IE56026B1 - Cysteine-depleted muteins of biologically active proteins - Google Patents
Cysteine-depleted muteins of biologically active proteinsInfo
- Publication number
- IE56026B1 IE56026B1 IE2380/83A IE238083A IE56026B1 IE 56026 B1 IE56026 B1 IE 56026B1 IE 2380/83 A IE2380/83 A IE 2380/83A IE 238083 A IE238083 A IE 238083A IE 56026 B1 IE56026 B1 IE 56026B1
- Authority
- IE
- Ireland
- Prior art keywords
- mutein
- amino acid
- codon
- ifn
- protein
- Prior art date
Links
- 108090000623 proteins and genes Proteins 0.000 title claims description 100
- 102000004169 proteins and genes Human genes 0.000 title claims description 59
- 235000018102 proteins Nutrition 0.000 title claims description 57
- 235000018417 cysteine Nutrition 0.000 title claims description 25
- XUJNEKJLAYXESH-UHFFFAOYSA-N cysteine Natural products SCC(N)C(O)=O XUJNEKJLAYXESH-UHFFFAOYSA-N 0.000 title claims description 22
- 108010002350 Interleukin-2 Proteins 0.000 claims abstract description 47
- 150000001413 amino acids Chemical class 0.000 claims abstract description 47
- 125000000151 cysteine group Chemical group N[C@@H](CS)C(=O)* 0.000 claims abstract description 41
- 235000001014 amino acid Nutrition 0.000 claims abstract description 39
- 102000000588 Interleukin-2 Human genes 0.000 claims abstract description 38
- 101001002657 Homo sapiens Interleukin-2 Proteins 0.000 claims abstract description 6
- 230000007935 neutral effect Effects 0.000 claims abstract description 6
- 102000055277 human IL2 Human genes 0.000 claims abstract description 3
- 108020004705 Codon Proteins 0.000 claims description 53
- 108020004414 DNA Proteins 0.000 claims description 53
- 238000000034 method Methods 0.000 claims description 43
- 229940024606 amino acid Drugs 0.000 claims description 37
- 108090000467 Interferon-beta Proteins 0.000 claims description 35
- 230000000694 effects Effects 0.000 claims description 31
- 102100026720 Interferon beta Human genes 0.000 claims description 28
- 108091034117 Oligonucleotide Proteins 0.000 claims description 26
- MTCFGRXMJLQNBG-UHFFFAOYSA-N Serine Natural products OCC(N)C(O)=O MTCFGRXMJLQNBG-UHFFFAOYSA-N 0.000 claims description 21
- 239000013612 plasmid Substances 0.000 claims description 21
- 239000000203 mixture Substances 0.000 claims description 20
- MTCFGRXMJLQNBG-REOHCLBHSA-N (2S)-2-Amino-3-hydroxypropansäure Chemical compound OC[C@H](N)C(O)=O MTCFGRXMJLQNBG-REOHCLBHSA-N 0.000 claims description 19
- 241000588724 Escherichia coli Species 0.000 claims description 17
- 230000004071 biological effect Effects 0.000 claims description 17
- 102000053602 DNA Human genes 0.000 claims description 15
- 239000002773 nucleotide Substances 0.000 claims description 14
- 230000008569 process Effects 0.000 claims description 13
- 125000003729 nucleotide group Chemical group 0.000 claims description 12
- 108091027305 Heteroduplex Proteins 0.000 claims description 11
- 238000009472 formulation Methods 0.000 claims description 11
- 239000013598 vector Substances 0.000 claims description 11
- 241000282414 Homo sapiens Species 0.000 claims description 10
- AYFVYJQAPQTCCC-UHFFFAOYSA-N Threonine Natural products CC(O)C(N)C(O)=O AYFVYJQAPQTCCC-UHFFFAOYSA-N 0.000 claims description 10
- 239000004473 Threonine Substances 0.000 claims description 10
- 230000000692 anti-sense effect Effects 0.000 claims description 10
- 239000013604 expression vector Substances 0.000 claims description 10
- 238000012217 deletion Methods 0.000 claims description 9
- 230000037430 deletion Effects 0.000 claims description 9
- 230000000869 mutational effect Effects 0.000 claims description 9
- DHMQDGOQFOQNFH-UHFFFAOYSA-N Glycine Chemical compound NCC(O)=O DHMQDGOQFOQNFH-UHFFFAOYSA-N 0.000 claims description 8
- QIVBCDIJIAJPQS-VIFPVBQESA-N L-tryptophane Chemical compound C1=CC=C2C(C[C@H](N)C(O)=O)=CNC2=C1 QIVBCDIJIAJPQS-VIFPVBQESA-N 0.000 claims description 8
- 108091028043 Nucleic acid sequence Proteins 0.000 claims description 8
- AYFVYJQAPQTCCC-GBXIJSLDSA-N L-threonine Chemical compound C[C@@H](O)[C@H](N)C(O)=O AYFVYJQAPQTCCC-GBXIJSLDSA-N 0.000 claims description 7
- QIVBCDIJIAJPQS-UHFFFAOYSA-N Tryptophan Natural products C1=CC=C2C(CC(N)C(O)=O)=CNC2=C1 QIVBCDIJIAJPQS-UHFFFAOYSA-N 0.000 claims description 6
- 230000001580 bacterial effect Effects 0.000 claims description 6
- 229930182817 methionine Natural products 0.000 claims description 6
- 108010014303 DNA-directed DNA polymerase Proteins 0.000 claims description 5
- 102000016928 DNA-directed DNA polymerase Human genes 0.000 claims description 5
- BWGNESOTFCXPMA-UHFFFAOYSA-N Dihydrogen disulfide Chemical compound SS BWGNESOTFCXPMA-UHFFFAOYSA-N 0.000 claims description 5
- OUYCCCASQSFEME-QMMMGPOBSA-N L-tyrosine Chemical compound OC(=O)[C@@H](N)CC1=CC=C(O)C=C1 OUYCCCASQSFEME-QMMMGPOBSA-N 0.000 claims description 5
- 230000000295 complement effect Effects 0.000 claims description 5
- OUYCCCASQSFEME-UHFFFAOYSA-N tyrosine Natural products OC(=O)C(N)CC1=CC=C(O)C=C1 OUYCCCASQSFEME-UHFFFAOYSA-N 0.000 claims description 5
- 239000004471 Glycine Substances 0.000 claims description 4
- 102000003996 Interferon-beta Human genes 0.000 claims description 4
- QNAYBMKLOCPYGJ-REOHCLBHSA-N L-alanine Chemical compound C[C@H](N)C(O)=O QNAYBMKLOCPYGJ-REOHCLBHSA-N 0.000 claims description 4
- HNDVDQJCIGZPNO-YFKPBYRVSA-N L-histidine Chemical compound OC(=O)[C@@H](N)CC1=CN=CN1 HNDVDQJCIGZPNO-YFKPBYRVSA-N 0.000 claims description 4
- AGPKZVBTJJNPAG-WHFBIAKZSA-N L-isoleucine Chemical compound CC[C@H](C)[C@H](N)C(O)=O AGPKZVBTJJNPAG-WHFBIAKZSA-N 0.000 claims description 4
- ROHFNLRQFUQHCH-YFKPBYRVSA-N L-leucine Chemical compound CC(C)C[C@H](N)C(O)=O ROHFNLRQFUQHCH-YFKPBYRVSA-N 0.000 claims description 4
- FFEARJCKVFRZRR-BYPYZUCNSA-N L-methionine Chemical compound CSCC[C@H](N)C(O)=O FFEARJCKVFRZRR-BYPYZUCNSA-N 0.000 claims description 4
- COLNVLDHVKWLRT-QMMMGPOBSA-N L-phenylalanine Chemical compound OC(=O)[C@@H](N)CC1=CC=CC=C1 COLNVLDHVKWLRT-QMMMGPOBSA-N 0.000 claims description 4
- KZSNJWFQEVHDMF-BYPYZUCNSA-N L-valine Chemical compound CC(C)[C@H](N)C(O)=O KZSNJWFQEVHDMF-BYPYZUCNSA-N 0.000 claims description 4
- ROHFNLRQFUQHCH-UHFFFAOYSA-N Leucine Natural products CC(C)CC(N)C(O)=O ROHFNLRQFUQHCH-UHFFFAOYSA-N 0.000 claims description 4
- 241001465754 Metazoa Species 0.000 claims description 4
- 108020004682 Single-Stranded DNA Proteins 0.000 claims description 4
- KZSNJWFQEVHDMF-UHFFFAOYSA-N Valine Natural products CC(C)C(N)C(O)=O KZSNJWFQEVHDMF-UHFFFAOYSA-N 0.000 claims description 4
- 235000004279 alanine Nutrition 0.000 claims description 4
- 238000012258 culturing Methods 0.000 claims description 4
- 239000002552 dosage form Substances 0.000 claims description 4
- 239000013613 expression plasmid Substances 0.000 claims description 4
- HNDVDQJCIGZPNO-UHFFFAOYSA-N histidine Natural products OC(=O)C(N)CC1=CN=CN1 HNDVDQJCIGZPNO-UHFFFAOYSA-N 0.000 claims description 4
- 229960001388 interferon-beta Drugs 0.000 claims description 4
- AGPKZVBTJJNPAG-UHFFFAOYSA-N isoleucine Natural products CCC(C)C(N)C(O)=O AGPKZVBTJJNPAG-UHFFFAOYSA-N 0.000 claims description 4
- 229960000310 isoleucine Drugs 0.000 claims description 4
- COLNVLDHVKWLRT-UHFFFAOYSA-N phenylalanine Natural products OC(=O)C(N)CC1=CC=CC=C1 COLNVLDHVKWLRT-UHFFFAOYSA-N 0.000 claims description 4
- 230000003362 replicative effect Effects 0.000 claims description 4
- 239000004474 valine Substances 0.000 claims description 4
- 238000003306 harvesting Methods 0.000 claims description 3
- 101001054334 Homo sapiens Interferon beta Proteins 0.000 claims description 2
- 108010046938 Macrophage Colony-Stimulating Factor Proteins 0.000 claims description 2
- 102100028123 Macrophage colony-stimulating factor 1 Human genes 0.000 claims description 2
- 238000003745 diagnosis Methods 0.000 claims description 2
- 125000003607 serino group Chemical group [H]N([H])[C@]([H])(C(=O)[*])C(O[H])([H])[H] 0.000 claims description 2
