(N)=N)C(=O)N[C@@H](CCC(O)=O)C(=O)NCC(=O)N[C@@H](C)C(=O)N[C@@H](CCCNC(N)=N)C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](CCC(N)=O)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)N[C@@H](CCC(N)=O)C(=O)NCC(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](C(C)C)C(N)=O)[C@@H](C)O)NC(=O)[C@@H](NC(=O)CNC(=O)[C@H](CC(O)=O)NC(=O)[C@H](CO)NC(=O)[C@@H](N)CC=1NC=NC=1)[C@@H](C)O)C1=CC=CC=C1 OWMZNFCDEHGFEP-NFBCVYDUSA-N 0.000 description 1
- 230000003248 secreting effect Effects 0.000 description 1
- 239000006152 selective media Substances 0.000 description 1
- 238000002864 sequence alignment Methods 0.000 description 1
- 239000004017 serum-free culture medium Substances 0.000 description 1
- 125000005629 sialic acid group Chemical group 0.000 description 1
- IZTQOLKUZKXIRV-YRVFCXMDSA-N sincalide Chemical compound C([C@@H](C(=O)N[C@@H](CCSC)C(=O)NCC(=O)N[C@@H](CC=1C2=CC=CC=C2NC=1)C(=O)N[C@@H](CCSC)C(=O)N[C@@H](CC(O)=O)C(=O)N[C@@H](CC=1C=CC=CC=1)C(N)=O)NC(=O)[C@@H](N)CC(O)=O)C1=CC=C(OS(O)(=O)=O)C=C1 IZTQOLKUZKXIRV-YRVFCXMDSA-N 0.000 description 1
- 239000001632 sodium acetate Substances 0.000 description 1
- 235000017281 sodium acetate Nutrition 0.000 description 1
- 239000001540 sodium lactate Substances 0.000 description 1
- 229940005581 sodium lactate Drugs 0.000 description 1
- 235000011088 sodium lactate Nutrition 0.000 description 1
- 239000001488 sodium phosphate Substances 0.000 description 1
- 229910000162 sodium phosphate Inorganic materials 0.000 description 1
- 239000007787 solid Substances 0.000 description 1
- 239000008223 sterile water Substances 0.000 description 1
- 230000001954 sterilising effect Effects 0.000 description 1
- 238000004659 sterilization and disinfection Methods 0.000 description 1
- 229960005202 streptokinase Drugs 0.000 description 1
- 230000004083 survival effect Effects 0.000 description 1
- 239000000725 suspension Substances 0.000 description 1
- 230000002459 sustained effect Effects 0.000 description 1
- 238000002560 therapeutic procedure Methods 0.000 description 1
- 229960004072 thrombin Drugs 0.000 description 1
- 108010093640 thrombin receptor peptide SFLLRNP Proteins 0.000 description 1
- 210000001519 tissue Anatomy 0.000 description 1
- 238000011200 topical administration Methods 0.000 description 1
- 239000003440 toxic substance Substances 0.000 description 1
- 230000001988 toxicity Effects 0.000 description 1
- 231100000419 toxicity Toxicity 0.000 description 1
- 230000001052 transient effect Effects 0.000 description 1
- RYFMWSXOAZQYPI-UHFFFAOYSA-K trisodium phosphate Chemical compound [Na+].[Na+].[Na+].[O-]P([O-])([O-])=O RYFMWSXOAZQYPI-UHFFFAOYSA-K 0.000 description 1
- 239000012588 trypsin Substances 0.000 description 1
- VBEQCZHXXJYVRD-GACYYNSASA-N uroanthelone Chemical compound C([C@@H](C(=O)N[C@H](C(=O)N[C@@H](CS)C(=O)N[C@@H](CC(N)=O)C(=O)N[C@@H](CS)C(=O)N[C@H](C(=O)N[C@@H]([C@@H](C)CC)C(=O)NCC(=O)N[C@@H](CC=1C=CC(O)=CC=1)C(=O)N[C@@H](CO)C(=O)NCC(=O)N[C@@H](CC(O)=O)C(=O)N[C@@H](CCCNC(N)=N)C(=O)N[C@@H](CS)C(=O)N[C@@H](CCC(N)=O)C(=O)N[C@@H]([C@@H](C)O)C(=O)N[C@@H](CCCNC(N)=N)C(=O)N[C@@H](CC(O)=O)C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](CCCNC(N)=N)C(=O)N[C@@H](CC=1C2=CC=CC=C2NC=1)C(=O)N[C@@H](CC=1C2=CC=CC=C2NC=1)C(=O)N[C@@H](CCC(O)=O)C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](CCCNC(N)=N)C(O)=O)C(C)C)[C@@H](C)O)NC(=O)[C@H](CO)NC(=O)[C@H](CC(O)=O)NC(=O)[C@H](CC(C)C)NC(=O)[C@H](CO)NC(=O)[C@H](CCC(O)=O)NC(=O)[C@@H](NC(=O)[C@H](CC=1NC=NC=1)NC(=O)[C@H](CCSC)NC(=O)[C@H](CS)NC(=O)[C@@H](NC(=O)CNC(=O)CNC(=O)[C@H](CC(N)=O)NC(=O)[C@H](CC(C)C)NC(=O)[C@H](CS)NC(=O)[C@H](CC=1C=CC(O)=CC=1)NC(=O)CNC(=O)[C@H](CC(O)=O)NC(=O)[C@H](CC=1C=CC(O)=CC=1)NC(=O)[C@H](CO)NC(=O)[C@H](CO)NC(=O)[C@H]1N(CCC1)C(=O)[C@H](CS)NC(=O)CNC(=O)[C@H]1N(CCC1)C(=O)[C@H](CC=1C=CC(O)=CC=1)NC(=O)[C@H](CO)NC(=O)[C@@H](N)CC(N)=O)C(C)C)[C@@H](C)CC)C1=CC=C(O)C=C1 VBEQCZHXXJYVRD-GACYYNSASA-N 0.000 description 1
- 229960005356 urokinase Drugs 0.000 description 1
- 239000003981 vehicle Substances 0.000 description 1
- XLYOFNOQVPJJNP-UHFFFAOYSA-N water Chemical compound O XLYOFNOQVPJJNP-UHFFFAOYSA-N 0.000 description 1
- 239000001993 wax Substances 0.000 description 1
- 238000001262 western blot Methods 0.000 description 1
- 101150001275 yl gene Proteins 0.000 description 1
- 235000021241 α-lactalbumin Nutrition 0.000 description 1
Classifications
-
- C—CHEMISTRY; METALLURGY
- C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
- C12N—MICROORGANISMS OR ENZYMES; COMPOSITIONS THEREOF; PROPAGATING, PRESERVING, OR MAINTAINING MICROORGANISMS; MUTATION OR GENETIC ENGINEERING; CULTURE MEDIA
- C12N15/00—Mutation or genetic engineering; DNA or RNA concerning genetic engineering, vectors, e.g. plasmids, or their isolation, preparation or purification; Use of hosts therefor
- C12N15/09—Recombinant DNA-technology
- C12N15/11—DNA or RNA fragments; Modified forms thereof; Non-coding nucleic acids having a biological activity
- C12N15/62—DNA sequences coding for fusion proteins
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K19/00—Hybrid peptides, i.e. peptides covalently bound to nucleic acids, or non-covalently bound protein-protein complexes
-
- 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
- A61P17/00—Drugs for dermatological disorders
- A61P17/06—Antipsoriatics
-
- 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
- A61P19/00—Drugs for skeletal disorders
- A61P19/08—Drugs for skeletal disorders for bone diseases, e.g. rachitism, Paget's disease
-
