CA2638772A1 - Genetically programmed expression of proteins containing the unnatural amino acid phenylselenocysteine - Google Patents
Genetically programmed expression of proteins containing the unnatural amino acid phenylselenocysteine Download PDFInfo
- Publication number
- CA2638772A1 CA2638772A1 CA002638772A CA2638772A CA2638772A1 CA 2638772 A1 CA2638772 A1 CA 2638772A1 CA 002638772 A CA002638772 A CA 002638772A CA 2638772 A CA2638772 A CA 2638772A CA 2638772 A1 CA2638772 A1 CA 2638772A1
- Authority
- CA
- Canada
- Prior art keywords
- trna
- amino acid
- protein
- unnatural amino
- phenylselenocysteine
- 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.)
- Abandoned
Links
- 150000001413 amino acids Chemical class 0.000 title claims abstract description 419
- 108090000623 proteins and genes Proteins 0.000 title claims abstract description 276
- 102000004169 proteins and genes Human genes 0.000 title claims abstract description 253
- FXTLFZWJXBBXGX-QMMMGPOBSA-N (2R)-2-anilino-3-selanylpropanoic acid Chemical compound OC(=O)[C@H](C[SeH])NC1=CC=CC=C1 FXTLFZWJXBBXGX-QMMMGPOBSA-N 0.000 title claims abstract description 107
- 230000014509 gene expression Effects 0.000 title description 13
- 238000000034 method Methods 0.000 claims abstract description 185
- 238000013519 translation Methods 0.000 claims abstract description 136
- 108091033319 polynucleotide Proteins 0.000 claims abstract description 123
- 102000040430 polynucleotide Human genes 0.000 claims abstract description 123
- 239000002157 polynucleotide Substances 0.000 claims abstract description 122
- 102000052866 Amino Acyl-tRNA Synthetases Human genes 0.000 claims abstract description 78
- 108700028939 Amino Acyl-tRNA Synthetases Proteins 0.000 claims abstract description 78
- 241000588724 Escherichia coli Species 0.000 claims abstract description 37
- 241001112695 Clostridiales Species 0.000 claims abstract description 16
- 108020004705 Codon Proteins 0.000 claims description 208
- 150000007523 nucleic acids Chemical class 0.000 claims description 120
- 102000039446 nucleic acids Human genes 0.000 claims description 113
- 108020004707 nucleic acids Proteins 0.000 claims description 113
- 108090000765 processed proteins & peptides Proteins 0.000 claims description 107
- 102000004196 processed proteins & peptides Human genes 0.000 claims description 105
- 229920001184 polypeptide Polymers 0.000 claims description 104
- 239000000203 mixture Substances 0.000 claims description 55
- 238000004519 manufacturing process Methods 0.000 claims description 36
- UQBOJOOOTLPNST-UHFFFAOYSA-N Dehydroalanine Chemical compound NC(=C)C(O)=O UQBOJOOOTLPNST-UHFFFAOYSA-N 0.000 claims description 32
- 230000004044 response Effects 0.000 claims description 27
- 239000013598 vector Substances 0.000 claims description 25
- 108091060545 Nonsense suppressor Proteins 0.000 claims description 20
- MHAJPDPJQMAIIY-UHFFFAOYSA-N Hydrogen peroxide Chemical compound OO MHAJPDPJQMAIIY-UHFFFAOYSA-N 0.000 claims description 16
- 239000002773 nucleotide Substances 0.000 claims description 16
- 125000003729 nucleotide group Chemical group 0.000 claims description 16
- 238000007248 oxidative elimination reaction Methods 0.000 claims description 10
- CFISTOPZXSTQOS-SFHVURJKSA-N (2r)-2-amino-3-hexadecylsulfanylpropanoic acid Chemical compound CCCCCCCCCCCCCCCCSC[C@H](N)C(O)=O CFISTOPZXSTQOS-SFHVURJKSA-N 0.000 claims description 8
- 238000002741 site-directed mutagenesis Methods 0.000 claims description 8
- 239000013604 expression vector Substances 0.000 claims description 7
- YYHOQQKJSHXDEN-KRWDZBQOSA-N N-palmitoyl-L-cysteine Chemical compound CCCCCCCCCCCCCCCC(=O)N[C@@H](CS)C(O)=O YYHOQQKJSHXDEN-KRWDZBQOSA-N 0.000 claims description 6
- 238000006845 Michael addition reaction Methods 0.000 claims description 5
- SYSLNQMKLROGCL-BCYUYYMPSA-N S-[(2E,6E)-farnesyl]-L-cysteine zwitterion Chemical compound CC(C)=CCC\C(C)=C\CC\C(C)=C\CSC[C@H](N)C(O)=O SYSLNQMKLROGCL-BCYUYYMPSA-N 0.000 claims description 4
- ORTRWBYBJVGVQC-UHFFFAOYSA-N hexadecane-1-thiol Chemical compound CCCCCCCCCCCCCCCCS ORTRWBYBJVGVQC-UHFFFAOYSA-N 0.000 claims description 4
- KPUXJBYSYFEKKB-UHFFFAOYSA-N hexadecanethioic s-acid Chemical compound CCCCCCCCCCCCCCCC(S)=O KPUXJBYSYFEKKB-UHFFFAOYSA-N 0.000 claims description 4
- CJWPDADGDASKGI-YFVJMOTDSA-N (2e,6e)-3,7,11-trimethyldodeca-2,6,10-triene-1-thiol Chemical compound CC(C)=CCC\C(C)=C\CC\C(C)=C\CS CJWPDADGDASKGI-YFVJMOTDSA-N 0.000 claims description 3
- 238000012258 culturing Methods 0.000 claims description 2
- 125000003473 lipid group Chemical group 0.000 claims 3
- 102000003960 Ligases Human genes 0.000 abstract description 76
- 108090000364 Ligases Proteins 0.000 abstract description 76
- 230000004048 modification Effects 0.000 abstract description 28
- 238000012986 modification Methods 0.000 abstract description 28
- 102000035118 modified proteins Human genes 0.000 abstract description 2
- 108091005573 modified proteins Proteins 0.000 abstract description 2
- 235000001014 amino acid Nutrition 0.000 description 391
- 229940024606 amino acid Drugs 0.000 description 387
- 235000018102 proteins Nutrition 0.000 description 209
- 210000004027 cell Anatomy 0.000 description 181
- 108020004566 Transfer RNA Proteins 0.000 description 155
- 230000014616 translation Effects 0.000 description 108
- 238000001727 in vivo Methods 0.000 description 52
- 238000010348 incorporation Methods 0.000 description 47
- 239000003550 marker Substances 0.000 description 45
- 230000002068 genetic effect Effects 0.000 description 43
- 230000001629 suppression Effects 0.000 description 43
- 125000003275 alpha amino acid group Chemical group 0.000 description 38
- 102000004190 Enzymes Human genes 0.000 description 35
- 108090000790 Enzymes Proteins 0.000 description 35
- 229940088598 enzyme Drugs 0.000 description 34
- 238000006243 chemical reaction Methods 0.000 description 32
- 238000009396 hybridization Methods 0.000 description 32
- 238000002703 mutagenesis Methods 0.000 description 32
- 231100000350 mutagenesis Toxicity 0.000 description 32
- 241000894006 Bacteria Species 0.000 description 31
- 241000894007 species Species 0.000 description 30
- -1 e.g. Substances 0.000 description 29
- 230000006870 function Effects 0.000 description 26
- 238000000338 in vitro Methods 0.000 description 26
- 108020004414 DNA Proteins 0.000 description 25
- 239000000523 sample Substances 0.000 description 24
- 238000012216 screening Methods 0.000 description 23
- 230000000295 complement effect Effects 0.000 description 22
- 108020005038 Terminator Codon Proteins 0.000 description 21
- 230000000694 effects Effects 0.000 description 20
- 239000000126 substance Substances 0.000 description 18
- 230000015572 biosynthetic process Effects 0.000 description 17
- 230000035772 mutation Effects 0.000 description 17
- 238000006467 substitution reaction Methods 0.000 description 17
- 238000003556 assay Methods 0.000 description 16
- 238000012360 testing method Methods 0.000 description 16
- 230000008569 process Effects 0.000 description 15
- 238000003786 synthesis reaction Methods 0.000 description 15
- 230000037361 pathway Effects 0.000 description 13
- 239000013612 plasmid Substances 0.000 description 13
- 230000001225 therapeutic effect Effects 0.000 description 13
- 230000001965 increasing effect Effects 0.000 description 12
- 150000002632 lipids Chemical group 0.000 description 12
- 108091028043 Nucleic acid sequence Proteins 0.000 description 11
- 230000006229 amino acid addition Effects 0.000 description 11
- 229960004441 tyrosine Drugs 0.000 description 11
- 238000013459 approach Methods 0.000 description 10
- 239000003795 chemical substances by application Substances 0.000 description 10
- 235000002374 tyrosine Nutrition 0.000 description 10
- 108091032973 (ribonucleotides)n+m Proteins 0.000 description 9
- 241000203069 Archaea Species 0.000 description 9
- 241000203407 Methanocaldococcus jannaschii Species 0.000 description 9
- 230000003115 biocidal effect Effects 0.000 description 9
- 239000000758 substrate Substances 0.000 description 9
- 241000206602 Eukaryota Species 0.000 description 8
- 102000002265 Human Growth Hormone Human genes 0.000 description 8
- 108010000521 Human Growth Hormone Proteins 0.000 description 8
- 239000000854 Human Growth Hormone Substances 0.000 description 8
- 108020004485 Nonsense Codon Proteins 0.000 description 8
- 101710146427 Probable tyrosine-tRNA ligase, cytoplasmic Proteins 0.000 description 8
- 102000018378 Tyrosine-tRNA ligase Human genes 0.000 description 8
- 101710107268 Tyrosine-tRNA ligase, mitochondrial Proteins 0.000 description 8
- 230000006696 biosynthetic metabolic pathway Effects 0.000 description 8
- 230000001413 cellular effect Effects 0.000 description 8
- 101150066555 lacZ gene Proteins 0.000 description 8
- 108020004999 messenger RNA Proteins 0.000 description 8
- 238000013518 transcription Methods 0.000 description 8
- 108020005098 Anticodon Proteins 0.000 description 7
- 241000196324 Embryophyta Species 0.000 description 7
- 108010043121 Green Fluorescent Proteins Proteins 0.000 description 7
- 102000004144 Green Fluorescent Proteins Human genes 0.000 description 7
- 238000007792 addition Methods 0.000 description 7
- 230000004071 biological effect Effects 0.000 description 7
- 230000008859 change Effects 0.000 description 7
- 239000003153 chemical reaction reagent Substances 0.000 description 7
- 150000001875 compounds Chemical class 0.000 description 7
- 230000021615 conjugation Effects 0.000 description 7
- 239000005090 green fluorescent protein Substances 0.000 description 7
- 230000007246 mechanism Effects 0.000 description 7
- 239000012528 membrane Substances 0.000 description 7
- 238000006011 modification reaction Methods 0.000 description 7
- 230000004481 post-translational protein modification Effects 0.000 description 7
- 230000002829 reductive effect Effects 0.000 description 7
- 238000012552 review Methods 0.000 description 7
- 230000035897 transcription Effects 0.000 description 7
- OUYCCCASQSFEME-UHFFFAOYSA-N tyrosine Natural products OC(=O)C(N)CC1=CC=C(O)C=C1 OUYCCCASQSFEME-UHFFFAOYSA-N 0.000 description 7
- 108010035563 Chloramphenicol O-acetyltransferase Proteins 0.000 description 6
- 241000205062 Halobacterium Species 0.000 description 6
- 241000238631 Hexapoda Species 0.000 description 6
- OUYCCCASQSFEME-QMMMGPOBSA-N L-tyrosine Chemical compound OC(=O)[C@@H](N)CC1=CC=C(O)C=C1 OUYCCCASQSFEME-QMMMGPOBSA-N 0.000 description 6
- 240000004808 Saccharomyces cerevisiae Species 0.000 description 6
- 241000700605 Viruses Species 0.000 description 6
- 230000029226 lipidation Effects 0.000 description 6
- 238000010369 molecular cloning Methods 0.000 description 6
- 230000009145 protein modification Effects 0.000 description 6
- 231100000331 toxic Toxicity 0.000 description 6
- 230000002588 toxic effect Effects 0.000 description 6
