JP2000515363A - Ｍｈｃ複合体及びその用途 - Google Patents
Ｍｈｃ複合体及びその用途Info
- Publication number
- JP2000515363A JP2000515363A JP09527863A JP52786397A JP2000515363A JP 2000515363 A JP2000515363 A JP 2000515363A JP 09527863 A JP09527863 A JP 09527863A JP 52786397 A JP52786397 A JP 52786397A JP 2000515363 A JP2000515363 A JP 2000515363A
- Authority
- JP
- Japan
- Prior art keywords
- mhc
- complex
- peptide
- cells
- cell
- 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.)
- Pending
Links
- 108090000765 processed proteins & peptides Proteins 0.000 claims abstract description 413
- 230000004927 fusion Effects 0.000 claims abstract description 303
- 210000001744 T-lymphocyte Anatomy 0.000 claims abstract description 223
- 238000000034 method Methods 0.000 claims abstract description 127
- 230000000694 effects Effects 0.000 claims abstract description 72
- 230000028993 immune response Effects 0.000 claims abstract description 68
- 108091054438 MHC class II family Proteins 0.000 claims abstract description 67
- 102000016266 T-Cell Antigen Receptors Human genes 0.000 claims abstract description 53
- 108091008874 T cell receptors Proteins 0.000 claims abstract description 52
- 241000124008 Mammalia Species 0.000 claims abstract description 49
- 102000043131 MHC class II family Human genes 0.000 claims abstract description 48
- 230000001939 inductive effect Effects 0.000 claims abstract description 22
- 210000004027 cell Anatomy 0.000 claims description 315
- 108020004414 DNA Proteins 0.000 claims description 166
- 108090000623 proteins and genes Proteins 0.000 claims description 151
- 150000001413 amino acids Chemical class 0.000 claims description 48
- 102000004169 proteins and genes Human genes 0.000 claims description 39
- 102000018713 Histocompatibility Antigens Class II Human genes 0.000 claims description 26
- 241001465754 Metazoa Species 0.000 claims description 26
- 108091028043 Nucleic acid sequence Proteins 0.000 claims description 26
- 230000001086 cytosolic effect Effects 0.000 claims description 21
- 230000006698 induction Effects 0.000 claims description 17
- 239000012528 membrane Substances 0.000 claims description 17
- 108700019146 Transgenes Proteins 0.000 claims description 16
- 208000023275 Autoimmune disease Diseases 0.000 claims description 15
- 230000009261 transgenic effect Effects 0.000 claims description 14
- 238000012258 culturing Methods 0.000 claims description 11
- 201000006417 multiple sclerosis Diseases 0.000 claims description 11
- 206010020751 Hypersensitivity Diseases 0.000 claims description 10
- 230000007815 allergy Effects 0.000 claims description 10
- 230000014621 translational initiation Effects 0.000 claims description 9
- 239000013599 cloning vector Substances 0.000 claims description 8
- 108091035707 Consensus sequence Proteins 0.000 claims description 7
- 108010027412 Histocompatibility Antigens Class II Proteins 0.000 claims description 7
- 238000003776 cleavage reaction Methods 0.000 claims description 7
- 230000007017 scission Effects 0.000 claims description 7
- 206010067584 Type 1 diabetes mellitus Diseases 0.000 claims description 6
- 241000700605 Viruses Species 0.000 claims description 5
- 208000026935 allergic disease Diseases 0.000 claims description 5
- 230000006907 apoptotic process Effects 0.000 claims description 5
- 210000000170 cell membrane Anatomy 0.000 claims description 5
- 230000001684 chronic effect Effects 0.000 claims description 5
- 230000001105 regulatory effect Effects 0.000 claims description 5
- 206010039073 rheumatoid arthritis Diseases 0.000 claims description 5
- 206010028417 myasthenia gravis Diseases 0.000 claims description 4
- 239000002253 acid Substances 0.000 claims description 3
- 210000002443 helper t lymphocyte Anatomy 0.000 claims description 3
- 230000022532 regulation of transcription, DNA-dependent Effects 0.000 claims description 3
- 238000002512 chemotherapy Methods 0.000 claims description 2
- 206010061598 Immunodeficiency Diseases 0.000 claims 2
- VZQHRKZCAZCACO-PYJNHQTQSA-N (2s)-2-[[(2s)-2-[2-[[(2s)-2-[[(2s)-2-amino-5-(diaminomethylideneamino)pentanoyl]amino]propanoyl]amino]prop-2-enoylamino]-3-methylbutanoyl]amino]propanoic acid Chemical compound OC(=O)[C@H](C)NC(=O)[C@H](C(C)C)NC(=O)C(=C)NC(=O)[C@H](C)NC(=O)[C@@H](N)CCCNC(N)=N VZQHRKZCAZCACO-PYJNHQTQSA-N 0.000 claims 1
- 241000283073 Equus caballus Species 0.000 claims 1
- 208000036142 Viral infection Diseases 0.000 claims 1
- 230000009385 viral infection Effects 0.000 claims 1
- 108700018351 Major Histocompatibility Complex Proteins 0.000 abstract description 488
- 230000020382 suppression by virus of host antigen processing and presentation of peptide antigen via MHC class I Effects 0.000 abstract description 474
- 102000004196 processed proteins & peptides Human genes 0.000 abstract description 78
- 239000005557 antagonist Substances 0.000 abstract description 21
- 238000000338 in vitro Methods 0.000 abstract description 17
- 239000004031 partial agonist Substances 0.000 abstract description 13
- 238000002955 isolation Methods 0.000 abstract description 8
- 239000013598 vector Substances 0.000 description 106
- 108010058846 Ovalbumin Proteins 0.000 description 105
- 239000012634 fragment Substances 0.000 description 90
- 229940092253 ovalbumin Drugs 0.000 description 86
- 238000003752 polymerase chain reaction Methods 0.000 description 84
- 241000699670 Mus sp. Species 0.000 description 74
- 238000003556 assay Methods 0.000 description 69
- 239000013604 expression vector Substances 0.000 description 62
- 239000000047 product Substances 0.000 description 62
- 239000013615 primer Substances 0.000 description 59
- 241000699666 Mus <mouse, genus> Species 0.000 description 56
- 108010019759 OVA 323-339 Proteins 0.000 description 53
- 235000001014 amino acid Nutrition 0.000 description 49
- 229940024606 amino acid Drugs 0.000 description 49
- 238000010367 cloning Methods 0.000 description 47
- 108010002350 Interleukin-2 Proteins 0.000 description 45
- 102000000588 Interleukin-2 Human genes 0.000 description 45
- 210000000612 antigen-presenting cell Anatomy 0.000 description 45
- 239000000499 gel Substances 0.000 description 39
- 108091034117 Oligonucleotide Proteins 0.000 description 38
- 238000002347 injection Methods 0.000 description 36
- 239000007924 injection Substances 0.000 description 36
- 230000006052 T cell proliferation Effects 0.000 description 34
- 239000000427 antigen Substances 0.000 description 33
- 230000000139 costimulatory effect Effects 0.000 description 33
- 235000018102 proteins Nutrition 0.000 description 33
- 108091007433 antigens Proteins 0.000 description 32
- 102000036639 antigens Human genes 0.000 description 32
- 239000000523 sample Substances 0.000 description 30
- 108091032973 (ribonucleotides)n+m Proteins 0.000 description 29
- 239000002609 medium Substances 0.000 description 28
- LFQSCWFLJHTTHZ-UHFFFAOYSA-N Ethanol Chemical compound CCO LFQSCWFLJHTTHZ-UHFFFAOYSA-N 0.000 description 26
- 239000000243 solution Substances 0.000 description 25
- FAPWRFPIFSIZLT-UHFFFAOYSA-M Sodium chloride Chemical compound [Na+].[Cl-] FAPWRFPIFSIZLT-UHFFFAOYSA-M 0.000 description 24
- 210000003719 b-lymphocyte Anatomy 0.000 description 24
- 238000001727 in vivo Methods 0.000 description 24
- 230000000890 antigenic effect Effects 0.000 description 23
- 239000002299 complementary DNA Substances 0.000 description 23
- 239000002773 nucleotide Substances 0.000 description 23
- 125000003729 nucleotide group Chemical group 0.000 description 23
- 238000013459 approach Methods 0.000 description 21
- 238000010790 dilution Methods 0.000 description 21
- 239000012895 dilution Substances 0.000 description 21
- 238000011534 incubation Methods 0.000 description 21
- 239000000203 mixture Substances 0.000 description 21
- 210000004681 ovum Anatomy 0.000 description 21
- 238000001516 cell proliferation assay Methods 0.000 description 20
- 238000006243 chemical reaction Methods 0.000 description 20
- 239000012091 fetal bovine serum Substances 0.000 description 20
- 239000013612 plasmid Substances 0.000 description 20
- JLCPHMBAVCMARE-UHFFFAOYSA-N [3-[[3-[[3-[[3-[[3-[[3-[[3-[[3-[[3-[[3-[[3-[[5-(2-amino-6-oxo-1H-purin-9-yl)-3-[[3-[[3-[[3-[[3-[[3-[[5-(2-amino-6-oxo-1H-purin-9-yl)-3-[[5-(2-amino-6-oxo-1H-purin-9-yl)-3-hydroxyoxolan-2-yl]methoxy-hydroxyphosphoryl]oxyoxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(5-methyl-2,4-dioxopyrimidin-1-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(6-aminopurin-9-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(6-aminopurin-9-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(6-aminopurin-9-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(6-aminopurin-9-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxyoxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(5-methyl-2,4-dioxopyrimidin-1-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(4-amino-2-oxopyrimidin-1-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(5-methyl-2,4-dioxopyrimidin-1-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(5-methyl-2,4-dioxopyrimidin-1-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(6-aminopurin-9-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(6-aminopurin-9-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(4-amino-2-oxopyrimidin-1-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(4-amino-2-oxopyrimidin-1-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(4-amino-2-oxopyrimidin-1-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(6-aminopurin-9-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(4-amino-2-oxopyrimidin-1-yl)oxolan-2-yl]methyl [5-(6-aminopurin-9-yl)-2-(hydroxymethyl)oxolan-3-yl] hydrogen phosphate Polymers Cc1cn(C2CC(OP(O)(=O)OCC3OC(CC3OP(O)(=O)OCC3OC(CC3O)n3cnc4c3nc(N)[nH]c4=O)n3cnc4c3nc(N)[nH]c4=O)C(COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3CO)n3cnc4c(N)ncnc34)n3ccc(N)nc3=O)n3cnc4c(N)ncnc34)n3ccc(N)nc3=O)n3ccc(N)nc3=O)n3ccc(N)nc3=O)n3cnc4c(N)ncnc34)n3cnc4c(N)ncnc34)n3cc(C)c(=O)[nH]c3=O)n3cc(C)c(=O)[nH]c3=O)n3ccc(N)nc3=O)n3cc(C)c(=O)[nH]c3=O)n3cnc4c3nc(N)[nH]c4=O)n3cnc4c(N)ncnc34)n3cnc4c(N)ncnc34)n3cnc4c(N)ncnc34)n3cnc4c(N)ncnc34)O2)c(=O)[nH]c1=O JLCPHMBAVCMARE-UHFFFAOYSA-N 0.000 description 19
- 230000004913 activation Effects 0.000 description 19
- 201000002491 encephalomyelitis Diseases 0.000 description 19
- 210000004408 hybridoma Anatomy 0.000 description 19
- 238000002360 preparation method Methods 0.000 description 19
- 230000004044 response Effects 0.000 description 19
- 238000002965 ELISA Methods 0.000 description 18
- 108060003951 Immunoglobulin Proteins 0.000 description 18
- 239000000872 buffer Substances 0.000 description 18
- 230000003053 immunization Effects 0.000 description 18
- 238000002649 immunization Methods 0.000 description 18
- 102000018358 immunoglobulin Human genes 0.000 description 18
- 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 18
- 101100229953 Saccharomyces cerevisiae (strain ATCC 204508 / S288c) SCT1 gene Proteins 0.000 description 17
- 101100194362 Schizosaccharomyces pombe (strain 972 / ATCC 24843) res1 gene Proteins 0.000 description 17
- 210000001165 lymph node Anatomy 0.000 description 17
- 239000006228 supernatant Substances 0.000 description 17
- 238000012360 testing method Methods 0.000 description 17
- DHMQDGOQFOQNFH-UHFFFAOYSA-N Glycine Chemical compound NCC(O)=O DHMQDGOQFOQNFH-UHFFFAOYSA-N 0.000 description 16
- 238000002835 absorbance Methods 0.000 description 16
- 230000035755 proliferation Effects 0.000 description 16
- NHBKXEKEPDILRR-UHFFFAOYSA-N 2,3-bis(butanoylsulfanyl)propyl butanoate Chemical compound CCCC(=O)OCC(SC(=O)CCC)CSC(=O)CCC NHBKXEKEPDILRR-UHFFFAOYSA-N 0.000 description 15
- 108010093013 HLA-DR1 Antigen Proteins 0.000 description 15
- 238000012408 PCR amplification Methods 0.000 description 15
- 230000006044 T cell activation Effects 0.000 description 15
- 238000010276 construction Methods 0.000 description 15
- 210000004962 mammalian cell Anatomy 0.000 description 15
- 239000013642 negative control Substances 0.000 description 15
- 229940104230 thymidine Drugs 0.000 description 15