- 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
- A61P19/08—Drugs for skeletal disorders for bone diseases, e.g. rachitism, Paget's disease
- A61P19/10—Drugs for skeletal disorders for bone diseases, e.g. rachitism, Paget's disease for osteoporosis
-
- 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
- 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
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P35/00—Antineoplastic agents
- A61P35/02—Antineoplastic agents specific for leukemia
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P37/00—Drugs for immunological or allergic disorders
- 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
- 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
- A61P5/00—Drugs for disorders of the endocrine system
- A61P5/06—Drugs for disorders of the endocrine system of the anterior pituitary hormones, e.g. TSH, ACTH, FSH, LH, PRL, GH
-
- 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
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K16/00—Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61K—PREPARATIONS FOR MEDICAL, DENTAL OR TOILETRY PURPOSES
- A61K38/00—Medicinal preparations containing peptides
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K2317/00—Immunoglobulins specific features
- C07K2317/50—Immunoglobulins specific features characterized by immunoglobulin fragments
- C07K2317/52—Constant or Fc region; Isotype
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K2317/00—Immunoglobulins specific features
- C07K2317/50—Immunoglobulins specific features characterized by immunoglobulin fragments
- C07K2317/52—Constant or Fc region; Isotype
- C07K2317/53—Hinge
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K2317/00—Immunoglobulins specific features
- C07K2317/60—Immunoglobulins specific features characterized by non-natural combinations of immunoglobulin fragments
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K2319/00—Fusion polypeptide
- C07K2319/30—Non-immunoglobulin-derived peptide or protein having an immunoglobulin constant or Fc region, or a fragment thereof, attached thereto
Landscapes
- Health & Medical Sciences (AREA)
- Life Sciences & Earth Sciences (AREA)
- Chemical & Material Sciences (AREA)
- Organic Chemistry (AREA)
- Engineering & Computer Science (AREA)
- General Health & Medical Sciences (AREA)
- Medicinal Chemistry (AREA)
- Bioinformatics & Cheminformatics (AREA)
- Veterinary Medicine (AREA)
- Public Health (AREA)
- General Chemical & Material Sciences (AREA)
- Pharmacology & Pharmacy (AREA)
- Chemical Kinetics & Catalysis (AREA)
- Animal Behavior & Ethology (AREA)
- Nuclear Medicine, Radiotherapy & Molecular Imaging (AREA)
- Genetics & Genomics (AREA)
- Immunology (AREA)
- Biomedical Technology (AREA)
- Molecular Biology (AREA)
- Physical Education & Sports Medicine (AREA)
- Biochemistry (AREA)
- Rheumatology (AREA)
- General Engineering & Computer Science (AREA)
- Biotechnology (AREA)
- Zoology (AREA)
- Wood Science & Technology (AREA)
- Biophysics (AREA)
- Orthopedic Medicine & Surgery (AREA)
- Microbiology (AREA)
- Diabetes (AREA)
- Hematology (AREA)
- Plant Pathology (AREA)
- Proteomics, Peptides & Aminoacids (AREA)
- Physics & Mathematics (AREA)
- Oncology (AREA)
- Communicable Diseases (AREA)
- Neurosurgery (AREA)
- Pain & Pain Management (AREA)
- Dermatology (AREA)
- Neurology (AREA)
Abstract
Description
Claims
Priority Applications (15)
Application Number | Priority Date | Filing Date | Title |
---|---|---|---|
KR1020097008080A KR101380732B1 (en) | 2007-05-30 | 2008-05-30 | Immunoglobulin fusion proteins |
RU2009141975/10A RU2530168C2 (en) | 2007-05-30 | 2008-05-30 | Fused immunoglobulin proteins |
CA2687377A CA2687377C (en) | 2007-05-30 | 2008-05-30 | Immunoglobulin fusion proteins |
CN201510683410.5A CN105175553B (en) | 2007-05-30 | 2008-05-30 | Domain-immunoglobulin fusion proteins |
EP16206809.2A EP3176264B1 (en) | 2007-05-30 | 2008-05-30 | Immunoglobulin fusion proteins |
KR1020147004294A KR101380729B1 (en) | 2007-05-30 | 2008-05-30 | Immunoglobulin fusion proteins |
CN200880016313.9A CN101687933B (en) | 2007-05-30 | 2008-05-30 | Domain-immunoglobulin fusion proteins |
JP2010510223A JP5577243B2 (en) | 2007-05-30 | 2008-05-30 | Immunoglobulin fusion protein |
ES08766022T ES2415604T3 (en) | 2007-05-30 | 2008-05-30 | Immunoglobulin Fusion Proteins |
EP08766022A EP2162472B1 (en) | 2007-05-30 | 2008-05-30 | Immunoglobulin fusion proteins |
EP16206834.0A EP3173484B1 (en) | 2007-05-30 | 2008-05-30 | Immunoglobulin fusion proteins |
AU2008257923A AU2008257923B2 (en) | 2007-05-30 | 2008-05-30 | Immunoglobulin fusion proteins |
BRPI0811637A BRPI0811637B8 (en) | 2007-05-30 | 2008-05-30 | immunoglobulin fusion proteins |
IL202128A IL202128A0 (en) | 2007-05-30 | 2009-11-15 | Immunoglobulin fusion proteins |
HK10107700.4A HK1141303A1 (en) | 2007-05-30 | 2010-08-12 | Immunoglobulin fusion proteins |
Applications Claiming Priority (2)
Application Number | Priority Date | Filing Date | Title |
---|---|---|---|
US94075307P | 2007-05-30 | 2007-05-30 | |
US60/940,753 | 2007-05-30 |
Publications (2)
Publication Number | Publication Date |
---|---|
WO2008147143A2 true WO2008147143A2 (en) | 2008-12-04 |
WO2008147143A3 WO2008147143A3 (en) | 2009-02-26 |
Family
ID=40088983
Family Applications (1)
Application Number | Title | Priority Date | Filing Date |
---|---|---|---|
PCT/KR2008/003060 WO2008147143A2 (en) | 2007-05-30 | 2008-05-30 | Immunoglobulin fusion proteins |
Country Status (14)
Country | Link |