- 108010016529 Bacillus amyloliquefaciens ribonuclease Proteins 0.000 description 5
- 241000233866 Fungi Species 0.000 description 5
- OAKJQQAXSVQMHS-UHFFFAOYSA-N Hydrazine Chemical compound NN OAKJQQAXSVQMHS-UHFFFAOYSA-N 0.000 description 5
- HNDVDQJCIGZPNO-YFKPBYRVSA-N L-histidine Chemical compound OC(=O)[C@@H](N)CC1=CN=CN1 HNDVDQJCIGZPNO-YFKPBYRVSA-N 0.000 description 5
- 108091034117 Oligonucleotide Proteins 0.000 description 5
- 125000000539 amino acid group Chemical group 0.000 description 5
- 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 5
- 229960000723 ampicillin Drugs 0.000 description 5
- 230000001851 biosynthetic effect Effects 0.000 description 5
- 238000010276 construction Methods 0.000 description 5
- 230000001186 cumulative effect Effects 0.000 description 5
- 230000001419 dependent effect Effects 0.000 description 5
- 210000003527 eukaryotic cell Anatomy 0.000 description 5
- 230000037433 frameshift Effects 0.000 description 5
- HNDVDQJCIGZPNO-UHFFFAOYSA-N histidine Natural products OC(=O)C(N)CC1=CN=CN1 HNDVDQJCIGZPNO-UHFFFAOYSA-N 0.000 description 5
- 229910052739 hydrogen Inorganic materials 0.000 description 5
- 239000001257 hydrogen Substances 0.000 description 5
- 230000001976 improved effect Effects 0.000 description 5
- 239000003262 industrial enzyme Substances 0.000 description 5
- 238000003780 insertion Methods 0.000 description 5
- 230000037431 insertion Effects 0.000 description 5
- 230000000269 nucleophilic effect Effects 0.000 description 5
- 235000008729 phenylalanine Nutrition 0.000 description 5
- 238000002708 random mutagenesis Methods 0.000 description 5
- 150000003668 tyrosines Chemical class 0.000 description 5
- 210000005253 yeast cell Anatomy 0.000 description 5
- 239000004475 Arginine Substances 0.000 description 4
- 244000063299 Bacillus subtilis Species 0.000 description 4
- 235000014469 Bacillus subtilis Nutrition 0.000 description 4
- 102000053602 DNA Human genes 0.000 description 4
- 102000018233 Fibroblast Growth Factor Human genes 0.000 description 4
- 108050007372 Fibroblast Growth Factor Proteins 0.000 description 4
- WSFSSNUMVMOOMR-UHFFFAOYSA-N Formaldehyde Chemical compound O=C WSFSSNUMVMOOMR-UHFFFAOYSA-N 0.000 description 4
- 108090000723 Insulin-Like Growth Factor I Proteins 0.000 description 4
- XUJNEKJLAYXESH-REOHCLBHSA-N L-Cysteine Chemical compound SC[C@H](N)C(O)=O XUJNEKJLAYXESH-REOHCLBHSA-N 0.000 description 4
- ODKSFYDXXFIFQN-BYPYZUCNSA-P L-argininium(2+) Chemical compound NC(=[NH2+])NCCC[C@H]([NH3+])C(O)=O ODKSFYDXXFIFQN-BYPYZUCNSA-P 0.000 description 4
- DCXYFEDJOCDNAF-REOHCLBHSA-N L-asparagine Chemical compound OC(=O)[C@@H](N)CC(N)=O DCXYFEDJOCDNAF-REOHCLBHSA-N 0.000 description 4
- KDXKERNSBIXSRK-UHFFFAOYSA-N Lysine Natural products NCCCCC(N)C(O)=O KDXKERNSBIXSRK-UHFFFAOYSA-N 0.000 description 4
- 239000004472 Lysine Substances 0.000 description 4
- 108020004711 Nucleic Acid Probes Proteins 0.000 description 4
- 108091005461 Nucleic proteins Proteins 0.000 description 4
- ISAKRJDGNUQOIC-UHFFFAOYSA-N Uracil Chemical compound O=C1C=CNC(=O)N1 ISAKRJDGNUQOIC-UHFFFAOYSA-N 0.000 description 4
- 239000002253 acid Substances 0.000 description 4
- 235000004279 alanine Nutrition 0.000 description 4
- 238000004458 analytical method Methods 0.000 description 4
- ODKSFYDXXFIFQN-UHFFFAOYSA-N arginine Natural products OC(=O)C(N)CCCNC(N)=N ODKSFYDXXFIFQN-UHFFFAOYSA-N 0.000 description 4
- 235000009697 arginine Nutrition 0.000 description 4
- 230000008901 benefit Effects 0.000 description 4
- 239000000872 buffer Substances 0.000 description 4
- 230000003197 catalytic effect Effects 0.000 description 4
- XUJNEKJLAYXESH-UHFFFAOYSA-N cysteine Natural products SCC(N)C(O)=O XUJNEKJLAYXESH-UHFFFAOYSA-N 0.000 description 4
- 235000018417 cysteine Nutrition 0.000 description 4
- 239000003814 drug Substances 0.000 description 4
- 230000002255 enzymatic effect Effects 0.000 description 4
- 229940126864 fibroblast growth factor Drugs 0.000 description 4
- 239000012634 fragment Substances 0.000 description 4
- 150000002308 glutamine derivatives Chemical class 0.000 description 4
- 239000002853 nucleic acid probe Substances 0.000 description 4
- 239000013641 positive control Substances 0.000 description 4
- 230000006798 recombination Effects 0.000 description 4
- 238000005215 recombination Methods 0.000 description 4
- 125000001424 substituent group Chemical group 0.000 description 4
- 230000002103 transcriptional effect Effects 0.000 description 4
- 241000205042 Archaeoglobus fulgidus Species 0.000 description 3
- 241000193830 Bacillus <bacterium> Species 0.000 description 3
- 241000195493 Cryptophyta Species 0.000 description 3
- WHUUTDBJXJRKMK-GSVOUGTGSA-N D-glutamic acid Chemical compound OC(=O)[C@H](N)CCC(O)=O WHUUTDBJXJRKMK-GSVOUGTGSA-N 0.000 description 3
- 108090000385 Fibroblast growth factor 7 Proteins 0.000 description 3
- 102000003972 Fibroblast growth factor 7 Human genes 0.000 description 3
- WHUUTDBJXJRKMK-UHFFFAOYSA-N Glutamic acid Natural products OC(=O)C(N)CCC(O)=O WHUUTDBJXJRKMK-UHFFFAOYSA-N 0.000 description 3
- 102100039620 Granulocyte-macrophage colony-stimulating factor Human genes 0.000 description 3
- 241000204933 Haloferax volcanii Species 0.000 description 3
- 101000611183 Homo sapiens Tumor necrosis factor Proteins 0.000 description 3
- 102000008100 Human Serum Albumin Human genes 0.000 description 3
- 108091006905 Human Serum Albumin Proteins 0.000 description 3
- 108091092195 Intron Proteins 0.000 description 3
- QNAYBMKLOCPYGJ-REOHCLBHSA-N L-alanine Chemical compound C[C@H](N)C(O)=O QNAYBMKLOCPYGJ-REOHCLBHSA-N 0.000 description 3
- KDXKERNSBIXSRK-YFKPBYRVSA-N L-lysine Chemical compound NCCCC[C@H](N)C(O)=O KDXKERNSBIXSRK-YFKPBYRVSA-N 0.000 description 3
- COLNVLDHVKWLRT-QMMMGPOBSA-N L-phenylalanine Chemical compound OC(=O)[C@@H](N)CC1=CC=CC=C1 COLNVLDHVKWLRT-QMMMGPOBSA-N 0.000 description 3
- 241000124008 Mammalia Species 0.000 description 3
- 241001465754 Metazoa Species 0.000 description 3
- 241001529871 Methanococcus maripaludis Species 0.000 description 3
- 241000204641 Methanopyrus kandleri Species 0.000 description 3
- 241000205274 Methanosarcina mazei Species 0.000 description 3
- 241000699670 Mus sp. Species 0.000 description 3
- 108010062374 Myoglobin Proteins 0.000 description 3
- 102100030856 Myoglobin Human genes 0.000 description 3
- 241000736843 Pyrobaculum aerophilum Species 0.000 description 3
- 241001148023 Pyrococcus abyssi Species 0.000 description 3
- 241000205156 Pyrococcus furiosus Species 0.000 description 3
- 241000522615 Pyrococcus horikoshii Species 0.000 description 3
- 102000013275 Somatomedins Human genes 0.000 description 3
- 241000205091 Sulfolobus solfataricus Species 0.000 description 3
- 241000160715 Sulfolobus tokodaii Species 0.000 description 3
- 241000204673 Thermoplasma acidophilum Species 0.000 description 3
- 241000489996 Thermoplasma volcanium Species 0.000 description 3
- 108060008683 Tumor Necrosis Factor Receptor Proteins 0.000 description 3
- 102100040247 Tumor necrosis factor Human genes 0.000 description 3
- 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 3
- 235000008206 alpha-amino acids Nutrition 0.000 description 3
- 239000003242 anti bacterial agent Substances 0.000 description 3
- 125000003118 aryl group Chemical group 0.000 description 3
- 229960001230 asparagine Drugs 0.000 description 3
- 125000000151 cysteine group Chemical group N[C@@H](CS)C(=O)* 0.000 description 3
- 238000012217 deletion Methods 0.000 description 3
- 230000037430 deletion Effects 0.000 description 3
- 241001493065 dsRNA viruses Species 0.000 description 3
- 230000007613 environmental effect Effects 0.000 description 3
- 230000007717 exclusion Effects 0.000 description 3
- 230000006801 homologous recombination Effects 0.000 description 3
- 238000002744 homologous recombination Methods 0.000 description 3
- 230000002757 inflammatory effect Effects 0.000 description 3
- 239000011159 matrix material Substances 0.000 description 3
- 238000012269 metabolic engineering Methods 0.000 description 3
- 239000002184 metal Substances 0.000 description 3
- 229910052751 metal Inorganic materials 0.000 description 3
- 244000005700 microbiome Species 0.000 description 3
- COLNVLDHVKWLRT-UHFFFAOYSA-N phenylalanine Natural products OC(=O)C(N)CC1=CC=CC=C1 COLNVLDHVKWLRT-UHFFFAOYSA-N 0.000 description 3
- 229960005190 phenylalanine Drugs 0.000 description 3
- 229920000570 polyether Polymers 0.000 description 3
- 230000004850 protein–protein interaction Effects 0.000 description 3
- 230000010076 replication Effects 0.000 description 3
- 238000011160 research Methods 0.000 description 3
- 210000003705 ribosome Anatomy 0.000 description 3
- 230000035945 sensitivity Effects 0.000 description 3
- 230000004083 survival effect Effects 0.000 description 3
- 125000003396 thiol group Chemical group [H]S* 0.000 description 3
- 231100000765 toxin Toxicity 0.000 description 3
- 239000003053 toxin Substances 0.000 description 3
- 108700012359 toxins Proteins 0.000 description 3
- 102000003298 tumor necrosis factor receptor Human genes 0.000 description 3
- 238000011179 visual inspection Methods 0.000 description 3
- 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 2
- PFLVUZBNZZOUSS-QMMMGPOBSA-N (2r)-2-amino-3-phenylselanylpropanoic acid Chemical compound OC(=O)[C@@H](N)C[Se]C1=CC=CC=C1 PFLVUZBNZZOUSS-QMMMGPOBSA-N 0.000 description 2
- FBTSQILOGYXGMD-LURJTMIESA-N 3-nitro-L-tyrosine Chemical compound OC(=O)[C@@H](N)CC1=CC=C(O)C([N+]([O-])=O)=C1 FBTSQILOGYXGMD-LURJTMIESA-N 0.000 description 2
- CMUHFUGDYMFHEI-QMMMGPOBSA-N 4-amino-L-phenylalanine Chemical compound OC(=O)[C@@H](N)CC1=CC=C(N)C=C1 CMUHFUGDYMFHEI-QMMMGPOBSA-N 0.000 description 2
- 102000007698 Alcohol dehydrogenase Human genes 0.000 description 2
- 108010021809 Alcohol dehydrogenase Proteins 0.000 description 2
- 244000105975 Antidesma platyphyllum Species 0.000 description 2
- CIWBSHSKHKDKBQ-JLAZNSOCSA-N Ascorbic acid Chemical compound OC[C@H](O)[C@H]1OC(=O)C(O)=C1O CIWBSHSKHKDKBQ-JLAZNSOCSA-N 0.000 description 2
- DCXYFEDJOCDNAF-UHFFFAOYSA-N Asparagine Natural products OC(=O)C(N)CC(N)=O DCXYFEDJOCDNAF-UHFFFAOYSA-N 0.000 description 2
- IJGRMHOSHXDMSA-UHFFFAOYSA-N Atomic nitrogen Chemical compound N#N IJGRMHOSHXDMSA-UHFFFAOYSA-N 0.000 description 2
- 102100021943 C-C motif chemokine 2 Human genes 0.000 description 2
- 101710155857 C-C motif chemokine 2 Proteins 0.000 description 2
- 108010071942 Colony-Stimulating Factors Proteins 0.000 description 2
- 241000192700 Cyanobacteria Species 0.000 description 2
- 102000004127 Cytokines Human genes 0.000 description 2
- 108090000695 Cytokines Proteins 0.000 description 2
- 108010014303 DNA-directed DNA polymerase Proteins 0.000 description 2
- 102000016928 DNA-directed DNA polymerase Human genes 0.000 description 2
- 102000004163 DNA-directed RNA polymerases Human genes 0.000 description 2
- 108090000626 DNA-directed RNA polymerases Proteins 0.000 description 2