- 238000005406 washing Methods 0.000 description 15
- 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 14
- 108091026890 Coding region Proteins 0.000 description 14
- 125000003275 alpha amino acid group Chemical group 0.000 description 14
- 108020001507 fusion proteins Proteins 0.000 description 14
- 102000037865 fusion proteins Human genes 0.000 description 14
- 239000011780 sodium chloride Substances 0.000 description 14
- 239000012228 culture supernatant Substances 0.000 description 13
- 230000035772 mutation Effects 0.000 description 13
- 239000000725 suspension Substances 0.000 description 13
- 239000002671 adjuvant Substances 0.000 description 12
- 239000006285 cell suspension Substances 0.000 description 12
- 201000010099 disease Diseases 0.000 description 12
- 208000037265 diseases, disorders, signs and symptoms Diseases 0.000 description 12
- 241000238631 Hexapoda Species 0.000 description 11
- ZDXPYRJPNDTMRX-VKHMYHEASA-N L-glutamine Chemical compound OC(=O)[C@@H](N)CCC(N)=O ZDXPYRJPNDTMRX-VKHMYHEASA-N 0.000 description 11
- 102000047918 Myelin Basic Human genes 0.000 description 11
- 238000000746 purification Methods 0.000 description 11
- 239000013605 shuttle vector Substances 0.000 description 11
- 238000011830 transgenic mouse model Methods 0.000 description 11
- 102100031780 Endonuclease Human genes 0.000 description 10
- 108090000978 Interleukin-4 Proteins 0.000 description 10
- 101710107068 Myelin basic protein Proteins 0.000 description 10
- NWIBSHFKIJFRCO-WUDYKRTCSA-N Mytomycin Chemical compound C1N2C(C(C(C)=C(N)C3=O)=O)=C3[C@@H](COC(N)=O)[C@@]2(OC)[C@@H]2[C@H]1N2 NWIBSHFKIJFRCO-WUDYKRTCSA-N 0.000 description 10
- 229920001213 Polysorbate 20 Polymers 0.000 description 10
- 108010092799 RNA-directed DNA polymerase Proteins 0.000 description 10
- 238000011161 development Methods 0.000 description 10
- 230000018109 developmental process Effects 0.000 description 10
- 239000000256 polyoxyethylene sorbitan monolaurate Substances 0.000 description 10
- 235000010486 polyoxyethylene sorbitan monolaurate Nutrition 0.000 description 10
- 239000013641 positive control Substances 0.000 description 10
- 210000002966 serum Anatomy 0.000 description 10
- 238000011282 treatment Methods 0.000 description 10
- XLYOFNOQVPJJNP-UHFFFAOYSA-N water Chemical compound O XLYOFNOQVPJJNP-UHFFFAOYSA-N 0.000 description 10
- KISWVXRQTGLFGD-UHFFFAOYSA-N 2-[[2-[[6-amino-2-[[2-[[2-[[5-amino-2-[[2-[[1-[2-[[6-amino-2-[(2,5-diamino-5-oxopentanoyl)amino]hexanoyl]amino]-5-(diaminomethylideneamino)pentanoyl]pyrrolidine-2-carbonyl]amino]-3-hydroxypropanoyl]amino]-5-oxopentanoyl]amino]-5-(diaminomethylideneamino)p Chemical compound C1CCN(C(=O)C(CCCN=C(N)N)NC(=O)C(CCCCN)NC(=O)C(N)CCC(N)=O)C1C(=O)NC(CO)C(=O)NC(CCC(N)=O)C(=O)NC(CCCN=C(N)N)C(=O)NC(CO)C(=O)NC(CCCCN)C(=O)NC(C(=O)NC(CC(C)C)C(O)=O)CC1=CC=C(O)C=C1 KISWVXRQTGLFGD-UHFFFAOYSA-N 0.000 description 9
- 101100041819 Arabidopsis thaliana SCE1 gene Proteins 0.000 description 9
- 229930182555 Penicillin Natural products 0.000 description 9
- 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 9
- 230000005867 T cell response Effects 0.000 description 9
- 210000004369 blood Anatomy 0.000 description 9
- 239000008280 blood Substances 0.000 description 9
- 230000008859 change Effects 0.000 description 9
- 235000019441 ethanol Nutrition 0.000 description 9
- 229960002743 glutamine Drugs 0.000 description 9
- 230000005764 inhibitory process Effects 0.000 description 9
- 238000003780 insertion Methods 0.000 description 9
- 230000037431 insertion Effects 0.000 description 9
- 230000004073 interleukin-2 production Effects 0.000 description 9
- 229940049954 penicillin Drugs 0.000 description 9
- 229920001184 polypeptide Polymers 0.000 description 9
- 238000012216 screening Methods 0.000 description 9
- 229960005322 streptomycin Drugs 0.000 description 9
- 239000003155 DNA primer Substances 0.000 description 8
- 102000011931 Nucleoproteins Human genes 0.000 description 8
- 108010061100 Nucleoproteins Proteins 0.000 description 8
- 239000004677 Nylon Substances 0.000 description 8
- 229920002684 Sepharose Polymers 0.000 description 8
- 230000011712 cell development Effects 0.000 description 8
- 230000001419 dependent effect Effects 0.000 description 8
- 230000012010 growth Effects 0.000 description 8
- 230000001506 immunosuppresive effect Effects 0.000 description 8
- 238000010348 incorporation Methods 0.000 description 8
- 230000003993 interaction Effects 0.000 description 8
- 239000007788 liquid Substances 0.000 description 8
- 229920001778 nylon Polymers 0.000 description 8
- 235000020030 perry Nutrition 0.000 description 8
- 210000000952 spleen Anatomy 0.000 description 8
- 210000001519 tissue Anatomy 0.000 description 8
- 238000012546 transfer Methods 0.000 description 8
- 239000011534 wash buffer Substances 0.000 description 8
- 239000004471 Glycine Substances 0.000 description 7
- 238000005119 centrifugation Methods 0.000 description 7
- 239000003085 diluting agent Substances 0.000 description 7
- 238000002474 experimental method Methods 0.000 description 7
- 239000011734 sodium Substances 0.000 description 7
- 241000894007 species Species 0.000 description 7
- 230000000638 stimulation Effects 0.000 description 7
- 230000001629 suppression Effects 0.000 description 7
- 238000001890 transfection Methods 0.000 description 7
- 241000701447 unidentified baculovirus Species 0.000 description 7
- 239000012980 RPMI-1640 medium Substances 0.000 description 6
- 238000004458 analytical method Methods 0.000 description 6
- 230000001580 bacterial effect Effects 0.000 description 6
- 238000004113 cell culture Methods 0.000 description 6
- 238000004587 chromatography analysis Methods 0.000 description 6
- 230000007423 decrease Effects 0.000 description 6
- 239000000412 dendrimer Substances 0.000 description 6
- 229920000736 dendritic polymer Polymers 0.000 description 6
- MHMNJMPURVTYEJ-UHFFFAOYSA-N fluorescein-5-isothiocyanate Chemical compound O1C(=O)C2=CC(N=C=S)=CC=C2C21C1=CC=C(O)C=C1OC1=CC(O)=CC=C21 MHMNJMPURVTYEJ-UHFFFAOYSA-N 0.000 description 6
- 230000006870 function Effects 0.000 description 6
- RAXXELZNTBOGNW-UHFFFAOYSA-N imidazole Natural products C1=CNC=N1 RAXXELZNTBOGNW-UHFFFAOYSA-N 0.000 description 6
- 208000026278 immune system disease Diseases 0.000 description 6
- 238000011068 loading method Methods 0.000 description 6
- WLWIMKWZMGJRBS-UHFFFAOYSA-N primin Chemical compound CCCCCC1=CC(=O)C=C(OC)C1=O WLWIMKWZMGJRBS-UHFFFAOYSA-N 0.000 description 6
- 230000037452 priming Effects 0.000 description 6
- 230000002829 reductive effect Effects 0.000 description 6
- 108091008146 restriction endonucleases Proteins 0.000 description 6
- 210000004989 spleen cell Anatomy 0.000 description 6
- 230000009466 transformation Effects 0.000 description 6
- 241000283707 Capra Species 0.000 description 5
- 108091006146 Channels Proteins 0.000 description 5
- 238000012286 ELISA Assay Methods 0.000 description 5
- 241000282412 Homo Species 0.000 description 5
- 206010062016 Immunosuppression Diseases 0.000 description 5
- 229930182816 L-glutamine Natural products 0.000 description 5
- 206010028980 Neoplasm Diseases 0.000 description 5
- 230000002411 adverse Effects 0.000 description 5
- OHDRQQURAXLVGJ-HLVWOLMTSA-N azane;(2e)-3-ethyl-2-[(e)-(3-ethyl-6-sulfo-1,3-benzothiazol-2-ylidene)hydrazinylidene]-1,3-benzothiazole-6-sulfonic acid Chemical compound [NH4+].[NH4+].S/1C2=CC(S([O-])(=O)=O)=CC=C2N(CC)C\1=N/N=C1/SC2=CC(S([O-])(=O)=O)=CC=C2N1CC OHDRQQURAXLVGJ-HLVWOLMTSA-N 0.000 description 5
- 229910002091 carbon monoxide Inorganic materials 0.000 description 5
- 125000003178 carboxy group Chemical group [H]OC(*)=O 0.000 description 5
- 230000010261 cell growth Effects 0.000 description 5
- 238000012761 co-transfection Methods 0.000 description 5
- 238000004581 coalescence Methods 0.000 description 5
- 239000011248 coating agent Substances 0.000 description 5
- 238000000576 coating method Methods 0.000 description 5
- 150000001875 compounds Chemical class 0.000 description 5
- 239000013078 crystal Substances 0.000 description 5
- 238000012217 deletion Methods 0.000 description 5
- 230000037430 deletion Effects 0.000 description 5
- 238000004520 electroporation Methods 0.000 description 5
- 206010014599 encephalitis Diseases 0.000 description 5
- 210000004013 groin Anatomy 0.000 description 5
- 238000000099 in vitro assay Methods 0.000 description 5
- 238000007918 intramuscular administration Methods 0.000 description 5
- 238000004519 manufacturing process Methods 0.000 description 5
- 238000005259 measurement Methods 0.000 description 5
- 229960004857 mitomycin Drugs 0.000 description 5
- 238000011533 pre-incubation Methods 0.000 description 5
- 125000002924 primary amino group Chemical group [H]N([H])* 0.000 description 5
- 239000002987 primer (paints) Substances 0.000 description 5
- 230000008569 process Effects 0.000 description 5
- NGVDGCNFYWLIFO-UHFFFAOYSA-N pyridoxal 5'-phosphate Chemical compound CC1=NC=C(COP(O)(O)=O)C(C=O)=C1O NGVDGCNFYWLIFO-UHFFFAOYSA-N 0.000 description 5
- 239000012898 sample dilution Substances 0.000 description 5
- 239000006152 selective media Substances 0.000 description 5
- 238000002415 sodium dodecyl sulfate polyacrylamide gel electrophoresis Methods 0.000 description 5
- 238000010561 standard procedure Methods 0.000 description 5
- 238000002560 therapeutic procedure Methods 0.000 description 5
- 238000002255 vaccination Methods 0.000 description 5
- YBJHBAHKTGYVGT-ZKWXMUAHSA-N (+)-Biotin Chemical compound N1C(=O)N[C@@H]2[C@H](CCCCC(=O)O)SC[C@@H]21 YBJHBAHKTGYVGT-ZKWXMUAHSA-N 0.000 description 4
- WFIYPADYPQQLNN-UHFFFAOYSA-N 2-[2-(4-bromopyrazol-1-yl)ethyl]isoindole-1,3-dione Chemical compound C1=C(Br)C=NN1CCN1C(=O)C2=CC=CC=C2C1=O WFIYPADYPQQLNN-UHFFFAOYSA-N 0.000 description 4
- UZOVYGYOLBIAJR-UHFFFAOYSA-N 4-isocyanato-4'-methyldiphenylmethane Chemical compound C1=CC(C)=CC=C1CC1=CC=C(N=C=O)C=C1 UZOVYGYOLBIAJR-UHFFFAOYSA-N 0.000 description 4
- 108700031361 Brachyury Proteins 0.000 description 4
- 102000053602 DNA Human genes 0.000 description 4
- 206010011968 Decreased immune responsiveness Diseases 0.000 description 4
- 108010010803 Gelatin Proteins 0.000 description 4
- 208000032843 Hemorrhage Diseases 0.000 description 4
- 108091092195 Intron Proteins 0.000 description 4
- QNAYBMKLOCPYGJ-REOHCLBHSA-N L-alanine Chemical compound C[C@H](N)C(O)=O QNAYBMKLOCPYGJ-REOHCLBHSA-N 0.000 description 4
- 102000007056 Recombinant Fusion Proteins Human genes 0.000 description 4
- 108010008281 Recombinant Fusion Proteins Proteins 0.000 description 4
- 230000017274 T cell anergy Effects 0.000 description 4
- 230000033540 T cell apoptotic process Effects 0.000 description 4
- 108010006785 Taq Polymerase Proteins 0.000 description 4
- 235000004279 alanine Nutrition 0.000 description 4
- 230000008901 benefit Effects 0.000 description 4
- 230000000740 bleeding effect Effects 0.000 description 4
- AIYUHDOJVYHVIT-UHFFFAOYSA-M caesium chloride Chemical compound [Cl-].[Cs+] AIYUHDOJVYHVIT-UHFFFAOYSA-M 0.000 description 4
- 230000004663 cell proliferation Effects 0.000 description 4
- 230000036755 cellular response Effects 0.000 description 4
- 239000003623 enhancer Substances 0.000 description 4
- 238000009472 formulation Methods 0.000 description 4
- 239000008273 gelatin Substances 0.000 description 4
- 229920000159 gelatin Polymers 0.000 description 4
- 235000019322 gelatine Nutrition 0.000 description 4
- 235000011852 gelatine desserts Nutrition 0.000 description 4
- ZDXPYRJPNDTMRX-UHFFFAOYSA-N glutamine Natural products OC(=O)C(N)CCC(N)=O ZDXPYRJPNDTMRX-UHFFFAOYSA-N 0.000 description 4
- 108020002326 glutamine synthetase Proteins 0.000 description 4
- 230000002209 hydrophobic effect Effects 0.000 description 4
- 210000000987 immune system Anatomy 0.000 description 4
- 229940072221 immunoglobulins Drugs 0.000 description 4
- 206010022000 influenza Diseases 0.000 description 4
- 230000003834 intracellular effect Effects 0.000 description 4
- 230000001404 mediated effect Effects 0.000 description 4