---|---|
US (5) | US7867491B2 (en) |
EP (4) | EP2662449B1 (en) |
JP (1) | JP5577243B2 (en) |
KR (3) | KR101380729B1 (en) |
CN (5) | CN105131127B (en) |
AU (1) | AU2008257923B2 (en) |
BR (1) | BRPI0811637B8 (en) |
CA (1) | CA2687377C (en) |
DK (1) | DK2662449T3 (en) |
ES (2) | ES2623925T3 (en) |
HK (5) | HK1141303A1 (en) |
IL (1) | IL202128A0 (en) |
RU (1) | RU2530168C2 (en) |
WO (1) | WO2008147143A2 (en) |
Cited By (30)
Publication number | Priority date | Publication date | Assignee | Title |
---|---|---|---|---|
CN101747440A (en) * | 2008-12-18 | 2010-06-23 | 欣润(上海)生物药业有限公司 | TNFR-Fc fusion protein and usage thereof |
WO2014145050A1 (en) | 2013-03-15 | 2014-09-18 | Atyr Pharma, Inc. | Histidyl-trna synthetase-fc conjugates |
US20140377280A1 (en) * | 2011-12-19 | 2014-12-25 | The Rockefeller University | Non-sialylated anti-inflammatory polypeptides |
WO2015031673A2 (en) | 2013-08-28 | 2015-03-05 | Bioasis Technologies Inc. | Cns-targeted conjugates having modified fc regions and methods of use thereof |
EP2842969A4 (en) * | 2012-04-23 | 2016-01-13 | Nrl Pharma Inc | Lactoferrin fusion protein and method for producing same |
US9273108B2 (en) | 2010-05-25 | 2016-03-01 | Generon (Shanghai) Corporation Ltd. | Recombinant human G-CSF dimer and use thereof for the treatment of neurological diseases |
US9474803B2 (en) | 2012-11-27 | 2016-10-25 | Alteogen Inc. | Composition for stabilizing fusion protein in which protein and FC domain are fused |
US9642917B2 (en) | 2011-07-25 | 2017-05-09 | Generon (Shanghai) Corporation, Ltd. | Use of G-CSF dimer in preparation of medicament for treatment of neurodegenerative diseases |
EP3243525A4 (en) * | 2015-01-09 | 2018-07-25 | Genexine, Inc. | Method for treating anemia using long-acting epo preparation |
WO2018195338A1 (en) | 2017-04-20 | 2018-10-25 | Atyr Pharma, Inc. | Compositions and methods for treating lung inflammation |
US10155811B2 (en) | 2013-11-20 | 2018-12-18 | Regeneron Pharmaceuticals, Inc. | APLNR modulators and uses thereof |
EP2726092B1 (en) * | 2011-06-28 | 2019-06-19 | Inhibrx, LP | Serpin fusion polypeptides and methods of use thereof |
EP3514171A1 (en) * | 2018-01-18 | 2019-07-24 | Molecular Cloning Laboratories (MCLAB) LLC | Long-acting therapeutic fusion proteins |
US10400029B2 (en) | 2011-06-28 | 2019-09-03 | Inhibrx, Lp | Serpin fusion polypeptides and methods of use thereof |
US10538569B2 (en) | 2014-12-31 | 2020-01-21 | Genexine, Inc. | Fusion polypeptide containing GLP and immunoglobulin hybrid Fc and use thereof |
US10639368B2 (en) | 2016-05-27 | 2020-05-05 | Agenus Inc. | Anti-TIM-3 antibodies and methods of use thereof |
WO2020184941A1 (en) * | 2019-03-08 | 2020-09-17 | Genexine, Inc. | Glp-1 fusion proteins and uses thereof |
CN111944058A (en) * | 2020-07-28 | 2020-11-17 | 中国农业大学 | Multifunctional hybrid peptide with antibacterial, anti-inflammatory, endotoxin neutralization and immunoregulation activities, and preparation method and application thereof |
US10844125B2 (en) | 2015-03-04 | 2020-11-24 | The Rockefeller University | Anti-inflammatory polypeptides |
US20210070833A1 (en) * | 2018-01-08 | 2021-03-11 | Gl INNOVATION, INC. | Extracellular domain of alpha subunit of ige fc receptor, pharmaceutical composition comprising same and method for producing same |
US10988537B2 (en) | 2013-02-01 | 2021-04-27 | Regeneren Pharmaceuticals, Inc. | Antibodies comprising chimeric constant domains |
US11041014B2 (en) | 2016-10-28 | 2021-06-22 | S & K Biopharma, Inc. | Lactoferrin/albumin fusion protein and production method therefor |
US11208452B2 (en) | 2015-06-02 | 2021-12-28 | Novo Nordisk A/S | Insulins with polar recombinant extensions |
US11292825B2 (en) | 2015-10-01 | 2022-04-05 | Novo Nordisk A/S | Protein conjugates |
US11434300B2 (en) | 2014-03-19 | 2022-09-06 | Regeneron Pharmaceuticals, Inc. | Methods and antibody compositions for tumor treatment |
US11471537B2 (en) | 2017-04-05 | 2022-10-18 | Novo Nordisk A/S | Oligomer extended insulin-Fc conjugates |
US11518807B2 (en) | 2015-03-30 | 2022-12-06 | Regeneron Pharmaceuticals, Inc. | Heavy chain constant regions with reduced binding to Fc gamma receptors |
US11560416B2 (en) | 2017-04-21 | 2023-01-24 | Yuhan Corporation | Method for producing dual function proteins and its derivatives |
US11590223B2 (en) | 2018-08-31 | 2023-02-28 | Regeneron Pharmaceuticals, Inc. | Dosing strategy that mitigates cytokine release syndrome for therapeutic antibodies |
US11834492B2 (en) | 2017-09-27 | 2023-12-05 | Epicentrx, Inc. | Human IL-10 receptor alpha fusion proteins |
Families Citing this family (108)
Publication number | Priority date | Publication date | Assignee | Title |
---|---|---|---|---|
WO2006104989A2 (en) * | 2005-03-29 | 2006-10-05 | Verenium Corporation | Altered antibody fc regions and uses thereof |
KR101030978B1 (en) * | 2008-07-10 | 2011-04-28 | (주) 에이프로젠 | Recombinant Expression Vectors for Animal Cells |
US20110117092A1 (en) * | 2009-10-20 | 2011-05-19 | The Regents Of The University Of Michigan | Compositions and methods for inhibiting g-csfr |
DK2526119T3 (en) | 2010-01-19 | 2018-07-30 | Harvard College | Manipulated opsonin for pathogen detection and treatment |
WO2012032520A1 (en) * | 2010-09-07 | 2012-03-15 | Yissum Research Development Company Of The Hebrew University Of Jerusalem Ltd. | Readthrough acetylcholinesterase (ache-r) for treating or preventing parkinson's disease |
KR101333958B1 (en) | 2010-10-20 | 2013-11-27 | 주식회사 한독 | Human Interleukin-1 receptor antagonist-hybrid Fc fusion protein |