- RTZKZFJDLAIYFH-UHFFFAOYSA-N Diethyl ether Chemical compound CCOCC RTZKZFJDLAIYFH-UHFFFAOYSA-N 0.000 description 2
- 241000186394 Eubacterium Species 0.000 description 2
- DHMQDGOQFOQNFH-UHFFFAOYSA-N Glycine Chemical compound NCC(O)=O DHMQDGOQFOQNFH-UHFFFAOYSA-N 0.000 description 2
- 108090000100 Hepatocyte Growth Factor Proteins 0.000 description 2
- 102100021866 Hepatocyte growth factor Human genes 0.000 description 2
- 102000007625 Hirudins Human genes 0.000 description 2
- 108010007267 Hirudins Proteins 0.000 description 2
- AVXURJPOCDRRFD-UHFFFAOYSA-N Hydroxylamine Chemical compound ON AVXURJPOCDRRFD-UHFFFAOYSA-N 0.000 description 2
- 108010021625 Immunoglobulin Fragments Proteins 0.000 description 2
- 108700005091 Immunoglobulin Genes Proteins 0.000 description 2
- 101000668058 Infectious salmon anemia virus (isolate Atlantic salmon/Norway/810/9/99) RNA-directed RNA polymerase catalytic subunit Proteins 0.000 description 2
- 108010050904 Interferons Proteins 0.000 description 2
- 102000014150 Interferons Human genes 0.000 description 2
- 108010002352 Interleukin-1 Proteins 0.000 description 2
- 108010002350 Interleukin-2 Proteins 0.000 description 2
- 108090001007 Interleukin-8 Proteins 0.000 description 2
- 108010063738 Interleukins Proteins 0.000 description 2
- 102000015696 Interleukins Human genes 0.000 description 2
- CKLJMWTZIZZHCS-REOHCLBHSA-N L-aspartic acid Chemical compound OC(=O)[C@@H](N)CC(O)=O CKLJMWTZIZZHCS-REOHCLBHSA-N 0.000 description 2
- ZDXPYRJPNDTMRX-VKHMYHEASA-N L-glutamine Chemical compound OC(=O)[C@@H](N)CCC(N)=O ZDXPYRJPNDTMRX-VKHMYHEASA-N 0.000 description 2
- AGPKZVBTJJNPAG-WHFBIAKZSA-N L-isoleucine Chemical compound CC[C@H](C)[C@H](N)C(O)=O AGPKZVBTJJNPAG-WHFBIAKZSA-N 0.000 description 2
- ROHFNLRQFUQHCH-YFKPBYRVSA-N L-leucine Chemical compound CC(C)C[C@H](N)C(O)=O ROHFNLRQFUQHCH-YFKPBYRVSA-N 0.000 description 2
- FFEARJCKVFRZRR-BYPYZUCNSA-N L-methionine Chemical compound CSCC[C@H](N)C(O)=O FFEARJCKVFRZRR-BYPYZUCNSA-N 0.000 description 2
- AYFVYJQAPQTCCC-GBXIJSLDSA-N L-threonine Chemical compound C[C@@H](O)[C@H](N)C(O)=O AYFVYJQAPQTCCC-GBXIJSLDSA-N 0.000 description 2
- QIVBCDIJIAJPQS-VIFPVBQESA-N L-tryptophane Chemical compound C1=CC=C2C(C[C@H](N)C(O)=O)=CNC2=C1 QIVBCDIJIAJPQS-VIFPVBQESA-N 0.000 description 2
- KZSNJWFQEVHDMF-BYPYZUCNSA-N L-valine Chemical compound CC(C)[C@H](N)C(O)=O KZSNJWFQEVHDMF-BYPYZUCNSA-N 0.000 description 2
- ROHFNLRQFUQHCH-UHFFFAOYSA-N Leucine Natural products CC(C)CC(N)C(O)=O ROHFNLRQFUQHCH-UHFFFAOYSA-N 0.000 description 2
- 102000003820 Lipoxygenases Human genes 0.000 description 2
- 108090000128 Lipoxygenases Proteins 0.000 description 2
- OFOBLEOULBTSOW-UHFFFAOYSA-L Malonate Chemical compound [O-]C(=O)CC([O-])=O OFOBLEOULBTSOW-UHFFFAOYSA-L 0.000 description 2
- 241001302042 Methanothermobacter thermautotrophicus Species 0.000 description 2
- 108700020796 Oncogene Proteins 0.000 description 2
- 102000043276 Oncogene Human genes 0.000 description 2
- 108091005804 Peptidases Proteins 0.000 description 2
- 239000002202 Polyethylene glycol Substances 0.000 description 2
- 239000004721 Polyphenylene oxide Substances 0.000 description 2
- RJKFOVLPORLFTN-LEKSSAKUSA-N Progesterone Chemical compound C1CC2=CC(=O)CC[C@]2(C)[C@@H]2[C@@H]1[C@@H]1CC[C@H](C(=O)C)[C@@]1(C)CC2 RJKFOVLPORLFTN-LEKSSAKUSA-N 0.000 description 2
- 239000004365 Protease Substances 0.000 description 2
- 102000007056 Recombinant Fusion Proteins Human genes 0.000 description 2
- 108010008281 Recombinant Fusion Proteins Proteins 0.000 description 2
- BUGBHKTXTAQXES-UHFFFAOYSA-N Selenium Chemical compound [Se] BUGBHKTXTAQXES-UHFFFAOYSA-N 0.000 description 2
- 102000019197 Superoxide Dismutase Human genes 0.000 description 2
- 108010012715 Superoxide dismutase Proteins 0.000 description 2
- MUMGGOZAMZWBJJ-DYKIIFRCSA-N Testostosterone Chemical compound O=C1CC[C@]2(C)[C@H]3CC[C@](C)([C@H](CC4)O)[C@@H]4[C@@H]3CCC2=C1 MUMGGOZAMZWBJJ-DYKIIFRCSA-N 0.000 description 2
- 241000589596 Thermus Species 0.000 description 2
- 241000589499 Thermus thermophilus Species 0.000 description 2
- AYFVYJQAPQTCCC-UHFFFAOYSA-N Threonine Natural products CC(O)C(N)C(O)=O AYFVYJQAPQTCCC-UHFFFAOYSA-N 0.000 description 2
- 239000004473 Threonine Substances 0.000 description 2
- QIVBCDIJIAJPQS-UHFFFAOYSA-N Tryptophan Natural products C1=CC=C2C(CC(N)C(O)=O)=CNC2=C1 QIVBCDIJIAJPQS-UHFFFAOYSA-N 0.000 description 2
- KZSNJWFQEVHDMF-UHFFFAOYSA-N Valine Natural products CC(C)C(N)C(O)=O KZSNJWFQEVHDMF-UHFFFAOYSA-N 0.000 description 2
- 150000007513 acids Chemical class 0.000 description 2
- 230000003213 activating effect Effects 0.000 description 2
- 239000002671 adjuvant Substances 0.000 description 2
- 125000000304 alkynyl group Chemical group 0.000 description 2
- 150000001371 alpha-amino acids Chemical class 0.000 description 2
- 230000004075 alteration Effects 0.000 description 2
- 150000001408 amides Chemical class 0.000 description 2
- 235000009582 asparagine Nutrition 0.000 description 2
- 238000003149 assay kit Methods 0.000 description 2
- 230000001580 bacterial effect Effects 0.000 description 2
- 239000011324 bead Substances 0.000 description 2
- 230000033228 biological regulation Effects 0.000 description 2
- 150000001720 carbohydrates Chemical class 0.000 description 2
- 229910052799 carbon Inorganic materials 0.000 description 2
- 125000003178 carboxy group Chemical group [H]OC(*)=O 0.000 description 2
- 230000010261 cell growth Effects 0.000 description 2
- 210000002421 cell wall Anatomy 0.000 description 2
- 210000004671 cell-free system Anatomy 0.000 description 2
- 230000005754 cellular signaling Effects 0.000 description 2
- 230000004700 cellular uptake Effects 0.000 description 2
- 229960005091 chloramphenicol Drugs 0.000 description 2
- WIIZWVCIJKGZOK-RKDXNWHRSA-N chloramphenicol Chemical compound ClC(Cl)C(=O)N[C@H](CO)[C@H](O)C1=CC=C([N+]([O-])=O)C=C1 WIIZWVCIJKGZOK-RKDXNWHRSA-N 0.000 description 2
- 210000000349 chromosome Anatomy 0.000 description 2
- 238000010367 cloning Methods 0.000 description 2
- 230000000052 comparative effect Effects 0.000 description 2
- 102000006834 complement receptors Human genes 0.000 description 2
- 108010047295 complement receptors Proteins 0.000 description 2
- 230000037029 cross reaction Effects 0.000 description 2
- 125000004122 cyclic group Chemical group 0.000 description 2
- 230000002950 deficient Effects 0.000 description 2
- 238000001514 detection method Methods 0.000 description 2
- 238000011161 development Methods 0.000 description 2
- 230000018109 developmental process Effects 0.000 description 2
- 239000000975 dye Substances 0.000 description 2
- 238000005516 engineering process Methods 0.000 description 2
- 239000003623 enhancer Substances 0.000 description 2
- 238000001943 fluorescence-activated cell sorting Methods 0.000 description 2
- 125000000524 functional group Chemical group 0.000 description 2
- BTCSSZJGUNDROE-UHFFFAOYSA-N gamma-aminobutyric acid Chemical compound NCCCC(O)=O BTCSSZJGUNDROE-UHFFFAOYSA-N 0.000 description 2
- 238000007429 general method Methods 0.000 description 2
- 235000013922 glutamic acid Nutrition 0.000 description 2
- 239000004220 glutamic acid Substances 0.000 description 2
- ZDXPYRJPNDTMRX-UHFFFAOYSA-N glutamine Natural products OC(=O)C(N)CCC(N)=O ZDXPYRJPNDTMRX-UHFFFAOYSA-N 0.000 description 2
- 235000004554 glutamine Nutrition 0.000 description 2
- 239000003102 growth factor Substances 0.000 description 2
- 239000001963 growth medium Substances 0.000 description 2
- 235000009424 haa Nutrition 0.000 description 2
- 125000001475 halogen functional group Chemical group 0.000 description 2
- WQPDUTSPKFMPDP-OUMQNGNKSA-N hirudin Chemical compound C([C@@H](C(=O)N[C@@H](CCC(O)=O)C(=O)N[C@@H](CCC(O)=O)C(=O)N[C@@H]([C@@H](C)CC)C(=O)N1[C@@H](CCC1)C(=O)N[C@@H](CCC(O)=O)C(=O)N[C@@H](CCC(O)=O)C(=O)N[C@@H](CC=1C=CC(OS(O)(=O)=O)=CC=1)C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](CCC(N)=O)C(O)=O)NC(=O)[C@H](CC(O)=O)NC(=O)CNC(=O)[C@H](CC(O)=O)NC(=O)[C@H](CC(N)=O)NC(=O)[C@H](CC=1NC=NC=1)NC(=O)[C@H](CO)NC(=O)[C@H](CCC(N)=O)NC(=O)[C@H]1N(CCC1)C(=O)[C@H](CCCCN)NC(=O)[C@H]1N(CCC1)C(=O)[C@@H](NC(=O)CNC(=O)[C@H](CCC(O)=O)NC(=O)CNC(=O)[C@@H](NC(=O)[C@@H](NC(=O)[C@H]1NC(=O)[C@H](CCC(N)=O)NC(=O)[C@H](CC(N)=O)NC(=O)[C@H](CCCCN)NC(=O)[C@H](CCC(O)=O)NC(=O)CNC(=O)[C@H](CC(O)=O)NC(=O)[C@H](CO)NC(=O)CNC(=O)[C@H](CC(C)C)NC(=O)[C@H]([C@@H](C)CC)NC(=O)[C@@H]2CSSC[C@@H](C(=O)N[C@@H](CCC(O)=O)C(=O)NCC(=O)N[C@@H](CO)C(=O)N[C@@H](CC(N)=O)C(=O)N[C@H](C(=O)N[C@H](C(NCC(=O)N[C@@H](CCC(N)=O)C(=O)NCC(=O)N[C@@H](CC(N)=O)C(=O)N[C@@H](CCCCN)C(=O)N2)=O)CSSC1)C(C)C)NC(=O)[C@H](CC(C)C)NC(=O)[C@H]1NC(=O)[C@H](CC(C)C)NC(=O)[C@H](CC(N)=O)NC(=O)[C@H](CCC(N)=O)NC(=O)CNC(=O)[C@H](CO)NC(=O)[C@H](CCC(O)=O)NC(=O)[C@H]([C@@H](C)O)NC(=O)[C@@H](NC(=O)[C@H](CC(O)=O)NC(=O)[C@@H](NC(=O)[C@H](CC=2C=CC(O)=CC=2)NC(=O)[C@@H](NC(=O)[C@@H](N)C(C)C)C(C)C)[C@@H](C)O)CSSC1)C(C)C)[C@@H](C)O)[C@@H](C)O)C1=CC=CC=C1 WQPDUTSPKFMPDP-OUMQNGNKSA-N 0.000 description 2
- 229940006607 hirudin Drugs 0.000 description 2
- 229930195733 hydrocarbon Natural products 0.000 description 2
- 150000002430 hydrocarbons Chemical class 0.000 description 2
- 230000002209 hydrophobic effect Effects 0.000 description 2
- 238000003018 immunoassay Methods 0.000 description 2
- 230000002163 immunogen Effects 0.000 description 2
- 230000006872 improvement Effects 0.000 description 2
- 208000015181 infectious disease Diseases 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
- 230000003993 interaction Effects 0.000 description 2
- 229940047124 interferons Drugs 0.000 description 2
- 229940047122 interleukins Drugs 0.000 description 2
- 239000000543 intermediate Substances 0.000 description 2
- 238000002955 isolation Methods 0.000 description 2
- AGPKZVBTJJNPAG-UHFFFAOYSA-N isoleucine Natural products CCC(C)C(N)C(O)=O AGPKZVBTJJNPAG-UHFFFAOYSA-N 0.000 description 2
- 229960000310 isoleucine Drugs 0.000 description 2
- 125000000468 ketone group Chemical group 0.000 description 2
- 238000011005 laboratory method Methods 0.000 description 2
- 239000003446 ligand Substances 0.000 description 2
- 210000004962 mammalian cell Anatomy 0.000 description 2
- 239000000463 material Substances 0.000 description 2
- 238000005259 measurement Methods 0.000 description 2
- 239000002609 medium Substances 0.000 description 2
- 210000005060 membrane bound organelle Anatomy 0.000 description 2
- 230000037353 metabolic pathway Effects 0.000 description 2
- 229930182817 methionine Natural products 0.000 description 2
- 125000002496 methyl group Chemical group [H]C([H])([H])* 0.000 description 2
- 238000001823 molecular biology technique Methods 0.000 description 2
- 210000001616 monocyte Anatomy 0.000 description 2
- 210000000440 neutrophil Anatomy 0.000 description 2
- 125000000449 nitro group Chemical group [O-][N+](*)=O 0.000 description 2
- 238000007899 nucleic acid hybridization Methods 0.000 description 2
- 210000004940 nucleus Anatomy 0.000 description 2
