ES2567704T3 - Proteínas de fusión de colectina de la superfamilia de TNF - Google Patents
Proteínas de fusión de colectina de la superfamilia de TNF Download PDFInfo
- Publication number
- ES2567704T3 ES2567704T3 ES12166865.1T ES12166865T ES2567704T3 ES 2567704 T3 ES2567704 T3 ES 2567704T3 ES 12166865 T ES12166865 T ES 12166865T ES 2567704 T3 ES2567704 T3 ES 2567704T3
- Authority
- ES
- Spain
- Prior art keywords
- seq
- trail
- fusion protein
- human
- protein
- Prior art date
- Legal status (The legal status is an assumption and is not a legal conclusion. Google has not performed a legal analysis and makes no representation as to the accuracy of the status listed.)
- Active
Links
- 108020001507 fusion proteins Proteins 0.000 title claims abstract description 199
- 102000037865 fusion proteins Human genes 0.000 title claims abstract description 199
- 150000001413 amino acids Chemical class 0.000 claims abstract description 152
- 241000282414 Homo sapiens Species 0.000 claims abstract description 90
- 230000027455 binding Effects 0.000 claims abstract description 88
- 102000005962 receptors Human genes 0.000 claims abstract description 85
- 108020003175 receptors Proteins 0.000 claims abstract description 85
- 108010007127 Pulmonary Surfactant-Associated Protein D Proteins 0.000 claims abstract description 62
- 238000005829 trimerization reaction Methods 0.000 claims abstract description 62
- 102100027845 Pulmonary surfactant-associated protein D Human genes 0.000 claims abstract description 60
- 102000004127 Cytokines Human genes 0.000 claims abstract description 37
- 108090000695 Cytokines Proteins 0.000 claims abstract description 37
- 210000004899 c-terminal region Anatomy 0.000 claims abstract description 17
- 108010038196 saccharide-binding proteins Proteins 0.000 claims abstract description 10
- 210000004027 cell Anatomy 0.000 claims description 91
- 238000006467 substitution reaction Methods 0.000 claims description 40
- 150000007523 nucleic acids Chemical class 0.000 claims description 39
- 108020004707 nucleic acids Proteins 0.000 claims description 38
- 102000039446 nucleic acids Human genes 0.000 claims description 38
- 208000037265 diseases, disorders, signs and symptoms Diseases 0.000 claims description 20
- 206010028980 Neoplasm Diseases 0.000 claims description 19
- DHMQDGOQFOQNFH-UHFFFAOYSA-N Glycine Natural products NCC(O)=O DHMQDGOQFOQNFH-UHFFFAOYSA-N 0.000 claims description 16
- MTCFGRXMJLQNBG-UHFFFAOYSA-N Serine Natural products OCC(N)C(O)=O MTCFGRXMJLQNBG-UHFFFAOYSA-N 0.000 claims description 10
- 230000006907 apoptotic process Effects 0.000 claims description 10
- 201000010099 disease Diseases 0.000 claims description 10
- 208000035475 disorder Diseases 0.000 claims description 10
- 239000004471 Glycine Substances 0.000 claims description 9
- 208000015122 neurodegenerative disease Diseases 0.000 claims description 8
- 239000008194 pharmaceutical composition Substances 0.000 claims description 8
- 239000000203 mixture Substances 0.000 claims description 7
- 238000011282 treatment Methods 0.000 claims description 7
- 239000013543 active substance Substances 0.000 claims description 6
- 208000035473 Communicable disease Diseases 0.000 claims description 5
- 230000002062 proliferating effect Effects 0.000 claims description 5
- 238000002560 therapeutic procedure Methods 0.000 claims description 5
- 206010052779 Transplant rejections Diseases 0.000 claims description 4
- 230000002917 arthritic effect Effects 0.000 claims description 4
- 230000004064 dysfunction Effects 0.000 claims description 4
- 208000027866 inflammatory disease Diseases 0.000 claims description 4
- 230000001926 lymphatic effect Effects 0.000 claims description 4
- 208000030159 metabolic disease Diseases 0.000 claims description 4
- 201000006417 multiple sclerosis Diseases 0.000 claims description 4
- 230000004770 neurodegeneration Effects 0.000 claims description 4
- 238000011321 prophylaxis Methods 0.000 claims description 4
- 239000007787 solid Substances 0.000 claims description 4
- 208000023275 Autoimmune disease Diseases 0.000 claims description 3
- 125000003630 glycyl group Chemical group [H]N([H])C([H])([H])C(*)=O 0.000 claims description 3
- 125000003275 alpha amino acid group Chemical group 0.000 claims 4
- 235000001014 amino acid Nutrition 0.000 description 127
- 102000046283 TNF-Related Apoptosis-Inducing Ligand Human genes 0.000 description 85
- 108700012411 TNFSF10 Proteins 0.000 description 85
- 101100369992 Homo sapiens TNFSF10 gene Proteins 0.000 description 83
- 108090000623 proteins and genes Proteins 0.000 description 80
- 102000004169 proteins and genes Human genes 0.000 description 77
- 235000018102 proteins Nutrition 0.000 description 75
- 108060008682 Tumor Necrosis Factor Proteins 0.000 description 56
- 102000000852 Tumor Necrosis Factor-alpha Human genes 0.000 description 56
- 239000003446 ligand Substances 0.000 description 48
- 102000002259 TNF-Related Apoptosis-Inducing Ligand Receptors Human genes 0.000 description 40
- 108010000449 TNF-Related Apoptosis-Inducing Ligand Receptors Proteins 0.000 description 40
- 101000830565 Homo sapiens Tumor necrosis factor ligand superfamily member 10 Proteins 0.000 description 33
- 102000044949 human TNFSF10 Human genes 0.000 description 32
- 108090000765 processed proteins & peptides Proteins 0.000 description 31
- 230000000694 effects Effects 0.000 description 29
- 101000632467 Homo sapiens Pulmonary surfactant-associated protein D Proteins 0.000 description 28
- 238000001542 size-exclusion chromatography Methods 0.000 description 25
- 239000002953 phosphate buffered saline Substances 0.000 description 23
- 238000002965 ELISA Methods 0.000 description 22
- 102000011727 Caspases Human genes 0.000 description 20
- 108010076667 Caspases Proteins 0.000 description 20
- 239000000872 buffer Substances 0.000 description 20
- 230000014509 gene expression Effects 0.000 description 18
- 229920001184 polypeptide Polymers 0.000 description 18
- 102000004196 processed proteins & peptides Human genes 0.000 description 18
- 102100031988 Tumor necrosis factor ligand superfamily member 6 Human genes 0.000 description 17
- 108010039471 Fas Ligand Protein Proteins 0.000 description 16
- 238000004132 cross linking Methods 0.000 description 15
- 230000028327 secretion Effects 0.000 description 15
- 101000880080 Homo sapiens Ectodysplasin-A Proteins 0.000 description 12
- 108010076504 Protein Sorting Signals Proteins 0.000 description 12
- 108010028230 Trp-Ser- His-Pro-Gln-Phe-Glu-Lys Proteins 0.000 description 12
- 239000006228 supernatant Substances 0.000 description 11
- 102100032937 CD40 ligand Human genes 0.000 description 10
- 102100037354 Ectodysplasin-A Human genes 0.000 description 10
- 201000011510 cancer Diseases 0.000 description 10
- 230000030833 cell death Effects 0.000 description 10
- 230000001965 increasing effect Effects 0.000 description 10
- 238000002415 sodium dodecyl sulfate polyacrylamide gel electrophoresis Methods 0.000 description 10
- 241000894007 species Species 0.000 description 10
- 108010029697 CD40 Ligand Proteins 0.000 description 9
- 238000011534 incubation Methods 0.000 description 9
- 101000764294 Homo sapiens Lymphotoxin-beta Proteins 0.000 description 8
- 241000699666 Mus <mouse, genus> Species 0.000 description 8
- 238000004458 analytical method Methods 0.000 description 8
- 235000014633 carbohydrates Nutrition 0.000 description 8
- 239000002523 lectin Substances 0.000 description 8
- 238000000034 method Methods 0.000 description 8
- 238000000746 purification Methods 0.000 description 8
- 238000010186 staining Methods 0.000 description 8
- 239000013638 trimer Substances 0.000 description 8