DE112012000404T5 (en) | 2011-01-04 | 2014-04-17 | Charitè Universitätsmedizin Berlin | Modulators of IL-12 and / or IL-23 for the prevention or treatment of Alzheimer's disease |
CN102585013B (en) * | 2011-01-07 | 2014-04-23 | 中国人民解放军军事医学科学院生物工程研究所 | Fusion protein containing omega interferon and method for preparing same |
MX2013009862A (en) | 2011-03-02 | 2013-10-25 | Novo Nordisk As | Coagulation factor-targeting to tlt-1 on activated platelets. |
WO2013012924A2 (en) | 2011-07-18 | 2013-01-24 | President And Fellows Of Harvard College | Engineered microbe-targeting molecules and uses thereof |
KR20130049671A (en) | 2011-11-04 | 2013-05-14 | 한미사이언스 주식회사 | Method for preparation of biological active polypeptide conjugate |
KR101183615B1 (en) * | 2011-12-28 | 2012-09-17 | 재단법인 경기과학기술진흥원 | Novel fusion protein binding to wnt |
AR090281A1 (en) | 2012-03-08 | 2014-10-29 | Hanmi Science Co Ltd | IMPROVED PROCESS FOR THE PREPARATION OF A PHYSIOLOGICALLY ACTIVE POLYPEPTIDE COMPLEX |
WO2013138338A2 (en) | 2012-03-12 | 2013-09-19 | Massachusetts Institute Of Technology | Methods for treating tissue damage associated with ischemia with apoliporotein d |
EP2956003A2 (en) | 2013-02-13 | 2015-12-23 | Laboratoire Français du Fractionnement et des Biotechnologies | Proteins with modified glycosylation and methods of production thereof |
MX2015010427A (en) | 2013-02-13 | 2016-03-17 | Lab Francais Du Fractionnement | Highly galactosylated anti-tnf-alpha antibodies and uses thereof. |
JP2016511275A (en) * | 2013-03-11 | 2016-04-14 | ノヴォ・ノルディスク・ヘルス・ケア・アーゲー | Growth hormone compounds |
SG11201506335YA (en) * | 2013-03-14 | 2015-09-29 | Regeneron Pharma | Apelin fusion proteins and uses thereof |
US10551379B2 (en) | 2013-03-15 | 2020-02-04 | President And Fellows Of Harvard College | Methods and compositions for improving detection and/or capture of a target entity |
EP2992017B1 (en) | 2013-05-02 | 2020-11-18 | AnaptysBio, Inc. | Antibodies directed against programmed death-1 (pd-1) |
AU2014268603B2 (en) | 2013-05-21 | 2018-03-22 | President And Fellows Of Harvard College | Engineered heme-binding compositions and uses thereof |
KR101895634B1 (en) * | 2013-05-31 | 2018-09-05 | 한미약품 주식회사 | IgG4 Fc fragment comprising modified hinge region |
AR096890A1 (en) * | 2013-07-12 | 2016-02-03 | Hanmi Pharm Ind Co Ltd | CONJUGATING FC OF IMMUNOGLOBULINA, THAT MAINTAINS THE UNION AFFINITY OF THE FC FRAGMENT OF THE IMMUNOGLOBULIN TO FCRN |
CN104231086B (en) * | 2013-08-27 | 2019-12-13 | 北京韩美药品有限公司 | Bifunctional fusion protein, preparation method and application thereof |
EP3912986B1 (en) | 2013-12-18 | 2023-12-13 | President and Fellows of Harvard College | Crp capture/detection of bacteria |
SG10202107752PA (en) * | 2014-03-31 | 2021-09-29 | Hanmi Pharmaceutical Co Ltd | Method for improving solubility of protein and peptide by using immunoglobulin fc fragment linkage |
KR20150135148A (en) * | 2014-05-23 | 2015-12-02 | 주식회사 제넥신 | PD-L1 Fused protein and use thereof |
KR20170040132A (en) | 2014-06-02 | 2017-04-12 | 라보라토이레 프란카이즈 듀 프락티온네먼트 에트 데스 바이오테크놀로지스 | Production of fc fragments |
US10441595B2 (en) * | 2014-06-26 | 2019-10-15 | Brigham Young University | Methods for treating fungal infections |
KR102272213B1 (en) * | 2014-07-08 | 2021-07-01 | 삼성전자주식회사 | Fusion protein comprising targeting moiety, cleavage site, and cell membrane penetrating domain, and use thereof |
TW201629100A (en) * | 2014-10-06 | 2016-08-16 | 格納西尼有限公司 | Human IgG4 Fc polypeptide variant |
EP3699198A1 (en) | 2014-11-17 | 2020-08-26 | Regeneron Pharmaceuticals, Inc. | Methods for tumor treatment using cd3xcd20 bispecific antibody |
KR102569813B1 (en) | 2014-11-21 | 2023-08-24 | 브리스톨-마이어스 스큅 컴퍼니 | Antibodies against cd73 and uses thereof |
EP3789399A1 (en) | 2014-11-21 | 2021-03-10 | Bristol-Myers Squibb Company | Antibodies comprising modified heavy constant regions |
MA40662B1 (en) | 2014-12-23 | 2020-12-31 | Bristol Myers Squibb Co | Antibodies against tigit |
CN110204617B (en) * | 2014-12-31 | 2023-06-16 | 天境生物科技(上海)有限公司 | Fusion polypeptide containing glucagon-like peptide-1 and immunoglobulin hybrid Fc and application thereof |
PL3288965T3 (en) * | 2015-04-29 | 2019-11-29 | Mediolanum Farm S P A | A soluble chimeric interleukin-10 receptor and therapeutic use thereof |
US20180139938A1 (en) | 2015-05-04 | 2018-05-24 | Laboratoire Français du Fractionnement et des, Biotechnologies | Transgenic production of fc fusion proteins |
WO2016178087A1 (en) | 2015-05-04 | 2016-11-10 | Biosourcing Sa | Transgenic production of chorionic gonadotropin |
AR105616A1 (en) * | 2015-05-07 | 2017-10-25 | Lilly Co Eli | FUSION PROTEINS |
MY188049A (en) | 2015-05-29 | 2021-11-12 | Bristol Myers Squibb Co | Antibodies against ox40 and uses thereof |
US10208099B2 (en) * | 2015-06-11 | 2019-02-19 | Genexine, Inc. | Modified interleukin-7 protein |
EA201890162A1 (en) | 2015-06-29 | 2018-07-31 | Бристол-Маерс Сквибб Компани | ANTIBODIES TO CD40 WITH ENHANCED AGONISTIC ACTIVITY |
CN108289928A (en) | 2015-08-06 | 2018-07-17 | 哈佛大学校长及研究员协会 | Improved microorganism-binding molecule and its purposes |
KR101773858B1 (en) | 2015-10-23 | 2017-09-01 | 명지대학교 산학협력단 | Composition for improving skin wrinkle |
KR102147997B1 (en) * | 2015-10-23 | 2020-08-25 | 주식회사 제넥신 | Composition for improving skin wrinkle |
KR20170049319A (en) * | 2015-10-28 | 2017-05-10 | 주식회사유한양행 | Long-acting fgf21 fusion proteins and pharmaceutical composition comprising the same |