- 238000002156 mixing Methods 0.000 description 4
- 210000000663 muscle cell Anatomy 0.000 description 4
- 239000008194 pharmaceutical composition Substances 0.000 description 4
- 238000012545 processing Methods 0.000 description 4
- 230000028327 secretion Effects 0.000 description 4
- 125000003607 serino group Chemical group [H]N([H])[C@]([H])(C(=O)[*])C(O[H])([H])[H] 0.000 description 4
- 238000010186 staining Methods 0.000 description 4
- 230000001225 therapeutic effect Effects 0.000 description 4
- DGVVWUTYPXICAM-UHFFFAOYSA-N β‐Mercaptoethanol Chemical compound OCCS DGVVWUTYPXICAM-UHFFFAOYSA-N 0.000 description 4
- 208000032116 Autoimmune Experimental Encephalomyelitis Diseases 0.000 description 3
- 208000003950 B-cell lymphoma Diseases 0.000 description 3
- 108091003079 Bovine Serum Albumin Proteins 0.000 description 3
- 108020004705 Codon Proteins 0.000 description 3
- 102000004190 Enzymes Human genes 0.000 description 3
- 108090000790 Enzymes Proteins 0.000 description 3
- 241000588724 Escherichia coli Species 0.000 description 3
- WSFSSNUMVMOOMR-UHFFFAOYSA-N Formaldehyde Chemical compound O=C WSFSSNUMVMOOMR-UHFFFAOYSA-N 0.000 description 3
- 102000008949 Histocompatibility Antigens Class I Human genes 0.000 description 3
- 108010088652 Histocompatibility Antigens Class I Proteins 0.000 description 3
- DGAQECJNVWCQMB-PUAWFVPOSA-M Ilexoside XXIX Chemical compound C[C@@H]1CC[C@@]2(CC[C@@]3(C(=CC[C@H]4[C@]3(CC[C@@H]5[C@@]4(CC[C@@H](C5(C)C)OS(=O)(=O)[O-])C)C)[C@@H]2[C@]1(C)O)C)C(=O)O[C@H]6[C@@H]([C@H]([C@@H]([C@H](O6)CO)O)O)O.[Na+] DGAQECJNVWCQMB-PUAWFVPOSA-M 0.000 description 3
- WHUUTDBJXJRKMK-VKHMYHEASA-N L-glutamic acid Chemical compound OC(=O)[C@@H](N)CCC(O)=O WHUUTDBJXJRKMK-VKHMYHEASA-N 0.000 description 3
- 108090000364 Ligases Proteins 0.000 description 3
- 102000043129 MHC class I family Human genes 0.000 description 3
- 108091054437 MHC class I family Proteins 0.000 description 3
- 108010033276 Peptide Fragments Proteins 0.000 description 3
- 102000007079 Peptide Fragments Human genes 0.000 description 3
- OAICVXFJPJFONN-UHFFFAOYSA-N Phosphorus Chemical compound [P] OAICVXFJPJFONN-UHFFFAOYSA-N 0.000 description 3
- 238000010240 RT-PCR analysis Methods 0.000 description 3
- VMHLLURERBWHNL-UHFFFAOYSA-M Sodium acetate Chemical compound [Na+].CC([O-])=O VMHLLURERBWHNL-UHFFFAOYSA-M 0.000 description 3
- HEMHJVSKTPXQMS-UHFFFAOYSA-M Sodium hydroxide Chemical compound [OH-].[Na+] HEMHJVSKTPXQMS-UHFFFAOYSA-M 0.000 description 3
- 239000007983 Tris buffer Substances 0.000 description 3
- 230000009471 action Effects 0.000 description 3
- 239000011543 agarose gel Substances 0.000 description 3
- 239000000556 agonist Substances 0.000 description 3
- 238000010171 animal model Methods 0.000 description 3
- 230000003042 antagnostic effect Effects 0.000 description 3
- -1 aromatic Amino acids Chemical class 0.000 description 3
- 239000012298 atmosphere Substances 0.000 description 3
- 239000003593 chromogenic compound Substances 0.000 description 3
- 230000003247 decreasing effect Effects 0.000 description 3
- 210000004443 dendritic cell Anatomy 0.000 description 3
- 238000000432 density-gradient centrifugation Methods 0.000 description 3
- 238000001514 detection method Methods 0.000 description 3
- 238000002405 diagnostic procedure Methods 0.000 description 3
- 230000029087 digestion Effects 0.000 description 3
- 229940088598 enzyme Drugs 0.000 description 3
- 238000005194 fractionation Methods 0.000 description 3
- 230000005714 functional activity Effects 0.000 description 3
- 102000005396 glutamine synthetase Human genes 0.000 description 3
- XKUKSGPZAADMRA-UHFFFAOYSA-N glycyl-glycyl-glycine Chemical compound NCC(=O)NCC(=O)NCC(O)=O XKUKSGPZAADMRA-UHFFFAOYSA-N 0.000 description 3
- ZJYYHGLJYGJLLN-UHFFFAOYSA-N guanidinium thiocyanate Chemical compound SC#N.NC(N)=N ZJYYHGLJYGJLLN-UHFFFAOYSA-N 0.000 description 3
- 235000014304 histidine Nutrition 0.000 description 3
- 125000001165 hydrophobic group Chemical group 0.000 description 3
- 230000036039 immunity Effects 0.000 description 3
- 238000005462 in vivo assay Methods 0.000 description 3
- 208000015181 infectious disease Diseases 0.000 description 3
- 238000011081 inoculation Methods 0.000 description 3
- 239000007927 intramuscular injection Substances 0.000 description 3
- 238000010253 intravenous injection Methods 0.000 description 3
- KFZMGEQAYNKOFK-UHFFFAOYSA-N isopropyl alcohol Natural products CC(C)O KFZMGEQAYNKOFK-UHFFFAOYSA-N 0.000 description 3
- 230000000670 limiting effect Effects 0.000 description 3
- 210000003712 lysosome Anatomy 0.000 description 3
- 230000001868 lysosomic effect Effects 0.000 description 3
- 238000012986 modification Methods 0.000 description 3
- 230000004048 modification Effects 0.000 description 3
- 238000003199 nucleic acid amplification method Methods 0.000 description 3
- 239000002777 nucleoside Substances 0.000 description 3
- 230000036961 partial effect Effects 0.000 description 3
- 239000008188 pellet Substances 0.000 description 3
- 229910052698 phosphorus Inorganic materials 0.000 description 3
- 239000011574 phosphorus Substances 0.000 description 3
- 230000009696 proliferative response Effects 0.000 description 3
- 238000010791 quenching Methods 0.000 description 3
- 230000009257 reactivity Effects 0.000 description 3
- 230000006798 recombination Effects 0.000 description 3
- 238000005215 recombination Methods 0.000 description 3
- 230000004043 responsiveness Effects 0.000 description 3
- 238000002741 site-directed mutagenesis Methods 0.000 description 3
- 210000002027 skeletal muscle Anatomy 0.000 description 3
- 229910052708 sodium Inorganic materials 0.000 description 3
- 239000001632 sodium acetate Substances 0.000 description 3
- 235000017281 sodium acetate Nutrition 0.000 description 3
- 238000006467 substitution reaction Methods 0.000 description 3
- 238000004448 titration Methods 0.000 description 3
- 238000013518 transcription Methods 0.000 description 3
- 230000035897 transcription Effects 0.000 description 3
- LENZDBCJOHFCAS-UHFFFAOYSA-N tris Chemical compound OCC(N)(CO)CO LENZDBCJOHFCAS-UHFFFAOYSA-N 0.000 description 3
- 229960005486 vaccine Drugs 0.000 description 3
- MTCFGRXMJLQNBG-REOHCLBHSA-N (2S)-2-Amino-3-hydroxypropansäure Chemical compound OC[C@H](N)C(O)=O MTCFGRXMJLQNBG-REOHCLBHSA-N 0.000 description 2
- 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 description 2
- 108700028369 Alleles Proteins 0.000 description 2
- 102100029464 Aquaporin-9 Human genes 0.000 description 2
- DCXYFEDJOCDNAF-UHFFFAOYSA-N Asparagine Natural products OC(=O)C(N)CC(N)=O DCXYFEDJOCDNAF-UHFFFAOYSA-N 0.000 description 2
- 101150089247 B7 gene Proteins 0.000 description 2
- 241000283690 Bos taurus Species 0.000 description 2
- 101100263837 Bovine ephemeral fever virus (strain BB7721) beta gene Proteins 0.000 description 2
- 108010009575 CD55 Antigens Proteins 0.000 description 2
- 108020004635 Complementary DNA Proteins 0.000 description 2
- 102000004127 Cytokines Human genes 0.000 description 2
- 108090000695 Cytokines Proteins 0.000 description 2
- 230000004544 DNA amplification Effects 0.000 description 2
- KCXVZYZYPLLWCC-UHFFFAOYSA-N EDTA Chemical compound OC(=O)CN(CC(O)=O)CCN(CC(O)=O)CC(O)=O KCXVZYZYPLLWCC-UHFFFAOYSA-N 0.000 description 2
- 101100316840 Enterobacteria phage P4 Beta gene Proteins 0.000 description 2
- WHUUTDBJXJRKMK-UHFFFAOYSA-N Glutamic acid Natural products OC(=O)C(N)CCC(O)=O WHUUTDBJXJRKMK-UHFFFAOYSA-N 0.000 description 2
- 102000003886 Glycoproteins Human genes 0.000 description 2
- 108090000288 Glycoproteins Proteins 0.000 description 2
- 101000771413 Homo sapiens Aquaporin-9 Proteins 0.000 description 2
- 101000921370 Homo sapiens Elongation of very long chain fatty acids protein 1 Proteins 0.000 description 2
- 241000700588 Human alphaherpesvirus 1 Species 0.000 description 2
- DCXYFEDJOCDNAF-REOHCLBHSA-N L-asparagine Chemical compound OC(=O)[C@@H](N)CC(N)=O DCXYFEDJOCDNAF-REOHCLBHSA-N 0.000 description 2
- 102000003960 Ligases Human genes 0.000 description 2
- 241000699660 Mus musculus Species 0.000 description 2
- 241000187479 Mycobacterium tuberculosis Species 0.000 description 2
- 108700026244 Open Reading Frames Proteins 0.000 description 2
- 229930040373 Paraformaldehyde Natural products 0.000 description 2
- 108010067902 Peptide Library Proteins 0.000 description 2
- 102000012288 Phosphopyruvate Hydratase Human genes 0.000 description 2
- 108010022181 Phosphopyruvate Hydratase Proteins 0.000 description 2
- 239000004365 Protease Substances 0.000 description 2
- 108010076504 Protein Sorting Signals Proteins 0.000 description 2
- 108020004511 Recombinant DNA Proteins 0.000 description 2
- 241000283984 Rodentia Species 0.000 description 2
- 240000004808 Saccharomyces cerevisiae Species 0.000 description 2
- 235000014680 Saccharomyces cerevisiae Nutrition 0.000 description 2
- MTCFGRXMJLQNBG-UHFFFAOYSA-N Serine Natural products OCC(N)C(O)=O MTCFGRXMJLQNBG-UHFFFAOYSA-N 0.000 description 2
- QAOWNCQODCNURD-UHFFFAOYSA-N Sulfuric acid Chemical compound OS(O)(=O)=O QAOWNCQODCNURD-UHFFFAOYSA-N 0.000 description 2
- IQFYYKKMVGJFEH-XLPZGREQSA-N Thymidine Chemical class O=C1NC(=O)C(C)=CN1[C@@H]1O[C@H](CO)[C@@H](O)C1 IQFYYKKMVGJFEH-XLPZGREQSA-N 0.000 description 2
- ISAKRJDGNUQOIC-UHFFFAOYSA-N Uracil Chemical group O=C1C=CNC(=O)N1 ISAKRJDGNUQOIC-UHFFFAOYSA-N 0.000 description 2
- 102000006943 Uracil-DNA Glycosidase Human genes 0.000 description 2
- 108010072685 Uracil-DNA Glycosidase Proteins 0.000 description 2
- 230000003213 activating effect Effects 0.000 description 2
- 238000001042 affinity chromatography Methods 0.000 description 2
- 238000000246 agarose gel electrophoresis Methods 0.000 description 2
- 101150087698 alpha gene Proteins 0.000 description 2
- BFNBIHQBYMNNAN-UHFFFAOYSA-N ammonium sulfate Chemical compound N.N.OS(O)(=O)=O BFNBIHQBYMNNAN-UHFFFAOYSA-N 0.000 description 2
- 229910052921 ammonium sulfate Inorganic materials 0.000 description 2
- 235000011130 ammonium sulphate Nutrition 0.000 description 2
- 230000003321 amplification Effects 0.000 description 2
- 230000030741 antigen processing and presentation Effects 0.000 description 2
- 239000007864 aqueous solution Substances 0.000 description 2
- 235000009582 asparagine Nutrition 0.000 description 2
- 229960001230 asparagine Drugs 0.000 description 2
- 229960002685 biotin Drugs 0.000 description 2
- 235000020958 biotin Nutrition 0.000 description 2
- 239000011616 biotin Substances 0.000 description 2
- 230000000903 blocking effect Effects 0.000 description 2
- 201000011510 cancer Diseases 0.000 description 2
- 230000015556 catabolic process Effects 0.000 description 2
- 230000020411 cell activation Effects 0.000 description 2
- 210000000991 chicken egg Anatomy 0.000 description 2
- 239000002131 composite material Substances 0.000 description 2
- 239000012141 concentrate Substances 0.000 description 2
- 238000007796 conventional method Methods 0.000 description 2
- 230000001351 cycling effect Effects 0.000 description 2
- 235000013365 dairy product Nutrition 0.000 description 2
- 230000006378 damage Effects 0.000 description 2
- 238000006731 degradation reaction Methods 0.000 description 2
- 238000013461 design Methods 0.000 description 2
- 238000002059 diagnostic imaging Methods 0.000 description 2
- 238000000502 dialysis Methods 0.000 description 2
- 231100000673 dose–response relationship Toxicity 0.000 description 2
- 239000006196 drop Substances 0.000 description 2
- 229940079593 drug Drugs 0.000 description 2
- 239000003814 drug Substances 0.000 description 2
- 239000003937 drug carrier Substances 0.000 description 2
- ZMMJGEGLRURXTF-UHFFFAOYSA-N ethidium bromide Chemical compound [Br-].C12=CC(N)=CC=C2C2=CC=C(N)C=C2[N+](CC)=C1C1=CC=CC=C1 ZMMJGEGLRURXTF-UHFFFAOYSA-N 0.000 description 2
- 229960005542 ethidium bromide Drugs 0.000 description 2
- 230000002068 genetic effect Effects 0.000 description 2
- 210000004602 germ cell Anatomy 0.000 description 2
- 239000011521 glass Substances 0.000 description 2
- 235000013922 glutamic acid Nutrition 0.000 description 2
- 239000004220 glutamic acid Substances 0.000 description 2