- 239000013598 vector Substances 0.000 description 8
- 101000764535 Homo sapiens Lymphotoxin-alpha Proteins 0.000 description 7
- 101000638251 Homo sapiens Tumor necrosis factor ligand superfamily member 9 Proteins 0.000 description 7
- 102100024587 Tumor necrosis factor ligand superfamily member 15 Human genes 0.000 description 7
- 102100032101 Tumor necrosis factor ligand superfamily member 9 Human genes 0.000 description 7
- 230000004913 activation Effects 0.000 description 7
- 150000001720 carbohydrates Chemical class 0.000 description 7
- 239000013078 crystal Substances 0.000 description 7
- 239000002609 medium Substances 0.000 description 7
- 102100025221 CD70 antigen Human genes 0.000 description 6
- 101100207063 Homo sapiens FASLG gene Proteins 0.000 description 6
- 101000830600 Homo sapiens Tumor necrosis factor ligand superfamily member 13 Proteins 0.000 description 6
- OKKJLVBELUTLKV-UHFFFAOYSA-N Methanol Chemical compound OC OKKJLVBELUTLKV-UHFFFAOYSA-N 0.000 description 6
- FAPWRFPIFSIZLT-UHFFFAOYSA-M Sodium chloride Chemical compound [Na+].[Cl-] FAPWRFPIFSIZLT-UHFFFAOYSA-M 0.000 description 6
- 239000012505 Superdex™ Substances 0.000 description 6
- 102100024584 Tumor necrosis factor ligand superfamily member 12 Human genes 0.000 description 6
- 102100024585 Tumor necrosis factor ligand superfamily member 13 Human genes 0.000 description 6
- 102100035283 Tumor necrosis factor ligand superfamily member 18 Human genes 0.000 description 6
- 102100032100 Tumor necrosis factor ligand superfamily member 8 Human genes 0.000 description 6
- -1 amino acid amino acid Chemical class 0.000 description 6
- 238000012512 characterization method Methods 0.000 description 6
- 238000010276 construction Methods 0.000 description 6
- 230000008030 elimination Effects 0.000 description 6
- 238000003379 elimination reaction Methods 0.000 description 6
- 230000007717 exclusion Effects 0.000 description 6
- 238000007478 fluorogenic assay Methods 0.000 description 6
- 230000004927 fusion Effects 0.000 description 6
- 230000014759 maintenance of location Effects 0.000 description 6
- 108010046080 CD27 Ligand Proteins 0.000 description 5
- 108091026890 Coding region Proteins 0.000 description 5
- WQZGKKKJIJFFOK-QTVWNMPRSA-N D-mannopyranose Chemical compound OC[C@H]1OC(O)[C@@H](O)[C@@H](O)[C@@H]1O WQZGKKKJIJFFOK-QTVWNMPRSA-N 0.000 description 5
- 108020004414 DNA Proteins 0.000 description 5
- 101100207070 Homo sapiens TNFSF8 gene Proteins 0.000 description 5
- 102000004856 Lectins Human genes 0.000 description 5
- 108090001090 Lectins Proteins 0.000 description 5
- 101100207071 Mus musculus Tnfsf8 gene Proteins 0.000 description 5
- 101000597780 Mus musculus Tumor necrosis factor ligand superfamily member 18 Proteins 0.000 description 5
- 102000004473 OX40 Ligand Human genes 0.000 description 5
- 108010042215 OX40 Ligand Proteins 0.000 description 5
- 229920001213 Polysorbate 20 Polymers 0.000 description 5
- 102000014128 RANK Ligand Human genes 0.000 description 5
- 108010025832 RANK Ligand Proteins 0.000 description 5
- 101710097155 Tumor necrosis factor ligand superfamily member 12 Proteins 0.000 description 5
- 102100036922 Tumor necrosis factor ligand superfamily member 13B Human genes 0.000 description 5
- 101710181056 Tumor necrosis factor ligand superfamily member 13B Proteins 0.000 description 5
- 108090000138 Tumor necrosis factor ligand superfamily member 15 Proteins 0.000 description 5
- 239000002246 antineoplastic agent Substances 0.000 description 5
- 238000003556 assay Methods 0.000 description 5
- 230000015572 biosynthetic process Effects 0.000 description 5
- 238000003776 cleavage reaction Methods 0.000 description 5
- 239000013604 expression vector Substances 0.000 description 5
- 238000011068 loading method Methods 0.000 description 5
- 230000035772 mutation Effects 0.000 description 5
- 239000000256 polyoxyethylene sorbitan monolaurate Substances 0.000 description 5
- 235000010486 polyoxyethylene sorbitan monolaurate Nutrition 0.000 description 5
- 238000002360 preparation method Methods 0.000 description 5
- 230000007017 scission Effects 0.000 description 5
- 210000002966 serum Anatomy 0.000 description 5
- 208000002109 Argyria Diseases 0.000 description 4
- AOJJSUZBOXZQNB-TZSSRYMLSA-N Doxorubicin Chemical compound O([C@H]1C[C@@](O)(CC=2C(O)=C3C(=O)C=4C=CC=C(C=4C(=O)C3=C(O)C=21)OC)C(=O)CO)[C@H]1C[C@H](N)[C@H](O)[C@H](C)O1 AOJJSUZBOXZQNB-TZSSRYMLSA-N 0.000 description 4
- 206010019851 Hepatotoxicity Diseases 0.000 description 4
- 101000830594 Homo sapiens Tumor necrosis factor ligand superfamily member 14 Proteins 0.000 description 4
- COLNVLDHVKWLRT-QMMMGPOBSA-N L-phenylalanine Chemical compound OC(=O)[C@@H](N)CC1=CC=CC=C1 COLNVLDHVKWLRT-QMMMGPOBSA-N 0.000 description 4
- 229920000057 Mannan Polymers 0.000 description 4
- 108010087870 Mannose-Binding Lectin Proteins 0.000 description 4
- 102000009112 Mannose-Binding Lectin Human genes 0.000 description 4
- 108010008281 Recombinant Fusion Proteins Proteins 0.000 description 4
- 102000007056 Recombinant Fusion Proteins Human genes 0.000 description 4
- 238000004220 aggregation Methods 0.000 description 4
- 230000003833 cell viability Effects 0.000 description 4
- 230000003247 decreasing effect Effects 0.000 description 4
- 231100000334 hepatotoxic Toxicity 0.000 description 4
- 230000003082 hepatotoxic effect Effects 0.000 description 4
- 102000051198 human TNFSF14 Human genes 0.000 description 4
- 239000000411 inducer Substances 0.000 description 4
- 210000004962 mammalian cell Anatomy 0.000 description 4
- 238000012986 modification Methods 0.000 description 4
- 230000004048 modification Effects 0.000 description 4
- 239000000178 monomer Substances 0.000 description 4
- 239000013642 negative control Substances 0.000 description 4
- 238000012545 processing Methods 0.000 description 4
- 230000011664 signaling Effects 0.000 description 4
- 239000000243 solution Substances 0.000 description 4
- UCSJYZPVAKXKNQ-HZYVHMACSA-N streptomycin Chemical compound CN[C@H]1[C@H](O)[C@@H](O)[C@H](CO)O[C@H]1O[C@@H]1[C@](C=O)(O)[C@H](C)O[C@H]1O[C@@H]1[C@@H](NC(N)=N)[C@H](O)[C@@H](NC(N)=N)[C@H](O)[C@H]1O UCSJYZPVAKXKNQ-HZYVHMACSA-N 0.000 description 4
- 238000001262 western blot Methods 0.000 description 4
- JKMHFZQWWAIEOD-UHFFFAOYSA-N 2-[4-(2-hydroxyethyl)piperazin-1-yl]ethanesulfonic acid Chemical compound OCC[NH+]1CCN(CCS([O-])(=O)=O)CC1 JKMHFZQWWAIEOD-UHFFFAOYSA-N 0.000 description 3
- UAIUNKRWKOVEES-UHFFFAOYSA-N 3,3',5,5'-tetramethylbenzidine Chemical compound CC1=C(N)C(C)=CC(C=2C=C(C)C(N)=C(C)C=2)=C1 UAIUNKRWKOVEES-UHFFFAOYSA-N 0.000 description 3
- HJCMDXDYPOUFDY-WHFBIAKZSA-N Ala-Gln Chemical compound C[C@H](N)C(=O)N[C@H](C(O)=O)CCC(N)=O HJCMDXDYPOUFDY-WHFBIAKZSA-N 0.000 description 3
- 241000588724 Escherichia coli Species 0.000 description 3
- 101000830596 Homo sapiens Tumor necrosis factor ligand superfamily member 15 Proteins 0.000 description 3
- 231100000070 MTS assay Toxicity 0.000 description 3
- 238000000719 MTS assay Methods 0.000 description 3
- 241000699670 Mus sp. Species 0.000 description 3
- 102000035195 Peptidases Human genes 0.000 description 3
- 108091005804 Peptidases Proteins 0.000 description 3
- 239000004365 Protease Substances 0.000 description 3
- QAOWNCQODCNURD-UHFFFAOYSA-N Sulfuric acid Chemical compound OS(O)(=O)=O QAOWNCQODCNURD-UHFFFAOYSA-N 0.000 description 3
- 238000002835 absorbance Methods 0.000 description 3
- 230000002776 aggregation Effects 0.000 description 3
- 230000003399 chemotactic effect Effects 0.000 description 3
- 229940044683 chemotherapy drug Drugs 0.000 description 3
- 238000010790 dilution Methods 0.000 description 3
- 239000012895 dilution Substances 0.000 description 3
- 210000003494 hepatocyte Anatomy 0.000 description 3