KR102386735B1 (en) * | 2015-11-06 | 2022-04-14 | 주식회사 제넥신 | Formulation for modified interleukin-7 fusion protein |
CN108697764A (en) * | 2015-12-04 | 2018-10-23 | 格纳西尼有限公司 | The pharmaceutical composition for preventing or treating influenza infection of interleukin 7 fusion protein is merged containing immunoglobulin FC |
TWI774651B (en) | 2015-12-04 | 2022-08-21 | 南韓商吉耐森股份有限公司 | PHARMACEUTICAL COMPOSITION FOR THE PREVENTION OR TREATMENT OF HUMAN PAPILLOMAVIRUS-RELATED DISEASES COMPRISING IMMUNOGLOBULIN Fc-FUSED INTERLEUKIN-7 |
AR107483A1 (en) | 2016-01-29 | 2018-05-02 | Hanmi Pharm Ind Co Ltd | CONJUGATE OF THERAPEUTIC ENZYMES |
WO2017142331A1 (en) | 2016-02-17 | 2017-08-24 | Genexine, Inc. | Pharmaceutical composition comprising recombinant hgh for the treatment of growth hormone deficiency |
BR112018016817A2 (en) * | 2016-02-17 | 2018-12-26 | Genexine Inc | pharmaceutical composition and method of treatment of growth hormone deficiency |
EP3423489A1 (en) | 2016-03-04 | 2019-01-09 | The Rockefeller University | Antibodies to cd40 with enhanced agonist activity |
SG10201913033UA (en) | 2016-03-04 | 2020-03-30 | Bristol Myers Squibb Co | Combination therapy with anti-cd73 antibodies |
KR20170123849A (en) * | 2016-04-29 | 2017-11-09 | 주식회사유한양행 | Fusion Protein Comprising CCL3 Variants And Use Thereof |
CN106191072A (en) * | 2016-08-04 | 2016-12-07 | 沈沭彤 | Recombination human source is fitted together to GcFc genetic fragment and fusion protein |
JOP20190019A1 (en) * | 2016-08-30 | 2019-02-12 | Genexine Inc | PHARMACEUTICAL COMPOSITION FOR TREATING GROWTH HORMONE DEFICIENCY CONTAINING hGH FUSION PROTEIN |
AU2017354070A1 (en) | 2016-11-01 | 2019-05-16 | Anaptysbio, Inc. | Antibodies directed against programmed death- 1 (PD-1) |
CN110461880A (en) * | 2016-11-10 | 2019-11-15 | 科乐斯疗法公司 | GDNF fused polypeptide and its application method |
CN108264562B (en) * | 2016-12-30 | 2021-08-10 | 惠和生物技术(上海)有限公司 | Bifunctional molecule combining CD3 and T cell positive co-stimulatory molecule and application thereof |
BR112019014187A2 (en) | 2017-01-09 | 2020-02-11 | Tesaro, Inc. | CANCER TREATMENT METHODS WITH ANTI-PD-1 ANTIBODIES |
CN106832002A (en) * | 2017-02-16 | 2017-06-13 | 上海科医联创生物科技有限公司 | The fusion protein and its related application of a kind of targeting PD 1 |
CN110785435B (en) | 2017-03-06 | 2024-01-23 | 艾尔特生物科技公司 | IL-15-based fusions with IL-12 and IL-18 |
CN108623692B (en) * | 2017-03-20 | 2020-11-17 | 徐寒梅 | Fusion protein, preparation method and application thereof |
TWI788340B (en) | 2017-04-07 | 2023-01-01 | 美商必治妥美雅史谷比公司 | Anti-icos agonist antibodies and uses thereof |
CA3064321A1 (en) | 2017-05-25 | 2018-11-29 | Bristol-Myers Squibb Company | Antibodies comprising modified heavy constant regions |
CN107082815A (en) * | 2017-06-28 | 2017-08-22 | 杭州皓阳生物技术有限公司 | A kind of FSH HSA fusion proteins and preparation method thereof |
US11883503B2 (en) | 2017-09-25 | 2024-01-30 | Dingfu Biotarget Co., Ltd. | Methods and compositions for cancer treatment |
NZ765453A (en) * | 2017-12-22 | 2024-03-22 | Hanmi Pharmaceutical Co Ltd | Therapeutic enzyme fusion protein having novel structure and use thereof |
WO2019133747A1 (en) | 2017-12-27 | 2019-07-04 | Bristol-Myers Squibb Company | Anti-cd40 antibodies and uses thereof |
WO2019135666A1 (en) * | 2018-01-08 | 2019-07-11 | 주식회사 프로젠 | Pharmaceutical composition containing extracellular domain of alpha subunit of ige fc receptor |
KR102038679B1 (en) | 2018-01-12 | 2019-10-30 | (주)지아이이노베이션 | Composition comprising probiotics and ige-binding polypeptide and use thereof |
CN112041333A (en) | 2018-04-26 | 2020-12-04 | 古德T细胞有限公司 | Novel fusion protein and pharmaceutical composition for preventing or treating cancer comprising the same |
US20210121529A1 (en) | 2018-05-04 | 2021-04-29 | Ilkogen Ilaç Sanayi Ve Ticaret A.S. | Stable hybrid fc fusion g-csf formulation |
US20210347849A1 (en) | 2018-07-24 | 2021-11-11 | Good T Cells, Inc. | Composition for Preventing or Treating Immune-Related Diseases |
KR20200011685A (en) | 2018-07-25 | 2020-02-04 | 주식회사유한양행 | Fusion Protein Comprising Thyrotropin Receptor Variants And Use Thereof |
KR102263105B1 (en) * | 2018-09-05 | 2021-06-09 | 주식회사 엘지화학 | Fusion polypeptide comprising o-glycosylated polypeptide region |
WO2020053661A1 (en) | 2018-09-13 | 2020-03-19 | Laboratoire Francais Du Fractionnement Et Des Biotechnologies | Methods of purifying antibodies from the milk of transgenic non-human mammals comprising the use of chitosan |
US20220008515A1 (en) | 2018-11-16 | 2022-01-13 | Neoimmunetech, Inc. | Method of treating a tumor with a combination of il-7 protein and an immune checkpoint inhibitor |
EP3887397A1 (en) | 2018-11-28 | 2021-10-06 | Bristol-Myers Squibb Company | Antibodies comprising modified heavy constant regions |
EP3923973B1 (en) | 2019-02-13 | 2023-02-01 | Ilkogen Ilaç Sanayi ve Ticaret A.S. | A long-acting g-csf for preventing neutropenia or reducing duration of neutropenia |
AU2020273903B2 (en) * | 2019-05-14 | 2024-05-09 | Progen Co Ltd | Novel modified immunoglobulin Fc-fusion protein and use thereof |
DK3744319T3 (en) | 2019-05-28 | 2023-01-16 | Ilkogen Ilac Sanayi Ve Ticaret A S | STABLE LYOPHILIZED FORMULATION FOR HYBRID FC-FUSIONED G-CSF |
US20220267396A1 (en) | 2019-07-08 | 2022-08-25 | Progen Co., Ltd. | Novel il-10 variant protein and use thereof |
MX2022000285A (en) * | 2019-07-08 | 2022-02-03 | Gi Innovation Inc | Polypeptide dimer with high sialic acid content, comprising extracellular domain of alpha subunit of ige fc receptor, and pharmaceutical composition comprising same. |