- 108010067216 glycyl-glycyl-glycine Proteins 0.000 description 2
- 239000001963 growth medium Substances 0.000 description 2
- 230000036541 health Effects 0.000 description 2
- 150000002411 histidines Chemical class 0.000 description 2
- 229910052739 hydrogen Inorganic materials 0.000 description 2
- 239000001257 hydrogen Substances 0.000 description 2
- AKPUJVVHYUHGKY-UHFFFAOYSA-N hydron;propan-2-ol;chloride Chemical compound Cl.CC(C)O AKPUJVVHYUHGKY-UHFFFAOYSA-N 0.000 description 2
- 230000000899 immune system response Effects 0.000 description 2
- 238000002650 immunosuppressive therapy Methods 0.000 description 2
- 230000002401 inhibitory effect 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
- 238000010255 intramuscular injection Methods 0.000 description 2
- 230000013011 mating Effects 0.000 description 2
- 230000007246 mechanism Effects 0.000 description 2
- 229910052751 metal Inorganic materials 0.000 description 2
- 239000002184 metal Substances 0.000 description 2
- 238000002703 mutagenesis Methods 0.000 description 2
- 231100000350 mutagenesis Toxicity 0.000 description 2
- 150000003833 nucleoside derivatives Chemical class 0.000 description 2
- 210000000056 organ Anatomy 0.000 description 2
- 229920002866 paraformaldehyde Polymers 0.000 description 2
- 229920000768 polyamine Polymers 0.000 description 2
- 230000001323 posttranslational effect Effects 0.000 description 2
- 210000001236 prokaryotic cell Anatomy 0.000 description 2
- 230000002062 proliferating effect Effects 0.000 description 2
- 125000001500 prolyl group Chemical group [H]N1C([H])(C(=O)[*])C([H])([H])C([H])([H])C1([H])[H] 0.000 description 2
- 230000002285 radioactive effect Effects 0.000 description 2
- 239000002464 receptor antagonist Substances 0.000 description 2
- 229940044551 receptor antagonist Drugs 0.000 description 2
- 108020003175 receptors Proteins 0.000 description 2
- 102000005962 receptors Human genes 0.000 description 2
- 238000011160 research Methods 0.000 description 2
- 102220240796 rs553605556 Human genes 0.000 description 2
- 230000003248 secreting effect Effects 0.000 description 2
- 238000013207 serial dilution Methods 0.000 description 2
- 239000007787 solid Substances 0.000 description 2
- 230000006641 stabilisation Effects 0.000 description 2
- 238000011105 stabilization Methods 0.000 description 2
- 230000004936 stimulating effect Effects 0.000 description 2
- 238000003756 stirring Methods 0.000 description 2
- 239000000758 substrate Substances 0.000 description 2
- 238000001356 surgical procedure Methods 0.000 description 2
- 238000013519 translation Methods 0.000 description 2
- 238000001262 western blot Methods 0.000 description 2
- KPYXMALABCDPGN-HYOZMBHHSA-N (4s)-5-[[(2s)-6-amino-1-[[(2s,3s)-1-[[(2s)-1-[[(2s)-1-[[(2s)-1-[[(2s)-1-[[(2r)-1-[[2-[[2-[[(1s)-3-amino-1-carboxy-3-oxopropyl]amino]-2-oxoethyl]amino]-2-oxoethyl]amino]-1-oxo-3-sulfanylpropan-2-yl]amino]-4-methyl-1-oxopentan-2-yl]amino]-1-oxopropan-2-yl]a Chemical compound NC(=O)C[C@@H](C(O)=O)NC(=O)CNC(=O)CNC(=O)[C@H](CS)NC(=O)[C@H](CC(C)C)NC(=O)[C@H](C)NC(=O)[C@H](C(C)C)NC(=O)[C@H](CC(C)C)NC(=O)[C@H]([C@@H](C)CC)NC(=O)[C@H](CCCCN)NC(=O)[C@H](CCC(O)=O)NC(=O)[C@@H](NC(=O)[C@H](CC(O)=O)NC(=O)CNC(=O)[C@@H](N)CCCCN)CC1=CC=C(O)C=C1 KPYXMALABCDPGN-HYOZMBHHSA-N 0.000 description 1
- 102000040650 (ribonucleotides)n+m Human genes 0.000 description 1
- IVLXQGJVBGMLRR-UHFFFAOYSA-N 2-aminoacetic acid;hydron;chloride Chemical compound Cl.NCC(O)=O IVLXQGJVBGMLRR-UHFFFAOYSA-N 0.000 description 1
- VOUAQYXWVJDEQY-QENPJCQMSA-N 33017-11-7 Chemical compound OC(=O)CC[C@H](N)C(=O)N[C@@H](C)C(=O)N[C@@H](CCC(O)=O)C(=O)N[C@@H](CC(O)=O)C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](CCC(N)=O)C(=O)N[C@@H](C(C)C)C(=O)NCC(=O)N[C@@H](CCC(N)=O)C(=O)N[C@@H](C(C)C)C(=O)N[C@@H](CCC(O)=O)C(=O)N[C@@H](CC(C)C)C(=O)NCC(=O)NCC(=O)NCC(=O)N1CCC[C@H]1C(=O)NCC(=O)N[C@@H](C)C(=O)NCC(=O)N[C@@H](CO)C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](CCC(N)=O)C(=O)N1[C@H](C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](C)C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](CCC(O)=O)C(=O)NCC(=O)N[C@@H](CO)C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](CCC(N)=O)C(O)=O)CCC1 VOUAQYXWVJDEQY-QENPJCQMSA-N 0.000 description 1
- QFVHZQCOUORWEI-UHFFFAOYSA-N 4-[(4-anilino-5-sulfonaphthalen-1-yl)diazenyl]-5-hydroxynaphthalene-2,7-disulfonic acid Chemical compound C=12C(O)=CC(S(O)(=O)=O)=CC2=CC(S(O)(=O)=O)=CC=1N=NC(C1=CC=CC(=C11)S(O)(=O)=O)=CC=C1NC1=CC=CC=C1 QFVHZQCOUORWEI-UHFFFAOYSA-N 0.000 description 1
- QCVGEOXPDFCNHA-UHFFFAOYSA-N 5,5-dimethyl-2,4-dioxo-1,3-oxazolidine-3-carboxamide Chemical compound CC1(C)OC(=O)N(C(N)=O)C1=O QCVGEOXPDFCNHA-UHFFFAOYSA-N 0.000 description 1
- 208000030507 AIDS Diseases 0.000 description 1
- 101710197241 Accessory gland-specific peptide 70A Proteins 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
- 108010088751 Albumins Proteins 0.000 description 1
- QGZKDVFQNNGYKY-UHFFFAOYSA-O Ammonium Chemical compound [NH4+] QGZKDVFQNNGYKY-UHFFFAOYSA-O 0.000 description 1
- 102100022717 Atypical chemokine receptor 1 Human genes 0.000 description 1
- 238000000122 Auger electron partial yield spectroscopy Methods 0.000 description 1
- 241000201370 Autographa californica nucleopolyhedrovirus Species 0.000 description 1
- 238000012935 Averaging Methods 0.000 description 1
- 108090001008 Avidin Proteins 0.000 description 1
- 241000193830 Bacillus <bacterium> Species 0.000 description 1
- 241000894006 Bacteria Species 0.000 description 1
- DWRXFEITVBNRMK-UHFFFAOYSA-N Beta-D-1-Arabinofuranosylthymine Natural products O=C1NC(=O)C(C)=CN1C1C(O)C(O)C(CO)O1 DWRXFEITVBNRMK-UHFFFAOYSA-N 0.000 description 1
- 101000583086 Bunodosoma granuliferum Delta-actitoxin-Bgr2b Proteins 0.000 description 1
- 101710117545 C protein Proteins 0.000 description 1
- 108010075254 C-Peptide Proteins 0.000 description 1
- 125000001433 C-terminal amino-acid group Chemical group 0.000 description 1
- LOYTUFQOTJYLPX-UHFFFAOYSA-N C1=CC=[Si]C=C1 Chemical compound C1=CC=[Si]C=C1 LOYTUFQOTJYLPX-UHFFFAOYSA-N 0.000 description 1
- 102100022002 CD59 glycoprotein Human genes 0.000 description 1
- 241000282472 Canis lupus familiaris Species 0.000 description 1
- BVKZGUZCCUSVTD-UHFFFAOYSA-L Carbonate Chemical compound [O-]C([O-])=O BVKZGUZCCUSVTD-UHFFFAOYSA-L 0.000 description 1
- 229920000742 Cotton Polymers 0.000 description 1
- 238000007399 DNA isolation Methods 0.000 description 1
- 230000006820 DNA synthesis Effects 0.000 description 1
- 102000004163 DNA-directed RNA polymerases Human genes 0.000 description 1
- 108090000626 DNA-directed RNA polymerases Proteins 0.000 description 1
- 102100023933 Deoxyuridine 5'-triphosphate nucleotidohydrolase, mitochondrial Human genes 0.000 description 1
- 101100364969 Dictyostelium discoideum scai gene Proteins 0.000 description 1
- 108010000912 Egg Proteins Proteins 0.000 description 1
- 102000002322 Egg Proteins Human genes 0.000 description 1
- 108700024394 Exon Proteins 0.000 description 1
- 206010015719 Exsanguination Diseases 0.000 description 1
- 241000282326 Felis catus Species 0.000 description 1
- 229920001917 Ficoll Polymers 0.000 description 1
- 241000287828 Gallus gallus Species 0.000 description 1
- 101000609762 Gallus gallus Ovalbumin Proteins 0.000 description 1
- 206010060891 General symptom Diseases 0.000 description 1
- 108010048896 HLA-D Antigens Proteins 0.000 description 1
- 102000009485 HLA-D Antigens Human genes 0.000 description 1
- 101710154606 Hemagglutinin Proteins 0.000 description 1
- 101000678879 Homo sapiens Atypical chemokine receptor 1 Proteins 0.000 description 1
- 101000897400 Homo sapiens CD59 glycoprotein Proteins 0.000 description 1
- 101000982010 Homo sapiens Myelin proteolipid protein Proteins 0.000 description 1
- 102000009786 Immunoglobulin Constant Regions Human genes 0.000 description 1
- 108010009817 Immunoglobulin Constant Regions Proteins 0.000 description 1
- 102000004877 Insulin Human genes 0.000 description 1
- 108090001061 Insulin Proteins 0.000 description 1
- 102000008070 Interferon-gamma Human genes 0.000 description 1
- 108010074328 Interferon-gamma Proteins 0.000 description 1
- 102100024319 Intestinal-type alkaline phosphatase Human genes 0.000 description 1
- 101710184243 Intestinal-type alkaline phosphatase Proteins 0.000 description 1
- 238000012218 Kunkel's method Methods 0.000 description 1
- 229930190887 Leptomycin Natural products 0.000 description 1
- 206010025323 Lymphomas Diseases 0.000 description 1
- 108700005092 MHC Class II Genes Proteins 0.000 description 1
- 108010066345 MHC binding peptide Proteins 0.000 description 1
- 101001129124 Mannheimia haemolytica Outer membrane lipoprotein 1 Proteins 0.000 description 1
- 101710110798 Mannose-binding protein C Proteins 0.000 description 1
- 101150076359 Mhc gene Proteins 0.000 description 1
- 102000016943 Muramidase Human genes 0.000 description 1
- 108010014251 Muramidase Proteins 0.000 description 1
- 101100364971 Mus musculus Scai gene Proteins 0.000 description 1
- 241001049988 Mycobacterium tuberculosis H37Ra Species 0.000 description 1
- 102100026784 Myelin proteolipid protein Human genes 0.000 description 1
- 101710204040 Myosin-3 Proteins 0.000 description 1
- 108010062010 N-Acetylmuramoyl-L-alanine Amidase Proteins 0.000 description 1
- 229930193140 Neomycin Natural products 0.000 description 1
- 108010047956 Nucleosomes Proteins 0.000 description 1
- 101000761187 Odontomachus monticola U-poneritoxin(01)-Om1a Proteins 0.000 description 1
- 101100028075 Oryza sativa subsp. japonica OPR13 gene Proteins 0.000 description 1
- 101100295825 Oryza sativa subsp. japonica OPR7 gene Proteins 0.000 description 1
- 101710093908 Outer capsid protein VP4 Proteins 0.000 description 1
- 101710135467 Outer capsid protein sigma-1 Proteins 0.000 description 1
- 238000012220 PCR site-directed mutagenesis Methods 0.000 description 1
- 241000282376 Panthera tigris Species 0.000 description 1
- 108090000526 Papain Proteins 0.000 description 1
- 241001483952 Peach chlorotic mottle virus Species 0.000 description 1
- 241001494479 Pecora Species 0.000 description 1
- 108091005804 Peptidases Proteins 0.000 description 1
- 102000035195 Peptidases Human genes 0.000 description 1
- 102000003992 Peroxidases Human genes 0.000 description 1
- 108010081690 Pertussis Toxin Proteins 0.000 description 1
- 206010057249 Phagocytosis Diseases 0.000 description 1
- 102000004160 Phosphoric Monoester Hydrolases Human genes 0.000 description 1
- 108090000608 Phosphoric Monoester Hydrolases Proteins 0.000 description 1
- 208000007452 Plasmacytoma Diseases 0.000 description 1
- 101710176177 Protein A56 Proteins 0.000 description 1
- 101000702488 Rattus norvegicus High affinity cationic amino acid transporter 1 Proteins 0.000 description 1
- 239000006146 Roswell Park Memorial Institute medium Substances 0.000 description 1
- 101100041820 Saccharomyces cerevisiae (strain ATCC 204508 / S288c) SCEI gene Proteins 0.000 description 1
- 241000269821 Scombridae Species 0.000 description 1
- 206010070834 Sensitisation Diseases 0.000 description 1
- 229920005654 Sephadex Polymers 0.000 description 1
- 239000012507 Sephadex™ Substances 0.000 description 1
- YMTLKLXDFCSCNX-BYPYZUCNSA-N Ser-Gly-Gly Chemical compound OC[C@H](N)C(=O)NCC(=O)NCC(O)=O YMTLKLXDFCSCNX-BYPYZUCNSA-N 0.000 description 1
- 108020004682 Single-Stranded DNA Proteins 0.000 description 1
- 241000187747 Streptomyces Species 0.000 description 1
- 101710120037 Toxin CcdB Proteins 0.000 description 1
- 229910052770 Uranium Inorganic materials 0.000 description 1
- 108010006886 Vitrogen Proteins 0.000 description 1
- 208000027418 Wounds and injury Diseases 0.000 description 1
- 108010027570 Xanthine phosphoribosyltransferase Proteins 0.000 description 1
- 230000002159 abnormal effect Effects 0.000 description 1
- 230000001154 acute effect Effects 0.000 description 1
- 230000032683 aging Effects 0.000 description 1
- 108010090535 alpha-albumin Proteins 0.000 description 1
- 229910000147 aluminium phosphate Inorganic materials 0.000 description 1