- 210000005260 human cell Anatomy 0.000 description 3
- 239000012528 membrane Substances 0.000 description 3
- 239000013612 plasmid Substances 0.000 description 3
- 235000019419 proteases Nutrition 0.000 description 3
- 230000001235 sensitizing effect Effects 0.000 description 3
- 239000011780 sodium chloride Substances 0.000 description 3
- 239000012089 stop solution Substances 0.000 description 3
- 235000011149 sulphuric acid Nutrition 0.000 description 3
- 239000004094 surface-active agent Substances 0.000 description 3
- GZDRODOYEFEHGG-NUDCOPPTSA-N (4s)-4-[[(2s)-2-acetamido-3-carboxypropanoyl]amino]-5-[[(2s)-1-[[(2s)-3-carboxy-1-oxo-1-[[2-oxo-4-(trifluoromethyl)chromen-7-yl]amino]propan-2-yl]amino]-3-methyl-1-oxobutan-2-yl]amino]-5-oxopentanoic acid Chemical compound FC(F)(F)C1=CC(=O)OC2=CC(NC(=O)[C@H](CC(O)=O)NC(=O)[C@@H](NC(=O)[C@H](CCC(O)=O)NC(=O)[C@H](CC(O)=O)NC(C)=O)C(C)C)=CC=C21 GZDRODOYEFEHGG-NUDCOPPTSA-N 0.000 description 2
- 102100021569 Apoptosis regulator Bcl-2 Human genes 0.000 description 2
- 101150017888 Bcl2 gene Proteins 0.000 description 2
- 101150013553 CD40 gene Proteins 0.000 description 2
- UXVMQQNJUSDDNG-UHFFFAOYSA-L Calcium chloride Chemical compound [Cl-].[Cl-].[Ca+2] UXVMQQNJUSDDNG-UHFFFAOYSA-L 0.000 description 2
- 101710194644 Collectin-11 Proteins 0.000 description 2
- 102100024331 Collectin-11 Human genes 0.000 description 2
- 108010013369 Enteropeptidase Proteins 0.000 description 2
- 102100029727 Enteropeptidase Human genes 0.000 description 2
- 108091006020 Fc-tagged proteins Proteins 0.000 description 2
- 201000008808 Fibrosarcoma Diseases 0.000 description 2
- 239000007995 HEPES buffer Substances 0.000 description 2
- 241000238631 Hexapoda Species 0.000 description 2
- 101000909536 Homo sapiens Collectin-11 Proteins 0.000 description 2
- 101000830603 Homo sapiens Tumor necrosis factor ligand superfamily member 11 Proteins 0.000 description 2
- 101000830598 Homo sapiens Tumor necrosis factor ligand superfamily member 12 Proteins 0.000 description 2
- 101000597779 Homo sapiens Tumor necrosis factor ligand superfamily member 18 Proteins 0.000 description 2
- 101000764263 Homo sapiens Tumor necrosis factor ligand superfamily member 4 Proteins 0.000 description 2
- 101000638255 Homo sapiens Tumor necrosis factor ligand superfamily member 8 Proteins 0.000 description 2
- 101000611023 Homo sapiens Tumor necrosis factor receptor superfamily member 6 Proteins 0.000 description 2
- ROHFNLRQFUQHCH-UHFFFAOYSA-N Leucine Natural products CC(C)CC(N)C(O)=O ROHFNLRQFUQHCH-UHFFFAOYSA-N 0.000 description 2
- TWRXJAOTZQYOKJ-UHFFFAOYSA-L Magnesium chloride Chemical compound [Mg+2].[Cl-].[Cl-] TWRXJAOTZQYOKJ-UHFFFAOYSA-L 0.000 description 2
- 108010061593 Member 14 Tumor Necrosis Factor Receptors Proteins 0.000 description 2
- 101800001340 N-terminal form Proteins 0.000 description 2
- 102400000874 N-terminal form Human genes 0.000 description 2
- 229930182555 Penicillin Natural products 0.000 description 2
- JGSARLDLIJGVTE-MBNYWOFBSA-N Penicillin G Chemical compound N([C@H]1[C@H]2SC([C@@H](N2C1=O)C(O)=O)(C)C)C(=O)CC1=CC=CC=C1 JGSARLDLIJGVTE-MBNYWOFBSA-N 0.000 description 2
- 102000003992 Peroxidases Human genes 0.000 description 2
- 108010007100 Pulmonary Surfactant-Associated Protein A Proteins 0.000 description 2
- 102000007615 Pulmonary Surfactant-Associated Protein A Human genes 0.000 description 2
- 239000012980 RPMI-1640 medium Substances 0.000 description 2
- 240000004808 Saccharomyces cerevisiae Species 0.000 description 2
- BQCADISMDOOEFD-UHFFFAOYSA-N Silver Chemical compound [Ag] BQCADISMDOOEFD-UHFFFAOYSA-N 0.000 description 2
- CDBYLPFSWZWCQE-UHFFFAOYSA-L Sodium Carbonate Chemical compound [Na+].[Na+].[O-]C([O-])=O CDBYLPFSWZWCQE-UHFFFAOYSA-L 0.000 description 2
- PXIPVTKHYLBLMZ-UHFFFAOYSA-N Sodium azide Chemical compound [Na+].[N-]=[N+]=[N-] PXIPVTKHYLBLMZ-UHFFFAOYSA-N 0.000 description 2
- UIIMBOGNXHQVGW-UHFFFAOYSA-M Sodium bicarbonate Chemical compound [Na+].OC([O-])=O UIIMBOGNXHQVGW-UHFFFAOYSA-M 0.000 description 2
- 239000007983 Tris buffer Substances 0.000 description 2
- 108010065323 Tumor Necrosis Factor Ligand Superfamily Member 13 Proteins 0.000 description 2
- 102100028785 Tumor necrosis factor receptor superfamily member 14 Human genes 0.000 description 2
- 102100033733 Tumor necrosis factor receptor superfamily member 1B Human genes 0.000 description 2
- 101710187830 Tumor necrosis factor receptor superfamily member 1B Proteins 0.000 description 2
- 102100040245 Tumor necrosis factor receptor superfamily member 5 Human genes 0.000 description 2
- 102100040403 Tumor necrosis factor receptor superfamily member 6 Human genes 0.000 description 2
- 238000010521 absorption reaction Methods 0.000 description 2
- 230000004075 alteration Effects 0.000 description 2
- 210000004102 animal cell Anatomy 0.000 description 2
- 230000004071 biological effect Effects 0.000 description 2
- 230000000903 blocking effect Effects 0.000 description 2
- 210000004369 blood Anatomy 0.000 description 2
- 239000008280 blood Substances 0.000 description 2
- 239000001110 calcium chloride Substances 0.000 description 2
- 235000011148 calcium chloride Nutrition 0.000 description 2
- 229910001628 calcium chloride Inorganic materials 0.000 description 2
- 238000004113 cell culture Methods 0.000 description 2
- 238000005119 centrifugation Methods 0.000 description 2
- 208000019065 cervical carcinoma Diseases 0.000 description 2
- 238000006243 chemical reaction Methods 0.000 description 2
- 239000003795 chemical substances by application Substances 0.000 description 2
- 238000005352 clarification Methods 0.000 description 2
- 150000001875 compounds Chemical class 0.000 description 2
- 239000012228 culture supernatant Substances 0.000 description 2
- YPHMISFOHDHNIV-FSZOTQKASA-N cycloheximide Chemical compound C1[C@@H](C)C[C@H](C)C(=O)[C@@H]1[C@H](O)CC1CC(=O)NC(=O)C1 YPHMISFOHDHNIV-FSZOTQKASA-N 0.000 description 2
- 235000018417 cysteine Nutrition 0.000 description 2
- 125000000151 cysteine group Chemical class N[C@@H](CS)C(=O)* 0.000 description 2
- 229940127089 cytotoxic agent Drugs 0.000 description 2
- 230000001472 cytotoxic effect Effects 0.000 description 2
- 231100000135 cytotoxicity Toxicity 0.000 description 2
- 230000003013 cytotoxicity Effects 0.000 description 2
- 201000001098 delayed sleep phase syndrome Diseases 0.000 description 2
- 208000033921 delayed sleep phase type circadian rhythm sleep disease Diseases 0.000 description 2
- 238000001514 detection method Methods 0.000 description 2
- 229960004679 doxorubicin Drugs 0.000 description 2
- 229940079593 drug Drugs 0.000 description 2
- 239000003814 drug Substances 0.000 description 2
- 238000010828 elution Methods 0.000 description 2
- 239000012634 fragment Substances 0.000 description 2
- SDUQYLNIPVEERB-QPPQHZFASA-N gemcitabine Chemical compound O=C1N=C(N)C=CN1[C@H]1C(F)(F)[C@H](O)[C@@H](CO)O1 SDUQYLNIPVEERB-QPPQHZFASA-N 0.000 description 2
- 229960005277 gemcitabine Drugs 0.000 description 2
- 102000055919 human Colec11 Human genes 0.000 description 2
- 102000052819 human EDA Human genes 0.000 description 2
- 102000055414 human LTB Human genes 0.000 description 2
- 230000003993 interaction Effects 0.000 description 2
- 210000004185 liver Anatomy 0.000 description 2
- 238000004519 manufacturing process Methods 0.000 description 2
- 201000001441 melanoma Diseases 0.000 description 2
- 229940049954 penicillin Drugs 0.000 description 2
- 108040007629 peroxidase activity proteins Proteins 0.000 description 2
- 210000002826 placenta Anatomy 0.000 description 2
- 210000001236 prokaryotic cell Anatomy 0.000 description 2
- 229960000856 protein c Drugs 0.000 description 2