- 235000015097 nutrients Nutrition 0.000 description 2
- 230000008520 organization Effects 0.000 description 2
- 239000002245 particle Substances 0.000 description 2
- 239000000546 pharmaceutical excipient Substances 0.000 description 2
- 150000002994 phenylalanines Chemical class 0.000 description 2
- BZQFBWGGLXLEPQ-REOHCLBHSA-N phosphoserine Chemical compound OC(=O)[C@@H](N)COP(O)(O)=O BZQFBWGGLXLEPQ-REOHCLBHSA-N 0.000 description 2
- 230000000704 physical effect Effects 0.000 description 2
- 229920001223 polyethylene glycol Polymers 0.000 description 2
- OXCMYAYHXIHQOA-UHFFFAOYSA-N potassium;[2-butyl-5-chloro-3-[[4-[2-(1,2,4-triaza-3-azanidacyclopenta-1,4-dien-5-yl)phenyl]phenyl]methyl]imidazol-4-yl]methanol Chemical compound [K+].CCCCC1=NC(Cl)=C(CO)N1CC1=CC=C(C=2C(=CC=CC=2)C2=N[N-]N=N2)C=C1 OXCMYAYHXIHQOA-UHFFFAOYSA-N 0.000 description 2
- 125000002924 primary amino group Chemical group [H]N([H])* 0.000 description 2
- 150000003148 prolines Chemical class 0.000 description 2
- 230000004853 protein function Effects 0.000 description 2
- 238000001243 protein synthesis Methods 0.000 description 2
- 238000000746 purification Methods 0.000 description 2
- 102000016914 ras Proteins Human genes 0.000 description 2
- 108091007054 readthrough proteins Proteins 0.000 description 2
- 102000005962 receptors Human genes 0.000 description 2
- 108020003175 receptors Proteins 0.000 description 2
- 102200021347 rs876659329 Human genes 0.000 description 2
- 229910052711 selenium Inorganic materials 0.000 description 2
- 239000011669 selenium Substances 0.000 description 2
- 238000012163 sequencing technique Methods 0.000 description 2
- 210000002966 serum Anatomy 0.000 description 2
- 238000007086 side reaction Methods 0.000 description 2
- 230000019491 signal transduction Effects 0.000 description 2
- 238000010561 standard procedure Methods 0.000 description 2
- RWQNBRDOKXIBIV-UHFFFAOYSA-N thymine Chemical compound CC1=CNC(=O)NC1=O RWQNBRDOKXIBIV-UHFFFAOYSA-N 0.000 description 2
- 210000001519 tissue Anatomy 0.000 description 2
- 238000006257 total synthesis reaction Methods 0.000 description 2
- 108091006106 transcriptional activators Proteins 0.000 description 2
- 230000012863 translational readthrough Effects 0.000 description 2
- 230000032258 transport Effects 0.000 description 2
- 229940035893 uracil Drugs 0.000 description 2
- VBEQCZHXXJYVRD-GACYYNSASA-N uroanthelone Chemical compound C([C@@H](C(=O)N[C@H](C(=O)N[C@@H](CS)C(=O)N[C@@H](CC(N)=O)C(=O)N[C@@H](CS)C(=O)N[C@H](C(=O)N[C@@H]([C@@H](C)CC)C(=O)NCC(=O)N[C@@H](CC=1C=CC(O)=CC=1)C(=O)N[C@@H](CO)C(=O)NCC(=O)N[C@@H](CC(O)=O)C(=O)N[C@@H](CCCNC(N)=N)C(=O)N[C@@H](CS)C(=O)N[C@@H](CCC(N)=O)C(=O)N[C@@H]([C@@H](C)O)C(=O)N[C@@H](CCCNC(N)=N)C(=O)N[C@@H](CC(O)=O)C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](CCCNC(N)=N)C(=O)N[C@@H](CC=1C2=CC=CC=C2NC=1)C(=O)N[C@@H](CC=1C2=CC=CC=C2NC=1)C(=O)N[C@@H](CCC(O)=O)C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](CCCNC(N)=N)C(O)=O)C(C)C)[C@@H](C)O)NC(=O)[C@H](CO)NC(=O)[C@H](CC(O)=O)NC(=O)[C@H](CC(C)C)NC(=O)[C@H](CO)NC(=O)[C@H](CCC(O)=O)NC(=O)[C@@H](NC(=O)[C@H](CC=1NC=NC=1)NC(=O)[C@H](CCSC)NC(=O)[C@H](CS)NC(=O)[C@@H](NC(=O)CNC(=O)CNC(=O)[C@H](CC(N)=O)NC(=O)[C@H](CC(C)C)NC(=O)[C@H](CS)NC(=O)[C@H](CC=1C=CC(O)=CC=1)NC(=O)CNC(=O)[C@H](CC(O)=O)NC(=O)[C@H](CC=1C=CC(O)=CC=1)NC(=O)[C@H](CO)NC(=O)[C@H](CO)NC(=O)[C@H]1N(CCC1)C(=O)[C@H](CS)NC(=O)CNC(=O)[C@H]1N(CCC1)C(=O)[C@H](CC=1C=CC(O)=CC=1)NC(=O)[C@H](CO)NC(=O)[C@@H](N)CC(N)=O)C(C)C)[C@@H](C)CC)C1=CC=C(O)C=C1 VBEQCZHXXJYVRD-GACYYNSASA-N 0.000 description 2
- 229960005486 vaccine Drugs 0.000 description 2
- 239000004474 valine Substances 0.000 description 2
- DNIAPMSPPWPWGF-VKHMYHEASA-N (+)-propylene glycol Chemical compound C[C@H](O)CO DNIAPMSPPWPWGF-VKHMYHEASA-N 0.000 description 1
- MTCFGRXMJLQNBG-REOHCLBHSA-N (2S)-2-Amino-3-hydroxypropansäure Chemical compound OC[C@H](N)C(O)=O MTCFGRXMJLQNBG-REOHCLBHSA-N 0.000 description 1
- VKYBWTVHQHFSJL-ZATYTLRZSA-N (2s)-2,5-diamino-5-oxopentanoic acid;(2s)-pyrrolidine-2-carboxylic acid Chemical compound OC(=O)[C@@H]1CCCN1.OC(=O)[C@@H](N)CCC(N)=O VKYBWTVHQHFSJL-ZATYTLRZSA-N 0.000 description 1
- RWLSBXBFZHDHHX-VIFPVBQESA-N (2s)-2-(naphthalen-2-ylamino)propanoic acid Chemical compound C1=CC=CC2=CC(N[C@@H](C)C(O)=O)=CC=C21 RWLSBXBFZHDHHX-VIFPVBQESA-N 0.000 description 1
- VFCYASLQFGXHTQ-VIFPVBQESA-N (2s)-2-[benzyl(nitro)amino]-3-hydroxypropanoic acid Chemical compound OC[C@@H](C(O)=O)N([N+]([O-])=O)CC1=CC=CC=C1 VFCYASLQFGXHTQ-VIFPVBQESA-N 0.000 description 1
- YYTDJPUFAVPHQA-VKHMYHEASA-N (2s)-2-amino-3-(2,3,4,5,6-pentafluorophenyl)propanoic acid Chemical compound OC(=O)[C@@H](N)CC1=C(F)C(F)=C(F)C(F)=C1F YYTDJPUFAVPHQA-VKHMYHEASA-N 0.000 description 1
- KQZQZOQFUQXPLW-YFKPBYRVSA-N (2s)-2-amino-3-(3,4,5-trihydroxyphenyl)propanoic acid Chemical compound OC(=O)[C@@H](N)CC1=CC(O)=C(O)C(O)=C1 KQZQZOQFUQXPLW-YFKPBYRVSA-N 0.000 description 1
- POGSZHUEECCEAP-ZETCQYMHSA-N (2s)-2-amino-3-(3-amino-4-hydroxyphenyl)propanoic acid Chemical compound OC(=O)[C@@H](N)CC1=CC=C(O)C(N)=C1 POGSZHUEECCEAP-ZETCQYMHSA-N 0.000 description 1
- PEMUHKUIQHFMTH-QMMMGPOBSA-N (2s)-2-amino-3-(4-bromophenyl)propanoic acid Chemical compound OC(=O)[C@@H](N)CC1=CC=C(Br)C=C1 PEMUHKUIQHFMTH-QMMMGPOBSA-N 0.000 description 1
- JSXMFBNJRFXRCX-NSHDSACASA-N (2s)-2-amino-3-(4-prop-2-ynoxyphenyl)propanoic acid Chemical compound OC(=O)[C@@H](N)CC1=CC=C(OCC#C)C=C1 JSXMFBNJRFXRCX-NSHDSACASA-N 0.000 description 1
- LJHYWUVYIKCPGU-VIFPVBQESA-N (2s)-2-amino-3-[4-(carboxymethyl)phenyl]propanoic acid Chemical compound OC(=O)[C@@H](N)CC1=CC=C(CC(O)=O)C=C1 LJHYWUVYIKCPGU-VIFPVBQESA-N 0.000 description 1
- ALBODLTZUXKBGZ-JUUVMNCLSA-N (2s)-2-amino-3-phenylpropanoic acid;(2s)-2,6-diaminohexanoic acid Chemical compound NCCCC[C@H](N)C(O)=O.OC(=O)[C@@H](N)CC1=CC=CC=C1 ALBODLTZUXKBGZ-JUUVMNCLSA-N 0.000 description 1
- NEMHIKRLROONTL-QMMMGPOBSA-N (2s)-2-azaniumyl-3-(4-azidophenyl)propanoate Chemical compound OC(=O)[C@@H](N)CC1=CC=C(N=[N+]=[N-])C=C1 NEMHIKRLROONTL-QMMMGPOBSA-N 0.000 description 1
- GTVVZTAFGPQSPC-QMMMGPOBSA-N (2s)-2-azaniumyl-3-(4-nitrophenyl)propanoate Chemical compound OC(=O)[C@@H](N)CC1=CC=C([N+]([O-])=O)C=C1 GTVVZTAFGPQSPC-QMMMGPOBSA-N 0.000 description 1
- ZXSBHXZKWRIEIA-JTQLQIEISA-N (2s)-3-(4-acetylphenyl)-2-azaniumylpropanoate Chemical compound CC(=O)C1=CC=C(C[C@H](N)C(O)=O)C=C1 ZXSBHXZKWRIEIA-JTQLQIEISA-N 0.000 description 1
- BNIFSVVAHBLNTN-XKKUQSFHSA-N (2s)-4-amino-2-[[(2s)-2-[[(2s)-2-[[(2s)-2-[[(2s)-1-[(2s)-4-amino-2-[[2-[[(2s)-2-[[(2s)-2-[[(2s)-1-[(2s)-6-amino-2-[[(2s)-2-[[(2s)-2-[[(2s,3r)-2-amino-3-hydroxybutanoyl]amino]-4-methylsulfanylbutanoyl]amino]-5-(diaminomethylideneamino)pentanoyl]amino]hexan Chemical compound C[C@@H](O)[C@H](N)C(=O)N[C@@H](CCSC)C(=O)N[C@@H](CCCN=C(N)N)C(=O)N[C@@H](CCCCN)C(=O)N1CCC[C@H]1C(=O)N[C@@H](CCCN=C(N)N)C(=O)N[C@@H](CO)C(=O)NCC(=O)N[C@@H](CC(N)=O)C(=O)N1[C@H](C(=O)N[C@@H](CC(O)=O)C(=O)N[C@@H](C(C)C)C(=O)N[C@@H](C)C(=O)N[C@@H](CC(N)=O)C(O)=O)CCC1 BNIFSVVAHBLNTN-XKKUQSFHSA-N 0.000 description 1
- 108010052418 (N-(2-((4-((2-((4-(9-acridinylamino)phenyl)amino)-2-oxoethyl)amino)-4-oxobutyl)amino)-1-(1H-imidazol-4-ylmethyl)-1-oxoethyl)-6-(((-2-aminoethyl)amino)methyl)-2-pyridinecarboxamidato) iron(1+) Proteins 0.000 description 1
- WHTVZRBIWZFKQO-AWEZNQCLSA-N (S)-chloroquine Chemical compound ClC1=CC=C2C(N[C@@H](C)CCCN(CC)CC)=CC=NC2=C1 WHTVZRBIWZFKQO-AWEZNQCLSA-N 0.000 description 1
- YPFDHNVEDLHUCE-UHFFFAOYSA-N 1,3-propanediol Substances OCCCO YPFDHNVEDLHUCE-UHFFFAOYSA-N 0.000 description 1
- 229940035437 1,3-propanediol Drugs 0.000 description 1
- RXMWXENJQAINCC-DMTCNVIQSA-N 2,5-didehydro-D-gluconic acid Chemical compound OCC(=O)[C@@H](O)[C@H](O)C(=O)C(O)=O RXMWXENJQAINCC-DMTCNVIQSA-N 0.000 description 1
- RXMWXENJQAINCC-UHFFFAOYSA-N 2,5-diketo-D-gluconic acid Natural products OCC(=O)C(O)C(O)C(=O)C(O)=O RXMWXENJQAINCC-UHFFFAOYSA-N 0.000 description 1
- 125000003903 2-propenyl group Chemical group [H]C([*])([H])C([H])=C([H])[H] 0.000 description 1
- JZRBSTONIYRNRI-VIFPVBQESA-N 3-methylphenylalanine Chemical compound CC1=CC=CC(C[C@H](N)C(O)=O)=C1 JZRBSTONIYRNRI-VIFPVBQESA-N 0.000 description 1
- IRZQDMYEJPNDEN-UHFFFAOYSA-N 3-phenyl-2-aminobutanoic acid Natural products OC(=O)C(N)C(C)C1=CC=CC=C1 IRZQDMYEJPNDEN-UHFFFAOYSA-N 0.000 description 1
- PZNQZSRPDOEBMS-QMMMGPOBSA-N 4-iodo-L-phenylalanine Chemical compound OC(=O)[C@@H](N)CC1=CC=C(I)C=C1 PZNQZSRPDOEBMS-QMMMGPOBSA-N 0.000 description 1
- GTVVZTAFGPQSPC-UHFFFAOYSA-N 4-nitrophenylalanine Chemical compound OC(=O)C(N)CC1=CC=C([N+]([O-])=O)C=C1 GTVVZTAFGPQSPC-UHFFFAOYSA-N 0.000 description 1
- CJIJXIFQYOPWTF-UHFFFAOYSA-N 7-hydroxycoumarin Natural products O1C(=O)C=CC2=CC(O)=CC=C21 CJIJXIFQYOPWTF-UHFFFAOYSA-N 0.000 description 1
- HBAQYPYDRFILMT-UHFFFAOYSA-N 8-[3-(1-cyclopropylpyrazol-4-yl)-1H-pyrazolo[4,3-d]pyrimidin-5-yl]-3-methyl-3,8-diazabicyclo[3.2.1]octan-2-one Chemical class C1(CC1)N1N=CC(=C1)C1=NNC2=C1N=C(N=C2)N1C2C(N(CC1CC2)C)=O HBAQYPYDRFILMT-UHFFFAOYSA-N 0.000 description 1
- 101150067361 Aars1 gene Proteins 0.000 description 1
- 229920001817 Agar Polymers 0.000 description 1
- PQSUYGKTWSAVDQ-ZVIOFETBSA-N Aldosterone Chemical compound C([C@@]1([C@@H](C(=O)CO)CC[C@H]1[C@@H]1CC2)C=O)[C@H](O)[C@@H]1[C@]1(C)C2=CC(=O)CC1 PQSUYGKTWSAVDQ-ZVIOFETBSA-N 0.000 description 1
- PQSUYGKTWSAVDQ-UHFFFAOYSA-N Aldosterone Natural products C1CC2C3CCC(C(=O)CO)C3(C=O)CC(O)C2C2(C)C1=CC(=O)CC2 PQSUYGKTWSAVDQ-UHFFFAOYSA-N 0.000 description 1
- 108700023418 Amidases Proteins 0.000 description 1
- 102000004092 Amidohydrolases Human genes 0.000 description 1
- 108090000531 Amidohydrolases Proteins 0.000 description 1
- 102000006534 Amino Acid Isomerases Human genes 0.000 description 1
- 108010008830 Amino Acid Isomerases Proteins 0.000 description 1
- 102400000068 Angiostatin Human genes 0.000 description 1
- 108010079709 Angiostatins Proteins 0.000 description 1
- 102000007592 Apolipoproteins Human genes 0.000 description 1
- 108010071619 Apolipoproteins Proteins 0.000 description 1
- 108010083590 Apoproteins Proteins 0.000 description 1
- 102000006410 Apoproteins Human genes 0.000 description 1
- OZDNDGXASTWERN-CTNGQTDRSA-N Apovincamine Chemical compound C1=CC=C2C(CCN3CCC4)=C5[C@@H]3[C@]4(CC)C=C(C(=O)OC)N5C2=C1 OZDNDGXASTWERN-CTNGQTDRSA-N 0.000 description 1
- 101000716807 Arabidopsis thaliana Protein SCO1 homolog 1, mitochondrial Proteins 0.000 description 1
- 241000712891 Arenavirus Species 0.000 description 1
- 241000238421 Arthropoda Species 0.000 description 1
- 241000228212 Aspergillus Species 0.000 description 1
- 101800001288 Atrial natriuretic factor Proteins 0.000 description 1
- 102400001282 Atrial natriuretic peptide Human genes 0.000 description 1
- 101800001890 Atrial natriuretic peptide Proteins 0.000 description 1
- 241000271566 Aves Species 0.000 description 1
- 108010062877 Bacteriocins Proteins 0.000 description 1
- BTBUEUYNUDRHOZ-UHFFFAOYSA-N Borate Chemical compound [O-]B([O-])[O-] BTBUEUYNUDRHOZ-UHFFFAOYSA-N 0.000 description 1