- 125000000539 amino acid group Chemical group 0.000 description 1
- 239000001166 ammonium sulphate Substances 0.000 description 1
- 239000003708 ampul Substances 0.000 description 1
- 210000004102 animal cell Anatomy 0.000 description 1
- 229940121363 anti-inflammatory agent Drugs 0.000 description 1
- 239000002260 anti-inflammatory agent Substances 0.000 description 1
- 229940124599 anti-inflammatory drug Drugs 0.000 description 1
- 230000005875 antibody response Effects 0.000 description 1
- 239000003963 antioxidant agent Substances 0.000 description 1
- 239000007900 aqueous suspension Substances 0.000 description 1
- 239000012911 assay medium Substances 0.000 description 1
- 210000001099 axilla Anatomy 0.000 description 1
- IQFYYKKMVGJFEH-UHFFFAOYSA-N beta-L-thymidine Natural products O=C1NC(=O)C(C)=CN1C1OC(CO)C(O)C1 IQFYYKKMVGJFEH-UHFFFAOYSA-N 0.000 description 1
- 239000011230 binding agent Substances 0.000 description 1
- 239000012148 binding buffer Substances 0.000 description 1
- 230000005540 biological transmission Effects 0.000 description 1
- 230000015572 biosynthetic process Effects 0.000 description 1
- 230000017531 blood circulation Effects 0.000 description 1
- 230000037396 body weight Effects 0.000 description 1
- 238000009395 breeding Methods 0.000 description 1
- 230000001488 breeding effect Effects 0.000 description 1
- 239000007853 buffer solution Substances 0.000 description 1
- 244000309466 calf Species 0.000 description 1
- CJFCGSLFEZPBNJ-UHFFFAOYSA-N carbamimidoylazanium;phosphate Chemical compound NC([NH3+])=N.NC([NH3+])=N.NC([NH3+])=N.[O-]P([O-])([O-])=O CJFCGSLFEZPBNJ-UHFFFAOYSA-N 0.000 description 1
- 150000001720 carbohydrates Chemical class 0.000 description 1
- BVKZGUZCCUSVTD-UHFFFAOYSA-N carbonic acid Chemical compound OC(O)=O BVKZGUZCCUSVTD-UHFFFAOYSA-N 0.000 description 1
- 239000000969 carrier Substances 0.000 description 1
- 239000012876 carrier material Substances 0.000 description 1
- 230000003915 cell function Effects 0.000 description 1
- 230000001413 cellular effect Effects 0.000 description 1
- 238000012512 characterization method Methods 0.000 description 1
- 239000013522 chelant Substances 0.000 description 1
- 239000003153 chemical reaction reagent Substances 0.000 description 1
- 229940096384 chicken egg white lysozyme Drugs 0.000 description 1
- YTRQFSDWAXHJCC-UHFFFAOYSA-N chloroform;phenol Chemical compound ClC(Cl)Cl.OC1=CC=CC=C1 YTRQFSDWAXHJCC-UHFFFAOYSA-N 0.000 description 1
- 239000013611 chromosomal DNA Substances 0.000 description 1
- 239000007979 citrate buffer Substances 0.000 description 1
- 210000000078 claw Anatomy 0.000 description 1
- 238000004140 cleaning Methods 0.000 description 1
- 230000001010 compromised effect Effects 0.000 description 1
- 238000005094 computer simulation Methods 0.000 description 1
- 238000009833 condensation Methods 0.000 description 1
- 230000005494 condensation Effects 0.000 description 1
- 239000000356 contaminant Substances 0.000 description 1
- 238000012937 correction Methods 0.000 description 1
- 239000003246 corticosteroid Substances 0.000 description 1
- 229960001334 corticosteroids Drugs 0.000 description 1
- 230000009260 cross reactivity Effects 0.000 description 1
- 238000005520 cutting process Methods 0.000 description 1
- 210000000805 cytoplasm Anatomy 0.000 description 1
- 210000005220 cytoplasmic tail Anatomy 0.000 description 1
- 231100000433 cytotoxic Toxicity 0.000 description 1
- 230000001472 cytotoxic effect Effects 0.000 description 1
- 108010011219 dUTP pyrophosphatase Proteins 0.000 description 1
- 230000007547 defect Effects 0.000 description 1
- 230000002950 deficient Effects 0.000 description 1
- 230000000249 desinfective effect Effects 0.000 description 1
- 206010012601 diabetes mellitus Diseases 0.000 description 1
- 238000003745 diagnosis Methods 0.000 description 1
- 239000000539 dimer Substances 0.000 description 1
- 238000009826 distribution Methods 0.000 description 1
- 230000002500 effect on skin Effects 0.000 description 1
- 210000000969 egg white Anatomy 0.000 description 1
- 235000014103 egg white Nutrition 0.000 description 1
- 230000003511 endothelial effect Effects 0.000 description 1
- 230000002255 enzymatic effect Effects 0.000 description 1
- 239000006167 equilibration buffer Substances 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
- 238000011156 evaluation Methods 0.000 description 1
- 230000029142 excretion Effects 0.000 description 1
- 238000013213 extrapolation Methods 0.000 description 1
- 210000003414 extremity Anatomy 0.000 description 1
- 239000003889 eye drop Substances 0.000 description 1
- 229940012356 eye drops Drugs 0.000 description 1
- 239000012894 fetal calf serum Substances 0.000 description 1
- 238000001914 filtration Methods 0.000 description 1
- 238000010304 firing Methods 0.000 description 1
- 238000004108 freeze drying Methods 0.000 description 1
- 239000012737 fresh medium Substances 0.000 description 1
- 125000000524 functional group Chemical group 0.000 description 1
- 239000000417 fungicide Substances 0.000 description 1
- 150000002240 furans Chemical class 0.000 description 1
- 229930195712 glutamate Natural products 0.000 description 1
- 210000002288 golgi apparatus Anatomy 0.000 description 1
- HNDVDQJCIGZPNO-UHFFFAOYSA-N histidine Natural products OC(=O)C(N)CC1=CN=CN1 HNDVDQJCIGZPNO-UHFFFAOYSA-N 0.000 description 1
- 238000000265 homogenisation Methods 0.000 description 1
- 238000009396 hybridization Methods 0.000 description 1
- 238000003384 imaging method Methods 0.000 description 1
- 210000002865 immune cell Anatomy 0.000 description 1
- 230000001900 immune effect Effects 0.000 description 1
- 238000003119 immunoblot Methods 0.000 description 1
- 230000005847 immunogenicity Effects 0.000 description 1
- 238000003364 immunohistochemistry Methods 0.000 description 1
- 239000003018 immunosuppressive agent Substances 0.000 description 1
- 229940124589 immunosuppressive drug Drugs 0.000 description 1
- 230000006872 improvement Effects 0.000 description 1
- 238000007901 in situ hybridization Methods 0.000 description 1
- 230000000415 inactivating effect Effects 0.000 description 1
- 239000000411 inducer Substances 0.000 description 1
- 239000012678 infectious agent Substances 0.000 description 1
- 239000004615 ingredient Substances 0.000 description 1
- 239000003112 inhibitor Substances 0.000 description 1
- 230000000977 initiatory effect Effects 0.000 description 1
- 208000014674 injury Diseases 0.000 description 1
- 239000012194 insect media Substances 0.000 description 1
- 238000007689 inspection Methods 0.000 description 1
- 229940125396 insulin Drugs 0.000 description 1
- 230000010354 integration Effects 0.000 description 1
- 230000002452 interceptive effect Effects 0.000 description 1
- 229960003130 interferon gamma Drugs 0.000 description 1
- 230000017307 interleukin-4 production Effects 0.000 description 1
- 210000004020 intracellular membrane Anatomy 0.000 description 1
- 238000001990 intravenous administration Methods 0.000 description 1
- 125000001449 isopropyl group Chemical group [H]C([H])([H])C([H])(*)C([H])([H])[H] 0.000 description 1
- 210000003734 kidney Anatomy 0.000 description 1
- 210000003127 knee Anatomy 0.000 description 1
- YACHGFWEQXFSBS-RJXCBBHPSA-N leptomycin Chemical compound OC(=O)/C=C(C)/C[C@H](C)[C@@H](O)[C@H](C)C(=O)[C@H](C)/C=C(\C)/C=C/C[C@@H](C)\C=C(/CC)\C=C\[C@@H]1OC(=O)C=C[C@@H]1C YACHGFWEQXFSBS-RJXCBBHPSA-N 0.000 description 1
- 239000002502 liposome Substances 0.000 description 1
- 244000144972 livestock Species 0.000 description 1
- 210000003141 lower extremity Anatomy 0.000 description 1
- 210000002751 lymph Anatomy 0.000 description 1
- 210000004698 lymphocyte Anatomy 0.000 description 1
- 230000002132 lysosomal effect Effects 0.000 description 1
- 229960000274 lysozyme Drugs 0.000 description 1
- 239000004325 lysozyme Substances 0.000 description 1
- 235000010335 lysozyme Nutrition 0.000 description 1
- 235000020640 mackerel Nutrition 0.000 description 1
- ADKOXSOCTOWDOP-UHFFFAOYSA-L magnesium;aluminum;dihydroxide;trihydrate Chemical group O.O.O.[OH-].[OH-].[Mg+2].[Al] ADKOXSOCTOWDOP-UHFFFAOYSA-L 0.000 description 1
- 201000004792 malaria Diseases 0.000 description 1
- 210000001161 mammalian embryo Anatomy 0.000 description 1
- 238000013507 mapping Methods 0.000 description 1
- 239000003550 marker Substances 0.000 description 1
- 239000000463 material Substances 0.000 description 1
- MIKKOBKEXMRYFQ-WZTVWXICSA-N meglumine amidotrizoate Chemical compound C[NH2+]C[C@H](O)[C@@H](O)[C@H](O)[C@H](O)CO.CC(=O)NC1=C(I)C(NC(C)=O)=C(I)C(C([O-])=O)=C1I MIKKOBKEXMRYFQ-WZTVWXICSA-N 0.000 description 1
- 201000001441 melanoma Diseases 0.000 description 1
- 210000003071 memory t lymphocyte Anatomy 0.000 description 1
- 108020004999 messenger RNA Proteins 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
- 235000013336 milk Nutrition 0.000 description 1
- 239000008267 milk Substances 0.000 description 1
- 210000004080 milk Anatomy 0.000 description 1
- 238000010369 molecular cloning Methods 0.000 description 1
- 230000004899 motility Effects 0.000 description 1
- 210000003098 myoblast Anatomy 0.000 description 1
- VMGAPWLDMVPYIA-HIDZBRGKSA-N n'-amino-n-iminomethanimidamide Chemical compound N\N=C\N=N VMGAPWLDMVPYIA-HIDZBRGKSA-N 0.000 description 1
- 229960004927 neomycin Drugs 0.000 description 1
- 238000007857 nested PCR Methods 0.000 description 1
- 230000001537 neural effect Effects 0.000 description 1
- 239000012457 nonaqueous media Substances 0.000 description 1
- 125000003835 nucleoside group Chemical group 0.000 description 1
- 210000001623 nucleosome Anatomy 0.000 description 1
- 235000015097 nutrients Nutrition 0.000 description 1
- 238000002515 oligonucleotide synthesis Methods 0.000 description 1
- 210000000287 oocyte Anatomy 0.000 description 1
- GSSMIHQEWAQUPM-AOLPDKKJSA-N ovalbumin peptide Chemical compound C([C@H](NC(=O)[C@H](C(C)C)NC(=O)[C@H](C)NC(=O)[C@H](CCC(N)=O)NC(=O)[C@H](CO)NC(=O)[C@@H](N)[C@@H](C)CC)C(=O)N[C@@H](C)C(=O)N[C@@H](C)C(=O)N[C@@H](CC=1NC=NC=1)C(=O)N[C@@H](C)C(=O)N[C@@H](CCC(O)=O)C(=O)N[C@@H]([C@@H](C)CC)C(=O)N[C@@H](CC(N)=O)C(=O)N[C@@H](CCC(O)=O)C(=O)N[C@@H](C)C(=O)NCC(=O)N[C@@H](CCCNC(N)=N)C(O)=O)C1=CN=CN1 GSSMIHQEWAQUPM-AOLPDKKJSA-N 0.000 description 1
- 229940055729 papain Drugs 0.000 description 1
- 235000019834 papain Nutrition 0.000 description 1
- 238000007911 parenteral administration Methods 0.000 description 1
- 239000002245 particle Substances 0.000 description 1
- 230000008506 pathogenesis Effects 0.000 description 1
- 108010011903 peptide receptors Proteins 0.000 description 1
- 108040007629 peroxidase activity proteins Proteins 0.000 description 1
- 230000008782 phagocytosis Effects 0.000 description 1
- 239000008363 phosphate buffer Substances 0.000 description 1
- NBIIXXVUZAFLBC-UHFFFAOYSA-N phosphoric acid Substances OP(O)(O)=O NBIIXXVUZAFLBC-UHFFFAOYSA-N 0.000 description 1
- 230000008288 physiological mechanism Effects 0.000 description 1
- 230000003169 placental effect Effects 0.000 description 1
- 238000007747 plating Methods 0.000 description 1
- 229920002401 polyacrylamide Polymers 0.000 description 1
- 230000004492 positive regulation of T cell proliferation Effects 0.000 description 1
- 238000002731 protein assay Methods 0.000 description 1
- 238000001742 protein purification Methods 0.000 description 1
- 230000002797 proteolythic effect Effects 0.000 description 1
- 230000002685 pulmonary effect Effects 0.000 description 1
- 239000012521 purified sample Substances 0.000 description 1
- 239000002510 pyrogen Substances 0.000 description 1
- 230000005855 radiation Effects 0.000 description 1
- 238000000163 radioactive labelling Methods 0.000 description 1
- 101150079601 recA gene Proteins 0.000 description 1
- 230000010837 receptor-mediated endocytosis Effects 0.000 description 1
- 230000009467 reduction Effects 0.000 description 1
- 230000011514 reflex Effects 0.000 description 1
- 230000019908 regulation of T cell activation Effects 0.000 description 1