- 238000011002 quantification Methods 0.000 description 2
- 238000011160 research Methods 0.000 description 2
- 229910052709 silver Inorganic materials 0.000 description 2
- 239000004332 silver Substances 0.000 description 2
- DAEPDZWVDSPTHF-UHFFFAOYSA-M sodium pyruvate Chemical compound [Na+].CC(=O)C([O-])=O DAEPDZWVDSPTHF-UHFFFAOYSA-M 0.000 description 2
- 230000006641 stabilisation Effects 0.000 description 2
- 238000011105 stabilization Methods 0.000 description 2
- 229960005322 streptomycin Drugs 0.000 description 2
- 238000012360 testing method Methods 0.000 description 2
- 230000001225 therapeutic effect Effects 0.000 description 2
- 238000004448 titration Methods 0.000 description 2
- 238000001890 transfection Methods 0.000 description 2
- 230000009261 transgenic effect Effects 0.000 description 2
- LENZDBCJOHFCAS-UHFFFAOYSA-N tris Chemical compound OCC(N)(CO)CO LENZDBCJOHFCAS-UHFFFAOYSA-N 0.000 description 2
- 241001515965 unidentified phage Species 0.000 description 2
- 230000035899 viability Effects 0.000 description 2
- 210000005253 yeast cell Anatomy 0.000 description 2
- MTCFGRXMJLQNBG-REOHCLBHSA-N (2S)-2-Amino-3-hydroxypropansäure Chemical compound OC[C@H](N)C(O)=O MTCFGRXMJLQNBG-REOHCLBHSA-N 0.000 description 1
- 108091032973 (ribonucleotides)n+m Proteins 0.000 description 1
- OWEGMIWEEQEYGQ-UHFFFAOYSA-N 100676-05-9 Natural products OC1C(O)C(O)C(CO)OC1OCC1C(O)C(O)C(O)C(OC2C(OC(O)C(O)C2O)CO)O1 OWEGMIWEEQEYGQ-UHFFFAOYSA-N 0.000 description 1
- QKNYBSVHEMOAJP-UHFFFAOYSA-N 2-amino-2-(hydroxymethyl)propane-1,3-diol;hydron;chloride Chemical compound Cl.OCC(N)(CO)CO QKNYBSVHEMOAJP-UHFFFAOYSA-N 0.000 description 1
- UMCMPZBLKLEWAF-BCTGSCMUSA-N 3-[(3-cholamidopropyl)dimethylammonio]propane-1-sulfonate Chemical compound C([C@H]1C[C@H]2O)[C@H](O)CC[C@]1(C)[C@@H]1[C@@H]2[C@@H]2CC[C@H]([C@@H](CCC(=O)NCCC[N+](C)(C)CCCS([O-])(=O)=O)C)[C@@]2(C)[C@@H](O)C1 UMCMPZBLKLEWAF-BCTGSCMUSA-N 0.000 description 1
- 102000016605 B-Cell Activating Factor Human genes 0.000 description 1
- 108010028006 B-Cell Activating Factor Proteins 0.000 description 1
- 241000894006 Bacteria Species 0.000 description 1
- 102000051485 Bcl-2 family Human genes 0.000 description 1
- 108700038897 Bcl-2 family Proteins 0.000 description 1
- 108090000342 C-Type Lectins Proteins 0.000 description 1
- 102000003930 C-Type Lectins Human genes 0.000 description 1
- 108020004705 Codon Proteins 0.000 description 1
- 108700010070 Codon Usage Proteins 0.000 description 1
- 108010035532 Collagen Proteins 0.000 description 1
- 102000008186 Collagen Human genes 0.000 description 1
- 238000001712 DNA sequencing Methods 0.000 description 1
- 102100037840 Dehydrogenase/reductase SDR family member 2, mitochondrial Human genes 0.000 description 1
- 239000006144 Dulbecco’s modified Eagle's medium Substances 0.000 description 1
- 102100031780 Endonuclease Human genes 0.000 description 1
- 108010042407 Endonucleases Proteins 0.000 description 1
- 108010054218 Factor VIII Proteins 0.000 description 1
- 102000001690 Factor VIII Human genes 0.000 description 1
- 108010074860 Factor Xa Proteins 0.000 description 1
- GHASVSINZRGABV-UHFFFAOYSA-N Fluorouracil Chemical compound FC1=CNC(=O)NC1=O GHASVSINZRGABV-UHFFFAOYSA-N 0.000 description 1
- 241000282412 Homo Species 0.000 description 1
- 101000868215 Homo sapiens CD40 ligand Proteins 0.000 description 1
- 101100059511 Homo sapiens CD40LG gene Proteins 0.000 description 1
- 101000934356 Homo sapiens CD70 antigen Proteins 0.000 description 1
- 101100273745 Homo sapiens CD70 gene Proteins 0.000 description 1
- 101000976075 Homo sapiens Insulin Proteins 0.000 description 1
- 101000886098 Homo sapiens Rho guanine nucleotide exchange factor 40 Proteins 0.000 description 1
- 101000836397 Homo sapiens SEC14 domain and spectrin repeat-containing protein 1 Proteins 0.000 description 1
- 101000851434 Homo sapiens Tumor necrosis factor ligand superfamily member 13B Proteins 0.000 description 1
- 101000638161 Homo sapiens Tumor necrosis factor ligand superfamily member 6 Proteins 0.000 description 1
- 101000795167 Homo sapiens Tumor necrosis factor receptor superfamily member 13B Proteins 0.000 description 1
- 101000679903 Homo sapiens Tumor necrosis factor receptor superfamily member 25 Proteins 0.000 description 1
- QNAYBMKLOCPYGJ-REOHCLBHSA-N L-alanine Chemical compound C[C@H](N)C(O)=O QNAYBMKLOCPYGJ-REOHCLBHSA-N 0.000 description 1
- ROHFNLRQFUQHCH-YFKPBYRVSA-N L-leucine Chemical compound CC(C)C[C@H](N)C(O)=O ROHFNLRQFUQHCH-YFKPBYRVSA-N 0.000 description 1
- GUBGYTABKSRVRQ-PICCSMPSSA-N Maltose Natural products O[C@@H]1[C@@H](O)[C@H](O)[C@@H](CO)O[C@@H]1O[C@@H]1[C@@H](CO)OC(O)[C@H](O)[C@H]1O GUBGYTABKSRVRQ-PICCSMPSSA-N 0.000 description 1
- 241001465754 Metazoa Species 0.000 description 1
- 125000001429 N-terminal alpha-amino-acid group Chemical group 0.000 description 1
- 108010050808 Procollagen Proteins 0.000 description 1
- 101710188053 Protein D Proteins 0.000 description 1
- 101710146873 Receptor-binding protein Proteins 0.000 description 1
- 101710132893 Resolvase Proteins 0.000 description 1
- 241000283984 Rodentia Species 0.000 description 1
- 102100027289 SEC14 domain and spectrin repeat-containing protein 1 Human genes 0.000 description 1
- 229920002684 Sepharose Polymers 0.000 description 1
- 241001613943 Staphylococcus virus 69 Species 0.000 description 1
- 108091081024 Start codon Proteins 0.000 description 1
- 229930006000 Sucrose Natural products 0.000 description 1
- CZMRCDWAGMRECN-UGDNZRGBSA-N Sucrose Chemical compound O[C@H]1[C@H](O)[C@@H](CO)O[C@@]1(CO)O[C@@H]1[C@H](O)[C@@H](O)[C@H](O)[C@@H](CO)O1 CZMRCDWAGMRECN-UGDNZRGBSA-N 0.000 description 1
- 210000001744 T-lymphocyte Anatomy 0.000 description 1
- 108700012920 TNF Proteins 0.000 description 1
- 108090000190 Thrombin Proteins 0.000 description 1
- 108700002109 Transmembrane Activator and CAML Interactor Proteins 0.000 description 1
- 102000050862 Transmembrane Activator and CAML Interactor Human genes 0.000 description 1
- 239000013504 Triton X-100 Substances 0.000 description 1
- 229920004890 Triton X-100 Polymers 0.000 description 1
- 108060008683 Tumor Necrosis Factor Receptor Proteins 0.000 description 1
- 102100024598 Tumor necrosis factor ligand superfamily member 10 Human genes 0.000 description 1
- 102100024568 Tumor necrosis factor ligand superfamily member 11 Human genes 0.000 description 1
- 102100026890 Tumor necrosis factor ligand superfamily member 4 Human genes 0.000 description 1
- 102100029675 Tumor necrosis factor receptor superfamily member 13B Human genes 0.000 description 1
- 102100022203 Tumor necrosis factor receptor superfamily member 25 Human genes 0.000 description 1
- 238000004847 absorption spectroscopy Methods 0.000 description 1
- 239000002253 acid Substances 0.000 description 1
- 230000002378 acidificating effect Effects 0.000 description 1
- 150000007513 acids Chemical class 0.000 description 1
- 230000003044 adaptive effect Effects 0.000 description 1
- 239000002671 adjuvant Substances 0.000 description 1
- 230000002411 adverse Effects 0.000 description 1
- MGSKVZWGBWPBTF-UHFFFAOYSA-N aebsf Chemical compound NCCC1=CC=C(S(F)(=O)=O)C=C1 MGSKVZWGBWPBTF-UHFFFAOYSA-N 0.000 description 1
- 238000001261 affinity purification Methods 0.000 description 1
- 235000004279 alanine Nutrition 0.000 description 1
- 239000005557 antagonist Substances 0.000 description 1
- 239000003242 anti bacterial agent Substances 0.000 description 1
- 229940088710 antibiotic agent Drugs 0.000 description 1
- 230000001640 apoptogenic effect Effects 0.000 description 1
- 125000003118 aryl group Chemical class 0.000 description 1
- 230000001363 autoimmune Effects 0.000 description 1
- 238000010822 cell death assay Methods 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