- 102100032367 C-C motif chemokine 5 Human genes 0.000 description 1
- 102100032366 C-C motif chemokine 7 Human genes 0.000 description 1
- 102100025248 C-X-C motif chemokine 10 Human genes 0.000 description 1
- 101710098275 C-X-C motif chemokine 10 Proteins 0.000 description 1
- 102100036150 C-X-C motif chemokine 5 Human genes 0.000 description 1
- 102100036153 C-X-C motif chemokine 6 Human genes 0.000 description 1
- 101710085504 C-X-C motif chemokine 6 Proteins 0.000 description 1
- 102100036170 C-X-C motif chemokine 9 Human genes 0.000 description 1
- 101710085500 C-X-C motif chemokine 9 Proteins 0.000 description 1
- YAUFUHHMTSOTFS-GRHHLOCNSA-N C1(=CC=CC=C1)N[C@@H](C[SeH])C(=O)O.C1(=CC=CC=C1)N[C@@H](C[SeH])C(=O)O Chemical compound C1(=CC=CC=C1)N[C@@H](C[SeH])C(=O)O.C1(=CC=CC=C1)N[C@@H](C[SeH])C(=O)O YAUFUHHMTSOTFS-GRHHLOCNSA-N 0.000 description 1
- 102000001902 CC Chemokines Human genes 0.000 description 1
- 108010040471 CC Chemokines Proteins 0.000 description 1
- 108010029697 CD40 Ligand Proteins 0.000 description 1
- 102100032937 CD40 ligand Human genes 0.000 description 1
- 102100032912 CD44 antigen Human genes 0.000 description 1
- 108050006947 CXC Chemokine Proteins 0.000 description 1
- 102000019388 CXC chemokine Human genes 0.000 description 1
- 102000055006 Calcitonin Human genes 0.000 description 1
- 108060001064 Calcitonin Proteins 0.000 description 1
- OYPRJOBELJOOCE-UHFFFAOYSA-N Calcium Chemical compound [Ca] OYPRJOBELJOOCE-UHFFFAOYSA-N 0.000 description 1
- 241000222120 Candida <Saccharomycetales> Species 0.000 description 1
- OKTJSMMVPCPJKN-UHFFFAOYSA-N Carbon Chemical compound [C] OKTJSMMVPCPJKN-UHFFFAOYSA-N 0.000 description 1
- 239000004215 Carbon black (E152) Substances 0.000 description 1
- 102000014914 Carrier Proteins Human genes 0.000 description 1
- 108010055166 Chemokine CCL5 Proteins 0.000 description 1
- 108010055124 Chemokine CCL7 Proteins 0.000 description 1
- 102000000012 Chemokine CCL8 Human genes 0.000 description 1
- 108010055204 Chemokine CCL8 Proteins 0.000 description 1
- 241000223782 Ciliophora Species 0.000 description 1
- 102100022641 Coagulation factor IX Human genes 0.000 description 1
- 102100023804 Coagulation factor VII Human genes 0.000 description 1
- 108091026890 Coding region Proteins 0.000 description 1
- 102000008186 Collagen Human genes 0.000 description 1
- 108010035532 Collagen Proteins 0.000 description 1
- 229940124073 Complement inhibitor Drugs 0.000 description 1
- 241000711573 Coronaviridae Species 0.000 description 1
- OMFXVFTZEKFJBZ-UHFFFAOYSA-N Corticosterone Natural products O=C1CCC2(C)C3C(O)CC(C)(C(CC4)C(=O)CO)C4C3CCC2=C1 OMFXVFTZEKFJBZ-UHFFFAOYSA-N 0.000 description 1
- 241000557626 Corvus corax Species 0.000 description 1
- 241000186216 Corynebacterium Species 0.000 description 1
- 241000938605 Crocodylia Species 0.000 description 1
- 239000004971 Cross linker Substances 0.000 description 1
- JPVYNHNXODAKFH-UHFFFAOYSA-N Cu2+ Chemical compound [Cu+2] JPVYNHNXODAKFH-UHFFFAOYSA-N 0.000 description 1
- FDKWRPBBCBCIGA-UWTATZPHSA-N D-Selenocysteine Natural products [Se]C[C@@H](N)C(O)=O FDKWRPBBCBCIGA-UWTATZPHSA-N 0.000 description 1
- QNAYBMKLOCPYGJ-UWTATZPHSA-N D-alanine Chemical compound C[C@@H](N)C(O)=O QNAYBMKLOCPYGJ-UWTATZPHSA-N 0.000 description 1
- QNAYBMKLOCPYGJ-UHFFFAOYSA-N D-alpha-Ala Natural products CC([NH3+])C([O-])=O QNAYBMKLOCPYGJ-UHFFFAOYSA-N 0.000 description 1
- ZZZCUOFIHGPKAK-UHFFFAOYSA-N D-erythro-ascorbic acid Natural products OCC1OC(=O)C(O)=C1O ZZZCUOFIHGPKAK-UHFFFAOYSA-N 0.000 description 1
- 229930195713 D-glutamate Natural products 0.000 description 1
- YAHZABJORDUQGO-NQXXGFSBSA-N D-ribulose 1,5-bisphosphate Chemical compound OP(=O)(O)OC[C@@H](O)[C@@H](O)C(=O)COP(O)(O)=O YAHZABJORDUQGO-NQXXGFSBSA-N 0.000 description 1
- 238000012270 DNA recombination Methods 0.000 description 1
- 230000004543 DNA replication Effects 0.000 description 1
- 241000450599 DNA viruses Species 0.000 description 1
- 101710141836 DNA-binding protein HU homolog Proteins 0.000 description 1
- 102000016680 Dioxygenases Human genes 0.000 description 1
- 108010028143 Dioxygenases Proteins 0.000 description 1
- 206010059866 Drug resistance Diseases 0.000 description 1
- 241000224431 Entamoeba Species 0.000 description 1
- 101710104662 Enterotoxin type C-3 Proteins 0.000 description 1
- 102400001368 Epidermal growth factor Human genes 0.000 description 1
- 101800003838 Epidermal growth factor Proteins 0.000 description 1
- 108020002908 Epoxide hydrolase Proteins 0.000 description 1
- 102000005486 Epoxide hydrolase Human genes 0.000 description 1
- 241001125671 Eretmochelys imbricata Species 0.000 description 1
- 102000003951 Erythropoietin Human genes 0.000 description 1
- 102100031939 Erythropoietin Human genes 0.000 description 1
- 108090000394 Erythropoietin Proteins 0.000 description 1
- 101900234631 Escherichia coli DNA polymerase I Proteins 0.000 description 1
- 108090000371 Esterases Proteins 0.000 description 1
- 102100030844 Exocyst complex component 1 Human genes 0.000 description 1
- 108010076282 Factor IX Proteins 0.000 description 1
- 108010023321 Factor VII Proteins 0.000 description 1
- 108010054218 Factor VIII Proteins 0.000 description 1
- 102000001690 Factor VIII Human genes 0.000 description 1
- 108010014173 Factor X Proteins 0.000 description 1
- 108010049003 Fibrinogen Proteins 0.000 description 1
- 102000008946 Fibrinogen Human genes 0.000 description 1
- 108090000368 Fibroblast growth factor 8 Proteins 0.000 description 1
- 102100037362 Fibronectin Human genes 0.000 description 1
- 108010067306 Fibronectins Proteins 0.000 description 1
- 108090000331 Firefly luciferases Proteins 0.000 description 1
- 241000710831 Flavivirus Species 0.000 description 1
- 102000003688 G-Protein-Coupled Receptors Human genes 0.000 description 1
- 108090000045 G-Protein-Coupled Receptors Proteins 0.000 description 1
- 102100040837 Galactoside alpha-(1,2)-fucosyltransferase 2 Human genes 0.000 description 1
- 101710115997 Gamma-tubulin complex component 2 Proteins 0.000 description 1
- 108700007698 Genetic Terminator Regions Proteins 0.000 description 1
- 241000193385 Geobacillus stearothermophilus Species 0.000 description 1
- 241000224466 Giardia Species 0.000 description 1
- 102000004547 Glucosylceramidase Human genes 0.000 description 1
- 108010017544 Glucosylceramidase Proteins 0.000 description 1
- XCLCVBYNGXEVDU-WHFBIAKZSA-N Gly-Asn-Ser Chemical compound NCC(=O)N[C@@H](CC(N)=O)C(=O)N[C@@H](CO)C(O)=O XCLCVBYNGXEVDU-WHFBIAKZSA-N 0.000 description 1
- NTBOEZICHOSJEE-YUMQZZPRSA-N Gly-Lys-Ser Chemical compound [H]NCC(=O)N[C@@H](CCCCN)C(=O)N[C@@H](CO)C(O)=O NTBOEZICHOSJEE-YUMQZZPRSA-N 0.000 description 1
- YYXJFBMCOUSYSF-RYUDHWBXSA-N Gly-Phe-Gln Chemical compound [H]NCC(=O)N[C@@H](CC1=CC=CC=C1)C(=O)N[C@@H](CCC(N)=O)C(O)=O YYXJFBMCOUSYSF-RYUDHWBXSA-N 0.000 description 1
- BCCRXDTUTZHDEU-VKHMYHEASA-N Gly-Ser Chemical compound NCC(=O)N[C@@H](CO)C(O)=O BCCRXDTUTZHDEU-VKHMYHEASA-N 0.000 description 1
- 239000004471 Glycine Substances 0.000 description 1
- 102000003886 Glycoproteins Human genes 0.000 description 1
- 108090000288 Glycoproteins Proteins 0.000 description 1
- 102000005744 Glycoside Hydrolases Human genes 0.000 description 1
- 108010031186 Glycoside Hydrolases Proteins 0.000 description 1
- 108700023372 Glycosyltransferases Proteins 0.000 description 1
- 102000006771 Gonadotropins Human genes 0.000 description 1
- 108010086677 Gonadotropins Proteins 0.000 description 1
- 108010017080 Granulocyte Colony-Stimulating Factor Proteins 0.000 description 1
- 102000004269 Granulocyte Colony-Stimulating Factor Human genes 0.000 description 1
- 108010017213 Granulocyte-Macrophage Colony-Stimulating Factor Proteins 0.000 description 1
- 102000018997 Growth Hormone Human genes 0.000 description 1
- 108010051696 Growth Hormone Proteins 0.000 description 1
- 101150009006 HIS3 gene Proteins 0.000 description 1
- 108090000031 Hedgehog Proteins Proteins 0.000 description 1
- 102000003693 Hedgehog Proteins Human genes 0.000 description 1
- 102000001554 Hemoglobins Human genes 0.000 description 1
- 108010054147 Hemoglobins Proteins 0.000 description 1
- HTTJABKRGRZYRN-UHFFFAOYSA-N Heparin Chemical compound OC1C(NC(=O)C)C(O)OC(COS(O)(=O)=O)C1OC1C(OS(O)(=O)=O)C(O)C(OC2C(C(OS(O)(=O)=O)C(OC3C(C(O)C(O)C(O3)C(O)=O)OS(O)(=O)=O)C(CO)O2)NS(O)(=O)=O)C(C(O)=O)O1 HTTJABKRGRZYRN-UHFFFAOYSA-N 0.000 description 1
- FBCURAVMSXNOLP-JYJNAYRXSA-N His-Phe-Gln Chemical compound C1=CC=C(C=C1)C[C@@H](C(=O)N[C@@H](CCC(=O)N)C(=O)O)NC(=O)[C@H](CC2=CN=CN2)N FBCURAVMSXNOLP-JYJNAYRXSA-N 0.000 description 1
- 102000006947 Histones Human genes 0.000 description 1
- 108010033040 Histones Proteins 0.000 description 1
- 241000282412 Homo Species 0.000 description 1
- 241000282414 Homo sapiens Species 0.000 description 1
- 101000947186 Homo sapiens C-X-C motif chemokine 5 Proteins 0.000 description 1
- 101000868273 Homo sapiens CD44 antigen Proteins 0.000 description 1
- 101000893710 Homo sapiens Galactoside alpha-(1,2)-fucosyltransferase 2 Proteins 0.000 description 1
- 101000973997 Homo sapiens Nucleosome assembly protein 1-like 4 Proteins 0.000 description 1
- 101000947178 Homo sapiens Platelet basic protein Proteins 0.000 description 1
- 101000582950 Homo sapiens Platelet factor 4 Proteins 0.000 description 1
- 101001076715 Homo sapiens RNA-binding protein 39 Proteins 0.000 description 1
- 101000652229 Homo sapiens Suppressor of cytokine signaling 7 Proteins 0.000 description 1
- 241000598436 Human T-cell lymphotropic virus Species 0.000 description 1
- UFHFLCQGNIYNRP-UHFFFAOYSA-N Hydrogen Chemical compound [H][H] UFHFLCQGNIYNRP-UHFFFAOYSA-N 0.000 description 1
- 108060003951 Immunoglobulin Proteins 0.000 description 1
- 102000001706 Immunoglobulin Fab Fragments Human genes 0.000 description 1
- 108010054477 Immunoglobulin Fab Fragments Proteins 0.000 description 1
- 102000008394 Immunoglobulin Fragments Human genes 0.000 description 1
- 235000000177 Indigofera tinctoria Nutrition 0.000 description 1
- 108090001061 Insulin Proteins 0.000 description 1
- 102000004877 Insulin Human genes 0.000 description 1
- 102000004218 Insulin-Like Growth Factor I Human genes 0.000 description 1
- 102000048143 Insulin-Like Growth Factor II Human genes 0.000 description 1
- 108090001117 Insulin-Like Growth Factor II Proteins 0.000 description 1
- 102100022339 Integrin alpha-L Human genes 0.000 description 1
- 108010008212 Integrin alpha4beta1 Proteins 0.000 description 1
- 108010064593 Intercellular Adhesion Molecule-1 Proteins 0.000 description 1
- 102100037877 Intercellular adhesion molecule 1 Human genes 0.000 description 1
- 108090000174 Interleukin-10 Proteins 0.000 description 1
- 108090000177 Interleukin-11 Proteins 0.000 description 1
- 108010065805 Interleukin-12 Proteins 0.000 description 1
- 108010002386 Interleukin-3 Proteins 0.000 description 1