- BOLDJAUMGUJJKM-LSDHHAIUSA-N renifolin D Natural products CC(=C)[C@@H]1Cc2c(O)c(O)ccc2[C@H]1CC(=O)c3ccc(O)cc3O BOLDJAUMGUJJKM-LSDHHAIUSA-N 0.000 description 1
- 230000003362 replicative effect Effects 0.000 description 1
- 230000029058 respiratory gaseous exchange Effects 0.000 description 1
- 238000003757 reverse transcription PCR Methods 0.000 description 1
- 210000003935 rough endoplasmic reticulum Anatomy 0.000 description 1
- 229940016590 sarkosyl Drugs 0.000 description 1
- 108700004121 sarkosyl Proteins 0.000 description 1
- 229920006395 saturated elastomer Polymers 0.000 description 1
- 230000035945 sensitivity Effects 0.000 description 1
- 230000008313 sensitization Effects 0.000 description 1
- 230000001235 sensitizing effect Effects 0.000 description 1
- KSAVQLQVUXSOCR-UHFFFAOYSA-M sodium lauroyl sarcosinate Chemical compound [Na+].CCCCCCCCCCCC(=O)N(C)CC([O-])=O KSAVQLQVUXSOCR-UHFFFAOYSA-M 0.000 description 1
- CIJQGPVMMRXSQW-UHFFFAOYSA-M sodium;2-aminoacetic acid;hydroxide Chemical compound O.[Na+].NCC([O-])=O CIJQGPVMMRXSQW-UHFFFAOYSA-M 0.000 description 1
- YEENEYXBHNNNGV-XEHWZWQGSA-M sodium;3-acetamido-5-[acetyl(methyl)amino]-2,4,6-triiodobenzoate;(2r,3r,4s,5s,6r)-2-[(2r,3s,4s,5r)-3,4-dihydroxy-2,5-bis(hydroxymethyl)oxolan-2-yl]oxy-6-(hydroxymethyl)oxane-3,4,5-triol Chemical compound [Na+].CC(=O)N(C)C1=C(I)C(NC(C)=O)=C(I)C(C([O-])=O)=C1I.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 YEENEYXBHNNNGV-XEHWZWQGSA-M 0.000 description 1
- 239000008279 sol Substances 0.000 description 1
- 239000008174 sterile solution Substances 0.000 description 1
- 238000007920 subcutaneous administration Methods 0.000 description 1
- 238000010254 subcutaneous injection Methods 0.000 description 1
- 239000007929 subcutaneous injection Substances 0.000 description 1
- 239000000126 substance Substances 0.000 description 1
- 239000004094 surface-active agent Substances 0.000 description 1
- 239000000375 suspending agent Substances 0.000 description 1
- 238000010189 synthetic method Methods 0.000 description 1
- 239000002562 thickening agent Substances 0.000 description 1
- 210000003371 toe Anatomy 0.000 description 1
- 238000011200 topical administration Methods 0.000 description 1
- 238000000844 transformation Methods 0.000 description 1
- 230000032258 transport Effects 0.000 description 1
- 230000001960 triggered effect Effects 0.000 description 1
- 208000035408 type 1 diabetes mellitus 1 Diseases 0.000 description 1
- 108010087967 type I signal peptidase Proteins 0.000 description 1
- 238000000108 ultra-filtration Methods 0.000 description 1
- 229940035893 uracil Drugs 0.000 description 1
- 230000002792 vascular Effects 0.000 description 1
- 210000003462 vein Anatomy 0.000 description 1
- 230000003612 virological effect Effects 0.000 description 1
- 239000002699 waste material Substances 0.000 description 1
- 239000008215 water for injection Substances 0.000 description 1
- 230000003442 weekly effect Effects 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
- C07K14/70503—Immunoglobulin superfamily
- C07K14/70539—MHC-molecules, e.g. HLA-molecules
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61K—PREPARATIONS FOR MEDICAL, DENTAL OR TOILETRY PURPOSES
- A61K40/00—Cellular immunotherapy
- A61K40/10—Cellular immunotherapy characterised by the cell type used
- A61K40/11—T-cells, e.g. tumour infiltrating lymphocytes [TIL] or regulatory T [Treg] cells; Lymphokine-activated killer [LAK] cells
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61K—PREPARATIONS FOR MEDICAL, DENTAL OR TOILETRY PURPOSES
- A61K40/00—Cellular immunotherapy
- A61K40/10—Cellular immunotherapy characterised by the cell type used
- A61K40/13—B-cells
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61K—PREPARATIONS FOR MEDICAL, DENTAL OR TOILETRY PURPOSES
- A61K40/00—Cellular immunotherapy
- A61K40/20—Cellular immunotherapy characterised by the effect or the function of the cells
- A61K40/24—Antigen-presenting cells [APC]
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61K—PREPARATIONS FOR MEDICAL, DENTAL OR TOILETRY PURPOSES
- A61K40/00—Cellular immunotherapy
- A61K40/40—Cellular immunotherapy characterised by antigens that are targeted or presented by cells of the immune system
- A61K40/41—Vertebrate antigens
- A61K40/42—Cancer antigens
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P21/00—Drugs for disorders of the muscular or neuromuscular system
- A61P21/04—Drugs for disorders of the muscular or neuromuscular system for myasthenia gravis
-
- 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
- A61P25/28—Drugs for disorders of the nervous system for treating neurodegenerative disorders of the central nervous system, e.g. nootropic agents, cognition enhancers, drugs for treating Alzheimer's disease or other forms of dementia
-
- 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
- A61P3/08—Drugs for disorders of the metabolism for glucose homeostasis
- A61P3/10—Drugs for disorders of the metabolism for glucose homeostasis for hyperglycaemia, e.g. antidiabetics
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P37/00—Drugs for immunological or allergic disorders
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P37/00—Drugs for immunological or allergic disorders
- A61P37/02—Immunomodulators
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P37/00—Drugs for immunological or allergic disorders
- A61P37/02—Immunomodulators
- A61P37/06—Immunosuppressants, e.g. drugs for graft rejection
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P37/00—Drugs for immunological or allergic disorders
- A61P37/08—Antiallergic agents
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P43/00—Drugs for specific purposes, not provided for in groups A61P1/00-A61P41/00
-
- A—HUMAN NECESSITIES
- A01—AGRICULTURE; FORESTRY; ANIMAL HUSBANDRY; HUNTING; TRAPPING; FISHING
- A01K—ANIMAL HUSBANDRY; AVICULTURE; APICULTURE; PISCICULTURE; FISHING; REARING OR BREEDING ANIMALS, NOT OTHERWISE PROVIDED FOR; NEW BREEDS OF ANIMALS
- A01K2217/00—Genetically modified animals
- A01K2217/05—Animals comprising random inserted nucleic acids (transgenic)
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61K—PREPARATIONS FOR MEDICAL, DENTAL OR TOILETRY PURPOSES
- A61K39/00—Medicinal preparations containing antigens or antibodies
- A61K2039/51—Medicinal preparations containing antigens or antibodies comprising whole cells, viruses or DNA/RNA
- A61K2039/53—DNA (RNA) vaccination
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61K—PREPARATIONS FOR MEDICAL, DENTAL OR TOILETRY PURPOSES
- A61K39/00—Medicinal preparations containing antigens or antibodies
- A61K2039/60—Medicinal preparations containing antigens or antibodies characteristics by the carrier linked to the antigen
- A61K2039/6031—Proteins
- A61K2039/6043—Heat shock proteins
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61K—PREPARATIONS FOR MEDICAL, DENTAL OR TOILETRY PURPOSES
- A61K39/00—Medicinal preparations containing antigens or antibodies
- A61K2039/62—Medicinal preparations containing antigens or antibodies characterised by the link between antigen and carrier
- A61K2039/622—Medicinal preparations containing antigens or antibodies characterised by the link between antigen and carrier non-covalent binding
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61K—PREPARATIONS FOR MEDICAL, DENTAL OR TOILETRY PURPOSES
- A61K38/00—Medicinal preparations containing peptides
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61K—PREPARATIONS FOR MEDICAL, DENTAL OR TOILETRY PURPOSES
- A61K39/00—Medicinal preparations containing antigens or antibodies
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61K—PREPARATIONS FOR MEDICAL, DENTAL OR TOILETRY PURPOSES
- A61K48/00—Medicinal preparations containing genetic material which is inserted into cells of the living body to treat genetic diseases; Gene therapy
-
- 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
Landscapes
- Health & Medical Sciences (AREA)
- Life Sciences & Earth Sciences (AREA)
- General Health & Medical Sciences (AREA)
- Public Health (AREA)
- Veterinary Medicine (AREA)
- Animal Behavior & Ethology (AREA)
- Chemical & Material Sciences (AREA)
- Organic Chemistry (AREA)
- Medicinal Chemistry (AREA)
- Immunology (AREA)
- Engineering & Computer Science (AREA)
- Bioinformatics & Cheminformatics (AREA)
- General Chemical & Material Sciences (AREA)
- Nuclear Medicine, Radiotherapy & Molecular Imaging (AREA)
- Chemical Kinetics & Catalysis (AREA)
- Pharmacology & Pharmacy (AREA)
- Epidemiology (AREA)
- Neurology (AREA)
- Diabetes (AREA)
- Genetics & Genomics (AREA)
- Cell Biology (AREA)
- Proteomics, Peptides & Aminoacids (AREA)
- Molecular Biology (AREA)
- Biophysics (AREA)
- Biochemistry (AREA)
- Biomedical Technology (AREA)
- Gastroenterology & Hepatology (AREA)
- Zoology (AREA)
- Neurosurgery (AREA)
- Toxicology (AREA)
- Hematology (AREA)
- Orthopedic Medicine & Surgery (AREA)
- Obesity (AREA)
- Hospice & Palliative Care (AREA)
- Rheumatology (AREA)
- Pain & Pain Management (AREA)
- Endocrinology (AREA)
- Pulmonology (AREA)
- Transplantation (AREA)
- Psychiatry (AREA)
Applications Claiming Priority (3)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| US08/596,387 US5869270A (en) | 1996-01-31 | 1996-01-31 | Single chain MHC complexes and uses thereof |
| US08/596,387 | 1996-01-31 | ||
| PCT/US1997/001617 WO1997028191A1 (en) | 1996-01-31 | 1997-01-30 | Mhc complexes and uses thereof |
Publications (2)
| Publication Number | Publication Date |
|---|---|
| JP2000515363A true JP2000515363A (ja) | 2000-11-21 |
| JP2000515363A5 JP2000515363A5 (cg-RX-API-DMAC7.html) | 2004-11-11 |
Family
ID=24387103
Family Applications (1)
| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| JP09527863A Pending JP2000515363A (ja) | 1996-01-31 | 1997-01-30 | Ｍｈｃ複合体及びその用途 |
Country Status (9)
| Country | Link |
|---|---|
| US (3) | US5869270A (cg-RX-API-DMAC7.html) |
| EP (2) | EP1526141A3 (cg-RX-API-DMAC7.html) |
| JP (1) | JP2000515363A (cg-RX-API-DMAC7.html) |
| AT (1) | ATE276275T1 (cg-RX-API-DMAC7.html) |
| AU (1) | AU729672B2 (cg-RX-API-DMAC7.html) |
| CA (1) | CA2244755A1 (cg-RX-API-DMAC7.html) |
| DE (1) | DE69730693T2 (cg-RX-API-DMAC7.html) |
| DK (1) | DK0877760T3 (cg-RX-API-DMAC7.html) |
| WO (1) | WO1997028191A1 (cg-RX-API-DMAC7.html) |
Cited By (11)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| JP2003519240A (ja) * | 2000-01-03 | 2003-06-17 | ティーアール アソシエイツ，エル．エル．シー． | タンパク質を移送する方法 |
| JP2011182702A (ja) * | 2010-03-08 | 2011-09-22 | Tokyo Univ Of Agriculture & Technology | 融合ｍｈｃ分子連結磁気微粒子、抗原ペプチドのスクリーニング方法、組換えベクター、及び磁性細菌の形質転換体 |
| JP2015514421A (ja) * | 2012-04-17 | 2015-05-21 | ザ ユニバーシティ オブ ワシントン スルー イッツ センター フォーコマーシャライゼーションＴｈｅ Ｕｎｉｖｅｒｓｉｔｙ Ｏｆ Ｗａｓｈｉｎｇｔｏｎ Ｔｈｒｏｕｇｈ Ｉｔｓ Ｃｅｎｔｅｒ Ｆｏｒ Ｃｏｍｍｅｒｃｉａｌｉｚａｔｉｏｎ | Ｈｌａクラスｉｉタンパク質の発現能を有するｈｌａクラスｉｉ欠損細胞、ｈｌａクラスｉ欠損細胞、及びその使用 |
| JP2017519491A (ja) * | 2014-06-18 | 2017-07-20 | アルバート アインシュタイン カレッジ オブ メディシン，インコーポレイティド | ｓｙｎＴａｃポリペプチド及びその使用 |
| US10927161B2 (en) | 2017-03-15 | 2021-02-23 | Cue Biopharma, Inc. | Methods for modulating an immune response |
| US10927158B2 (en) | 2016-12-22 | 2021-02-23 | Cue Biopharma, Inc. | T-cell modulatory multimeric polypeptides and methods of use thereof |
| US11226339B2 (en) | 2012-12-11 | 2022-01-18 | Albert Einstein College Of Medicine | Methods for high throughput receptor:ligand identification |
| US11339201B2 (en) | 2016-05-18 | 2022-05-24 | Albert Einstein College Of Medicine | Variant PD-L1 polypeptides, T-cell modulatory multimeric polypeptides, and methods of use thereof |
| US11505591B2 (en) | 2016-05-18 | 2022-11-22 | Cue Biopharma, Inc. | T-cell modulatory multimeric polypeptides and methods of use thereof |
| US11702461B2 (en) | 2018-01-09 | 2023-07-18 | Cue Biopharma, Inc. | T-cell modulatory multimeric polypeptides comprising reduced-affinity immunomodulatory polypeptides |
| US12257311B2 (en) | 2020-05-12 | 2025-03-25 | Cue Biopharma, Inc. | Multimeric T-cell modulatory polypeptides and methods of use thereof |
Families Citing this family (78)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| US5869270A (en) * | 1996-01-31 | 1999-02-09 | Sunol Molecular Corporation | Single chain MHC complexes and uses thereof |