- 238000002560 therapeutic procedure Methods 0.000 claims description 2
- 230000001131 transforming effect Effects 0.000 claims 3
- 239000003085 diluting agent Substances 0.000 claims 2
- 238000004519 manufacturing process Methods 0.000 claims 2
- 239000000546 pharmaceutical excipient Substances 0.000 claims 2
- 206010054094 Tumour necrosis Diseases 0.000 claims 1
- 238000011321 prophylaxis Methods 0.000 claims 1
- 238000003860 storage Methods 0.000 abstract description 2
- 239000013615 primer Substances 0.000 description 37
- XUJNEKJLAYXESH-REOHCLBHSA-N L-Cysteine Chemical compound SC[C@H](N)C(O)=O XUJNEKJLAYXESH-REOHCLBHSA-N 0.000 description 34
- 210000004027 cell Anatomy 0.000 description 26
- FAPWRFPIFSIZLT-UHFFFAOYSA-M Sodium chloride Chemical compound [Na+].[Cl-] FAPWRFPIFSIZLT-UHFFFAOYSA-M 0.000 description 20
- 239000000872 buffer Substances 0.000 description 16
- 239000000284 extract Substances 0.000 description 16
- 235000004400 serine Nutrition 0.000 description 14
- 238000009396 hybridization Methods 0.000 description 13
- TWRXJAOTZQYOKJ-UHFFFAOYSA-L Magnesium chloride Chemical compound [Mg+2].[Cl-].[Cl-] TWRXJAOTZQYOKJ-UHFFFAOYSA-L 0.000 description 12
- DBMJMQXJHONAFJ-UHFFFAOYSA-M Sodium laurylsulphate Chemical compound [Na+].CCCCCCCCCCCCOS([O-])(=O)=O DBMJMQXJHONAFJ-UHFFFAOYSA-M 0.000 description 12
- 239000000523 sample Substances 0.000 description 12
- 238000002741 site-directed mutagenesis Methods 0.000 description 12
- 239000011780 sodium chloride Substances 0.000 description 11
- 239000000243 solution Substances 0.000 description 10
- 230000001225 therapeutic effect Effects 0.000 description 10
- 101100498071 Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987) cys-17 gene Proteins 0.000 description 9
- HEMHJVSKTPXQMS-UHFFFAOYSA-M Sodium hydroxide Chemical compound [OH-].[Na+] HEMHJVSKTPXQMS-UHFFFAOYSA-M 0.000 description 9
- 239000002299 complementary DNA Substances 0.000 description 9
- 239000012634 fragment Substances 0.000 description 9
- ISWSIDIOOBJBQZ-UHFFFAOYSA-N Phenol Chemical compound OC1=CC=CC=C1 ISWSIDIOOBJBQZ-UHFFFAOYSA-N 0.000 description 8
- 108091008146 restriction endonucleases Proteins 0.000 description 8
- 108091081021 Sense strand Proteins 0.000 description 7
- 230000008859 change Effects 0.000 description 7
- 239000000499 gel Substances 0.000 description 7
- 230000035772 mutation Effects 0.000 description 7
- 238000002360 preparation method Methods 0.000 description 7
- 238000000746 purification Methods 0.000 description 7
- WEVYAHXRMPXWCK-UHFFFAOYSA-N Acetonitrile Chemical compound CC#N WEVYAHXRMPXWCK-UHFFFAOYSA-N 0.000 description 6
- 102000012410 DNA Ligases Human genes 0.000 description 6
- 108010061982 DNA Ligases Proteins 0.000 description 6
- 102000014150 Interferons Human genes 0.000 description 6
- 108010050904 Interferons Proteins 0.000 description 6
- WYURNTSHIVDZCO-UHFFFAOYSA-N Tetrahydrofuran Chemical compound C1CCOC1 WYURNTSHIVDZCO-UHFFFAOYSA-N 0.000 description 6
- BTANRVKWQNVYAZ-UHFFFAOYSA-N butan-2-ol Chemical compound CCC(C)O BTANRVKWQNVYAZ-UHFFFAOYSA-N 0.000 description 6
- 229910001629 magnesium chloride Inorganic materials 0.000 description 6
- XLYOFNOQVPJJNP-UHFFFAOYSA-N water Chemical compound O XLYOFNOQVPJJNP-UHFFFAOYSA-N 0.000 description 6
- 229920001817 Agar Polymers 0.000 description 5
- 102000004594 DNA Polymerase I Human genes 0.000 description 5
- 108010017826 DNA Polymerase I Proteins 0.000 description 5
- 108020004511 Recombinant DNA Proteins 0.000 description 5
- 239000008272 agar Substances 0.000 description 5
- 238000003556 assay Methods 0.000 description 5
- 238000010586 diagram Methods 0.000 description 5
- 229940079322 interferon Drugs 0.000 description 5
- 238000012216 screening Methods 0.000 description 5
- 239000003155 DNA primer Substances 0.000 description 4
- 101000959820 Homo sapiens Interferon alpha-1/13 Proteins 0.000 description 4
- 102100040019 Interferon alpha-1/13 Human genes 0.000 description 4
- 241000700605 Viruses Species 0.000 description 4
- 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 4
- 239000011543 agarose gel Substances 0.000 description 4
- 230000015572 biosynthetic process Effects 0.000 description 4
- 238000006664 bond formation reaction Methods 0.000 description 4
- 238000006243 chemical reaction Methods 0.000 description 4
- 230000000120 cytopathologic effect Effects 0.000 description 4
- VHJLVAABSRFDPM-QWWZWVQMSA-N dithiothreitol Chemical compound SC[C@@H](O)[C@H](O)CS VHJLVAABSRFDPM-QWWZWVQMSA-N 0.000 description 4
- 108020004999 messenger RNA Proteins 0.000 description 4
- 238000002703 mutagenesis Methods 0.000 description 4
- 231100000350 mutagenesis Toxicity 0.000 description 4
- 239000002953 phosphate buffered saline Substances 0.000 description 4
- 230000007704 transition Effects 0.000 description 4
- 229960004799 tryptophan Drugs 0.000 description 4
- 241000972773 Aulopiformes Species 0.000 description 3
- KRKNYBCHXYNGOX-UHFFFAOYSA-K Citrate Chemical compound [O-]C(=O)CC(O)(CC([O-])=O)C([O-])=O KRKNYBCHXYNGOX-UHFFFAOYSA-K 0.000 description 3
- 108091033380 Coding strand Proteins 0.000 description 3
- 229920001917 Ficoll Polymers 0.000 description 3
- 241000282412 Homo Species 0.000 description 3
- 239000000020 Nitrocellulose Substances 0.000 description 3
- AVKUERGKIZMTKX-NJBDSQKTSA-N ampicillin Chemical compound C1([C@@H](N)C(=O)N[C@H]2[C@H]3SC([C@@H](N3C2=O)C(O)=O)(C)C)=CC=CC=C1 AVKUERGKIZMTKX-NJBDSQKTSA-N 0.000 description 3
- 229960000723 ampicillin Drugs 0.000 description 3
- 239000012141 concentrate Substances 0.000 description 3
- 150000001945 cysteines Chemical class 0.000 description 3
- 238000000605 extraction Methods 0.000 description 3
- 238000010438 heat treatment Methods 0.000 description 3
- 230000007062 hydrolysis Effects 0.000 description 3
- 238000006460 hydrolysis reaction Methods 0.000 description 3
- 229920001220 nitrocellulos Polymers 0.000 description 3
- 231100000252 nontoxic Toxicity 0.000 description 3
- 230000003000 nontoxic effect Effects 0.000 description 3
- 239000012074 organic phase Substances 0.000 description 3
- 239000008188 pellet Substances 0.000 description 3
- 239000013641 positive control Substances 0.000 description 3
- 239000000047 product Substances 0.000 description 3
- 239000011541 reaction mixture Substances 0.000 description 3
- 230000010076 replication Effects 0.000 description 3
- 235000019515 salmon Nutrition 0.000 description 3
- 239000012064 sodium phosphate buffer Substances 0.000 description 3
- YLQBMQCUIZJEEH-UHFFFAOYSA-N tetrahydrofuran Natural products C=1C=COC=1 YLQBMQCUIZJEEH-UHFFFAOYSA-N 0.000 description 3
- DGVVWUTYPXICAM-UHFFFAOYSA-N β‐Mercaptoethanol Chemical compound OCCS DGVVWUTYPXICAM-UHFFFAOYSA-N 0.000 description 3
- QTBSBXVTEAMEQO-UHFFFAOYSA-N Acetic acid Chemical compound CC(O)=O QTBSBXVTEAMEQO-UHFFFAOYSA-N 0.000 description 2
- 108091003079 Bovine Serum Albumin Proteins 0.000 description 2
- 108091026890 Coding region Proteins 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
- 102100031780 Endonuclease Human genes 0.000 description 2
- 102000004190 Enzymes Human genes 0.000 description 2
- 108090000790 Enzymes Proteins 0.000 description 2
- ZHNUHDYFZUAESO-UHFFFAOYSA-N Formamide Chemical compound NC=O ZHNUHDYFZUAESO-UHFFFAOYSA-N 0.000 description 2
- WQZGKKKJIJFFOK-GASJEMHNSA-N Glucose Natural products OC[C@H]1OC(O)[C@H](O)[C@@H](O)[C@@H]1O WQZGKKKJIJFFOK-GASJEMHNSA-N 0.000 description 2
- 239000012981 Hank's balanced salt solution Substances 0.000 description 2
- 108091006905 Human Serum Albumin Proteins 0.000 description 2
- 102000008100 Human Serum Albumin Human genes 0.000 description 2
- CSNNHWWHGAXBCP-UHFFFAOYSA-L Magnesium sulfate Chemical compound [Mg+2].[O-][S+2]([O-])([O-])[O-] CSNNHWWHGAXBCP-UHFFFAOYSA-L 0.000 description 2
- 108020005187 Oligonucleotide Probes Proteins 0.000 description 2