- 108010002616 Interleukin-5 Proteins 0.000 description 1
- 108090001005 Interleukin-6 Proteins 0.000 description 1
- 108010002586 Interleukin-7 Proteins 0.000 description 1
- 108010002335 Interleukin-9 Proteins 0.000 description 1
- 108090000769 Isomerases Proteins 0.000 description 1
- 102000004195 Isomerases Human genes 0.000 description 1
- 229930194542 Keto Natural products 0.000 description 1
- 102100020880 Kit ligand Human genes 0.000 description 1
- 101710177504 Kit ligand Proteins 0.000 description 1
- WTDRDQBEARUVNC-LURJTMIESA-N L-DOPA Chemical compound OC(=O)[C@@H](N)CC1=CC=C(O)C(O)=C1 WTDRDQBEARUVNC-LURJTMIESA-N 0.000 description 1
- WTDRDQBEARUVNC-UHFFFAOYSA-N L-Dopa Natural products OC(=O)C(N)CC1=CC=C(O)C(O)=C1 WTDRDQBEARUVNC-UHFFFAOYSA-N 0.000 description 1
- ONIBWKKTOPOVIA-BYPYZUCNSA-N L-Proline Chemical compound OC(=O)[C@@H]1CCCN1 ONIBWKKTOPOVIA-BYPYZUCNSA-N 0.000 description 1
- WHUUTDBJXJRKMK-VKHMYHEASA-N L-glutamic acid Chemical compound OC(=O)[C@@H](N)CCC(O)=O WHUUTDBJXJRKMK-VKHMYHEASA-N 0.000 description 1
- ZFOMKMMPBOQKMC-KXUCPTDWSA-N L-pyrrolysine Chemical compound C[C@@H]1CC=N[C@H]1C(=O)NCCCC[C@H]([NH3+])C([O-])=O ZFOMKMMPBOQKMC-KXUCPTDWSA-N 0.000 description 1
- ZKZBPNGNEQAJSX-REOHCLBHSA-N L-selenocysteine Chemical compound [SeH]C[C@H](N)C(O)=O ZKZBPNGNEQAJSX-REOHCLBHSA-N 0.000 description 1
- 108010001831 LDL receptors Proteins 0.000 description 1
- 241000186660 Lactobacillus Species 0.000 description 1
- 102000010445 Lactoferrin Human genes 0.000 description 1
- 108010063045 Lactoferrin Proteins 0.000 description 1
- 241000222722 Leishmania <genus> Species 0.000 description 1
- 102000004058 Leukemia inhibitory factor Human genes 0.000 description 1
- 108090000581 Leukemia inhibitory factor Proteins 0.000 description 1
- 108010054320 Lignin peroxidase Proteins 0.000 description 1
- 101710155614 Ligninase A Proteins 0.000 description 1
- 101710155621 Ligninase B Proteins 0.000 description 1
- 241000209510 Liliopsida Species 0.000 description 1
- 108090001060 Lipase Proteins 0.000 description 1
- 102000004882 Lipase Human genes 0.000 description 1
- 239000004367 Lipase Substances 0.000 description 1
- 102100024640 Low-density lipoprotein receptor Human genes 0.000 description 1
- 108060001084 Luciferase Proteins 0.000 description 1
- 239000005089 Luciferase Substances 0.000 description 1
- 108010064548 Lymphocyte Function-Associated Antigen-1 Proteins 0.000 description 1
- 102000004083 Lymphotoxin-alpha Human genes 0.000 description 1
- 108090000542 Lymphotoxin-alpha Proteins 0.000 description 1
- 102100027754 Mast/stem cell growth factor receptor Kit Human genes 0.000 description 1
- 241000202974 Methanobacterium Species 0.000 description 1
- 241000191938 Micrococcus luteus Species 0.000 description 1
- 241000243190 Microsporidia Species 0.000 description 1
- 102000008109 Mixed Function Oxygenases Human genes 0.000 description 1
- 108010074633 Mixed Function Oxygenases Proteins 0.000 description 1
- 101710174628 Modulating protein YmoA Proteins 0.000 description 1
- 101710154541 Modulator protein Proteins 0.000 description 1
- 241000699666 Mus <mouse, genus> Species 0.000 description 1
- 108010021466 Mutant Proteins Proteins 0.000 description 1
- 102000008300 Mutant Proteins Human genes 0.000 description 1
- 241000204031 Mycoplasma Species 0.000 description 1
- 231100000678 Mycotoxin Toxicity 0.000 description 1
- 108010015406 Neurturin Proteins 0.000 description 1
- 102000001839 Neurturin Human genes 0.000 description 1
- 108010033272 Nitrilase Proteins 0.000 description 1
- 108010024026 Nitrile hydratase Proteins 0.000 description 1
- 238000000636 Northern blotting Methods 0.000 description 1
- 101710163270 Nuclease Proteins 0.000 description 1
- CIQHWLTYGMYQQR-QMMMGPOBSA-N O(4')-sulfo-L-tyrosine Chemical compound OC(=O)[C@@H](N)CC1=CC=C(OS(O)(=O)=O)C=C1 CIQHWLTYGMYQQR-QMMMGPOBSA-N 0.000 description 1
- GEYBMYRBIABFTA-VIFPVBQESA-N O-methyl-L-tyrosine Chemical compound COC1=CC=C(C[C@H](N)C(O)=O)C=C1 GEYBMYRBIABFTA-VIFPVBQESA-N 0.000 description 1
- 102000004140 Oncostatin M Human genes 0.000 description 1
- 108090000630 Oncostatin M Proteins 0.000 description 1
- 108700026244 Open Reading Frames Proteins 0.000 description 1
- 241000713112 Orthobunyavirus Species 0.000 description 1
- 241000702244 Orthoreovirus Species 0.000 description 1
- 102000004316 Oxidoreductases Human genes 0.000 description 1
- 108090000854 Oxidoreductases Proteins 0.000 description 1
- 108090000417 Oxygenases Proteins 0.000 description 1
- 102000004020 Oxygenases Human genes 0.000 description 1
- 108090000445 Parathyroid hormone Proteins 0.000 description 1
- 102000003982 Parathyroid hormone Human genes 0.000 description 1
- 102000035195 Peptidases Human genes 0.000 description 1
- 108700019535 Phosphoprotein Phosphatases Proteins 0.000 description 1
- 102000045595 Phosphoprotein Phosphatases Human genes 0.000 description 1
- 241000709664 Picornaviridae Species 0.000 description 1
- 108010064851 Plant Proteins Proteins 0.000 description 1
- 102100036154 Platelet basic protein Human genes 0.000 description 1
- 102100030304 Platelet factor 4 Human genes 0.000 description 1
- 208000000474 Poliomyelitis Diseases 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
- 102000016971 Proto-Oncogene Proteins c-kit Human genes 0.000 description 1
- 108010014608 Proto-Oncogene Proteins c-kit Proteins 0.000 description 1
- 208000003251 Pruritus Diseases 0.000 description 1
- ASNFTDCKZKHJSW-REOHCLBHSA-N Quisqualic acid Chemical class OC(=O)[C@@H](N)CN1OC(=O)NC1=O ASNFTDCKZKHJSW-REOHCLBHSA-N 0.000 description 1
- 101150040459 RAS gene Proteins 0.000 description 1
- 101150076031 RAS1 gene Proteins 0.000 description 1
- 108010092799 RNA-directed DNA polymerase Proteins 0.000 description 1
- 102000004879 Racemases and epimerases Human genes 0.000 description 1
- 108090001066 Racemases and epimerases Proteins 0.000 description 1
- 108020004511 Recombinant DNA Proteins 0.000 description 1
- 102000003743 Relaxin Human genes 0.000 description 1
- 108090000103 Relaxin Proteins 0.000 description 1
- 102100037486 Reverse transcriptase/ribonuclease H Human genes 0.000 description 1
- 101100394989 Rhodopseudomonas palustris (strain ATCC BAA-98 / CGA009) hisI gene Proteins 0.000 description 1
- 108010083644 Ribonucleases Proteins 0.000 description 1
- 102000006382 Ribonucleases Human genes 0.000 description 1
- 102000002278 Ribosomal Proteins Human genes 0.000 description 1
- 108010000605 Ribosomal Proteins Proteins 0.000 description 1
- 108010003581 Ribulose-bisphosphate carboxylase Proteins 0.000 description 1
- 102100023361 SAP domain-containing ribonucleoprotein Human genes 0.000 description 1
- 101710194492 SET-binding protein Proteins 0.000 description 1
- 206010040070 Septic Shock Diseases 0.000 description 1
- MTCFGRXMJLQNBG-UHFFFAOYSA-N Serine Natural products OCC(N)C(O)=O MTCFGRXMJLQNBG-UHFFFAOYSA-N 0.000 description 1
- 108010056088 Somatostatin Proteins 0.000 description 1
- 102000005157 Somatostatin Human genes 0.000 description 1
- 238000002105 Southern blotting Methods 0.000 description 1
- 241000295644 Staphylococcaceae Species 0.000 description 1
- 101000882406 Staphylococcus aureus Enterotoxin type C-1 Proteins 0.000 description 1
- 101000882403 Staphylococcus aureus Enterotoxin type C-2 Proteins 0.000 description 1
- 101001057112 Staphylococcus aureus Enterotoxin type D Proteins 0.000 description 1
- 229920002472 Starch Polymers 0.000 description 1
- 108010090804 Streptavidin Proteins 0.000 description 1
- 108010023197 Streptokinase Proteins 0.000 description 1
- 102100021669 Stromal cell-derived factor 1 Human genes 0.000 description 1
- 101710088580 Stromal cell-derived factor 1 Proteins 0.000 description 1
- 102000005158 Subtilisins Human genes 0.000 description 1
- 108010056079 Subtilisins Proteins 0.000 description 1
- 102100030529 Suppressor of cytokine signaling 7 Human genes 0.000 description 1
- 108010078233 Thymalfasin Proteins 0.000 description 1
- 102400000800 Thymosin alpha-1 Human genes 0.000 description 1
- 108090000373 Tissue Plasminogen Activator Proteins 0.000 description 1
- 102000003978 Tissue Plasminogen Activator Human genes 0.000 description 1
- 206010044248 Toxic shock syndrome Diseases 0.000 description 1
- 231100000650 Toxic shock syndrome Toxicity 0.000 description 1
- 101710120037 Toxin CcdB Proteins 0.000 description 1
- 102000003929 Transaminases Human genes 0.000 description 1
- 108090000340 Transaminases Proteins 0.000 description 1
- 108091023040 Transcription factor Proteins 0.000 description 1
- 102000040945 Transcription factor Human genes 0.000 description 1
- 241000224526 Trichomonas Species 0.000 description 1
- NXJZCPKZIKTYLX-XEGUGMAKSA-N Trp-Glu-Ala Chemical compound C[C@@H](C(=O)O)NC(=O)[C@H](CCC(=O)O)NC(=O)[C@H](CC1=CNC2=CC=CC=C21)N NXJZCPKZIKTYLX-XEGUGMAKSA-N 0.000 description 1
- ORQGVWIUHICVKE-KCTSRDHCSA-N Trp-His-Ala Chemical compound [H]N[C@@H](CC1=CNC2=C1C=CC=C2)C(=O)N[C@@H](CC1=CNC=N1)C(=O)N[C@@H](C)C(O)=O ORQGVWIUHICVKE-KCTSRDHCSA-N 0.000 description 1
- XLVRTKPAIXJYOH-HOCLYGCPSA-N Trp-His-Gly Chemical compound C1=CC=C2C(=C1)C(=CN2)C[C@@H](C(=O)N[C@@H](CC3=CN=CN3)C(=O)NCC(=O)O)N XLVRTKPAIXJYOH-HOCLYGCPSA-N 0.000 description 1
- 241000223104 Trypanosoma Species 0.000 description 1
- 108060008682 Tumor Necrosis Factor Proteins 0.000 description 1
- 102000000852 Tumor Necrosis Factor-alpha Human genes 0.000 description 1
- GULIUBBXCYPDJU-CQDKDKBSSA-N Tyr-Leu-Ala Chemical compound [O-]C(=O)[C@H](C)NC(=O)[C@H](CC(C)C)NC(=O)[C@@H]([NH3+])CC1=CC=C(O)C=C1 GULIUBBXCYPDJU-CQDKDKBSSA-N 0.000 description 1
- 108090000435 Urokinase-type plasminogen activator Proteins 0.000 description 1
- 102000003990 Urokinase-type plasminogen activator Human genes 0.000 description 1
- 206010046865 Vaccinia virus infection Diseases 0.000 description 1
- 108010000134 Vascular Cell Adhesion Molecule-1 Proteins 0.000 description 1
- 108010073929 Vascular Endothelial Growth Factor A Proteins 0.000 description 1
- 108010019530 Vascular Endothelial Growth Factors Proteins 0.000 description 1
- 102100023543 Vascular cell adhesion protein 1 Human genes 0.000 description 1
- 102100039037 Vascular endothelial growth factor A Human genes 0.000 description 1
- ZVNYJIZDIRKMBF-UHFFFAOYSA-N Vesnarinone Chemical compound C1=C(OC)C(OC)=CC=C1C(=O)N1CCN(C=2C=C3CCC(=O)NC3=CC=2)CC1 ZVNYJIZDIRKMBF-UHFFFAOYSA-N 0.000 description 1
- 229930003268 Vitamin C Natural products 0.000 description 1
- 108700040099 Xylose isomerases Proteins 0.000 description 1
- 238000009825 accumulation Methods 0.000 description 1
- 125000002777 acetyl group Chemical group [H]C([H])([H])C(*)=O 0.000 description 1
- UELITFHSCLAHKR-UHFFFAOYSA-N acibenzolar-S-methyl Chemical group CSC(=O)C1=CC=CC2=C1SN=N2 UELITFHSCLAHKR-UHFFFAOYSA-N 0.000 description 1
- 125000002252 acyl group Chemical group 0.000 description 1
- 230000006978 adaptation Effects 0.000 description 1