- 239000003638 chemical reducing agent Substances 0.000 description 1
- 239000005482 chemotactic factor Substances 0.000 description 1
- 238000004587 chromatography analysis Methods 0.000 description 1
- 230000002759 chromosomal effect Effects 0.000 description 1
- DQLATGHUWYMOKM-UHFFFAOYSA-L cisplatin Chemical compound N[Pt](N)(Cl)Cl DQLATGHUWYMOKM-UHFFFAOYSA-L 0.000 description 1
- 229960004316 cisplatin Drugs 0.000 description 1
- 238000011278 co-treatment Methods 0.000 description 1
- 239000011248 coating agent Substances 0.000 description 1
- 238000000576 coating method Methods 0.000 description 1
- 229920001436 collagen Polymers 0.000 description 1
- 238000002648 combination therapy Methods 0.000 description 1
- 239000012141 concentrate Substances 0.000 description 1
- 239000003246 corticosteroid Substances 0.000 description 1
- 229960001334 corticosteroids Drugs 0.000 description 1
- 102000003675 cytokine receptors Human genes 0.000 description 1
- 108010057085 cytokine receptors Proteins 0.000 description 1
- 210000004292 cytoskeleton Anatomy 0.000 description 1
- 239000000824 cytostatic agent Substances 0.000 description 1
- 230000001085 cytostatic effect Effects 0.000 description 1
- 231100000433 cytotoxic Toxicity 0.000 description 1
- 231100000263 cytotoxicity test Toxicity 0.000 description 1
- 238000012217 deletion Methods 0.000 description 1
- 230000037430 deletion Effects 0.000 description 1
- 238000011161 development Methods 0.000 description 1
- 239000003085 diluting agent Substances 0.000 description 1
- 238000006471 dimerization reaction Methods 0.000 description 1
- LOKCTEFSRHRXRJ-UHFFFAOYSA-I dipotassium trisodium dihydrogen phosphate hydrogen phosphate dichloride Chemical compound P(=O)(O)(O)[O-].[K+].P(=O)(O)([O-])[O-].[Na+].[Na+].[Cl-].[K+].[Cl-].[Na+] LOKCTEFSRHRXRJ-UHFFFAOYSA-I 0.000 description 1
- 239000003937 drug carrier Substances 0.000 description 1
- 230000003511 endothelial effect Effects 0.000 description 1
- DEFVIWRASFVYLL-UHFFFAOYSA-N ethylene glycol bis(2-aminoethyl)tetraacetic acid Chemical compound OC(=O)CN(CC(O)=O)CCOCCOCCN(CC(O)=O)CC(O)=O DEFVIWRASFVYLL-UHFFFAOYSA-N 0.000 description 1
- 229960005420 etoposide Drugs 0.000 description 1
- VJJPUSNTGOMMGY-MRVIYFEKSA-N etoposide Chemical compound COC1=C(O)C(OC)=CC([C@@H]2C3=CC=4OCOC=4C=C3[C@@H](O[C@H]3[C@@H]([C@@H](O)[C@@H]4O[C@H](C)OC[C@H]4O3)O)[C@@H]3[C@@H]2C(OC3)=O)=C1 VJJPUSNTGOMMGY-MRVIYFEKSA-N 0.000 description 1
- 210000003527 eukaryotic cell Anatomy 0.000 description 1
- 230000005284 excitation Effects 0.000 description 1
- 239000013613 expression plasmid Substances 0.000 description 1
- 238000001914 filtration Methods 0.000 description 1
- 229960002949 fluorouracil Drugs 0.000 description 1
- 238000002523 gelfiltration Methods 0.000 description 1
- 230000030414 genetic transfer Effects 0.000 description 1
- 231100000304 hepatotoxicity Toxicity 0.000 description 1
- 230000007686 hepatotoxicity Effects 0.000 description 1
- 230000006801 homologous recombination Effects 0.000 description 1
- 238000002744 homologous recombination Methods 0.000 description 1
- 102000047270 human LTA Human genes 0.000 description 1
- 102000053529 human TNFSF11 Human genes 0.000 description 1
- 102000058177 human TNFSF12 Human genes 0.000 description 1
- 102000050326 human TNFSF13B Human genes 0.000 description 1
- 102000043656 human TNFSF15 Human genes 0.000 description 1
- 102000053830 human TNFSF18 Human genes 0.000 description 1
- 102000051450 human TNFSF4 Human genes 0.000 description 1
- 102000054539 human TNFSF8 Human genes 0.000 description 1
- 230000002209 hydrophobic effect Effects 0.000 description 1
- 230000002519 immonomodulatory effect Effects 0.000 description 1
- 210000002865 immune cell Anatomy 0.000 description 1
- 230000001900 immune effect Effects 0.000 description 1
- 210000000987 immune system Anatomy 0.000 description 1
- 230000002163 immunogen Effects 0.000 description 1
- 230000006872 improvement Effects 0.000 description 1
- 230000001939 inductive effect Effects 0.000 description 1
- 208000015181 infectious disease Diseases 0.000 description 1
- 238000003780 insertion Methods 0.000 description 1
- 230000037431 insertion Effects 0.000 description 1
- PBGKTOXHQIOBKM-FHFVDXKLSA-N insulin (human) Chemical compound C([C@@H](C(=O)N[C@@H](CC(C)C)C(=O)N[C@H]1CSSC[C@H]2C(=O)N[C@H](C(=O)N[C@@H](CO)C(=O)N[C@H](C(=O)N[C@H](C(N[C@@H](CO)C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](CC=3C=CC(O)=CC=3)C(=O)N[C@@H](CCC(N)=O)C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](CCC(O)=O)C(=O)N[C@@H](CC(N)=O)C(=O)N[C@@H](CC=3C=CC(O)=CC=3)C(=O)N[C@@H](CSSC[C@H](NC(=O)[C@H](C(C)C)NC(=O)[C@H](CC(C)C)NC(=O)[C@H](CC=3C=CC(O)=CC=3)NC(=O)[C@H](CC(C)C)NC(=O)[C@H](C)NC(=O)[C@H](CCC(O)=O)NC(=O)[C@H](C(C)C)NC(=O)[C@H](CC(C)C)NC(=O)[C@H](CC=3NC=NC=3)NC(=O)[C@H](CO)NC(=O)CNC1=O)C(=O)NCC(=O)N[C@@H](CCC(O)=O)C(=O)N[C@@H](CCCNC(N)=N)C(=O)NCC(=O)N[C@@H](CC=1C=CC=CC=1)C(=O)N[C@@H](CC=1C=CC=CC=1)C(=O)N[C@@H](CC=1C=CC(O)=CC=1)C(=O)N[C@@H]([C@@H](C)O)C(=O)N1[C@@H](CCC1)C(=O)N[C@@H](CCCCN)C(=O)N[C@@H]([C@@H](C)O)C(O)=O)C(=O)N[C@@H](CC(N)=O)C(O)=O)=O)CSSC[C@@H](C(N2)=O)NC(=O)[C@H](CCC(N)=O)NC(=O)[C@H](CCC(O)=O)NC(=O)[C@H](C(C)C)NC(=O)[C@@H](NC(=O)CN)[C@@H](C)CC)[C@@H](C)CC)[C@@H](C)O)NC(=O)[C@H](CCC(N)=O)NC(=O)[C@H](CC(N)=O)NC(=O)[C@@H](NC(=O)[C@@H](N)CC=1C=CC=CC=1)C(C)C)C1=CN=CN1 PBGKTOXHQIOBKM-FHFVDXKLSA-N 0.000 description 1
- 230000010354 integration Effects 0.000 description 1
- 230000031146 intracellular signal transduction Effects 0.000 description 1
- 238000001990 intravenous administration Methods 0.000 description 1
- 229960004768 irinotecan Drugs 0.000 description 1
- UWKQSNNFCGGAFS-XIFFEERXSA-N irinotecan Chemical compound C1=C2C(CC)=C3CN(C(C4=C([C@@](C(=O)OC4)(O)CC)C=4)=O)C=4C3=NC2=CC=C1OC(=O)N(CC1)CCC1N1CCCCC1 UWKQSNNFCGGAFS-XIFFEERXSA-N 0.000 description 1
- 150000002632 lipids Chemical class 0.000 description 1
- 210000005265 lung cell Anatomy 0.000 description 1
- 239000012139 lysis buffer Substances 0.000 description 1
- 229910001629 magnesium chloride Inorganic materials 0.000 description 1
- 239000000463 material Substances 0.000 description 1
- 239000011159 matrix material Substances 0.000 description 1
- 230000001404 mediated effect Effects 0.000 description 1
- 238000002483 medication Methods 0.000 description 1
- 239000007758 minimum essential medium Substances 0.000 description 1
- 238000010369 molecular cloning Methods 0.000 description 1
- 210000000440 neutrophil Anatomy 0.000 description 1
- 230000003287 optical effect Effects 0.000 description 1
- DWAFYCQODLXJNR-BNTLRKBRSA-L oxaliplatin Chemical compound O1C(=O)C(=O)O[Pt]11N[C@@H]2CCCC[C@H]2N1 DWAFYCQODLXJNR-BNTLRKBRSA-L 0.000 description 1
- 229960001756 oxaliplatin Drugs 0.000 description 1
- COLNVLDHVKWLRT-UHFFFAOYSA-N phenylalanine Natural products OC(=O)C(N)CC1=CC=CC=C1 COLNVLDHVKWLRT-UHFFFAOYSA-N 0.000 description 1
- 230000035790 physiological processes and functions Effects 0.000 description 1
- 230000003334 potential effect Effects 0.000 description 1
- 230000003389 potentiating effect Effects 0.000 description 1
- 239000002243 precursor Substances 0.000 description 1
- 238000000159 protein binding assay Methods 0.000 description 1
- 230000002797 proteolythic effect Effects 0.000 description 1
- 238000003908 quality control method Methods 0.000 description 1
- 108091008146 restriction endonucleases Proteins 0.000 description 1
- 238000009097 single-agent therapy Methods 0.000 description 1
- 235000017557 sodium bicarbonate Nutrition 0.000 description 1
- 229910000030 sodium bicarbonate Inorganic materials 0.000 description 1
- 235000017550 sodium carbonate Nutrition 0.000 description 1