- 108091000080 Phosphotransferase Proteins 0.000 description 2
- DTQVDTLACAAQTR-UHFFFAOYSA-N Trifluoroacetic acid Chemical compound OC(=O)C(F)(F)F DTQVDTLACAAQTR-UHFFFAOYSA-N 0.000 description 2
- 208000036142 Viral infection Diseases 0.000 description 2
- 239000002253 acid Substances 0.000 description 2
- OIRDTQYFTABQOQ-KQYNXXCUSA-N adenosine Chemical compound C1=NC=2C(N)=NC=NC=2N1[C@@H]1O[C@H](CO)[C@@H](O)[C@H]1O OIRDTQYFTABQOQ-KQYNXXCUSA-N 0.000 description 2
- 230000000840 anti-viral effect Effects 0.000 description 2
- 210000003719 b-lymphocyte Anatomy 0.000 description 2
- 229940098773 bovine serum albumin Drugs 0.000 description 2
- 230000010261 cell growth Effects 0.000 description 2
- 238000010367 cloning Methods 0.000 description 2
- 239000012228 culture supernatant Substances 0.000 description 2
- 239000000539 dimer Substances 0.000 description 2
- 239000012153 distilled water Substances 0.000 description 2
- 239000003814 drug Substances 0.000 description 2
- 238000002474 experimental method Methods 0.000 description 2
- 239000000706 filtrate Substances 0.000 description 2
- 238000010353 genetic engineering Methods 0.000 description 2
- 239000001963 growth medium Substances 0.000 description 2
- 238000000338 in vitro Methods 0.000 description 2
- 230000001965 increasing effect Effects 0.000 description 2
- 238000007918 intramuscular administration Methods 0.000 description 2
- 238000007912 intraperitoneal administration Methods 0.000 description 2
- 238000002955 isolation Methods 0.000 description 2
- 238000013507 mapping Methods 0.000 description 2
- 125000001360 methionine group Chemical group N[C@@H](CCSC)C(=O)* 0.000 description 2
- 102000039446 nucleic acids Human genes 0.000 description 2
- 108020004707 nucleic acids Proteins 0.000 description 2
- 150000007523 nucleic acids Chemical class 0.000 description 2
- 239000002751 oligonucleotide probe Substances 0.000 description 2
- 210000000287 oocyte Anatomy 0.000 description 2
- 210000005105 peripheral blood lymphocyte Anatomy 0.000 description 2
- 102000020233 phosphotransferase Human genes 0.000 description 2
- 239000002504 physiological saline solution Substances 0.000 description 2
- 229920002401 polyacrylamide Polymers 0.000 description 2
- 229920006316 polyvinylpyrrolidine Polymers 0.000 description 2
- 230000002829 reductive effect Effects 0.000 description 2
- 238000011160 research Methods 0.000 description 2
- 230000035945 sensitivity Effects 0.000 description 2
- 238000000926 separation method Methods 0.000 description 2
- 238000012163 sequencing technique Methods 0.000 description 2
- 238000007920 subcutaneous administration Methods 0.000 description 2
- 239000000126 substance Substances 0.000 description 2
- 239000006228 supernatant Substances 0.000 description 2
- 230000002194 synthesizing effect Effects 0.000 description 2
- CWERGRDVMFNCDR-UHFFFAOYSA-N thioglycolic acid Chemical compound OC(=O)CS CWERGRDVMFNCDR-UHFFFAOYSA-N 0.000 description 2
- 125000003396 thiol group Chemical group [H]S* 0.000 description 2
- GPRLSGONYQIRFK-MNYXATJNSA-N triton Chemical compound [3H+] GPRLSGONYQIRFK-MNYXATJNSA-N 0.000 description 2
- 230000003612 virological effect Effects 0.000 description 2
- 239000011534 wash buffer Substances 0.000 description 2
- QKNYBSVHEMOAJP-UHFFFAOYSA-N 2-amino-2-(hydroxymethyl)propane-1,3-diol;hydron;chloride Chemical compound Cl.OCC(N)(CO)CO QKNYBSVHEMOAJP-UHFFFAOYSA-N 0.000 description 1
- LJGHYPLBDBRCRZ-UHFFFAOYSA-N 3-(3-aminophenyl)sulfonylaniline Chemical compound NC1=CC=CC(S(=O)(=O)C=2C=C(N)C=CC=2)=C1 LJGHYPLBDBRCRZ-UHFFFAOYSA-N 0.000 description 1
- 241000193830 Bacillus <bacterium> Species 0.000 description 1
- 244000063299 Bacillus subtilis Species 0.000 description 1
- 235000014469 Bacillus subtilis Nutrition 0.000 description 1
- 241000770536 Bacillus thermophilus Species 0.000 description 1
- 241000193388 Bacillus thuringiensis Species 0.000 description 1
- 208000035143 Bacterial infection Diseases 0.000 description 1
- 239000002126 C01EB10 - Adenosine Substances 0.000 description 1
- 108020004638 Circular DNA Proteins 0.000 description 1
- 241000699802 Cricetulus griseus Species 0.000 description 1
- 108050009160 DNA polymerase 1 Proteins 0.000 description 1
- 101100408379 Drosophila melanogaster piwi gene Proteins 0.000 description 1
- 108010042407 Endonucleases Proteins 0.000 description 1
- 241001524679 Escherichia virus M13 Species 0.000 description 1
- 108060002716 Exonuclease Proteins 0.000 description 1
- 206010017533 Fungal infection Diseases 0.000 description 1
- 101001033280 Homo sapiens Cytokine receptor common subunit beta Proteins 0.000 description 1
- 101100232904 Homo sapiens IL2 gene Proteins 0.000 description 1
- 101150103227 IFN gene Proteins 0.000 description 1
- 206010061598 Immunodeficiency Diseases 0.000 description 1
- 208000029462 Immunodeficiency disease Diseases 0.000 description 1
- 108010047761 Interferon-alpha Proteins 0.000 description 1
- 102000006992 Interferon-alpha Human genes 0.000 description 1
- 102000008070 Interferon-gamma Human genes 0.000 description 1
- 108010074328 Interferon-gamma Proteins 0.000 description 1
- 108010002352 Interleukin-1 Proteins 0.000 description 1
- ONIBWKKTOPOVIA-BYPYZUCNSA-N L-Proline Chemical compound OC(=O)[C@@H]1CCCN1 ONIBWKKTOPOVIA-BYPYZUCNSA-N 0.000 description 1
- 102000003960 Ligases Human genes 0.000 description 1
- 108090000364 Ligases Proteins 0.000 description 1
- 102000008072 Lymphokines Human genes 0.000 description 1
- 108010074338 Lymphokines Proteins 0.000 description 1
- 241000699666 Mus <mouse, genus> Species 0.000 description 1
- 241000699670 Mus sp. Species 0.000 description 1
- 208000031888 Mycoses Diseases 0.000 description 1
- 208000030852 Parasitic disease Diseases 0.000 description 1
- 241000364057 Peoria Species 0.000 description 1
- ONIBWKKTOPOVIA-UHFFFAOYSA-N Proline Natural products OC(=O)C1CCCN1 ONIBWKKTOPOVIA-UHFFFAOYSA-N 0.000 description 1
- 102000001253 Protein Kinase Human genes 0.000 description 1
- 208000010362 Protozoan Infections Diseases 0.000 description 1
- 241000589516 Pseudomonas Species 0.000 description 1
- 108010092799 RNA-directed DNA polymerase Proteins 0.000 description 1
- 241000700159 Rattus Species 0.000 description 1
- 240000004808 Saccharomyces cerevisiae Species 0.000 description 1
- 238000012300 Sequence Analysis Methods 0.000 description 1
- 108010071390 Serum Albumin Proteins 0.000 description 1
- 102000007562 Serum Albumin Human genes 0.000 description 1
- VMHLLURERBWHNL-UHFFFAOYSA-M Sodium acetate Chemical compound [Na+].CC([O-])=O VMHLLURERBWHNL-UHFFFAOYSA-M 0.000 description 1
- 229930006000 Sucrose Natural products 0.000 description 1
- CZMRCDWAGMRECN-UGDNZRGBSA-N Sucrose Chemical compound O[C@H]1[C@H](O)[C@@H](CO)O[C@@]1(CO)O[C@@H]1[C@H](O)[C@@H](O)[C@H](O)[C@@H](CO)O1 CZMRCDWAGMRECN-UGDNZRGBSA-N 0.000 description 1
- 210000001744 T-lymphocyte Anatomy 0.000 description 1
- NSOXQYCFHDMMGV-UHFFFAOYSA-N Tetrakis(2-hydroxypropyl)ethylenediamine Chemical compound CC(O)CN(CC(C)O)CCN(CC(C)O)CC(C)O NSOXQYCFHDMMGV-UHFFFAOYSA-N 0.000 description 1
- JZRWCGZRTZMZEH-UHFFFAOYSA-N Thiamine Natural products CC1=C(CCO)SC=[N+]1CC1=CN=C(C)N=C1N JZRWCGZRTZMZEH-UHFFFAOYSA-N 0.000 description 1
- 239000006035 Tryptophane Substances 0.000 description 1
- 108060008682 Tumor Necrosis Factor Proteins 0.000 description 1
- 241000269368 Xenopus laevis Species 0.000 description 1
- 238000002835 absorbance Methods 0.000 description 1
- 229960000583 acetic acid Drugs 0.000 description 1
- 238000003916 acid precipitation Methods 0.000 description 1
- 239000000654 additive Substances 0.000 description 1
- 229960005305 adenosine Drugs 0.000 description 1
- 230000002411 adverse Effects 0.000 description 1
- 230000004075 alteration Effects 0.000 description 1
- 230000003321 amplification Effects 0.000 description 1
- 238000004458 analytical method Methods 0.000 description 1