- 239000007801 affinity label Substances 0.000 description 1
- 239000008272 agar Substances 0.000 description 1
- 108010047495 alanylglycine Proteins 0.000 description 1
- 150000001298 alcohols Chemical class 0.000 description 1
- 150000001299 aldehydes Chemical class 0.000 description 1
- 229960002478 aldosterone Drugs 0.000 description 1
- 125000001931 aliphatic group Chemical group 0.000 description 1
- 150000001336 alkenes Chemical class 0.000 description 1
- 125000003342 alkenyl group Chemical group 0.000 description 1
- 125000000217 alkyl group Chemical group 0.000 description 1
- 102000015395 alpha 1-Antitrypsin Human genes 0.000 description 1
- 108010050122 alpha 1-Antitrypsin Proteins 0.000 description 1
- 229940024142 alpha 1-antitrypsin Drugs 0.000 description 1
- KOSRFJWDECSPRO-UHFFFAOYSA-N alpha-L-glutamyl-L-glutamic acid Natural products OC(=O)CCC(N)C(=O)NC(CCC(O)=O)C(O)=O KOSRFJWDECSPRO-UHFFFAOYSA-N 0.000 description 1
- 150000001370 alpha-amino acid derivatives Chemical class 0.000 description 1
- 102000005922 amidase Human genes 0.000 description 1
- 150000001412 amines Chemical class 0.000 description 1
- 229940093740 amino acid and derivative Drugs 0.000 description 1
- 150000003862 amino acid derivatives Chemical class 0.000 description 1
- 125000003277 amino group Chemical group 0.000 description 1
- 229940124277 aminobutyric acid Drugs 0.000 description 1
- 239000012491 analyte Substances 0.000 description 1
- 210000004102 animal cell Anatomy 0.000 description 1
- 230000002587 anti-hemolytic effect Effects 0.000 description 1
- 108010082685 antiarrhythmic peptide Proteins 0.000 description 1
- 229940088710 antibiotic agent Drugs 0.000 description 1
- 239000000427 antigen Substances 0.000 description 1
- 108091007433 antigens Proteins 0.000 description 1
- 102000036639 antigens Human genes 0.000 description 1
- 239000003430 antimalarial agent Substances 0.000 description 1
- 229940033495 antimalarials Drugs 0.000 description 1
- 239000002246 antineoplastic agent Substances 0.000 description 1
- OZDNDGXASTWERN-UHFFFAOYSA-N apovincamine Natural products C1=CC=C2C(CCN3CCC4)=C5C3C4(CC)C=C(C(=O)OC)N5C2=C1 OZDNDGXASTWERN-UHFFFAOYSA-N 0.000 description 1
- 230000011681 asexual reproduction Effects 0.000 description 1
- 238000013465 asexual reproduction Methods 0.000 description 1
- 229940009098 aspartate Drugs 0.000 description 1
- 235000003704 aspartic acid Nutrition 0.000 description 1
- FZCSTZYAHCUGEM-UHFFFAOYSA-N aspergillomarasmine B Natural products OC(=O)CNC(C(O)=O)CNC(C(O)=O)CC(O)=O FZCSTZYAHCUGEM-UHFFFAOYSA-N 0.000 description 1
- 125000004429 atom Chemical group 0.000 description 1
- 230000001746 atrial effect Effects 0.000 description 1
- 244000052616 bacterial pathogen Species 0.000 description 1
- 238000007630 basic procedure Methods 0.000 description 1
- 125000003236 benzoyl group Chemical group [H]C1=C([H])C([H])=C(C([H])=C1[H])C(*)=O 0.000 description 1
- OQFSQFPPLPISGP-UHFFFAOYSA-N beta-carboxyaspartic acid Natural products OC(=O)C(N)C(C(O)=O)C(O)=O OQFSQFPPLPISGP-UHFFFAOYSA-N 0.000 description 1
- 108091008324 binding proteins Proteins 0.000 description 1
- 239000011942 biocatalyst Substances 0.000 description 1
- 230000008827 biological function Effects 0.000 description 1
- 229960002685 biotin Drugs 0.000 description 1
- 235000020958 biotin Nutrition 0.000 description 1
- 239000011616 biotin Substances 0.000 description 1
- LWISPDYGRSGXME-YDHLFZDLSA-N biotin peg2 amine Chemical compound N1C(=O)N[C@@H]2[C@H](CCCCC(=O)NCCOCCOCCN)SC[C@@H]21 LWISPDYGRSGXME-YDHLFZDLSA-N 0.000 description 1
- 150000001615 biotins Chemical class 0.000 description 1
- JCZLABDVDPYLRZ-AWEZNQCLSA-N biphenylalanine Chemical compound C1=CC(C[C@H](N)C(O)=O)=CC=C1C1=CC=CC=C1 JCZLABDVDPYLRZ-AWEZNQCLSA-N 0.000 description 1
- 230000000903 blocking effect Effects 0.000 description 1
- 238000006664 bond formation reaction Methods 0.000 description 1
- ZADPBFCGQRWHPN-UHFFFAOYSA-N boronic acid Chemical compound OBO ZADPBFCGQRWHPN-UHFFFAOYSA-N 0.000 description 1
- BBBFJLBPOGFECG-VJVYQDLKSA-N calcitonin Chemical compound N([C@H](C(=O)N[C@@H](CC(C)C)C(=O)NCC(=O)N[C@@H](CCCCN)C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](CO)C(=O)N[C@@H](CCC(N)=O)C(=O)N[C@@H](CCC(O)=O)C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](CC=1NC=NC=1)C(=O)N[C@@H](CCCCN)C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](CCC(N)=O)C(=O)N[C@@H]([C@@H](C)O)C(=O)N[C@@H](CC=1C=CC(O)=CC=1)C(=O)N1[C@@H](CCC1)C(=O)N[C@@H](CCCNC(N)=N)C(=O)N[C@@H]([C@@H](C)O)C(=O)N[C@@H](CC(N)=O)C(=O)N[C@@H]([C@@H](C)O)C(=O)NCC(=O)N[C@@H](CO)C(=O)NCC(=O)N[C@@H]([C@@H](C)O)C(=O)N1[C@@H](CCC1)C(N)=O)C(C)C)C(=O)[C@@H]1CSSC[C@H](N)C(=O)N[C@@H](CO)C(=O)N[C@@H](CC(N)=O)C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](CO)C(=O)N[C@@H]([C@@H](C)O)C(=O)N1 BBBFJLBPOGFECG-VJVYQDLKSA-N 0.000 description 1
- 229960004015 calcitonin Drugs 0.000 description 1
- 229910052791 calcium Inorganic materials 0.000 description 1
- 239000011575 calcium Substances 0.000 description 1
- 150000001719 carbohydrate derivatives Chemical class 0.000 description 1
- 235000014633 carbohydrates Nutrition 0.000 description 1
- 150000001735 carboxylic acids Chemical class 0.000 description 1
- NSQLIUXCMFBZME-MPVJKSABSA-N carperitide Chemical compound C([C@H]1C(=O)NCC(=O)NCC(=O)N[C@@H](CCCNC(N)=N)C(=O)N[C@@H](CCSC)C(=O)N[C@@H](CC(O)=O)C(=O)N[C@@H](CCCNC(N)=N)C(=O)N[C@H](C(NCC(=O)N[C@@H](C)C(=O)N[C@@H](CCC(N)=O)C(=O)N[C@@H](CO)C(=O)NCC(=O)N[C@@H](CC(C)C)C(=O)NCC(=O)N[C@@H](CSSC[C@@H](C(=O)N1)NC(=O)[C@H](CO)NC(=O)[C@H](CO)NC(=O)[C@H](CCCNC(N)=N)NC(=O)[C@H](CCCNC(N)=N)NC(=O)[C@H](CC(C)C)NC(=O)[C@@H](N)CO)C(=O)N[C@@H](CC(N)=O)C(=O)N[C@@H](CO)C(=O)N[C@@H](CC=1C=CC=CC=1)C(=O)N[C@@H](CCCNC(N)=N)C(=O)N[C@@H](CC=1C=CC(O)=CC=1)C(O)=O)=O)[C@@H](C)CC)C1=CC=CC=C1 NSQLIUXCMFBZME-MPVJKSABSA-N 0.000 description 1
- 101150055766 cat gene Proteins 0.000 description 1
- 230000034303 cell budding Effects 0.000 description 1
- 230000030833 cell death Effects 0.000 description 1
- 230000024245 cell differentiation Effects 0.000 description 1
- 239000013592 cell lysate Substances 0.000 description 1
- 210000000170 cell membrane Anatomy 0.000 description 1
- 230000009134 cell regulation Effects 0.000 description 1
- 230000003833 cell viability Effects 0.000 description 1
- 239000002738 chelating agent Substances 0.000 description 1
- 239000003638 chemical reducing agent Substances 0.000 description 1
- 229960003677 chloroquine Drugs 0.000 description 1
- WHTVZRBIWZFKQO-UHFFFAOYSA-N chloroquine Natural products ClC1=CC=C2C(NC(C)CCCN(CC)CC)=CC=NC2=C1 WHTVZRBIWZFKQO-UHFFFAOYSA-N 0.000 description 1
- 239000013599 cloning vector Substances 0.000 description 1
- 230000015271 coagulation Effects 0.000 description 1
- 238000005345 coagulation Methods 0.000 description 1
- 229920001436 collagen Polymers 0.000 description 1
- 239000004074 complement inhibitor Substances 0.000 description 1
- 238000004590 computer program Methods 0.000 description 1
- 239000000470 constituent Substances 0.000 description 1
- OMFXVFTZEKFJBZ-HJTSIMOOSA-N corticosterone Chemical compound O=C1CC[C@]2(C)[C@H]3[C@@H](O)C[C@](C)([C@H](CC4)C(=O)CO)[C@@H]4[C@@H]3CCC2=C1 OMFXVFTZEKFJBZ-HJTSIMOOSA-N 0.000 description 1
- 238000004132 cross linking Methods 0.000 description 1
- 239000003431 cross linking reagent Substances 0.000 description 1
- 239000013078 crystal Substances 0.000 description 1
- 231100000433 cytotoxic Toxicity 0.000 description 1
- 230000001472 cytotoxic effect Effects 0.000 description 1
- 230000006324 decarbonylation Effects 0.000 description 1
- 238000006606 decarbonylation reaction Methods 0.000 description 1
- 230000003247 decreasing effect Effects 0.000 description 1
- 230000000593 degrading effect Effects 0.000 description 1
- 238000013461 design Methods 0.000 description 1
- 239000003599 detergent Substances 0.000 description 1
- 238000001784 detoxification Methods 0.000 description 1
- 229950006137 dexfosfoserine Drugs 0.000 description 1
- 235000014113 dietary fatty acids Nutrition 0.000 description 1
- 239000002934 diuretic Substances 0.000 description 1
- 230000012361 double-strand break repair Effects 0.000 description 1
- 239000003937 drug carrier Substances 0.000 description 1
- 241001492478 dsDNA viruses, no RNA stage Species 0.000 description 1
- 230000009977 dual effect Effects 0.000 description 1
- 238000007350 electrophilic reaction Methods 0.000 description 1
- 238000004520 electroporation Methods 0.000 description 1
- 230000008030 elimination Effects 0.000 description 1
- 238000003379 elimination reaction Methods 0.000 description 1
- 108010048367 enhanced green fluorescent protein Proteins 0.000 description 1
- 231100000655 enterotoxin Toxicity 0.000 description 1
- 230000009088 enzymatic function Effects 0.000 description 1
- 230000009483 enzymatic pathway Effects 0.000 description 1
- 229940116977 epidermal growth factor Drugs 0.000 description 1
- 229940105423 erythropoietin Drugs 0.000 description 1
- 150000002148 esters Chemical class 0.000 description 1
- 229940011871 estrogen Drugs 0.000 description 1
- 239000000262 estrogen Substances 0.000 description 1
- 241001233957 eudicotyledons Species 0.000 description 1
- 239000002095 exotoxin Substances 0.000 description 1
- 231100000776 exotoxin Toxicity 0.000 description 1
- 238000002474 experimental method Methods 0.000 description 1
- 229960004222 factor ix Drugs 0.000 description 1
- 229940012413 factor vii Drugs 0.000 description 1
- 229960000301 factor viii Drugs 0.000 description 1
- 229940012426 factor x Drugs 0.000 description 1
- 125000004030 farnesyl group Chemical group [H]C([*])([H])C([H])=C(C([H])([H])[H])C([H])([H])C([H])([H])C([H])=C(C([H])([H])[H])C([H])([H])C([H])([H])C([H])=C(C([H])([H])[H])C([H])([H])[H] 0.000 description 1
- 229930195729 fatty acid Natural products 0.000 description 1
- 239000000194 fatty acid Substances 0.000 description 1
- 150000004665 fatty acids Chemical class 0.000 description 1
- 229940012952 fibrinogen Drugs 0.000 description 1
- 230000004992 fission Effects 0.000 description 1
- ZHNUHDYFZUAESO-UHFFFAOYSA-N formamide Substances NC=O ZHNUHDYFZUAESO-UHFFFAOYSA-N 0.000 description 1
- 238000013467 fragmentation Methods 0.000 description 1
- 238000006062 fragmentation reaction Methods 0.000 description 1
- 231100000221 frame shift mutation induction Toxicity 0.000 description 1
- UHBYWPGGCSDKFX-VKHMYHEASA-N gamma-carboxy-L-glutamic acid Chemical compound OC(=O)[C@@H](N)CC(C(O)=O)C(O)=O UHBYWPGGCSDKFX-VKHMYHEASA-N 0.000 description 1
- 230000002496 gastric effect Effects 0.000 description 1
- 238000012248 genetic selection Methods 0.000 description 1
- 229930195712 glutamate Natural products 0.000 description 1
- 108010055341 glutamyl-glutamic acid Proteins 0.000 description 1
- 102000045442 glycosyltransferase activity proteins Human genes 0.000 description 1
- 108700014210 glycosyltransferase activity proteins Proteins 0.000 description 1