- 229910000029 sodium carbonate Inorganic materials 0.000 description 1
- 229940054269 sodium pyruvate Drugs 0.000 description 1
- 230000009870 specific binding Effects 0.000 description 1
- 239000003381 stabilizer Substances 0.000 description 1
- 230000000638 stimulation Effects 0.000 description 1
- 239000000758 substrate Substances 0.000 description 1
- 239000005720 sucrose Substances 0.000 description 1
- 238000003786 synthesis reaction Methods 0.000 description 1
- 229960004072 thrombin Drugs 0.000 description 1
- 230000001988 toxicity Effects 0.000 description 1
- 231100000419 toxicity Toxicity 0.000 description 1
- 238000003146 transient transfection Methods 0.000 description 1
- 238000013519 translation Methods 0.000 description 1
- 102000035160 transmembrane proteins Human genes 0.000 description 1
- 108091005703 transmembrane proteins Proteins 0.000 description 1
- 102000003298 tumor necrosis factor receptor Human genes 0.000 description 1
- 108010087967 type I signal peptidase Proteins 0.000 description 1
- 238000000108 ultra-filtration Methods 0.000 description 1
- 239000013603 viral vector Substances 0.000 description 1
- 238000005406 washing Methods 0.000 description 1
- XLYOFNOQVPJJNP-UHFFFAOYSA-N water Substances O XLYOFNOQVPJJNP-UHFFFAOYSA-N 0.000 description 1
Classifications
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K14/00—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof
- C07K14/435—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from animals; from humans
- C07K14/705—Receptors; Cell surface antigens; Cell surface determinants
- C07K14/70575—NGF/TNF-superfamily, e.g. CD70, CD95L, CD153, CD154
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P19/00—Drugs for skeletal disorders
- A61P19/02—Drugs for skeletal disorders for joint disorders, e.g. arthritis, arthrosis
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P25/00—Drugs for disorders of the nervous system
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- 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
- A61P3/00—Drugs for disorders of the metabolism
-
- 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
-
- 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
- A61P43/00—Drugs for specific purposes, not provided for in groups A61P1/00-A61P41/00
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K14/00—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof
- C07K14/415—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from plants
- C07K14/42—Lectins, e.g. concanavalin, phytohaemagglutinin
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K14/00—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof
- C07K14/435—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from animals; from humans
- C07K14/46—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from animals; from humans from vertebrates
- C07K14/47—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from animals; from humans from vertebrates from mammals
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K14/00—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof
- C07K14/435—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from animals; from humans
- C07K14/46—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from animals; from humans from vertebrates
- C07K14/47—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from animals; from humans from vertebrates from mammals
- C07K14/4701—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from animals; from humans from vertebrates from mammals not used
- C07K14/4726—Lectins
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K14/00—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof
- C07K14/435—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from animals; from humans
- C07K14/52—Cytokines; Lymphokines; Interferons
- C07K14/525—Tumour necrosis factor [TNF]
-
- 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
-
- 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
- C07K2319/00—Fusion polypeptide
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K2319/00—Fusion polypeptide
- C07K2319/01—Fusion polypeptide containing a localisation/targetting motif
- C07K2319/02—Fusion polypeptide containing a localisation/targetting motif containing a signal sequence
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K2319/00—Fusion polypeptide
- C07K2319/20—Fusion polypeptide containing a tag with affinity for a non-protein ligand
- C07K2319/21—Fusion polypeptide containing a tag with affinity for a non-protein ligand containing a His-tag
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K2319/00—Fusion polypeptide
- C07K2319/20—Fusion polypeptide containing a tag with affinity for a non-protein ligand
- C07K2319/22—Fusion polypeptide containing a tag with affinity for a non-protein ligand containing a Strep-tag
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K2319/00—Fusion polypeptide
- C07K2319/32—Fusion polypeptide fusions with soluble part of a cell surface receptor, "decoy receptors"
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K2319/00—Fusion polypeptide
- C07K2319/70—Fusion polypeptide containing domain for protein-protein interaction
Landscapes
- Health & Medical Sciences (AREA)
- Chemical & Material Sciences (AREA)
- Life Sciences & Earth Sciences (AREA)
- Organic Chemistry (AREA)
- General Health & Medical Sciences (AREA)
- Genetics & Genomics (AREA)
- Medicinal Chemistry (AREA)
- Engineering & Computer Science (AREA)
- Molecular Biology (AREA)
- Biochemistry (AREA)
- Biophysics (AREA)
- Zoology (AREA)
- Bioinformatics & Cheminformatics (AREA)
- Proteomics, Peptides & Aminoacids (AREA)
- Gastroenterology & Hepatology (AREA)
- Veterinary Medicine (AREA)
- Chemical Kinetics & Catalysis (AREA)
- General Chemical & Material Sciences (AREA)
- Nuclear Medicine, Radiotherapy & Molecular Imaging (AREA)
- Pharmacology & Pharmacy (AREA)
- Animal Behavior & Ethology (AREA)
- Public Health (AREA)
- Immunology (AREA)
- Toxicology (AREA)
- Biomedical Technology (AREA)
- Biotechnology (AREA)
- Wood Science & Technology (AREA)
- General Engineering & Computer Science (AREA)
- Botany (AREA)
- Physics & Mathematics (AREA)
- Microbiology (AREA)
- Plant Pathology (AREA)
- Cell Biology (AREA)
- Rheumatology (AREA)
- Obesity (AREA)
- Communicable Diseases (AREA)
- Diabetes (AREA)
- Neurology (AREA)
- Transplantation (AREA)
- Physical Education & Sports Medicine (AREA)
Applications Claiming Priority (2)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| EP07013506 | 2007-07-10 | ||
| EP07013506 | 2007-07-10 |
Publications (1)
| Publication Number | Publication Date |
|---|---|
| ES2567704T3 true ES2567704T3 (es) | 2016-04-26 |
Family
ID=39865190
Family Applications (3)
| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| ES12166865.1T Active ES2567704T3 (es) | 2007-07-10 | 2008-07-10 | Proteínas de fusión de colectina de la superfamilia de TNF |
| ES16150412.1T Active ES2657801T3 (es) | 2007-07-10 | 2008-07-10 | Proteínas de fusión de colectina de la superfamilia de TNF |
| ES08773964.5T Active ES2560871T3 (es) | 2007-07-10 | 2008-07-10 | Proteínas de fusión de colectina de la superfamilia de TNF |
Family Applications After (2)
| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| ES16150412.1T Active ES2657801T3 (es) | 2007-07-10 | 2008-07-10 | Proteínas de fusión de colectina de la superfamilia de TNF |
| ES08773964.5T Active ES2560871T3 (es) | 2007-07-10 | 2008-07-10 | Proteínas de fusión de colectina de la superfamilia de TNF |
Country Status (7)
| Country | Link |
|---|---|
| US (6) | US8383774B2 (enExample) |
| EP (4) | EP3321277B1 (enExample) |
| JP (2) | JP6002903B2 (enExample) |
| AU (1) | AU2008274490B2 (enExample) |