- 210000004102 animal cell Anatomy 0.000 description 1
- 238000013459 approach Methods 0.000 description 1
- 239000008346 aqueous phase Substances 0.000 description 1
- 229940097012 bacillus thuringiensis Drugs 0.000 description 1
- 208000022362 bacterial infectious disease Diseases 0.000 description 1
- 230000003115 biocidal effect Effects 0.000 description 1
- 230000000903 blocking effect Effects 0.000 description 1
- 239000006285 cell suspension Substances 0.000 description 1
- 238000005119 centrifugation Methods 0.000 description 1
- 238000012512 characterization method Methods 0.000 description 1
- 239000003153 chemical reaction reagent Substances 0.000 description 1
- 239000003638 chemical reducing agent Substances 0.000 description 1
- 210000004978 chinese hamster ovary cell Anatomy 0.000 description 1
- 238000011097 chromatography purification Methods 0.000 description 1
- 208000027618 chronic mucocutaneous candidiasis due to lymphokine deficiency Diseases 0.000 description 1
- 239000013599 cloning vector Substances 0.000 description 1
- 238000004132 cross linking Methods 0.000 description 1
- 230000002559 cytogenic effect Effects 0.000 description 1
- 230000003247 decreasing effect Effects 0.000 description 1
- 238000001514 detection method Methods 0.000 description 1
- 238000011161 development Methods 0.000 description 1
- 239000008121 dextrose Substances 0.000 description 1
- 238000010790 dilution Methods 0.000 description 1
- 239000012895 dilution Substances 0.000 description 1
- LOKCTEFSRHRXRJ-UHFFFAOYSA-I dipotassium trisodium dihydrogen phosphate hydrogen phosphate dichloride Chemical compound P(=O)(O)(O)[O-].[K+].P(=O)(O)([O-])[O-].[Na+].[Na+].[Cl-].[K+].[Cl-].[Na+] LOKCTEFSRHRXRJ-UHFFFAOYSA-I 0.000 description 1
- 230000008034 disappearance Effects 0.000 description 1
- BNIILDVGGAEEIG-UHFFFAOYSA-L disodium hydrogen phosphate Chemical compound [Na+].[Na+].OP([O-])([O-])=O BNIILDVGGAEEIG-UHFFFAOYSA-L 0.000 description 1
- 229910000397 disodium phosphate Inorganic materials 0.000 description 1
- 235000019800 disodium phosphate Nutrition 0.000 description 1
- 125000002228 disulfide group Chemical group 0.000 description 1
- 229940079593 drug Drugs 0.000 description 1
- -1 e.g. Substances 0.000 description 1
- 230000008030 elimination Effects 0.000 description 1
- 238000003379 elimination reaction Methods 0.000 description 1
- 230000002255 enzymatic effect Effects 0.000 description 1
- 238000012869 ethanol precipitation Methods 0.000 description 1
- 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 1
- 229960005542 ethidium bromide Drugs 0.000 description 1
- 210000003527 eukaryotic cell Anatomy 0.000 description 1
- 230000001747 exhibiting effect Effects 0.000 description 1
- 102000013165 exonuclease Human genes 0.000 description 1
- 238000000855 fermentation Methods 0.000 description 1
- 230000004151 fermentation Effects 0.000 description 1
- 210000002950 fibroblast Anatomy 0.000 description 1
- 229940044627 gamma-interferon Drugs 0.000 description 1
- 230000002068 genetic effect Effects 0.000 description 1
- 239000012362 glacial acetic acid Substances 0.000 description 1
- 239000008103 glucose Substances 0.000 description 1
- 125000003147 glycosyl group Chemical group 0.000 description 1
- 230000013595 glycosylation Effects 0.000 description 1
- 238000006206 glycosylation reaction Methods 0.000 description 1
- 239000003102 growth factor Substances 0.000 description 1
- 102000055647 human CSF2RB Human genes 0.000 description 1
- 230000007813 immunodeficiency Effects 0.000 description 1
- 230000001939 inductive effect Effects 0.000 description 1
- 239000004615 ingredient Substances 0.000 description 1
- 229940047124 interferons Drugs 0.000 description 1
- 238000001990 intravenous administration Methods 0.000 description 1
- BAUYGSIQEAFULO-UHFFFAOYSA-L iron(2+) sulfate (anhydrous) Chemical compound [Fe+2].[O-]S([O-])(=O)=O BAUYGSIQEAFULO-UHFFFAOYSA-L 0.000 description 1
- 229910000359 iron(II) sulfate Inorganic materials 0.000 description 1
- 230000000670 limiting effect Effects 0.000 description 1
- 239000007791 liquid phase Substances 0.000 description 1
- 239000006166 lysate Substances 0.000 description 1
- 229920002521 macromolecule Polymers 0.000 description 1
- 229910052943 magnesium sulfate Inorganic materials 0.000 description 1
- 235000019341 magnesium sulphate Nutrition 0.000 description 1
- 239000000463 material Substances 0.000 description 1
- NSDFGJHUGMTLFI-UHFFFAOYSA-N methylaminomethanol tetrahydrochloride Chemical compound Cl.Cl.Cl.Cl.CNCO NSDFGJHUGMTLFI-UHFFFAOYSA-N 0.000 description 1
- 238000007392 microtiter assay Methods 0.000 description 1
- 238000013508 migration Methods 0.000 description 1
- 230000005012 migration Effects 0.000 description 1
- 239000007758 minimum essential medium Substances 0.000 description 1
- 238000002156 mixing Methods 0.000 description 1
- 238000012986 modification Methods 0.000 description 1
- 230000004048 modification Effects 0.000 description 1
- 238000012544 monitoring process Methods 0.000 description 1
- 229910000402 monopotassium phosphate Inorganic materials 0.000 description 1
- OHDXDNUPVVYWOV-UHFFFAOYSA-N n-methyl-1-(2-naphthalen-1-ylsulfanylphenyl)methanamine Chemical compound CNCC1=CC=CC=C1SC1=CC=CC2=CC=CC=C12 OHDXDNUPVVYWOV-UHFFFAOYSA-N 0.000 description 1
- 210000000822 natural killer cell Anatomy 0.000 description 1
- 239000013642 negative control Substances 0.000 description 1
- 238000003199 nucleic acid amplification method Methods 0.000 description 1
- 238000011275 oncology therapy Methods 0.000 description 1
- 230000003287 optical effect Effects 0.000 description 1
- 210000001672 ovary Anatomy 0.000 description 1
- 230000003647 oxidation Effects 0.000 description 1
- 238000007254 oxidation reaction Methods 0.000 description 1
- 230000003071 parasitic effect Effects 0.000 description 1
- 230000036961 partial effect Effects 0.000 description 1
- VLTRZXGMWDSKGL-UHFFFAOYSA-M perchlorate Inorganic materials [O-]Cl(=O)(=O)=O VLTRZXGMWDSKGL-UHFFFAOYSA-M 0.000 description 1
- VLTRZXGMWDSKGL-UHFFFAOYSA-N perchloric acid Chemical compound OCl(=O)(=O)=O VLTRZXGMWDSKGL-UHFFFAOYSA-N 0.000 description 1
- 229920001184 polypeptide Polymers 0.000 description 1
- 229920000036 polyvinylpyrrolidone Polymers 0.000 description 1
- 239000001267 polyvinylpyrrolidone Substances 0.000 description 1
- 235000013855 polyvinylpyrrolidone Nutrition 0.000 description 1
- 239000002244 precipitate Substances 0.000 description 1
- 102000004196 processed proteins & peptides Human genes 0.000 description 1
- 108090000765 processed proteins & peptides Proteins 0.000 description 1
- 108060006633 protein kinase Proteins 0.000 description 1
- 238000000163 radioactive labelling Methods 0.000 description 1
- 102000005962 receptors Human genes 0.000 description 1
- 108020003175 receptors Proteins 0.000 description 1
- 238000010405 reoxidation reaction Methods 0.000 description 1
- 239000011347 resin Substances 0.000 description 1
- 229920005989 resin Polymers 0.000 description 1
- 238000004007 reversed phase HPLC Methods 0.000 description 1
- 150000003355 serines Chemical class 0.000 description 1
- 239000001632 sodium acetate Substances 0.000 description 1
- 235000017281 sodium acetate Nutrition 0.000 description 1
- 239000007974 sodium acetate buffer Substances 0.000 description 1
- 239000007787 solid Substances 0.000 description 1
- 230000003381 solubilizing effect Effects 0.000 description 1
- LXMSZDCAJNLERA-ZHYRCANASA-N spironolactone Chemical compound C([C@@H]1[C@]2(C)CC[C@@H]3[C@@]4(C)CCC(=O)C=C4C[C@H]([C@@H]13)SC(=O)C)C[C@@]21CCC(=O)O1 LXMSZDCAJNLERA-ZHYRCANASA-N 0.000 description 1
- 230000000087 stabilizing effect Effects 0.000 description 1
- 238000006467 substitution reaction Methods 0.000 description 1
- 239000005720 sucrose Substances 0.000 description 1