WO2021006375A1 (en) * | 2019-07-08 | 2021-01-14 | (주)지아이이노베이션 | Polypeptide dimer containing high amount of sialic acid and including extracellular domain of alpha subunit of ige fc receptor, and pharmaceutical composition containing same |
WO2021006603A1 (en) * | 2019-07-08 | 2021-01-14 | 주식회사 프로젠 | Novel pharmaceutical composition for treating allergic diseases |
EP3998282A4 (en) * | 2019-07-08 | 2023-08-09 | Progen Co., Ltd. | Novel fusion protein and use of same |
AU2020400805B2 (en) * | 2019-12-11 | 2024-03-28 | Lg Chem, Ltd. | Fusion polypeptide comprising GDF15 and polypeptide region capable of O-glycosylation |
CN111057154B (en) * | 2019-12-23 | 2023-06-06 | 南京融捷康生物科技有限公司 | Preparation and application of immunogen based on camel source Fc fragment |
JP2023512456A (en) | 2020-01-13 | 2023-03-27 | ネオイミューンテック, インコーポレイテッド | Methods of treating tumors with a combination of IL-7 protein and bispecific antibody |
EP4186517A1 (en) * | 2020-01-23 | 2023-05-31 | Genexine, Inc. | Fusion protein comprising pd-l1 protein and use thereof |
WO2021158783A1 (en) | 2020-02-05 | 2021-08-12 | Washington University | Method of treating a solid tumor with a combination of an il-7 protein and car-bearing immune cells |
WO2021182928A1 (en) | 2020-03-12 | 2021-09-16 | 주식회사 에스엘메타젠 | Novel bispecific protein and use thereof |
KR20210141406A (en) * | 2020-05-14 | 2021-11-23 | 주식회사 프로젠 | A novel recombinant protein and use thereof |
WO2021231732A1 (en) | 2020-05-15 | 2021-11-18 | Bristol-Myers Squibb Company | Antibodies to garp |
WO2022000136A1 (en) * | 2020-06-28 | 2022-01-06 | Dingfu Biotarget Co., Ltd. | Methods and compositions for cancer treatment |
WO2022080912A1 (en) * | 2020-10-16 | 2022-04-21 | 주식회사 아이엠바이오로직스 | Fusion protein platform using igm region |
EP4232070A1 (en) | 2020-10-26 | 2023-08-30 | NeoImmuneTech, Inc. | Methods of inducing stem cell mobilization |
WO2022094475A1 (en) | 2020-11-02 | 2022-05-05 | Neoimmunetech, Inc. | Use of interleukin-7 for the treatment of coronavirus |
EP4240408A1 (en) | 2020-11-05 | 2023-09-13 | Neoimmunetech, Inc. | Method of treating a tumor with a combination of an il-7 protein and a nucleotide vaccine |
WO2022131889A1 (en) | 2020-12-16 | 2022-06-23 | 주식회사 굳티셀 | Use of taci protein |
CA3211978A1 (en) | 2021-03-09 | 2022-09-15 | Gi Innovation, Inc. | Formulation of fusion protein including extracellular domain of alpha subunit of ige fc receptor |
CN113603791A (en) * | 2021-08-11 | 2021-11-05 | 厦门目青股权投资合伙企业(有限合伙) | Fusion protein and application thereof |
WO2023130081A1 (en) | 2021-12-30 | 2023-07-06 | Neoimmunetech, Inc. | Method of treating a tumor with a combination of il-7 protein and vegf antagonist |
WO2023173084A1 (en) | 2022-03-11 | 2023-09-14 | University Of Rochester | Cyclopeptibodies and uses thereof |
CN115850517A (en) * | 2022-11-14 | 2023-03-28 | 沈阳药科大学 | Method for improving yield of GLP-1Fc fusion protein |
Family Cites Families (12)
Publication number | Priority date | Publication date | Assignee | Title |
---|---|---|---|---|
US5541087A (en) | 1994-09-14 | 1996-07-30 | Fuji Immunopharmaceuticals Corporation | Expression and export technology of proteins as immunofusins |
WO1997020062A1 (en) | 1995-12-01 | 1997-06-05 | University Of Massachusetts | Il-12 p40 subunit fusion polypeptides and uses thereof |
US6808902B1 (en) | 1999-11-12 | 2004-10-26 | Amgen Inc. | Process for correction of a disulfide misfold in IL-1Ra Fc fusion molecules |
EP1252192B1 (en) * | 2000-02-11 | 2006-08-16 | MERCK PATENT GmbH | Enhancing the circulating half-life of antibody-based fusion proteins |
US7829084B2 (en) * | 2001-01-17 | 2010-11-09 | Trubion Pharmaceuticals, Inc. | Binding constructs and methods for use thereof |
RU2319709C2 (en) * | 2001-07-17 | 2008-03-20 | Рисерч Дивелопмент Фаундейшн | Proapoptosis proteins-containing therapeutic agents |
US6797493B2 (en) * | 2001-10-01 | 2004-09-28 | Lee-Hwei K. Sun | Fc fusion proteins of human granulocyte colony-stimulating factor with increased biological activities |
US6919426B2 (en) | 2002-09-19 | 2005-07-19 | Amgen Inc. | Peptides and related molecules that modulate nerve growth factor activity |
BRPI0406605B8 (en) * | 2003-11-13 | 2021-05-25 | Hanmi Holdings Co Ltd | protein conjugate, method for its preparation and pharmaceutical composition to enhance the duration and in vivo stability of a physiologically active polypeptide |
WO2005063816A2 (en) * | 2003-12-19 | 2005-07-14 | Genentech, Inc. | Monovalent antibody fragments useful as therapeutics |
KR20120133403A (en) * | 2004-06-01 | 2012-12-10 | 도만티스 리미티드 | Bispecific fusion antibodies with enhanced serum half-life |
EP2471813B1 (en) * | 2004-07-15 | 2014-12-31 | Xencor, Inc. | Optimized Fc variants |
-
2008
- 2008-05-30 WO PCT/KR2008/003060 patent/WO2008147143A2/en active Application Filing
- 2008-05-30 CN CN201510684598.5A patent/CN105131127B/en active Active
- 2008-05-30 EP EP12198380.3A patent/EP2662449B1/en active Active
- 2008-05-30 EP EP16206834.0A patent/EP3173484B1/en active Active
- 2008-05-30 ES ES12198380.3T patent/ES2623925T3/en active Active
- 2008-05-30 JP JP2010510223A patent/JP5577243B2/en active Active
- 2008-05-30 BR BRPI0811637A patent/BRPI0811637B8/en active IP Right Grant
- 2008-05-30 DK DK12198380.3T patent/DK2662449T3/en active
- 2008-05-30 CN CN200880016313.9A patent/CN101687933B/en active Active
- 2008-05-30 RU RU2009141975/10A patent/RU2530168C2/en active