| US6458354B1 (en) | 1996-03-28 | 2002-10-01 | The Johns Hopkins University | Molecular complexes which modify immune responses |
| AU729406B2 (en) | 1996-03-28 | 2001-02-01 | Johns Hopkins University, The | Soluble divalent and multivalent heterodimeric analogs of proteins |
| US6211342B1 (en) * | 1996-07-18 | 2001-04-03 | Children's Hospital Medical Center | Multivalent MHC complex peptide fusion protein complex for stimulating specific T cell function |
| US6268411B1 (en) | 1997-09-11 | 2001-07-31 | The Johns Hopkins University | Use of multivalent chimeric peptide-loaded, MHC/ig molecules to detect, activate or suppress antigen-specific T cell-dependent immune responses |
| DE69840600D1 (de) * | 1997-09-16 | 2009-04-09 | Univ Oregon Health & Science | Rekombinante mhc-moleküle welche nützlich sind für die manipulation von antigen-spezifischen t-zellen |
| US20030007978A1 (en) * | 1997-09-16 | 2003-01-09 | Burrows Gregory G. | Recombinant MHC molecules useful for manipulation of antigen-specific T-cells |
| US6232445B1 (en) * | 1997-10-29 | 2001-05-15 | Sunol Molecular Corporation | Soluble MHC complexes and methods of use thereof |
| GB2339782A (en) * | 1998-06-05 | 2000-02-09 | Philip Michael Savage | Chimeric protein complexes comprising HLA class I antigens |
| IL144845A0 (en) * | 1999-03-03 | 2002-06-30 | Univ Pennsylvania | Vaccines and gene therapy compositions and methods of making and using the same |
| ATE322683T1 (de) * | 1999-04-16 | 2006-04-15 | Ortho Mcneil Pharm Inc | Verfahren zur detektion von antigenspezifischen t-zellen |
| AU4700100A (en) * | 1999-05-06 | 2000-11-21 | Wake Forest University | Compositions and methods for identifying antigens which elicit an immune response |
| FR2796953B1 (fr) * | 1999-07-29 | 2003-10-10 | Centre Nat Rech Scient | Proteines recombinantes, et complexes moleculaires derives de ces proteines, analogues a des molecules impliquees dans les reponses immunitaires |
| US6995237B1 (en) * | 1999-10-27 | 2006-02-07 | Cel-Sci Corporation | Preparation and composition of peptides useful for treatment of autoimmune and transplant related graft versus host conditions |
| US7541184B2 (en) * | 2000-02-24 | 2009-06-02 | Invitrogen Corporation | Activation and expansion of cells |
| US7572631B2 (en) | 2000-02-24 | 2009-08-11 | Invitrogen Corporation | Activation and expansion of T cells |
| US20040191260A1 (en) | 2003-03-26 | 2004-09-30 | Technion Research & Development Foundation Ltd. | Compositions capable of specifically binding particular human antigen presenting molecule/pathogen-derived antigen complexes and uses thereof |
| CA2404489A1 (en) * | 2000-03-27 | 2001-10-04 | Technion Research And Development Foundation Ltd. | Single chain class i major histo-compatibility complexes, constructs encoding same and methods of generating same |
| US20020006397A1 (en) * | 2000-04-28 | 2002-01-17 | Roberts Bruce L. | In VIVO loading of MHC |
| CA2410642A1 (en) * | 2000-05-25 | 2001-11-29 | Sunol Molecular Corporation | Modulation of t-cell receptor interactions |
| GB0110547D0 (en) * | 2001-04-30 | 2001-06-20 | Avidex Ltd | Method |
| US6811785B2 (en) * | 2001-05-07 | 2004-11-02 | Mount Sinai School Of Medicine Of New York University | Multivalent MHC class II—peptide chimeras |
| CA2487779C (en) | 2001-06-05 | 2012-10-02 | Altor Bioscience Corporation | P53 binding t cell receptor molecules and uses thereof |
| US8022190B2 (en) * | 2001-06-19 | 2011-09-20 | Technion Research & Development Foundation Ltd. | Immuno-molecules containing viral proteins, compositions thereof and methods of using |
| US20030017134A1 (en) * | 2001-06-19 | 2003-01-23 | Technion Research And Development Foundation Ltd. | Methods and pharmaceutical compositions for immune deception, particularly useful in the treatment of cancer |
| WO2003029475A1 (fr) * | 2001-09-28 | 2003-04-10 | Dnavec Research Inc. | Vecteur viral infectant une cellule de mammifere, codant pour la $g(b)2m liee a un epitope |
| CN1617888A (zh) * | 2002-01-18 | 2005-05-18 | 伊诺维奥埃斯 | 用于肌内给药的双特异性抗体dna的构建 |
| US20030199024A1 (en) * | 2002-04-19 | 2003-10-23 | Hansen Ted H. | Single chain trimers of class I MHC molecules |
| US20050084967A1 (en) | 2002-06-28 | 2005-04-21 | Xcyte Therapies, Inc. | Compositions and methods for eliminating undesired subpopulations of T cells in patients with immunological defects related to autoimmunity and organ or hematopoietic stem cell transplantation |
| US20040175373A1 (en) * | 2002-06-28 | 2004-09-09 | Xcyte Therapies, Inc. | Compositions and methods for eliminating undesired subpopulations of T cells in patients with immunological defects related to autoimmunity and organ or hematopoietic stem cell transplantation |
| AU2003253684A1 (en) * | 2002-06-28 | 2004-01-19 | Xcyte Therapies, Inc. | Compositions and methods for restoring immune repertoire in patients with immunological defects related to autoimmunity and organ or hematopoietic stem cell transplantation |
| DE60334474D1 (de) * | 2002-07-12 | 2010-11-18 | Univ Johns Hopkins | Reagenzien und verfahren zum eingriff in einzigartige klonotype lymphozyten-rezeptoren |
| US8314210B2 (en) * | 2002-07-12 | 2012-11-20 | Dana-Farber Cancer Institute, Inc. | Compositions and methods for the generation of MHC class II compounds by peptide exchange |
| CA2500413A1 (en) * | 2002-10-01 | 2004-04-15 | Dnavec Research Inc. | Method of strengthening foreign epitope presentation by mhc class i by inhibiting tap activity |
| CA2501946C (en) * | 2002-10-16 | 2014-12-23 | Gen-Probe Incorporated | Compositions and methods for detecting west nile virus |
| US7927840B2 (en) | 2006-09-11 | 2011-04-19 | Gen Probe Incorporated | Method for detecting West Nile Virus nucleic acids in the 3′ non-coding region |
| EP2316844A3 (en) * | 2003-05-21 | 2011-07-20 | Biotech Tools S.A. | Peptide complex |
| DK1625148T3 (da) | 2003-05-21 | 2013-01-14 | Biotech Tools Sa | Peptidkompleks |
| EP2783699A1 (en) | 2003-09-05 | 2014-10-01 | Oregon Health & Science University | Monomeric recombinant MHC molecules useful for manipulation of antigen-specific T cells |
| CN1901839A (zh) | 2003-11-10 | 2007-01-24 | 阿尔特生物科学公司 | 可溶性tcr分子及其用途 |
| US20050227351A1 (en) * | 2004-04-08 | 2005-10-13 | Awdalla Essam T | Methods and compound protein molecules used for inducing cytotoxic cell-mediated immune response in a mammal against a pathogenic cell |
| DE102004019803A1 (de) * | 2004-04-23 | 2005-11-10 | Imusyn Gmbh & Co.Kg | Verfahren zur Herstellung löslicher MHC-Proteine |
| GB2422834B8 (en) * | 2005-02-04 | 2007-01-04 | Proimmune Ltd | MHC oligomer and method of making the same |
| EP1982176A1 (en) * | 2006-01-30 | 2008-10-22 | Dako Denmark A/S | High-speed quantification of antigen specific t-cells in whole blood by flow cytometry |
| US8518697B2 (en) * | 2006-04-04 | 2013-08-27 | Washington University | Single chain trimers and uses therefor |
| US7977457B2 (en) * | 2006-05-19 | 2011-07-12 | Teva Pharmaceutical Industries Ltd. | Fusion proteins, uses thereof and processes for producing same |
| EP2155782A2 (en) | 2007-03-26 | 2010-02-24 | Dako Denmark A/S | Mhc peptide complexes and uses thereof in infectious diseases |
| EP2167536A1 (en) | 2007-07-03 | 2010-03-31 | Dako Denmark A/S | Mhc multimers, methods for their generation, labeling and use |
| WO2009039854A2 (en) | 2007-09-27 | 2009-04-02 | Dako Denmark A/S | Mhc multimers in tuberculosis diagnostics, vaccine and therapeutics |
| US10968269B1 (en) | 2008-02-28 | 2021-04-06 | Agilent Technologies, Inc. | MHC multimers in borrelia diagnostics and disease |
| US10722562B2 (en) * | 2008-07-23 | 2020-07-28 | Immudex Aps | Combinatorial analysis and repair |
| GB0817244D0 (en) * | 2008-09-20 | 2008-10-29 | Univ Cardiff | Use of a protein kinase inhibitor to detect immune cells, such as T cells |
| US10369204B2 (en) | 2008-10-02 | 2019-08-06 | Dako Denmark A/S | Molecular vaccines for infectious disease |
| US11992518B2 (en) | 2008-10-02 | 2024-05-28 | Agilent Technologies, Inc. | Molecular vaccines for infectious disease |
| US20110124019A1 (en) * | 2009-11-25 | 2011-05-26 | The Charlotte-Mecklenburg Hospital Authority | Method of using carbonic anhydrase to detect hemolysis |
| WO2011147894A1 (en) | 2010-05-25 | 2011-12-01 | Forschungsverbund Berlin E.V. | Chimeric mhc class ii proteinpeptide |
| GB201013767D0 (en) * | 2010-08-17 | 2010-09-29 | Isis Innovation | Identification of ligands and their use |
| WO2012145384A1 (en) | 2011-04-20 | 2012-10-26 | University Of Washington Through Its Center For Commercialization | Beta-2 microglobulin-deficient cells |
| US8753309B2 (en) | 2011-06-24 | 2014-06-17 | The Invention Science Fund I, Llc | Device, system, and method including micro-patterned cell treatment array |
| US10228312B2 (en) | 2012-02-23 | 2019-03-12 | Juno Therapeutics Gmbh | Chromatographic isolation of cells and other complex biological materials |
| US10274499B2 (en) | 2012-03-27 | 2019-04-30 | The University Of Western Ontario | SH2 domain variants |
| JP6445427B2 (ja) * | 2012-05-08 | 2018-12-26 | ウエスタン ユニバーシティ オブ ヘルス サイエンシズ | ＣＤ４＋Ｔ細胞集団の抗原特異的な拡大のために標準化されたｅｘｖｉｖｏプラットフォーム |
| WO2014141244A1 (en) | 2013-03-12 | 2014-09-18 | Tel Hashomer Medical Research Infrastructure And Services Ltd. | Synthetic peptides for the treatment of autoimmune diseases |
| GB201313352D0 (en) | 2013-07-26 | 2013-09-11 | Isis Innovation | Identification of peptide ligands |
| US20160081314A1 (en) | 2014-09-19 | 2016-03-24 | Regeneron Pharmaceuticals, Inc. | Chimeric Antigen Receptors |
| WO2017068419A2 (en) | 2015-10-22 | 2017-04-27 | Juno Therapeutics Gmbh | Methods, kits, agents and apparatuses for transduction |
| MA45489A (fr) | 2015-10-22 | 2018-08-29 | Juno Therapeutics Gmbh | Procédés de culture de cellules, kits et appareil associés |
| CN109963584B (zh) | 2016-09-06 | 2024-03-15 | 豪夫迈·罗氏有限公司 | 结合mhc的肽阵列及其使用方法 |
| US11851471B2 (en) | 2017-01-09 | 2023-12-26 | Cue Biopharma, Inc. | T-cell modulatory multimeric polypeptides and methods of use thereof |
| WO2018197949A1 (en) | 2017-04-27 | 2018-11-01 | Juno Therapeutics Gmbh | Oligomeric particle reagents and methods of use thereof |
| US12258373B2 (en) | 2018-12-17 | 2025-03-25 | Immudex Aps | Panel comprising Borrelia MHC multimers |
| AU2020204994A1 (en) * | 2019-01-03 | 2021-07-29 | Regents Of The University Of Minnesota | Genetically modified cells, tissues, and organs for treating disease |
| TWI852977B (zh) | 2019-01-10 | 2024-08-21 | 美商健生生物科技公司 | 前列腺新抗原及其用途 |
| TW202144389A (zh) | 2020-02-14 | 2021-12-01 | 美商健生生物科技公司 | 在多發性骨髓瘤中表現之新抗原及其用途 |
| TW202144388A (zh) | 2020-02-14 | 2021-12-01 | 美商健生生物科技公司 | 在卵巢癌中表現之新抗原及其用途 |
| US12295997B2 (en) | 2020-07-06 | 2025-05-13 | Janssen Biotech, Inc. | Prostate neoantigens and their uses |
| EP4211149A4 (en) | 2020-09-09 | 2024-10-09 | Cue Biopharma, Inc. | MULTIMERIC POLYPEPTIDES MODULATING MHC CLASS II T CELLS FOR THE TREATMENT OF TYPE 1 DIABETES MELLITUS (T1D) AND METHODS OF USE THEREOF |
| US11926667B2 (en) | 2020-10-13 | 2024-03-12 | Janssen Biotech, Inc. | Bioengineered T cell mediated immunity, materials and other methods for modulating cluster of differentiation IV and/or VIII |
Family Cites Families (18)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| EP0420913B1 (en) * | 1988-06-14 | 1995-11-15 | Cell Med, Inc. | Heterofunctional cellular immunological reagents, vaccines containing same and methods for the use of same |
| US5130297A (en) * | 1988-06-23 | 1992-07-14 | Anergen, Inc. | Conjugates useful in ameliorating autoimmunity MHC-II-peptide |
| US5260422A (en) * | 1988-06-23 | 1993-11-09 | Anergen, Inc. | MHC conjugates useful in ameliorating autoimmunity |
| US5194425A (en) * | 1988-06-23 | 1993-03-16 | Anergen, Inc. | Mhc-mediated toxic conjugates useful in ameliorating autoimmunity |
| US5976551A (en) * | 1991-11-15 | 1999-11-02 | Institut Pasteur And Institut Nationale De La Sante Et De La Recherche Medicale | Altered major histocompatibility complex (MHC) determinant and method of using the determinant |