- 239000000725 suspension Substances 0.000 description 1
- 238000012360 testing method Methods 0.000 description 1
- WROMPOXWARCANT-UHFFFAOYSA-N tfa trifluoroacetic acid Chemical compound OC(=O)C(F)(F)F.OC(=O)C(F)(F)F WROMPOXWARCANT-UHFFFAOYSA-N 0.000 description 1
- 229940124597 therapeutic agent Drugs 0.000 description 1
- 235000019157 thiamine Nutrition 0.000 description 1
- KYMBYSLLVAOCFI-UHFFFAOYSA-N thiamine Chemical compound CC1=C(CCO)SCN1CC1=CN=C(C)N=C1N KYMBYSLLVAOCFI-UHFFFAOYSA-N 0.000 description 1
- 229960003495 thiamine Drugs 0.000 description 1
- 239000011721 thiamine Substances 0.000 description 1
- 230000000699 topical effect Effects 0.000 description 1
- 239000001226 triphosphate Substances 0.000 description 1
- 235000011178 triphosphate Nutrition 0.000 description 1
- UNXRWKVEANCORM-UHFFFAOYSA-N triphosphoric acid Chemical compound OP(O)(=O)OP(O)(=O)OP(O)(O)=O UNXRWKVEANCORM-UHFFFAOYSA-N 0.000 description 1
- 102000003390 tumor necrosis factor Human genes 0.000 description 1
- 210000003462 vein Anatomy 0.000 description 1
- 230000009385 viral infection Effects 0.000 description 1
Classifications
-
- C—CHEMISTRY; METALLURGY
- C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
- C12N—MICROORGANISMS OR ENZYMES; COMPOSITIONS THEREOF; PROPAGATING, PRESERVING, OR MAINTAINING MICROORGANISMS; MUTATION OR GENETIC ENGINEERING; CULTURE MEDIA
- C12N15/00—Mutation or genetic engineering; DNA or RNA concerning genetic engineering, vectors, e.g. plasmids, or their isolation, preparation or purification; Use of hosts therefor
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K14/00—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof
- C07K14/435—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from animals; from humans
- C07K14/52—Cytokines; Lymphokines; Interferons
- C07K14/54—Interleukins [IL]
- C07K14/55—IL-2
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P31/00—Antiinfectives, i.e. antibiotics, antiseptics, chemotherapeutics
- A61P31/12—Antivirals
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P35/00—Antineoplastic agents
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P37/00—Drugs for immunological or allergic disorders
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K14/00—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof
- C07K14/435—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from animals; from humans
- C07K14/52—Cytokines; Lymphokines; Interferons
- C07K14/555—Interferons [IFN]
- C07K14/565—IFN-beta
-
- C—CHEMISTRY; METALLURGY
- C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
- C12N—MICROORGANISMS OR ENZYMES; COMPOSITIONS THEREOF; PROPAGATING, PRESERVING, OR MAINTAINING MICROORGANISMS; MUTATION OR GENETIC ENGINEERING; CULTURE MEDIA
- C12N15/00—Mutation or genetic engineering; DNA or RNA concerning genetic engineering, vectors, e.g. plasmids, or their isolation, preparation or purification; Use of hosts therefor
- C12N15/09—Recombinant DNA-technology
- C12N15/10—Processes for the isolation, preparation or purification of DNA or RNA
- C12N15/102—Mutagenizing nucleic acids
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61K—PREPARATIONS FOR MEDICAL, DENTAL OR TOILETRY PURPOSES
- A61K38/00—Medicinal preparations containing peptides
-
- Y—GENERAL TAGGING OF NEW TECHNOLOGICAL DEVELOPMENTS; GENERAL TAGGING OF CROSS-SECTIONAL TECHNOLOGIES SPANNING OVER SEVERAL SECTIONS OF THE IPC; TECHNICAL SUBJECTS COVERED BY FORMER USPC CROSS-REFERENCE ART COLLECTIONS [XRACs] AND DIGESTS
- Y10—TECHNICAL SUBJECTS COVERED BY FORMER USPC
- Y10S—TECHNICAL SUBJECTS COVERED BY FORMER USPC CROSS-REFERENCE ART COLLECTIONS [XRACs] AND DIGESTS
- Y10S530/00—Chemistry: natural resins or derivatives; peptides or proteins; lignins or reaction products thereof
- Y10S530/808—Materials and products related to genetic engineering or hybrid or fused cell technology, e.g. hybridoma, monoclonal products
- Y10S530/809—Fused cells, e.g. hybridoma
-
- Y—GENERAL TAGGING OF NEW TECHNOLOGICAL DEVELOPMENTS; GENERAL TAGGING OF CROSS-SECTIONAL TECHNOLOGIES SPANNING OVER SEVERAL SECTIONS OF THE IPC; TECHNICAL SUBJECTS COVERED BY FORMER USPC CROSS-REFERENCE ART COLLECTIONS [XRACs] AND DIGESTS
- Y10—TECHNICAL SUBJECTS COVERED BY FORMER USPC
- Y10S—TECHNICAL SUBJECTS COVERED BY FORMER USPC CROSS-REFERENCE ART COLLECTIONS [XRACs] AND DIGESTS
- Y10S930/00—Peptide or protein sequence
- Y10S930/01—Peptide or protein sequence
- Y10S930/14—Lymphokine; related peptides
- Y10S930/141—Interleukin
-
- Y—GENERAL TAGGING OF NEW TECHNOLOGICAL DEVELOPMENTS; GENERAL TAGGING OF CROSS-SECTIONAL TECHNOLOGIES SPANNING OVER SEVERAL SECTIONS OF THE IPC; TECHNICAL SUBJECTS COVERED BY FORMER USPC CROSS-REFERENCE ART COLLECTIONS [XRACs] AND DIGESTS
- Y10—TECHNICAL SUBJECTS COVERED BY FORMER USPC
- Y10S—TECHNICAL SUBJECTS COVERED BY FORMER USPC CROSS-REFERENCE ART COLLECTIONS [XRACs] AND DIGESTS
- Y10S930/00—Peptide or protein sequence
- Y10S930/01—Peptide or protein sequence
- Y10S930/14—Lymphokine; related peptides
- Y10S930/142—Interferon
Landscapes
- Health & Medical Sciences (AREA)
- Life Sciences & Earth Sciences (AREA)
- Chemical & Material Sciences (AREA)
- Organic Chemistry (AREA)
- Genetics & Genomics (AREA)
- Engineering & Computer Science (AREA)
- General Health & Medical Sciences (AREA)
- Zoology (AREA)
- Medicinal Chemistry (AREA)
- Bioinformatics & Cheminformatics (AREA)
- Biomedical Technology (AREA)
- Biochemistry (AREA)
- Biophysics (AREA)
- General Engineering & Computer Science (AREA)
- Molecular Biology (AREA)
- Wood Science & Technology (AREA)
- Biotechnology (AREA)
- Pharmacology & Pharmacy (AREA)
- General Chemical & Material Sciences (AREA)
- Nuclear Medicine, Radiotherapy & Molecular Imaging (AREA)
- Chemical Kinetics & Catalysis (AREA)
- Animal Behavior & Ethology (AREA)
- Veterinary Medicine (AREA)
- Public Health (AREA)
- Microbiology (AREA)
- Proteomics, Peptides & Aminoacids (AREA)
- Gastroenterology & Hepatology (AREA)
- Toxicology (AREA)
- Plant Pathology (AREA)
- Physics & Mathematics (AREA)
- Virology (AREA)
- Oncology (AREA)
- Communicable Diseases (AREA)
- Crystallography & Structural Chemistry (AREA)
- Immunology (AREA)
- Preparation Of Compounds By Using Micro-Organisms (AREA)
- Medicines That Contain Protein Lipid Enzymes And Other Medicines (AREA)
- Peptides Or Proteins (AREA)
- Micro-Organisms Or Cultivation Processes Thereof (AREA)
- Medicines Containing Material From Animals Or Micro-Organisms (AREA)
Priority Applications (1)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| BG096076A BG60510B2 (bg) | 1983-10-10 | 1992-03-16 | Структурни гени,плазмиди и трансформирани клетки за получаване на бедни на цистеин мутеини на биологично активни протеини |
Applications Claiming Priority (2)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| US43515482A | 1982-10-19 | 1982-10-19 | |
| US48616283A | 1983-04-15 | 1983-04-15 |
Publications (2)
| Publication Number | Publication Date |
|---|---|
| IE832380L IE832380L (en) | 1984-04-19 |
| IE56026B1 true IE56026B1 (en) | 1991-03-27 |
Family
ID=27030446
Family Applications (1)
| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| IE2380/83A IE56026B1 (en) | 1982-10-19 | 1983-10-10 | Cysteine-depleted muteins of biologically active proteins |
Country Status (23)
| Country | Link |
|---|---|
| EP (4) | EP0192811B1 (cg-RX-API-DMAC7.html) |
| JP (2) | JPS6128392A (cg-RX-API-DMAC7.html) |
| KR (1) | KR910009900B1 (cg-RX-API-DMAC7.html) |
| AT (4) | ATE73493T1 (cg-RX-API-DMAC7.html) |
| AU (1) | AU563962B2 (cg-RX-API-DMAC7.html) |
| BE (1) | BE898016A (cg-RX-API-DMAC7.html) |
| CA (1) | CA1340861C (cg-RX-API-DMAC7.html) |
| CH (1) | CH669395A5 (cg-RX-API-DMAC7.html) |
| DE (4) | DE3376271D1 (cg-RX-API-DMAC7.html) |
| DK (2) | DK168767B1 (cg-RX-API-DMAC7.html) |
| ES (4) | ES526541A0 (cg-RX-API-DMAC7.html) |
| FI (1) | FI82266C (cg-RX-API-DMAC7.html) |