| CA (3) | CA2963124C (enExample) |
| ES (3) | ES2567704T3 (enExample) |
| WO (1) | WO2009007120A2 (enExample) |
Families Citing this family (81)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| CN101969990B (zh) * | 2007-11-01 | 2014-07-09 | 阿肯色大学评议会 | 增强针对艾美球虫属的免疫反应的组合物和方法 |
| WO2010003766A2 (en) | 2008-06-17 | 2010-01-14 | Apogenix Gmbh | Multimeric tnf receptors |
| PL2310509T3 (pl) | 2008-07-21 | 2015-08-31 | Apogenix Ag | Jednołańcuchowe cząsteczki TNFSF |
| EP2370068A4 (en) | 2008-12-10 | 2015-09-23 | Paka Pulmonary Pharmaceuticals Inc | METHOD AND COMPOSITIONS FOR DELIVERING MEDICAMENTS TO THE LUNG |
| US8664366B2 (en) | 2009-01-09 | 2014-03-04 | Apogenix Gmbh | Fusion proteins forming trimers |
| CN101698852B (zh) * | 2009-10-23 | 2014-08-13 | 江苏先声药物研究有限公司 | 具有cd137l功能的蛋白或多肽及其基因和应用 |
| JP4918627B2 (ja) * | 2010-02-26 | 2012-04-18 | 積水メディカル株式会社 | 偽陽性反応を抑制する検体抽出液 |
| US8932575B2 (en) | 2010-09-21 | 2015-01-13 | University Of Miami | Compositions and methods for inducing migration by dendritic cells and an immune response |
| WO2012040266A2 (en) * | 2010-09-24 | 2012-03-29 | University Of Miami | Gene-based adjuvants and compositions thereof to increase antibody production in response to gene-based vaccines |
| NZ609216A (en) * | 2010-12-03 | 2014-05-30 | Adamed Sp Zoo | Anticancer fusion protein |
| EP2586793A1 (en) * | 2011-10-27 | 2013-05-01 | Centre National de la Recherche Scientifique | Chimeric molecule involving oligomerized FasL extracellular domain |
| JP6152379B2 (ja) * | 2012-06-29 | 2017-06-21 | 旭化成メディカル株式会社 | プロテインａのｂドメイン変異体を含むポリペプチドが結合された担体からなる吸着材 |
| NO2776305T3 (enExample) | 2014-04-23 | 2018-01-27 | ||
| WO2016079527A1 (en) | 2014-11-19 | 2016-05-26 | Tetralogic Birinapant Uk Ltd | Combination therapy |
| WO2016097773A1 (en) | 2014-12-19 | 2016-06-23 | Children's Cancer Institute | Therapeutic iap antagonists for treating proliferative disorders |
| MA41460A (fr) | 2015-02-03 | 2017-12-12 | Oncomed Pharm Inc | Agents de liaison à la tnfrsf et leurs utilisations |
| KR20180063885A (ko) | 2015-09-24 | 2018-06-12 | 더 유니버시티 오브 노쓰 캐롤라이나 엣 채플 힐 | 전이 감소를 위한 방법 및 조성물 |
| WO2017068185A1 (en) | 2015-10-23 | 2017-04-27 | Apogenix Ag | Single-chain gitr-receptor agonist proteins |
| WO2017072080A1 (en) * | 2015-10-28 | 2017-05-04 | Apogenix Ag | Single-chain tl1a receptor agonist proteins |
| TWI788307B (zh) | 2016-10-31 | 2023-01-01 | 美商艾歐凡斯生物治療公司 | 用於擴增腫瘤浸潤性淋巴細胞之工程化人造抗原呈現細胞 |
| CA3049165A1 (en) | 2017-01-06 | 2018-07-12 | Iovance Biotherapeutics, Inc. | Expansion of tumor infiltrating lymphocytes with potassium channel agonists and therapeutic uses thereof |
| CN110462027A (zh) | 2017-01-06 | 2019-11-15 | 艾欧凡斯生物治疗公司 | 用肿瘤坏死因子受体超家族（tnfrsf）激动剂扩增肿瘤浸润淋巴细胞（til）及til和tnfrsf激动剂的治疗组合 |
| JP7370580B2 (ja) * | 2017-04-06 | 2023-10-30 | ウニヴェルズィテート シュトゥットガルト | 結合および生物活性を改善した腫瘍壊死因子受容体（ｔｎｆｒ）結合タンパク質複合体 |
| IL270412B2 (en) | 2017-05-10 | 2025-03-01 | Iovance Biotherapeutics Inc | Expansion of infiltrating lymphocytes from liquid samples and their medical uses |
| US11819517B2 (en) | 2017-06-05 | 2023-11-21 | Iovance Biotherapeutics, Inc. | Methods of using tumor infiltrating lymphocytes in double-refractory melanoma |
| JP7551496B2 (ja) | 2017-10-31 | 2024-09-17 | カリヴィル イムノセラピューティクス， インコーポレイテッド | 全身送達のためのプラットフォーム腫瘍溶解性ベクター |
| KR20200100060A (ko) | 2017-11-17 | 2020-08-25 | 이오반스 바이오테라퓨틱스, 인크. | 미세 바늘 흡인물 및 소형 생검물로부터의 til 확장 |
| EP3714041A1 (en) | 2017-11-22 | 2020-09-30 | Iovance Biotherapeutics, Inc. | Expansion of peripheral blood lymphocytes (pbls) from peripheral blood |
| WO2019118873A2 (en) | 2017-12-15 | 2019-06-20 | Iovance Biotherapeutics, Inc. | Systems and methods for determining the beneficial administration of tumor infiltrating lymphocytes, and methods of use thereof and beneficial administration of tumor infiltrating lymphocytes, and methods of use thereof |
| WO2019136459A1 (en) | 2018-01-08 | 2019-07-11 | Iovance Biotherapeutics, Inc. | Processes for generating til products enriched for tumor antigen-specific t-cells |
| JP2021509586A (ja) | 2018-01-08 | 2021-04-01 | アイオバンス バイオセラピューティクス，インコーポレイテッド | 腫瘍抗原特異的ｔ細胞について濃縮されたｔｉｌ製品を生成するためのプロセス |
| US11713446B2 (en) | 2018-01-08 | 2023-08-01 | Iovance Biotherapeutics, Inc. | Processes for generating TIL products enriched for tumor antigen-specific T-cells |
| EP3752600A1 (en) | 2018-02-13 | 2020-12-23 | Iovance Biotherapeutics, Inc. | Expansion of tumor infiltrating lymphocytes (tils) with adenosine a2a receptor antagonists and therapeutic combinations of tils and adenosine a2a receptor antagonists |
| EA202092319A1 (ru) | 2018-03-29 | 2021-03-04 | Айовэнс Байотерапьютикс, Инк. | Способы получения опухоль-инфильтрирующих лимфоцитов и применения их в иммунотерапии |
| TWI831776B (zh) | 2018-04-27 | 2024-02-11 | 美商艾歐凡斯生物治療公司 | 腫瘤浸潤性淋巴細胞之基因編輯和彼於免疫治療之用途 |
| US12473532B2 (en) | 2018-05-10 | 2025-11-18 | Iovance Biotherapeutics, Inc. | Processes for production of tumor infiltrating lymphocytes and uses of same in immunotherapy |
| US20200024326A1 (en) * | 2018-06-14 | 2020-01-23 | Nantbio, Inc. | Tnf-type receptor-ligand fusion proteins and methods |
| TW202031273A (zh) | 2018-08-31 | 2020-09-01 | 美商艾歐凡斯生物治療公司 | 抗ｐｄ－１抗體難治療性之非小細胞肺癌（ｎｓｃｌｃ）病患的治療 |
| TWI862515B (zh) | 2018-09-20 | 2024-11-21 | 美商艾歐凡斯生物治療公司 | 來自經冷凍保存之腫瘤樣本之腫瘤浸潤性淋巴細胞（ｔｉｌ）之擴增 |
| WO2020096989A1 (en) | 2018-11-05 | 2020-05-14 | Iovance Biotherapeutics, Inc. | Treatment of nsclc patients refractory for anti-pd-1 antibody |
| WO2020096988A2 (en) | 2018-11-05 | 2020-05-14 | Iovance Biotherapeutics, Inc. | Processes for production of tumor infiltrating lymphocytes and uses of the same in immunotherapy |
| WO2020096927A1 (en) | 2018-11-05 | 2020-05-14 | Iovance Biotherapeutics, Inc. | Expansion of tils utilizing akt pathway inhibitors |
| AU2019375416A1 (en) | 2018-11-05 | 2021-05-27 | Iovance Biotherapeutics, Inc. | Selection of improved tumor reactive T-cells |
| CA3123392A1 (en) | 2018-12-19 | 2020-06-25 | Iovance Biotherapeutics, Inc. | Methods of expanding tumor infiltrating lymphocytes using engineered cytokine receptor pairs and uses thereof |
| US20220135649A1 (en) * | 2019-02-06 | 2022-05-05 | The Regents Of The University Of California | Dominant negative cd40l polypeptides |
| WO2020168151A2 (en) * | 2019-02-15 | 2020-08-20 | Epicypher, Inc. | Quantitative mapping of chromatin associated proteins |
| MX2021010288A (es) | 2019-03-01 | 2021-09-23 | Iovance Biotherapeutics Inc | Expansion de linfocitos infiltrantes de tumores a partir de tumores liquidos y usos terapeuticos de los mismos. |
| EP3946437B1 (en) | 2019-03-29 | 2025-11-19 | H. Lee Moffitt Cancer Center and Research Institute, Inc. | Ex vivo methods for producing a t cell therapeutic and related compositions and methods |
| US20220249559A1 (en) | 2019-05-13 | 2022-08-11 | Iovance Biotherapeutics, Inc. | Methods and compositions for selecting tumor infiltrating lymphocytes and uses of the same in immunotherapy |
| EP4582442A3 (en) | 2019-06-24 | 2025-10-29 | Universität Stuttgart | Tnfr2 agonists with improved stability |
| WO2021081378A1 (en) | 2019-10-25 | 2021-04-29 | Iovance Biotherapeutics, Inc. | Gene editing of tumor infiltrating lymphocytes and uses of same in immunotherapy |
| CN115023270A (zh) | 2019-11-27 | 2022-09-06 | 迈斯特治疗公司 | 使用调节剂产生肿瘤反应性t细胞组合物的方法 |
| WO2021118990A1 (en) | 2019-12-11 | 2021-06-17 | Iovance Biotherapeutics, Inc. | Processes for the production of tumor infiltrating lymphocytes (tils) and methods of using the same |
| IL295990A (en) | 2020-02-27 | 2022-11-01 | Myst Therapeutics Llc | Methods for in vitro enrichment and expansion of tumor-reactive t cells and preparations related thereto |
| JP2023523855A (ja) | 2020-05-04 | 2023-06-07 | アイオバンス バイオセラピューティクス，インコーポレイテッド | 腫瘍浸潤リンパ球の製造方法及び免疫療法におけるその使用 |