- 2008-05-30 CN CN201310553839.3A patent/CN103626875B/en active Active
- 2008-05-30 AU AU2008257923A patent/AU2008257923B2/en active Active
- 2008-05-30 KR KR1020147004294A patent/KR101380729B1/en active IP Right Grant
- 2008-05-30 CN CN201310554079.8A patent/CN103641919B/en active Active
- 2008-05-30 KR KR1020097008080A patent/KR101380732B1/en active IP Right Grant
- 2008-05-30 EP EP16206809.2A patent/EP3176264B1/en active Active
- 2008-05-30 EP EP08766022A patent/EP2162472B1/en not_active Not-in-force
- 2008-05-30 CN CN201510684679.5A patent/CN105198998A/en active Pending
- 2008-05-30 US US12/130,002 patent/US7867491B2/en active Active
- 2008-05-30 ES ES08766022T patent/ES2415604T3/en active Active
- 2008-05-30 CA CA2687377A patent/CA2687377C/en active Active
- 2008-05-30 KR KR1020087018012A patent/KR100897938B1/en active IP Right Grant
-
2009
- 2009-11-15 IL IL202128A patent/IL202128A0/en active IP Right Grant
-
2010
- 2010-08-12 HK HK10107700.4A patent/HK1141303A1/en unknown
- 2010-08-12 HK HK16106168.5A patent/HK1218127A1/en unknown
- 2010-11-19 US US12/950,500 patent/US8586038B2/en active Active
-
2012
- 2012-06-11 US US13/493,549 patent/US8529899B2/en active Active
- 2012-06-11 US US13/493,508 patent/US8586531B2/en active Active
- 2012-06-11 US US13/493,585 patent/US8586048B2/en active Active
-
2014
- 2014-06-05 HK HK14105294.6A patent/HK1191959A1/en unknown
-
2016
- 2016-06-23 HK HK16107328.0A patent/HK1219284A1/en unknown
- 2016-06-28 HK HK16107537.7A patent/HK1219490A1/en unknown
Non-Patent Citations (1)
Title |
---|
See references of EP2162472A4 * |
Cited By (53)
Publication number | Priority date | Publication date | Assignee | Title |
---|---|---|---|---|
CN101747440A (en) * | 2008-12-18 | 2010-06-23 | 欣润(上海)生物药业有限公司 | TNFR-Fc fusion protein and usage thereof |
US9273108B2 (en) | 2010-05-25 | 2016-03-01 | Generon (Shanghai) Corporation Ltd. | Recombinant human G-CSF dimer and use thereof for the treatment of neurological diseases |
US10400029B2 (en) | 2011-06-28 | 2019-09-03 | Inhibrx, Lp | Serpin fusion polypeptides and methods of use thereof |
US11965017B2 (en) | 2011-06-28 | 2024-04-23 | Inhibrx, Inc. | Serpin fusion polypeptides and methods of use thereof |
US11827691B2 (en) | 2011-06-28 | 2023-11-28 | Inhibrx, Inc. | Serpin fusion polypeptides and methods of use thereof |
US11046752B2 (en) | 2011-06-28 | 2021-06-29 | Inhibrx, Inc. | Serpin fusion polypeptides and methods of use thereof |
US10723785B2 (en) | 2011-06-28 | 2020-07-28 | Inhibrx, Inc. | Serpin fusion polypeptides and methods of use thereof |
EP2726092B1 (en) * | 2011-06-28 | 2019-06-19 | Inhibrx, LP | Serpin fusion polypeptides and methods of use thereof |
US10730929B2 (en) | 2011-06-28 | 2020-08-04 | Inhibrx Lp | Serpin fusion polypeptides and methods of use thereof |
US9642917B2 (en) | 2011-07-25 | 2017-05-09 | Generon (Shanghai) Corporation, Ltd. | Use of G-CSF dimer in preparation of medicament for treatment of neurodegenerative diseases |
US20140377280A1 (en) * | 2011-12-19 | 2014-12-25 | The Rockefeller University | Non-sialylated anti-inflammatory polypeptides |
US9587025B2 (en) * | 2011-12-19 | 2017-03-07 | The Rockefeller University | Non-sialylated anti-inflammatory polypeptides |
US11613579B2 (en) | 2011-12-19 | 2023-03-28 | The Rockefeller University | Anti-inflammatory polypeptides |
US10894832B2 (en) | 2011-12-19 | 2021-01-19 | The Rockefeller University | Anti-inflammatory polypeptides |
US9845358B2 (en) | 2011-12-19 | 2017-12-19 | The Rockefeller University | Anti-inflammatory polypeptides |
US11608379B2 (en) | 2011-12-19 | 2023-03-21 | The Rockefeller University | Anti-inflammatory polypeptides |
US9809641B2 (en) | 2012-04-23 | 2017-11-07 | Nrl Pharma, Inc. | Lactoferrin fusion protein and method for preparation thereof |
US10562959B2 (en) | 2012-04-23 | 2020-02-18 | Nrl Pharma, Inc. | Lactoferrin fusion protein and method for preparation thereof |
EP2842969A4 (en) * | 2012-04-23 | 2016-01-13 | Nrl Pharma Inc | Lactoferrin fusion protein and method for producing same |
US9474803B2 (en) | 2012-11-27 | 2016-10-25 | Alteogen Inc. | Composition for stabilizing fusion protein in which protein and FC domain are fused |
US10988537B2 (en) | 2013-02-01 | 2021-04-27 | Regeneren Pharmaceuticals, Inc. | Antibodies comprising chimeric constant domains |
EP3460054A1 (en) | 2013-03-15 | 2019-03-27 | Atyr Pharma, Inc. | Histidyl-trna synthetase-fc conjugates |
WO2014145050A1 (en) | 2013-03-15 | 2014-09-18 | Atyr Pharma, Inc. | Histidyl-trna synthetase-fc conjugates |
WO2015031673A2 (en) | 2013-08-28 | 2015-03-05 | Bioasis Technologies Inc. | Cns-targeted conjugates having modified fc regions and methods of use thereof |
US10189901B2 (en) | 2013-11-20 | 2019-01-29 | Regeneron Pharmaceuticals, Inc. | Methods for improving cardiac function by administering an antibody that activates APLNR |
US10947310B2 (en) | 2013-11-20 | 2021-03-16 | Regeneron Pharmaceuticals, Inc. | Fusion protein comprising apelin and an anti-APLNR antibody |
US10626173B2 (en) | 2013-11-20 | 2020-04-21 | Regeneron Pharmaceuticals, Inc. | Method for treating pathological angiogenesis by administering an antibody that inhibits APLNR |
US11642390B2 (en) | 2013-11-20 | 2023-05-09 | Regeneran Pharmaceuticals, Inc. | Method of treatment with a fusion protein comprising apelin and an anti-APLNR antibody |
US10155811B2 (en) | 2013-11-20 | 2018-12-18 | Regeneron Pharmaceuticals, Inc. | APLNR modulators and uses thereof |