| FR (1) | FR2534594B1 (cg-RX-API-DMAC7.html) |
| GB (1) | GB2130219B (cg-RX-API-DMAC7.html) |
| GR (1) | GR79408B (cg-RX-API-DMAC7.html) |
| IE (1) | IE56026B1 (cg-RX-API-DMAC7.html) |
| IL (1) | IL69970A (cg-RX-API-DMAC7.html) |
| LU (3) | LU88761I2 (cg-RX-API-DMAC7.html) |
| NL (2) | NL930119I2 (cg-RX-API-DMAC7.html) |
| NO (1) | NO173740C (cg-RX-API-DMAC7.html) |
| NZ (1) | NZ205922A (cg-RX-API-DMAC7.html) |
| PH (2) | PH20343A (cg-RX-API-DMAC7.html) |
| PT (1) | PT77512B (cg-RX-API-DMAC7.html) |
Families Citing this family (125)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| FI82266C (fi) * | 1982-10-19 | 1991-02-11 | Cetus Corp | Foerfarande foer framstaellning av il-2 -mutein. |
| DK265384A (da) * | 1983-06-01 | 1984-12-02 | Hoffmann La Roche | Polypeptider med interferonaktivitet |
| WO1985000817A1 (en) * | 1983-08-10 | 1985-02-28 | Amgen | Microbial expression of interleukin ii |
| GB8334102D0 (en) * | 1983-12-21 | 1984-02-01 | Searle & Co | Interferons with cysteine pattern |
| DE3575072D1 (de) | 1984-03-28 | 1990-02-08 | Cetus Corp | Pharmazeutische zusammensetzungen von mikrobenerzeugtem interleukin-2. |
| US4530787A (en) * | 1984-03-28 | 1985-07-23 | Cetus Corporation | Controlled oxidation of microbially produced cysteine-containing proteins |
| EP0163603B1 (en) * | 1984-05-08 | 1989-12-13 | Genetics Institute, Inc. | A human t-cell growth factor |
| GB8412564D0 (en) * | 1984-05-17 | 1984-06-20 | Searle & Co | Structure and properties |
| US5683688A (en) * | 1984-05-31 | 1997-11-04 | Genentech, Inc. | Unglycosylated recombinant human lymphotoxin polypeptides and compositions |
| NZ212207A (en) * | 1984-05-31 | 1991-07-26 | Genentech Inc | Recombinant lymphotoxin |
| US5672347A (en) * | 1984-07-05 | 1997-09-30 | Genentech, Inc. | Tumor necrosis factor antagonists and their use |
| CA1275954C (en) | 1984-08-31 | 1990-11-06 | Hing Cheug Wong | 3'-expression enhancing fragments and method |
| WO1986002068A1 (fr) * | 1984-09-26 | 1986-04-10 | Takeda Chemical Industries, Ltd. | Separation mutuelle de proteines |
| IL76360A0 (en) | 1984-09-26 | 1986-01-31 | Takeda Chemical Industries Ltd | Mutual separation of proteins |
| US4857316A (en) * | 1984-10-03 | 1989-08-15 | Syntex (U.S.A.) Inc. | Synergistic antiviral composition |
| US4606917A (en) * | 1984-10-03 | 1986-08-19 | Syntex (U.S.A) Inc. | Synergistic antiviral composition |
| US4959314A (en) | 1984-11-09 | 1990-09-25 | Cetus Corporation | Cysteine-depleted muteins of biologically active proteins |
| US4572798A (en) * | 1984-12-06 | 1986-02-25 | Cetus Corporation | Method for promoting disulfide bond formation in recombinant proteins |
| US6107465A (en) * | 1984-12-21 | 2000-08-22 | Otsuka Pharmaceutical Co., Ltd. | IL-1β and derivatives thereof and drugs |
| US5342614A (en) * | 1984-12-21 | 1994-08-30 | Otsuka Pharmaceutical Co., Ltd. | Method of treating arthritus or inflammation with IL-1β or derivatives thereof |
| DK172052B1 (da) * | 1984-12-21 | 1997-09-29 | Otsuka Pharma Co Ltd | Antitumor-aktivt stof, fremgangsmåde til dets fremstilling, lægemiddel indeholdende stoffet, gen kodende for stoffet, vektor indeholdende genet samt rekombinant mikroorganisme transformet med en sådan vektor |
| DE3500681A1 (de) * | 1985-01-11 | 1986-07-17 | Hoechst Ag, 6230 Frankfurt | Verfahren zur isolierung und reinigung von lymphokinen |
| US4863849A (en) * | 1985-07-18 | 1989-09-05 | New York Medical College | Automatable process for sequencing nucleotide |
| US4810643A (en) * | 1985-08-23 | 1989-03-07 | Kirin- Amgen Inc. | Production of pluripotent granulocyte colony-stimulating factor |
| US6004548A (en) | 1985-08-23 | 1999-12-21 | Amgen, Inc. | Analogs of pluripotent granulocyte colony-stimulating factor |
| CA1297003C (en) * | 1985-09-20 | 1992-03-10 | Jack H. Nunberg | Composition and method for treating animals |
| US5359035A (en) * | 1985-12-21 | 1994-10-25 | Hoechst Aktiengesellschaft | Bifunctional proteins including interleukin-2 (IL-2) and granuloctyte macrophage colony stimulating factor (GM-CSF) |
| US5008374A (en) * | 1986-03-14 | 1991-04-16 | Otsuka Pharmaceutical Co., Ltd. | IL-1α derivatives and drugs |
| AU595864B2 (en) * | 1986-03-14 | 1990-04-12 | Otsuka Pharmaceutical Co., Ltd. | Il-1 alpha derivatives and drugs |
| ATE72582T1 (de) * | 1986-09-05 | 1992-02-15 | Cetus Corp | Oxidationsresistente muteine von beta-interferon, deren herstellung und diese muteine enthaltende praeparate. |
| JP2526965B2 (ja) * | 1987-02-24 | 1996-08-21 | 武田薬品工業株式会社 | ムテイン，ｄｎａおよびその用途 |
| US4987070A (en) * | 1987-03-04 | 1991-01-22 | Suntory Limited | Use of a 97 amino acid leader sequence from the E. coli B-galactosidase gene for the production of hanp and hptc as fusion proteins |
| AU629176B2 (en) * | 1987-07-07 | 1992-10-01 | Scios Nova Inc. | Recombinant fibroblast growth factors |
| AU625394B2 (en) * | 1987-11-04 | 1992-07-09 | Byk Gulden Lomberg Chemische Fabrik Gmbh | Alveolar surfactant proteins |
| DE68929273T2 (de) * | 1988-08-24 | 2001-07-05 | American Cyanamid Co., Wayne | Stabilisierung von Somatotropinen durch Modifikation von Cystein-Resten durch orts-spezifische Mutagenese oder chemische Derivatisierung |
| US5079230A (en) * | 1988-09-12 | 1992-01-07 | Pitman-Moore, Inc. | Stable bioactive somatotropins |
| CA2003886A1 (en) * | 1988-12-16 | 1990-06-16 | Anthony F. Purchio | Cloning and expression of simian transforming growth factor-beta 1 |
| EP0456642A1 (en) * | 1989-01-31 | 1991-11-21 | The Upjohn Company | Somatotropin analogs |
| ATE133993T1 (de) * | 1989-02-17 | 1996-02-15 | Merck & Co Inc | Protein-antikrebsmittel |
| US5621078A (en) * | 1989-03-22 | 1997-04-15 | Merck & Co., Inc. | Modified pseudomonas exotoxin PE40 |
| AU5355790A (en) * | 1989-04-19 | 1990-11-16 | Cetus Corporation | Multifunctional m-csf proteins and genes encoding therefor |
| US6207798B1 (en) | 1989-08-03 | 2001-03-27 | Merck & Co., Inc. | Modified PE40 toxin fusion proteins |
| US5173297A (en) * | 1991-07-01 | 1992-12-22 | Quest International Flavors & Food Ingredients Company Division Of Indopco, Inc. | Bacteriocin from lactococcus lactis subspecies lactis |
| IL98528A0 (en) * | 1990-06-21 | 1992-07-15 | Merck & Co Inc | Pharmaceutical compositions containing hybrid for killing bladder cancer cells |
| FR2671554A1 (fr) * | 1991-01-11 | 1992-07-17 | Clonatec Sa | Peptides synthetiques derivant de l'antigene hbc du virus de l'hepatite b, leurs applications a la detection d'une infection par ce virus et a la vaccination contre l'hepatite b. |
| FR2686899B1 (fr) | 1992-01-31 | 1995-09-01 | Rhone Poulenc Rorer Sa | Nouveaux polypeptides biologiquement actifs, leur preparation et compositions pharmaceutiques les contenant. |
| US5545723A (en) * | 1994-03-15 | 1996-08-13 | Biogen Inc. | Muteins of IFN-β |
| US5814485A (en) * | 1995-06-06 | 1998-09-29 | Chiron Corporation | Production of interferon-β (IFN-β) in E. coli |
| DE19544167A1 (de) * | 1995-11-17 | 1997-05-22 | Schering Ag | Verwendung von Interferon-ß zur Behandlung von Bronchialkarzinom bei Bestrahlungstherapie |
| AU6399996A (en) * | 1996-06-19 | 1998-01-07 | Chiron Corporation | Bacterial production of interferon-beta using low levels of sodium and potassium ions |
| CN1100875C (zh) * | 1998-03-06 | 2003-02-05 | 上海华晨生物技术研究所 | 新型重组人白细胞介素2的制备方法及其表达载体和工程菌 |
| EP1983055A1 (en) | 2000-04-12 | 2008-10-22 | Human Genome Sciences, Inc. | Albumin fusion proteins |
| EP1935431A3 (en) | 2000-05-15 | 2008-08-13 | Health Research, Inc. | Cancer treatments by using a combination of an antibody against her2 and interleukin-2 |
| DE10112825A1 (de) | 2001-03-16 | 2002-10-02 | Fresenius Kabi De Gmbh | HESylierung von Wirkstoffen in wässriger Lösung |
| US6887462B2 (en) | 2001-04-09 | 2005-05-03 | Chiron Corporation | HSA-free formulations of interferon-beta |
| AU2002326991A1 (en) * | 2001-09-18 | 2003-04-01 | Chiron Corporation | Methods for treating multiple sclerosis |