| WO1993009810A1 (en) * | 1991-11-19 | 1993-05-27 | Anergen, Inc. | Mhc subunit conjugates useful in ameliorating deleterious immune responses |
| WO1993010220A1 (en) * | 1991-11-19 | 1993-05-27 | Anergen, Inc. | Soluble mhc molecules and their uses |
| US5583031A (en) * | 1992-02-06 | 1996-12-10 | President And Fellows Of Harvard College | Empty major histocompatibility class II heterodimers |
| US5314813A (en) * | 1992-02-19 | 1994-05-24 | Scripps Research Institute | Drosophila cell lines expressing genes encoding MHC class I antigens and B2-microglobulin and capable of assembling empty complexes and methods of making said cell lines |
| AU6270794A (en) * | 1993-02-25 | 1994-09-14 | Anergen, Inc. | Treatment of allergic responses using mhc-peptide complexes |
| WO1994025054A1 (en) * | 1993-04-29 | 1994-11-10 | Andrew Atkin | Recombinant vaccine |
| US5820866A (en) * | 1994-03-04 | 1998-10-13 | National Jewish Center For Immunology And Respiratory Medicine | Product and process for T cell regulation |
| AU696177B2 (en) * | 1994-07-29 | 1998-09-03 | Sunol Molecular Corporation | Mhc complexes and uses thereof |
| US5888773A (en) | 1994-08-17 | 1999-03-30 | The United States Of America As Represented By The Department Of Health And Human Services | Method of producing single-chain Fv molecules |
| EP0833930A2 (en) * | 1995-06-07 | 1998-04-08 | ZymoGenetics, Inc. | Fused soluble mhc heterodimer:peptide complexes and their uses |
| US5869270A (en) * | 1996-01-31 | 1999-02-09 | Sunol Molecular Corporation | Single chain MHC complexes and uses thereof |
| AU729406B2 (en) * | 1996-03-28 | 2001-02-01 | Johns Hopkins University, The | Soluble divalent and multivalent heterodimeric analogs of proteins |
| US6232445B1 (en) * | 1997-10-29 | 2001-05-15 | Sunol Molecular Corporation | Soluble MHC complexes and methods of use thereof |
-
1996
- 1996-01-31 US US08/596,387 patent/US5869270A/en not_active Expired - Lifetime
-
1997
- 1997-01-30 DE DE69730693T patent/DE69730693T2/de not_active Expired - Lifetime
- 1997-01-30 EP EP04019176A patent/EP1526141A3/en not_active Withdrawn
- 1997-01-30 AU AU22538/97A patent/AU729672B2/en not_active Ceased
- 1997-01-30 WO PCT/US1997/001617 patent/WO1997028191A1/en not_active Ceased
- 1997-01-30 DK DK97905709T patent/DK0877760T3/da active
- 1997-01-30 CA CA002244755A patent/CA2244755A1/en not_active Abandoned
- 1997-01-30 EP EP97905709A patent/EP0877760B1/en not_active Expired - Lifetime
- 1997-01-30 AT AT97905709T patent/ATE276275T1/de not_active IP Right Cessation
- 1997-01-30 JP JP09527863A patent/JP2000515363A/ja active Pending
-
1998
- 1998-04-28 US US09/067,615 patent/US6309645B1/en not_active Expired - Lifetime
-
2001
- 2001-05-03 US US09/848,164 patent/US7141656B2/en not_active Expired - Fee Related
Cited By (42)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| JP2003519240A (ja) * | 2000-01-03 | 2003-06-17 | ティーアール アソシエイツ，エル．エル．シー． | タンパク質を移送する方法 |
| JP2011182702A (ja) * | 2010-03-08 | 2011-09-22 | Tokyo Univ Of Agriculture & Technology | 融合ｍｈｃ分子連結磁気微粒子、抗原ペプチドのスクリーニング方法、組換えベクター、及び磁性細菌の形質転換体 |
| JP2015514421A (ja) * | 2012-04-17 | 2015-05-21 | ザ ユニバーシティ オブ ワシントン スルー イッツ センター フォーコマーシャライゼーションＴｈｅ Ｕｎｉｖｅｒｓｉｔｙ Ｏｆ Ｗａｓｈｉｎｇｔｏｎ Ｔｈｒｏｕｇｈ Ｉｔｓ Ｃｅｎｔｅｒ Ｆｏｒ Ｃｏｍｍｅｒｃｉａｌｉｚａｔｉｏｎ | Ｈｌａクラスｉｉタンパク質の発現能を有するｈｌａクラスｉｉ欠損細胞、ｈｌａクラスｉ欠損細胞、及びその使用 |
| JP7531925B2 (ja) | 2012-04-17 | 2024-08-13 | ザ ユニバーシティ オブ ワシントン スルー イッツ センター フォー コマーシャライゼーション | Ｈｌａクラスｉｉタンパク質の発現能を有するｈｌａクラスｉｉ欠損細胞、ｈｌａクラスｉ欠損細胞、及びその使用 |
| JP2019068856A (ja) * | 2012-04-17 | 2019-05-09 | ザ ユニバーシティ オブ ワシントン スルー イッツ センター フォー コマーシャライゼーションＴｈｅ Ｕｎｉｖｅｒｓｉｔｙ Ｏｆ Ｗａｓｈｉｎｇｔｏｎ Ｔｈｒｏｕｇｈ Ｉｔｓ Ｃｅｎｔｅｒ Ｆｏｒ Ｃｏｍｍｅｒｃｉａｌｉｚａｔｉｏｎ | Ｈｌａクラスｉｉタンパク質の発現能を有するｈｌａクラスｉｉ欠損細胞、ｈｌａクラスｉ欠損細胞、及びその使用 |
| JP2022162047A (ja) * | 2012-04-17 | 2022-10-21 | ザ ユニバーシティ オブ ワシントン スルー イッツ センター フォー コマーシャライゼーション | Ｈｌａクラスｉｉタンパク質の発現能を有するｈｌａクラスｉｉ欠損細胞、ｈｌａクラスｉ欠損細胞、及びその使用 |
| JP2024144548A (ja) * | 2012-04-17 | 2024-10-11 | ザ ユニバーシティ オブ ワシントン スルー イッツ センター フォー コマーシャライゼーション | Ｈｌａクラスｉｉタンパク質の発現能を有するｈｌａクラスｉｉ欠損細胞、ｈｌａクラスｉ欠損細胞、及びその使用 |
| JP7130571B2 (ja) | 2012-04-17 | 2022-09-05 | ザ ユニバーシティ オブ ワシントン スルー イッツ センター フォー コマーシャライゼーション | Ｈｌａクラスｉｉタンパク質の発現能を有するｈｌａクラスｉｉ欠損細胞、ｈｌａクラスｉ欠損細胞、及びその使用 |
| US11226339B2 (en) | 2012-12-11 | 2022-01-18 | Albert Einstein College Of Medicine | Methods for high throughput receptor:ligand identification |
| JP7331075B2 (ja) | 2014-06-18 | 2023-08-22 | アルバート アインシュタイン カレッジ オブ メディシン | ｓｙｎＴａｃポリペプチド及びその使用 |
| JP2020072733A (ja) * | 2014-06-18 | 2020-05-14 | アルバート アインシュタイン カレッジ オブ メディシン | ｓｙｎＴａｃポリペプチド及びその使用 |
| JP6995151B2 (ja) | 2014-06-18 | 2022-02-21 | アルバート アインシュタイン カレッジ オブ メディシン | ｓｙｎＴａｃポリペプチド及びその使用 |
| JP2022046544A (ja) * | 2014-06-18 | 2022-03-23 | アルバート アインシュタイン カレッジ オブ メディシン | ｓｙｎＴａｃポリペプチド及びその使用 |
| JP2020022491A (ja) * | 2014-06-18 | 2020-02-13 | アルバート アインシュタイン カレッジ オブ メディシン | ｓｙｎＴａｃポリペプチド及びその使用 |
| JP2017519491A (ja) * | 2014-06-18 | 2017-07-20 | アルバート アインシュタイン カレッジ オブ メディシン，インコーポレイティド | ｓｙｎＴａｃポリペプチド及びその使用 |
| US11505591B2 (en) | 2016-05-18 | 2022-11-22 | Cue Biopharma, Inc. | T-cell modulatory multimeric polypeptides and methods of use thereof |
| US11339201B2 (en) | 2016-05-18 | 2022-05-24 | Albert Einstein College Of Medicine | Variant PD-L1 polypeptides, T-cell modulatory multimeric polypeptides, and methods of use thereof |
| US11377478B2 (en) | 2016-12-22 | 2022-07-05 | Cue Biopharma, Inc. | T-cell modulatory multimeric polypeptides and methods of use thereof |
| US11401314B2 (en) | 2016-12-22 | 2022-08-02 | Cue Biopharma, Inc. | T-cell modulatory multimeric polypeptides and methods of use thereof |
| US11370821B2 (en) | 2016-12-22 | 2022-06-28 | Cue Biopharma, Inc. | T-cell modulatory multimeric polypeptides and methods of use thereof |
| US11117945B2 (en) | 2016-12-22 | 2021-09-14 | Cue Biopharma, Inc. | T-cell modulatory multimeric polypeptides and methods of use thereof |
| US11505588B2 (en) | 2016-12-22 | 2022-11-22 | Cue Biopharma, Inc. | T-cell modulatory multimeric polypeptides and methods of use thereof |
| US12180258B2 (en) | 2016-12-22 | 2024-12-31 | Cue Biopharma, Inc. | T-cell modulatory multimeric polypeptides and methods of use thereof |
| US11530248B2 (en) | 2016-12-22 | 2022-12-20 | Cue Biopharma, Inc. | T-cell modulatory multimeric polypeptides and methods of use thereof |
| US12152061B2 (en) | 2016-12-22 | 2024-11-26 | Cue Biopharma, Inc. | T-cell modulatory multimeric polypeptides and methods of use thereof |
| US11708400B2 (en) | 2016-12-22 | 2023-07-25 | Cue Biopharma, Inc. | T-cell modulatory multimeric polypeptides and methods of use thereof |
| US10927158B2 (en) | 2016-12-22 | 2021-02-23 | Cue Biopharma, Inc. | T-cell modulatory multimeric polypeptides and methods of use thereof |
| US11739133B2 (en) | 2016-12-22 | 2023-08-29 | Cue Biopharma, Inc. | T-cell modulatory multimeric polypeptides and methods of use thereof |
| US12145973B2 (en) | 2016-12-22 | 2024-11-19 | Cue Biopharma, Inc. | T-cell modulatory multimeric polypeptides and methods of use thereof |
| US11905320B2 (en) | 2016-12-22 | 2024-02-20 | Cue Biopharma, Inc. | T-cell modulatory multimeric polypeptides and methods of use thereof |
| US12421287B2 (en) | 2016-12-22 | 2025-09-23 | Cue Biopharma, Inc. | T-cell modulatory multimeric polypeptides and methods of use thereof |
| US11987610B2 (en) | 2016-12-22 | 2024-05-21 | Cue Biopharma, Inc. | T-cell modulatory multimeric polypeptides and methods of use thereof |
| US11479595B2 (en) | 2017-03-15 | 2022-10-25 | Cue Biopharma, Inc. | Methods for modulating an immune response |
| US11993641B2 (en) | 2017-03-15 | 2024-05-28 | Cue Biopharma, Inc. | Methods for modulating an immune response |
| US11958893B2 (en) | 2017-03-15 | 2024-04-16 | Cue Biopharma, Inc. | Methods for modulating an immune response |
| US11767355B2 (en) | 2017-03-15 | 2023-09-26 | Cue Biopharma, Inc. | Methods for modulating an immune response |
| US11104712B2 (en) | 2017-03-15 | 2021-08-31 | Cue Biopharma, Inc. | Methods for modulating an immune response |
| US10927161B2 (en) | 2017-03-15 | 2021-02-23 | Cue Biopharma, Inc. | Methods for modulating an immune response |
| US11702461B2 (en) | 2018-01-09 | 2023-07-18 | Cue Biopharma, Inc. | T-cell modulatory multimeric polypeptides comprising reduced-affinity immunomodulatory polypeptides |
| US12257311B2 (en) | 2020-05-12 | 2025-03-25 | Cue Biopharma, Inc. | Multimeric T-cell modulatory polypeptides and methods of use thereof |
| US12485184B2 (en) | 2020-05-12 | 2025-12-02 | Cue Biopharma, Inc. | Multimeric T-cell modulatory polypeptides and methods of use thereof |
| US12485183B2 (en) | 2020-05-12 | 2025-12-02 | Cue Biopharma, Inc. | Multimeric T-cell modulatory polypeptides and methods of use thereof |
Also Published As
| Publication number | Publication date |
|---|---|
| DE69730693D1 (de) | 2004-10-21 |
| EP1526141A2 (en) | 2005-04-27 |
| AU729672B2 (en) | 2001-02-08 |
| DK0877760T3 (da) | 2004-12-20 |
| AU2253897A (en) | 1997-08-22 |
| US6309645B1 (en) | 2001-10-30 |
| EP1526141A3 (en) | 2005-08-24 |
| EP0877760A4 (cg-RX-API-DMAC7.html) | 1998-12-30 |
| CA2244755A1 (en) | 1997-08-07 |
| DE69730693T2 (de) | 2005-10-06 |
| EP0877760A1 (en) | 1998-11-18 |
| WO1997028191A1 (en) | 1997-08-07 |
| EP0877760B1 (en) | 2004-09-15 |
| US7141656B2 (en) | 2006-11-28 |
| US5869270A (en) | 1999-02-09 |
| US20020034513A1 (en) | 2002-03-21 |
| ATE276275T1 (de) | 2004-10-15 |
Similar Documents
| Publication | Publication Date | Title |
|---|---|---|
| JP2000515363A (ja) | Ｍｈｃ複合体及びその用途 | |
| US7074904B2 (en) | MHC complexes and uses thereof | |
| EP0776339B1 (en) | Mhc complexes and uses thereof | |
| JP4350301B2 (ja) | 可溶性ｍｈｃ複合体とその利用法 | |
| JP4214173B2 (ja) | 寛容原性融合タンパク質による寛容性の誘発 | |
| US7459544B2 (en) | Nucleic acids encoding B7-2 fusion proteins | |
| US7034121B2 (en) | Antibodies against CTLA4 | |
| WO1997028191A9 (en) | Mhc complexes and uses thereof | |
| WO1996004314A9 (en) | Mhc complexes and uses thereof | |
| EP2042596A1 (en) | Polypeptides involved in immune response | |
| US20070014809A1 (en) | B Cell Activation and Polypeptides Having CD14 Activity | |
| HK1160665A (en) | Polypeptides involved in immune response | |
| AU7208600A (en) | B7-2:CTL A4/CD 28 counter receptor |
Legal Events
| Date | Code | Title | Description |
|---|---|---|---|
| A521 | Request for written amendment filed |
Free format text: JAPANESE INTERMEDIATE CODE: A523 Effective date: 20040120 |
|
| A621 | Written request for application examination |
Free format text: JAPANESE INTERMEDIATE CODE: A621 Effective date: 20040120 |
|
| A711 | Notification of change in applicant |
Free format text: JAPANESE INTERMEDIATE CODE: A711 Effective date: 20040610 |
|
| A131 | Notification of reasons for refusal |
Free format text: JAPANESE INTERMEDIATE CODE: A131 Effective date: 20061010 |
|
| A601 | Written request for extension of time |
Free format text: JAPANESE INTERMEDIATE CODE: A601 Effective date: 20070110 |
|
| A602 | Written permission of extension of time |
Free format text: JAPANESE INTERMEDIATE CODE: A602 Effective date: 20070226 |
|
| A521 | Request for written amendment filed |
Free format text: JAPANESE INTERMEDIATE CODE: A523 Effective date: 20070409 |
|
| A131 | Notification of reasons for refusal |
Free format text: JAPANESE INTERMEDIATE CODE: A131 Effective date: 20080422 |
|
| A601 | Written request for extension of time |
Free format text: JAPANESE INTERMEDIATE CODE: A601 Effective date: 20080714 |
|
| A602 | Written permission of extension of time |
Free format text: JAPANESE INTERMEDIATE CODE: A602 Effective date: 20080818 |
|
| A601 | Written request for extension of time |
Free format text: JAPANESE INTERMEDIATE CODE: A601 Effective date: 20080822 |
|
| A602 | Written permission of extension of time |
Free format text: JAPANESE INTERMEDIATE CODE: A602 Effective date: 20080929 |
|
| A521 | Request for written amendment filed |
Free format text: JAPANESE INTERMEDIATE CODE: A523 Effective date: 20080922 |
|
| A02 | Decision of refusal |
Free format text: JAPANESE INTERMEDIATE CODE: A02 Effective date: 20090324 |
|
| A521 | Request for written amendment filed |
Free format text: JAPANESE INTERMEDIATE CODE: A821 Effective date: 20090622 |