| JP2023524108A (ja) | 2020-05-04 | 2023-06-08 | アイオバンス バイオセラピューティクス，インコーポレイテッド | 改良された腫瘍反応性ｔ細胞の選択 |
| JP2023546359A (ja) | 2020-10-06 | 2023-11-02 | アイオバンス バイオセラピューティクス，インコーポレイテッド | 腫瘍浸潤リンパ球療法によるｎｓｃｌｃ患者の治療 |
| WO2022076606A1 (en) | 2020-10-06 | 2022-04-14 | Iovance Biotherapeutics, Inc. | Treatment of nsclc patients with tumor infiltrating lymphocyte therapies |
| WO2022079308A1 (en) * | 2020-10-16 | 2022-04-21 | Institut Pasteur | Chimeric constructs useful in vaccination and cancer therapy |
| WO2022109133A1 (en) | 2020-11-19 | 2022-05-27 | Kalivir Immunotherapeutics, Inc. | Oncolytic immunotherapy by tumor micro-environment remodeling |
| WO2022125941A1 (en) | 2020-12-11 | 2022-06-16 | Iovance Biotherapeutics, Inc. | Treatment of cancer patients with tumor infiltrating lymphocyte therapies in combination with braf inhibitors and/or mek inhibitors |
| JP2023554395A (ja) | 2020-12-17 | 2023-12-27 | アイオバンス バイオセラピューティクス，インコーポレイテッド | Ｃｔｌａ－４及びｐｄ－１阻害剤と併用した腫瘍浸潤リンパ球療法による治療 |
| JP2024500403A (ja) | 2020-12-17 | 2024-01-09 | アイオバンス バイオセラピューティクス，インコーポレイテッド | 腫瘍浸潤リンパ球によるがんの治療 |
| US20240299540A1 (en) | 2021-02-05 | 2024-09-12 | Iovance Biotherapeutics, Inc. | Adjuvant therapy for cancer |
| EP4301138A2 (en) | 2021-03-05 | 2024-01-10 | Iovance Biotherapeutics, Inc. | Tumor storage and cell culture compositions |
| CA3215830A1 (en) | 2021-04-19 | 2022-10-27 | Rafael CUBAS | Chimeric costimulatory receptors, chemokine receptors, and the use of same in cellular immunotherapies |
| WO2022232375A1 (en) | 2021-04-30 | 2022-11-03 | Kalivir Immunotherapeutics, Inc. | Oncolytic viruses for modified mhc expression |
| EP4340850A1 (en) | 2021-05-17 | 2024-03-27 | Iovance Biotherapeutics, Inc. | Pd-1 gene-edited tumor infiltrating lymphocytes and uses of same in immunotherapy |
| JP2024523314A (ja) * | 2021-06-17 | 2024-06-28 | カリヴィル イムノセラピューティクス， インコーポレイテッド | Ｔｎｆｓｆ－ｌ融合タンパク質およびその使用 |
| WO2023009716A1 (en) | 2021-07-28 | 2023-02-02 | Iovance Biotherapeutics, Inc. | Treatment of cancer patients with tumor infiltrating lymphocyte therapies in combination with kras inhibitors |
| WO2023049862A1 (en) | 2021-09-24 | 2023-03-30 | Iovance Biotherapeutics, Inc. | Expansion processes and agents for tumor infiltrating lymphocytes |
| CA3235824A1 (en) | 2021-10-27 | 2023-05-04 | Frederick G. Vogt | Systems and methods for coordinating manufacturing of cells for patient-specific immunotherapy |
| US20250032618A1 (en) | 2021-11-10 | 2025-01-30 | Iovance Biotherapeutics, Inc. | Methods of expansion treatment utilizing cd8 tumor infiltrating lymphocytes |
| WO2023088889A1 (en) | 2021-11-16 | 2023-05-25 | Apogenix Ag | CD137 ligands |
| JP2025503987A (ja) | 2022-01-28 | 2025-02-06 | アイオバンス バイオセラピューティクス，インコーポレイテッド | ペイロードを発現するように操作された腫瘍浸潤リンパ球 |
| CA3248034A1 (en) | 2022-04-15 | 2023-10-19 | Iovance Biotherapeutics Inc | METHODS FOR EXPANSION OF TIL CELLS BY MEANS OF SPECIFIC CYTOKINE COMBINATIONS AND/OR AKT INHIBITOR TREATMENT |
| CN119654339A (zh) | 2022-07-01 | 2025-03-18 | 特兰斯吉恩股份有限公司 | 包含表面活性蛋白-d和tnfsf成员的融合蛋白 |
| WO2024030758A1 (en) | 2022-08-01 | 2024-02-08 | Iovance Biotherapeutics, Inc. | Chimeric costimulatory receptors, chemokine receptors, and the use of same in cellular immunotherapies |
| WO2024098024A1 (en) | 2022-11-04 | 2024-05-10 | Iovance Biotherapeutics, Inc. | Expansion of tumor infiltrating lymphocytes from liquid tumors and therapeutic uses thereof |
| WO2024151885A1 (en) | 2023-01-13 | 2024-07-18 | Iovance Biotherapeutics, Inc. | Use of til as maintenance therapy for nsclc patients who achieved pr/cr after prior therapy |
| WO2025101484A1 (en) | 2023-11-06 | 2025-05-15 | Iovance Biotherapeutics, Inc. | Treatment of endometrial cancers with tumor infiltrating lymphocyte therapies |
Family Cites Families (16)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| GB9409768D0 (en) * | 1994-05-16 | 1994-07-06 | Medical Res Council | Trimerising polypeptides |
| KR101004174B1 (ko) | 1995-06-29 | 2010-12-24 | 임뮤넥스 코포레이션 | 세포소멸을 유도하는 시토킨 |
| US7300774B1 (en) | 1999-12-09 | 2007-11-27 | The Regents Of The University Of California | Multimeric fusion proteins of the TNF superfamily ligands |
| DE19963859A1 (de) | 1999-12-30 | 2001-07-12 | Apotech Res & Dev Ltd | Bi- oder Oligomer eines Di-, Tri-, Quattro- oder Pentamers von rekombinanten Fusionsproteinen |
| GB0015426D0 (en) | 2000-06-24 | 2000-08-16 | Univ Southampton | Method for generating soluble highly multimeric proteins |
| US20040247563A1 (en) * | 2000-11-02 | 2004-12-09 | Lynch David H. | Method of enhancing lymphocyte-mediated immune responses |
| DE10122140A1 (de) * | 2001-05-08 | 2002-11-28 | Apotech Res & Dev Ltd | Rekombinante Fusionsproteine und deren Trimere |
| MXPA04005909A (es) | 2001-12-21 | 2005-05-17 | Immunex Corp | Polipeptidos recombinantes. |
| CA2482938A1 (en) * | 2002-04-12 | 2003-10-23 | Human Genome Sciences, Inc. | Antibodies that specifically bind to tr2 |
| CN1694961A (zh) | 2002-09-10 | 2005-11-09 | 内蒂穆恩公司 | 胶原凝集素－补体激活蛋白嵌合体 |
| GB0524316D0 (en) * | 2005-11-29 | 2006-01-04 | Medical Res Council | Tumour necrosis factor-related apoptosis-inducing ligands (TRAILs) |
| WO2007120368A2 (en) * | 2006-01-09 | 2007-10-25 | The Regents Of The University Of California | Immunostimulatory combinations for vaccine adjuvants |
| WO2007102690A1 (en) * | 2006-03-06 | 2007-09-13 | Postech Foundation | Vector including the codon-optimized dna cassette for producing secretory recombinant dodecamer trail |
| EP1894940A1 (en) | 2006-08-28 | 2008-03-05 | Apogenix GmbH | TNF superfamily fusion proteins |
| DK2101877T3 (da) * | 2006-12-28 | 2013-09-23 | Deutsches Krebsforsch | Neutralisering af virkningen af CD95 til blokering af invasion af glioblastomceller in vivo |
| US8664366B2 (en) | 2009-01-09 | 2014-03-04 | Apogenix Gmbh | Fusion proteins forming trimers |
-
2008
- 2008-07-10 CA CA2963124A patent/CA2963124C/en not_active Expired - Fee Related
- 2008-07-10 ES ES12166865.1T patent/ES2567704T3/es active Active
- 2008-07-10 ES ES16150412.1T patent/ES2657801T3/es active Active
- 2008-07-10 ES ES08773964.5T patent/ES2560871T3/es active Active
- 2008-07-10 CA CA2860950A patent/CA2860950C/en not_active Expired - Fee Related
- 2008-07-10 EP EP17197297.9A patent/EP3321277B1/en active Active
- 2008-07-10 AU AU2008274490A patent/AU2008274490B2/en not_active Ceased
- 2008-07-10 WO PCT/EP2008/005644 patent/WO2009007120A2/en not_active Ceased
- 2008-07-10 JP JP2010515417A patent/JP6002903B2/ja not_active Expired - Fee Related
- 2008-07-10 EP EP08773964.5A patent/EP2176288B1/en not_active Not-in-force
- 2008-07-10 US US12/668,188 patent/US8383774B2/en not_active Expired - Fee Related
- 2008-07-10 EP EP12166865.1A patent/EP2484691B1/en not_active Not-in-force
- 2008-07-10 EP EP16150412.1A patent/EP3072903B1/en not_active Not-in-force
- 2008-07-10 CA CA2692802A patent/CA2692802C/en not_active Expired - Fee Related
-
2013
- 2013-02-25 US US13/776,559 patent/US8907063B2/en not_active Expired - Fee Related
-
2014
- 2014-07-02 US US14/322,830 patent/US9212211B2/en not_active Expired - Fee Related
- 2014-12-19 JP JP2014258068A patent/JP6029646B2/ja not_active Expired - Fee Related
-
2015
- 2015-12-14 US US14/968,198 patent/US9527897B2/en not_active Expired - Fee Related
-
2016
- 2016-12-02 US US15/367,434 patent/US10000550B2/en active Active
-
2018
- 2018-06-15 US US16/010,301 patent/US10519217B2/en not_active Expired - Fee Related
Also Published As
Similar Documents
| Publication | Publication Date | Title |
|---|---|---|
| ES2567704T3 (es) | Proteínas de fusión de colectina de la superfamilia de TNF | |
| ES2593049T3 (es) | Proteínas de fusión que forman trímeros | |
| AU2017201232B2 (en) | TNF superfamily collectin fusion proteins |