| KR100511749B1 (ko) * | 2001-11-06 | 2005-09-02 | 선바이오(주) | 변형된 인터페론-베타, 및 이의 화학적으로 변형된 배합체 |
| EP2261250B1 (en) | 2001-12-21 | 2015-07-01 | Human Genome Sciences, Inc. | GCSF-Albumin fusion proteins |
| WO2005003296A2 (en) | 2003-01-22 | 2005-01-13 | Human Genome Sciences, Inc. | Albumin fusion proteins |
| DE10209822A1 (de) | 2002-03-06 | 2003-09-25 | Biotechnologie Ges Mittelhesse | Kopplung niedermolekularer Substanzen an ein modifiziertes Polysaccharid |
| DE10209821A1 (de) | 2002-03-06 | 2003-09-25 | Biotechnologie Ges Mittelhesse | Kopplung von Proteinen an ein modifiziertes Polysaccharid |
| CA2496317C (en) | 2002-09-11 | 2014-02-18 | Fresenius Kabi Deutschland Gmbh | Method of producing hydroxyalkyl starch derivatives |
| US7538092B2 (en) | 2002-10-08 | 2009-05-26 | Fresenius Kabi Deutschland Gmbh | Pharmaceutically active oligosaccharide conjugates |
| WO2005014655A2 (en) | 2003-08-08 | 2005-02-17 | Fresenius Kabi Deutschland Gmbh | Conjugates of hydroxyalkyl starch and a protein |
| WO2005044294A2 (en) | 2003-11-04 | 2005-05-19 | Chiron Corporation | Method of therapy for cancers expressing the cd40 antigen |
| JP2007527242A (ja) * | 2004-03-05 | 2007-09-27 | カイロン コーポレーション | 治療剤の患者耐容性を予測するためのインビトロ試験システム |
| BRPI0508607A (pt) | 2004-03-11 | 2007-07-31 | Fresenius Kabi De Gmbh | conjugados de amido de hidroxialquila e uma proteìna, preparados pela aminação redutiva |
| US7642072B2 (en) * | 2004-07-26 | 2010-01-05 | Enzon Pharmaceuticals, Inc. | Optimized interferon-beta gene |
| GB0523282D0 (en) | 2005-11-15 | 2005-12-21 | Isis Innovation | Methods using pores |
| GB2453377A (en) | 2007-10-05 | 2009-04-08 | Isis Innovation | Transmembrane protein pores and molecular adapters therefore. |
| EP2070950A1 (en) | 2007-12-14 | 2009-06-17 | Fresenius Kabi Deutschland GmbH | Hydroxyalkyl starch derivatives and process for their preparation |
| ATE548052T1 (de) | 2008-01-17 | 2012-03-15 | Philogen Spa | Kombination aus einem anti-edb-fibronectin- antikörper-il-2-fusionsprotein und einem b-zellen bindenden molekül, b-zellen-vorläufern und/oder deren krebserregendem gegenspieler |
| US20110229877A1 (en) | 2008-07-07 | 2011-09-22 | Oxford Nanopore Technologies Limited | Enzyme-pore constructs |
| WO2010004273A1 (en) | 2008-07-07 | 2010-01-14 | Oxford Nanopore Technologies Limited | Base-detecting pore |
| US9077937B2 (en) * | 2008-11-06 | 2015-07-07 | Alcatel Lucent | Method and apparatus for fast channel change |
| GB0820927D0 (en) | 2008-11-14 | 2008-12-24 | Isis Innovation | Method |
| KR101797773B1 (ko) | 2009-01-30 | 2017-11-15 | 옥스포드 나노포어 테크놀로지즈 리미티드 | 막횡단 시퀀싱에서 핵산 구축물용 어댑터 |
| CN102482330A (zh) | 2009-01-30 | 2012-05-30 | 牛津纳米孔技术有限公司 | 酶突变体 |
| GB0905140D0 (en) | 2009-03-25 | 2009-05-06 | Isis Innovation | Method |
| AU2012215135B9 (en) | 2011-02-11 | 2017-03-09 | Oxford Nanopore Technologies Limited | Mutant pores |
| AU2012228418B2 (en) | 2011-03-11 | 2016-09-29 | Assistance Publique - Hopitaux De Paris | Use of low dose IL-2 for treating autoimmune - related or inflammatory disorders |
| CA2843136C (en) | 2011-07-25 | 2020-12-29 | Oxford Nanopore Technologies Limited | Hairpin loop method for double strand polynucleotide sequencing using transmembrane pores |
| GB201119244D0 (en) | 2011-11-08 | 2011-12-21 | British American Tobacco Co | Smoking article |
| KR102083695B1 (ko) | 2012-04-10 | 2020-03-02 | 옥스포드 나노포어 테크놀로지즈 리미티드 | 돌연변이체 리세닌 기공 |
| US11155860B2 (en) | 2012-07-19 | 2021-10-26 | Oxford Nanopore Technologies Ltd. | SSB method |
| SG11201507138RA (en) | 2013-03-08 | 2015-10-29 | Oxford Nanopore Tech Ltd | Enzyme stalling method |
| GB201314695D0 (en) | 2013-08-16 | 2013-10-02 | Oxford Nanopore Tech Ltd | Method |
| GB201313477D0 (en) | 2013-07-29 | 2013-09-11 | Univ Leuven Kath | Nanopore biosensors for detection of proteins and nucleic acids |
| WO2014206899A1 (en) | 2013-06-25 | 2014-12-31 | Icm (Institut Du Cerveau Et De La Moelle Épinière) | Boosting treg cells for treating alzheimer disease and related disorders |
| GB201403096D0 (en) | 2014-02-21 | 2014-04-09 | Oxford Nanopore Tech Ltd | Sample preparation method |
| EP2918285A1 (en) | 2014-03-11 | 2015-09-16 | Université Pierre et Marie Curie (Paris 6) | Interleukin-2 for treating food allergy |
| US10443097B2 (en) | 2014-05-02 | 2019-10-15 | Oxford Nanopore Technologies Ltd. | Method of improving the movement of a target polynucleotide with respect to a transmembrane pore |
| CN117164683A (zh) | 2014-09-01 | 2023-12-05 | 弗拉芒区生物技术研究所 | 突变csgg孔 |
| EP3204511B1 (en) | 2014-10-07 | 2021-07-28 | Oxford Nanopore Technologies Limited | Mutant pores |
| GB201418159D0 (en) | 2014-10-14 | 2014-11-26 | Oxford Nanopore Tech Ltd | Method |
| WO2016172445A2 (en) * | 2015-04-24 | 2016-10-27 | The University Of Florida Research Foundation, Inc. | Methods of identifying biologically active random peptides in plants and libraries of plants expressing candidate biologically active random peptides |
| US10876109B2 (en) | 2015-04-24 | 2020-12-29 | University Of Florida Research Foundation, Inc. | Methods of identifying biologically active random peptides in prokaryotic cells and libraries of prokaryotic cells expressing candidate biologically active random peptides |
| US10801023B2 (en) * | 2015-04-24 | 2020-10-13 | University Of Florida Research Foundation, Inc. | Methods of identifying biologically active random peptides in plants and libraries of plants expressing candidate biologically active random peptides |
| KR102740102B1 (ko) | 2015-10-22 | 2024-12-06 | 일투 파마 | Il-2의 약학 조성물 |
| GB201609220D0 (en) | 2016-05-25 | 2016-07-06 | Oxford Nanopore Tech Ltd | Method |
| AU2017281469B2 (en) | 2016-06-22 | 2023-08-31 | David Klatzmann | Genetically modified T lymphocytes |
| AU2018234810B2 (en) | 2017-03-15 | 2023-05-11 | Pandion Operations, Inc. | Targeted immunotolerance |
| SG11201909949XA (en) | 2017-05-24 | 2019-11-28 | Pandion Therapeutics Inc | Targeted immunotolerance |
| US10946068B2 (en) | 2017-12-06 | 2021-03-16 | Pandion Operations, Inc. | IL-2 muteins and uses thereof |
| US10174092B1 (en) | 2017-12-06 | 2019-01-08 | Pandion Therapeutics, Inc. | IL-2 muteins |
| USRE50550E1 (en) | 2017-12-06 | 2025-08-26 | Pandion Operations, Inc. | IL-2 muteins and uses thereof |
| US11534479B2 (en) | 2018-02-16 | 2022-12-27 | Iltoo Pharma | Use of interleukin 2 for treating Sjögren's syndrome |
| GB201807793D0 (en) | 2018-05-14 | 2018-06-27 | Oxford Nanopore Tech Ltd | Method |
| WO2019241315A1 (en) | 2018-06-12 | 2019-12-19 | Obsidian Therapeutics, Inc. | Pde5 derived regulatory constructs and methods of use in immunotherapy |
| WO2020007937A1 (en) | 2018-07-03 | 2020-01-09 | Iltoo Pharma | Use of interleukin-2 for treating systemic sclerosis |
| EP3836954B1 (en) | 2018-08-13 | 2025-05-07 | Iltoo Pharma | Combination of interleukin-2 with an interleukin 1 inhibitor, conjugates and therapeutic uses thereof |
| EP3880838B1 (en) | 2018-11-15 | 2024-12-25 | The Board of Trustees of the Leland Stanford Junior University | Compositions and methods of prognosis and classification for preeclampsia |
| KR20220035333A (ko) | 2019-05-20 | 2022-03-22 | 팬디온 오퍼레이션스, 인코포레이티드 | Madcam 표적 면역관용 |
| WO2021116444A1 (en) | 2019-12-12 | 2021-06-17 | Iltoo Pharma | Interleukin 2 chimeric constructs |
| US11981715B2 (en) | 2020-02-21 | 2024-05-14 | Pandion Operations, Inc. | Tissue targeted immunotolerance with a CD39 effector |
| AU2021230103A1 (en) | 2020-03-06 | 2022-09-22 | Assistance Publique - Hopitaux De Paris | Low dose human interleukin-2 for the treatment of amyotrophic lateral sclerosis |
| CN116075523A (zh) * | 2020-04-29 | 2023-05-05 | 基因制药株式会社 | 具有融合的干扰素-β突变蛋白和抗体的重组蛋白以及包含其的药物组合物 |
| BR112022022035A2 (pt) * | 2020-04-29 | 2023-01-03 | Abion Inc | Interferon-beta humano variante, polinucleotídeo, vetor de expressão, célula animal transformada, métodos para preparar um interferon-beta humano variante, melhorar a estabilidade de um interferon-beta r27t humano variante e tratar uma doença, composição farmacêutica e uso |