US11434300B2 (en) | 2014-03-19 | 2022-09-06 | Regeneron Pharmaceuticals, Inc. | Methods and antibody compositions for tumor treatment |
TWI685506B (en) * | 2014-12-31 | 2020-02-21 | 格納西尼有限公司 | Fusion polypeptide comprising glp and immunoglobulin hybrid fc and use thereof |
TWI691513B (en) * | 2014-12-31 | 2020-04-21 | 格納西尼有限公司 | Fusion polypeptide containing GLP and immunoglobulin hybrid Fc and use thereof |
US10538569B2 (en) | 2014-12-31 | 2020-01-21 | Genexine, Inc. | Fusion polypeptide containing GLP and immunoglobulin hybrid Fc and use thereof |
EP3243525A4 (en) * | 2015-01-09 | 2018-07-25 | Genexine, Inc. | Method for treating anemia using long-acting epo preparation |
US10844125B2 (en) | 2015-03-04 | 2020-11-24 | The Rockefeller University | Anti-inflammatory polypeptides |
US11518807B2 (en) | 2015-03-30 | 2022-12-06 | Regeneron Pharmaceuticals, Inc. | Heavy chain constant regions with reduced binding to Fc gamma receptors |
US11208452B2 (en) | 2015-06-02 | 2021-12-28 | Novo Nordisk A/S | Insulins with polar recombinant extensions |
US11292825B2 (en) | 2015-10-01 | 2022-04-05 | Novo Nordisk A/S | Protein conjugates |
US10639368B2 (en) | 2016-05-27 | 2020-05-05 | Agenus Inc. | Anti-TIM-3 antibodies and methods of use thereof |
US10912828B2 (en) | 2016-05-27 | 2021-02-09 | Agenus Inc. | Anti-TIM-3 antibodies and methods of use thereof |
US11839653B2 (en) | 2016-05-27 | 2023-12-12 | Agenus Inc. | Anti-TIM-3 antibodies and methods of use thereof |
US11041014B2 (en) | 2016-10-28 | 2021-06-22 | S & K Biopharma, Inc. | Lactoferrin/albumin fusion protein and production method therefor |
US11471537B2 (en) | 2017-04-05 | 2022-10-18 | Novo Nordisk A/S | Oligomer extended insulin-Fc conjugates |
WO2018195338A1 (en) | 2017-04-20 | 2018-10-25 | Atyr Pharma, Inc. | Compositions and methods for treating lung inflammation |
US11560416B2 (en) | 2017-04-21 | 2023-01-24 | Yuhan Corporation | Method for producing dual function proteins and its derivatives |
US11834492B2 (en) | 2017-09-27 | 2023-12-05 | Epicentrx, Inc. | Human IL-10 receptor alpha fusion proteins |
US20210070833A1 (en) * | 2018-01-08 | 2021-03-11 | Gl INNOVATION, INC. | Extracellular domain of alpha subunit of ige fc receptor, pharmaceutical composition comprising same and method for producing same |
JP7128291B2 (en) | 2018-01-08 | 2022-08-30 | ジーアイ・イノベイション・インコーポレイテッド | Extracellular domain of the alpha subunit of the IgE Fc receptor, pharmaceutical compositions containing the same, and methods of making the same |
JP2021509590A (en) * | 2018-01-08 | 2021-04-01 | ジーアイ・イノベイション・インコーポレイテッドGi Innovation, Inc. | The extracellular domain of the alpha subunit of the IgE Fc receptor, a pharmaceutical composition containing the same, and a method for producing the same. |
EP3514171A1 (en) * | 2018-01-18 | 2019-07-24 | Molecular Cloning Laboratories (MCLAB) LLC | Long-acting therapeutic fusion proteins |
US11590223B2 (en) | 2018-08-31 | 2023-02-28 | Regeneron Pharmaceuticals, Inc. | Dosing strategy that mitigates cytokine release syndrome for therapeutic antibodies |
WO2020184941A1 (en) * | 2019-03-08 | 2020-09-17 | Genexine, Inc. | Glp-1 fusion proteins and uses thereof |
CN111944058A (en) * | 2020-07-28 | 2020-11-17 | 中国农业大学 | Multifunctional hybrid peptide with antibacterial, anti-inflammatory, endotoxin neutralization and immunoregulation activities, and preparation method and application thereof |
Also Published As
Similar Documents
Publication | Publication Date | Title |
---|---|---|
CA2687377C (en) | Immunoglobulin fusion proteins | |
KR102041412B1 (en) | Derivatives of Immunglobulin Fc fragment | |
CA2535515A1 (en) | Cd20-binding polypeptide compositions | |
CA2356401A1 (en) | Expression and export of anti-obesity proteins as fc fusion proteins | |
CN105175553B (en) | Domain-immunoglobulin fusion proteins | |
TW201714894A (en) | Immunoglobulin fusion proteins | |
TW201716445A (en) | Immunoglobulin fusion proteins |
Legal Events
Date | Code | Title | Description |
---|---|---|---|
WWE | Wipo information: entry into national phase |
Ref document number: 200880016313.9 Country of ref document: CN |
|
121 | Ep: the epo has been informed by wipo that ep was designated in this application |
Ref document number: 08766022 Country of ref document: EP Kind code of ref document: A2 |
|
WWE | Wipo information: entry into national phase |
Ref document number: 1020097008080 Country of ref document: KR |
|
WWE | Wipo information: entry into national phase |
Ref document number: 2008257923 Country of ref document: AU |
|
WWE | Wipo information: entry into national phase |
Ref document number: 2010510223 Country of ref document: JP |
|
WWE | Wipo information: entry into national phase |
Ref document number: 2009141975 Country of ref document: RU |
|
WWE | Wipo information: entry into national phase |
Ref document number: 2687377 Country of ref document: CA Ref document number: 2127/MUMNP/2009 Country of ref document: IN |
|
NENP | Non-entry into the national phase |
Ref country code: DE |
|
ENP | Entry into the national phase |
Ref document number: 2008257923 Country of ref document: AU Date of ref document: 20080530 Kind code of ref document: A |
|
WWE | Wipo information: entry into national phase |
Ref document number: 2008766022 Country of ref document: EP |
|
WWE | Wipo information: entry into national phase |
Ref document number: 1020147004294 Country of ref document: KR |
|
ENP | Entry into the national phase |
Ref document number: PI0811637 Country of ref document: BR Kind code of ref document: A2 Effective date: 20091113 |