| KR20230092880A (ko) * | 2020-08-28 | 2023-06-26 | 조인트 스탁 컴퍼니 "바이오케드" | AAV5-기반의 SARS-CoV-2 백신 |
| CA3233644A1 (en) | 2021-10-06 | 2023-04-13 | David Klatzmann | Interleukin 2 chimeric constructs with targeting specificy to inflamed tissues |
| WO2023226873A1 (en) * | 2022-05-24 | 2023-11-30 | Jhm Biopharmaceutical (Hangzhou) Co., Ltd. | Recombinant botulinum neurotoxin of type a and preparation method thereof |
| WO2023245097A2 (en) | 2022-06-16 | 2023-12-21 | Cephalon Llc | Anti-pd-1 antibody-attenuated il-2 immunoconjugates and uses thereof |
| AU2022477937A1 (en) | 2022-09-12 | 2025-04-10 | Assistance Publique - Hôpitaux De Paris | Interleukin-2 for use in treating autism spectrum disorder |
| EP4630035A1 (en) | 2022-12-05 | 2025-10-15 | Centre Hospitalier Universitaire de Nimes | Low dose human interleukin-2 for the treatment of amyotrophic lateral sclerosis in a subgroup of patients |
| WO2025032158A1 (en) | 2023-08-08 | 2025-02-13 | Institut National de la Santé et de la Recherche Médicale | Method to treat tauopathies |
Family Cites Families (9)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| JPS5359688A (en) * | 1976-11-11 | 1978-05-29 | Tanpakushitsu Kenkiyuu Shiyour | Production of novel polypeptide |
| US4399216A (en) * | 1980-02-25 | 1983-08-16 | The Trustees Of Columbia University | Processes for inserting DNA into eucaryotic cells and for producing proteinaceous materials |
| NO811118L (no) * | 1980-04-03 | 1981-10-05 | Biogen Nv | Dna-sekvenser, rekombinante dna-molekyler og fremgangsmaate ved fremstilling av polypeptider |
| JPS58110548A (ja) * | 1981-12-24 | 1983-07-01 | Asahi Chem Ind Co Ltd | 新規な生理活性ペプチド |
| US6936694B1 (en) * | 1982-05-06 | 2005-08-30 | Intermune, Inc. | Manufacture and expression of large structural genes |
| FI82266C (fi) * | 1982-10-19 | 1991-02-11 | Cetus Corp | Foerfarande foer framstaellning av il-2 -mutein. |
| DK265384A (da) * | 1983-06-01 | 1984-12-02 | Hoffmann La Roche | Polypeptider med interferonaktivitet |
| WO1985000817A1 (en) * | 1983-08-10 | 1985-02-28 | Amgen | Microbial expression of interleukin ii |
| US4959314A (en) * | 1984-11-09 | 1990-09-25 | Cetus Corporation | Cysteine-depleted muteins of biologically active proteins |
-
1983
- 1983-10-10 FI FI833681A patent/FI82266C/fi not_active IP Right Cessation
- 1983-10-10 IE IE2380/83A patent/IE56026B1/en active Protection Beyond IP Right Term
- 1983-10-11 NZ NZ205922A patent/NZ205922A/en unknown
- 1983-10-12 AU AU20086/83A patent/AU563962B2/en not_active Expired
- 1983-10-12 PH PH29685A patent/PH20343A/en unknown
- 1983-10-12 CA CA000438878A patent/CA1340861C/en not_active Expired - Lifetime
- 1983-10-13 EP EP85109295A patent/EP0192811B1/en not_active Expired - Lifetime
- 1983-10-13 GB GB08327490A patent/GB2130219B/en not_active Expired
- 1983-10-13 LU LU88761C patent/LU88761I2/fr unknown
- 1983-10-13 EP EP87103350A patent/EP0234599B1/en not_active Expired - Lifetime
- 1983-10-13 DE DE8383306221T patent/DE3376271D1/de not_active Expired
- 1983-10-13 DE DE8686110595T patent/DE3380598D1/de not_active Expired
- 1983-10-13 AT AT87103350T patent/ATE73493T1/de not_active IP Right Cessation
- 1983-10-13 AT AT86110595T patent/ATE46539T1/de active
- 1983-10-13 DE DE8787103350T patent/DE3382528D1/de not_active Expired - Lifetime
- 1983-10-13 DE DE8585109295T patent/DE3382197D1/de not_active Expired - Lifetime
- 1983-10-13 EP EP83306221A patent/EP0109748B1/en not_active Expired
- 1983-10-13 AT AT83306221T patent/ATE33503T1/de not_active IP Right Cessation
- 1983-10-13 AT AT85109295T patent/ATE61407T1/de not_active IP Right Cessation
- 1983-10-13 EP EP86110595A patent/EP0218825B1/en not_active Expired
- 1983-10-14 IL IL69970A patent/IL69970A/xx not_active IP Right Cessation
- 1983-10-17 PT PT77512A patent/PT77512B/pt unknown
- 1983-10-17 GR GR72712A patent/GR79408B/el unknown
- 1983-10-18 BE BE0/211722A patent/BE898016A/fr not_active IP Right Cessation
- 1983-10-18 CH CH5667/83A patent/CH669395A5/fr not_active IP Right Cessation
- 1983-10-18 NO NO833793A patent/NO173740C/no not_active IP Right Cessation
- 1983-10-18 ES ES526541A patent/ES526541A0/es active Granted
- 1983-10-18 KR KR1019830004927A patent/KR910009900B1/ko not_active Expired
- 1983-10-18 FR FR8316543A patent/FR2534594B1/fr not_active Expired
- 1983-10-19 DK DK481383A patent/DK168767B1/da not_active IP Right Cessation
-
1984
- 1984-06-01 ES ES533054A patent/ES8506801A1/es not_active Expired
- 1984-06-01 ES ES533053A patent/ES533053A0/es active Granted
- 1984-09-08 JP JP18730184A patent/JPS6128392A/ja active Granted
-
1985
- 1985-05-03 ES ES542829A patent/ES8608043A1/es not_active Expired
-
1986
- 1986-03-13 PH PH33519A patent/PH23702A/en unknown
-
1988
- 1988-03-14 JP JP63058544A patent/JPS6420096A/ja active Pending
-
1992
- 1992-08-26 DK DK105892A patent/DK171681B1/da not_active IP Right Cessation
-
1993
- 1993-06-30 NL NL930119C patent/NL930119I2/nl unknown
- 1993-07-01 LU LU88357C patent/LU88357I2/fr unknown
-
1996
- 1996-05-29 NL NL960013C patent/NL960013I2/nl unknown
-
1999
- 1999-07-07 LU LU90413C patent/LU90413I2/fr unknown
Also Published As
Similar Documents
| Publication | Publication Date | Title |
|---|---|---|
| EP0192811B1 (en) | Cysteine-depleted muteins of biologically active proteins, their preparation, formulations containing them, and structural genes, vectors and organisms, and their production, suitable for use in the preparation of said muteins | |
| US4853332A (en) | Structural genes, plasmids and transformed cells for producing cysteine depleted muteins of biologically active proteins | |
| US4518584A (en) | Human recombinant interleukin-2 muteins | |
| US4588585A (en) | Human recombinant cysteine depleted interferon-β muteins | |
| US4959314A (en) | Cysteine-depleted muteins of biologically active proteins | |
| US4737462A (en) | Structural genes, plasmids and transformed cells for producing cysteine depleted muteins of interferon-β | |
| FI86559C (fi) | Foerfarande foer framstaellning av humant immuninterferon, daervid anvaendbara medel och dessas framstaellning. | |
| US4753795A (en) | Modified (80-113) beta interferons | |
| EP0187991B1 (en) | Antitumor active substance, process for preparing the same, drug containing the substance, gene coding for the substance, vector containing the gene and recombinant microorganism | |
| PL149079B1 (en) | Method of obtaining polypeptides of ifn-beta type | |
| JPH0240080B2 (cg-RX-API-DMAC7.html) | ||
| JPH057996B2 (cg-RX-API-DMAC7.html) | ||
| US4761375A (en) | Human interleukin-2 cDNA sequence | |
| EP0163603B1 (en) | A human t-cell growth factor | |
| FI87233B (fi) | Gen vilken kodar en mutein. | |
| BG60510B2 (bg) | Структурни гени,плазмиди и трансформирани клетки за получаване на бедни на цистеин мутеини на биологично активни протеини | |
| BG60506B2 (bg) | Човешки рекомбинантни интерлевкин-2 мутеини | |
| NO306951B1 (no) | DNA-sekvens som koder for et modifisert human-IFM-(beta) samt fremgangsmåte for fremstilling derav |
Legal Events
| Date | Code | Title | Description |
|---|---|---|---|
| SPCF | Request for grant of supplementary protection certificate |
Free format text: SPC 67/93:19930629 |
|
| SPCG | Supplementary protection certificate granted |
Free format text: SPC 67/93 EXPIRES:20040702 |
|
| SPCF | Request for grant of supplementary protection certificate |
Free format text: SPC 11/96 19960530 |
|
| SPCG | Supplementary protection certificate granted |
Free format text: SPC 11/96 EXPIRES:20081009 |
|
| SPCF | Request for grant of supplementary protection certificate |
Free format text: SPC 11/99, 19990602 |
|
| MK9A | Patent expired | ||
| SPCW | Supplementary protection certificate withdrawn |
Spc suppl protection certif: SPC011/1999 |