- 239000002622 gonadotropin Substances 0.000 description 1
- 230000036541 health Effects 0.000 description 1
- 229960002897 heparin Drugs 0.000 description 1
- 229920000669 heparin Polymers 0.000 description 1
- 208000002672 hepatitis B Diseases 0.000 description 1
- 230000006658 host protein synthesis Effects 0.000 description 1
- 125000002887 hydroxy group Chemical group [H]O* 0.000 description 1
- 150000002466 imines Chemical class 0.000 description 1
- 150000007976 iminium ions Chemical class 0.000 description 1
- 230000003053 immunization Effects 0.000 description 1
- 238000002649 immunization Methods 0.000 description 1
- 230000005847 immunogenicity Effects 0.000 description 1
- 102000018358 immunoglobulin Human genes 0.000 description 1
- 229940072221 immunoglobulins Drugs 0.000 description 1
- 238000010324 immunological assay Methods 0.000 description 1
- 229940097275 indigo Drugs 0.000 description 1
- COHYTHOBJLSHDF-UHFFFAOYSA-N indigo powder Natural products N1C2=CC=CC=C2C(=O)C1=C1C(=O)C2=CC=CC=C2N1 COHYTHOBJLSHDF-UHFFFAOYSA-N 0.000 description 1
- 230000001939 inductive effect Effects 0.000 description 1
- 230000002458 infectious effect Effects 0.000 description 1
- 206010022000 influenza Diseases 0.000 description 1
- 230000002401 inhibitory effect Effects 0.000 description 1
- 230000000977 initiatory effect Effects 0.000 description 1
- 229940125396 insulin Drugs 0.000 description 1
- 230000010354 integration Effects 0.000 description 1
- 102000002467 interleukin receptors Human genes 0.000 description 1
- 108010093036 interleukin receptors Proteins 0.000 description 1
- 230000003834 intracellular effect Effects 0.000 description 1
- JEIPFZHSYJVQDO-UHFFFAOYSA-N iron(III) oxide Inorganic materials O=[Fe]O[Fe]=O JEIPFZHSYJVQDO-UHFFFAOYSA-N 0.000 description 1
- YOBAEOGBNPPUQV-UHFFFAOYSA-N iron;trihydrate Chemical compound O.O.O.[Fe].[Fe] YOBAEOGBNPPUQV-UHFFFAOYSA-N 0.000 description 1
- 230000002427 irreversible effect Effects 0.000 description 1
- 125000001449 isopropyl group Chemical group [H]C([H])([H])C([H])(*)C([H])([H])[H] 0.000 description 1
- CSSYQJWUGATIHM-IKGCZBKSSA-N l-phenylalanyl-l-lysyl-l-cysteinyl-l-arginyl-l-arginyl-l-tryptophyl-l-glutaminyl-l-tryptophyl-l-arginyl-l-methionyl-l-lysyl-l-lysyl-l-leucylglycyl-l-alanyl-l-prolyl-l-seryl-l-isoleucyl-l-threonyl-l-cysteinyl-l-valyl-l-arginyl-l-arginyl-l-alanyl-l-phenylal Chemical compound C([C@H](N)C(=O)N[C@@H](CCCCN)C(=O)N[C@@H](CS)C(=O)N[C@@H](CCCNC(N)=N)C(=O)N[C@@H](CCCNC(N)=N)C(=O)N[C@@H](CC=1C2=CC=CC=C2NC=1)C(=O)N[C@@H](CCC(N)=O)C(=O)N[C@@H](CC=1C2=CC=CC=C2NC=1)C(=O)N[C@@H](CCCNC(N)=N)C(=O)N[C@@H](CCSC)C(=O)N[C@@H](CCCCN)C(=O)N[C@@H](CCCCN)C(=O)N[C@@H](CC(C)C)C(=O)NCC(=O)N[C@@H](C)C(=O)N1CCC[C@H]1C(=O)N[C@@H](CO)C(=O)N[C@@H]([C@@H](C)CC)C(=O)N[C@@H]([C@@H](C)O)C(=O)N[C@@H](CS)C(=O)N[C@@H](C(C)C)C(=O)N[C@@H](CCCNC(N)=N)C(=O)N[C@@H](CCCNC(N)=N)C(=O)N[C@@H](C)C(=O)N[C@@H](CC=1C=CC=CC=1)C(O)=O)C1=CC=CC=C1 CSSYQJWUGATIHM-IKGCZBKSSA-N 0.000 description 1
- 238000002372 labelling Methods 0.000 description 1
- 229940039696 lactobacillus Drugs 0.000 description 1
- 229940078795 lactoferrin Drugs 0.000 description 1
- 235000021242 lactoferrin Nutrition 0.000 description 1
- 230000000670 limiting effect Effects 0.000 description 1
- 235000019421 lipase Nutrition 0.000 description 1
- 239000007788 liquid Substances 0.000 description 1
- 239000006194 liquid suspension Substances 0.000 description 1
- 230000004807 localization Effects 0.000 description 1
- 238000004020 luminiscence type Methods 0.000 description 1
- 101150109301 lys2 gene Proteins 0.000 description 1
- 229920002521 macromolecule Polymers 0.000 description 1
- 238000004949 mass spectrometry Methods 0.000 description 1
- 238000002844 melting Methods 0.000 description 1
- 230000008018 melting Effects 0.000 description 1
- 125000000956 methoxy group Chemical group [H]C([H])([H])O* 0.000 description 1
- 230000000813 microbial effect Effects 0.000 description 1
- 230000002906 microbiologic effect Effects 0.000 description 1
- 230000033607 mismatch repair Effects 0.000 description 1
- 230000000877 morphologic effect Effects 0.000 description 1
- 230000000869 mutational effect Effects 0.000 description 1
- 239000002636 mycotoxin Substances 0.000 description 1
- 125000001419 myristoyl group Chemical group O=C([*])C([H])([H])C([H])([H])C([H])([H])C([H])([H])C([H])([H])C([H])([H])C([H])([H])C([H])([H])C([H])([H])C([H])([H])C([H])([H])C([H])([H])C([H])([H])[H] 0.000 description 1
- 230000001452 natriuretic effect Effects 0.000 description 1
- 239000013642 negative control Substances 0.000 description 1
- 229910052757 nitrogen Inorganic materials 0.000 description 1
- 238000007344 nucleophilic reaction Methods 0.000 description 1
- 239000002777 nucleoside Substances 0.000 description 1
- 150000003833 nucleoside derivatives Chemical class 0.000 description 1
- JRZJOMJEPLMPRA-UHFFFAOYSA-N olefin Natural products CCCCCCCC=C JRZJOMJEPLMPRA-UHFFFAOYSA-N 0.000 description 1
- 239000003960 organic solvent Substances 0.000 description 1
- 230000002188 osteogenic effect Effects 0.000 description 1
- PSWJVKKJYCAPTI-UHFFFAOYSA-N oxido-oxo-phosphonophosphanylphosphanium Chemical compound OP(O)(=O)PP(=O)=O PSWJVKKJYCAPTI-UHFFFAOYSA-N 0.000 description 1
- 238000012856 packing Methods 0.000 description 1
- 125000001312 palmitoyl group Chemical group O=C([*])C([H])([H])C([H])([H])C([H])([H])C([H])([H])C([H])([H])C([H])([H])C([H])([H])C([H])([H])C([H])([H])C([H])([H])C([H])([H])C([H])([H])C([H])([H])C([H])([H])C([H])([H])[H] 0.000 description 1
- 230000026792 palmitoylation Effects 0.000 description 1
- 239000000199 parathyroid hormone Substances 0.000 description 1
- 229960001319 parathyroid hormone Drugs 0.000 description 1
- 230000035515 penetration Effects 0.000 description 1
- 108010012038 peptide 78 Proteins 0.000 description 1
- 229940125863 peptide 78 Drugs 0.000 description 1
- 239000000813 peptide hormone Substances 0.000 description 1
- 239000000816 peptidomimetic Substances 0.000 description 1
- 230000035699 permeability Effects 0.000 description 1
- 238000002823 phage display Methods 0.000 description 1
- 150000002993 phenylalanine derivatives Chemical class 0.000 description 1
- ORQWTLCYLDRDHK-UHFFFAOYSA-N phenylselanylbenzene Chemical compound C=1C=CC=CC=1[Se]C1=CC=CC=C1 ORQWTLCYLDRDHK-UHFFFAOYSA-N 0.000 description 1
- DTBNBXWJWCWCIK-UHFFFAOYSA-K phosphonatoenolpyruvate Chemical compound [O-]C(=O)C(=C)OP([O-])([O-])=O DTBNBXWJWCWCIK-UHFFFAOYSA-K 0.000 description 1
- DCWXELXMIBXGTH-QMMMGPOBSA-N phosphonotyrosine Chemical compound OC(=O)[C@@H](N)CC1=CC=C(OP(O)(O)=O)C=C1 DCWXELXMIBXGTH-QMMMGPOBSA-N 0.000 description 1
- 230000004962 physiological condition Effects 0.000 description 1
- 230000008635 plant growth Effects 0.000 description 1
- 102000005162 pleiotrophin Human genes 0.000 description 1
- 230000001402 polyadenylating effect Effects 0.000 description 1
- 229920000642 polymer Polymers 0.000 description 1
- 229920000166 polytrimethylene carbonate Polymers 0.000 description 1
- 238000012545 processing Methods 0.000 description 1
- 229960003387 progesterone Drugs 0.000 description 1
- 239000000186 progesterone Substances 0.000 description 1
- 210000001236 prokaryotic cell Anatomy 0.000 description 1
- 235000013930 proline Nutrition 0.000 description 1
- 238000003498 protein array Methods 0.000 description 1
- 230000013498 protein farnesylation Effects 0.000 description 1
- 108060006633 protein kinase Proteins 0.000 description 1
- 230000026447 protein localization Effects 0.000 description 1
- 230000001698 pyrogenic effect Effects 0.000 description 1
- 238000011002 quantification Methods 0.000 description 1
- 230000002285 radioactive effect Effects 0.000 description 1
- 108010014186 ras Proteins Proteins 0.000 description 1
- 239000000376 reactant Substances 0.000 description 1
- 230000009467 reduction Effects 0.000 description 1
- 230000001105 regulatory effect Effects 0.000 description 1
- 230000008439 repair process Effects 0.000 description 1
- 125000006853 reporter group Chemical group 0.000 description 1
- 238000012827 research and development Methods 0.000 description 1
- 239000011347 resin Substances 0.000 description 1
- 229920005989 resin Polymers 0.000 description 1
- 230000032537 response to toxin Effects 0.000 description 1
- 238000010839 reverse transcription Methods 0.000 description 1
- 230000002441 reversible effect Effects 0.000 description 1
- 108020004418 ribosomal RNA Proteins 0.000 description 1
- 238000007363 ring formation reaction Methods 0.000 description 1
- 102200012545 rs111033635 Human genes 0.000 description 1
- 201000005404 rubella Diseases 0.000 description 1
- 150000003839 salts Chemical class 0.000 description 1
- 229920006395 saturated elastomer Polymers 0.000 description 1
- 229930195734 saturated hydrocarbon Natural products 0.000 description 1
- 235000016491 selenocysteine Nutrition 0.000 description 1
- 229940055619 selenocysteine Drugs 0.000 description 1
- ZKZBPNGNEQAJSX-UHFFFAOYSA-N selenocysteine Natural products [SeH]CC(N)C(O)=O ZKZBPNGNEQAJSX-UHFFFAOYSA-N 0.000 description 1
- 150000003962 selenoxides Chemical class 0.000 description 1
- 239000013605 shuttle vector Substances 0.000 description 1
- 150000003384 small molecules Chemical class 0.000 description 1
- 239000002904 solvent Substances 0.000 description 1
- NHXLMOGPVYXJNR-ATOGVRKGSA-N somatostatin Chemical compound C([C@H]1C(=O)N[C@H](C(N[C@@H](CO)C(=O)N[C@@H](CSSC[C@@H](C(=O)N[C@@H](CCCCN)C(=O)N[C@@H](CC(N)=O)C(=O)N[C@@H](CC=2C=CC=CC=2)C(=O)N[C@@H](CC=2C=CC=CC=2)C(=O)N[C@@H](CC=2C3=CC=CC=C3NC=2)C(=O)N[C@@H](CCCCN)C(=O)N[C@H](C(=O)N1)[C@@H](C)O)NC(=O)CNC(=O)[C@H](C)N)C(O)=O)=O)[C@H](O)C)C1=CC=CC=C1 NHXLMOGPVYXJNR-ATOGVRKGSA-N 0.000 description 1
- 229960000553 somatostatin Drugs 0.000 description 1
- 230000002269 spontaneous effect Effects 0.000 description 1
- 235000019698 starch Nutrition 0.000 description 1
- 239000008107 starch Substances 0.000 description 1
- 239000007858 starting material Substances 0.000 description 1
- 238000007619 statistical method Methods 0.000 description 1
- 230000000707 stereoselective effect Effects 0.000 description 1
- 108020003113 steroid hormone receptors Proteins 0.000 description 1
- 102000005969 steroid hormone receptors Human genes 0.000 description 1
- 230000004936 stimulating effect Effects 0.000 description 1
- 229960005202 streptokinase Drugs 0.000 description 1
- 125000003107 substituted aryl group Chemical group 0.000 description 1
- 125000002653 sulfanylmethyl group Chemical group [H]SC([H])([H])[*] 0.000 description 1
- 231100000617 superantigen Toxicity 0.000 description 1
- 238000001308 synthesis method Methods 0.000 description 1
- 230000009897 systematic effect Effects 0.000 description 1
- 229960003604 testosterone Drugs 0.000 description 1
- 229940124597 therapeutic agent Drugs 0.000 description 1
- RYYWUUFWQRZTIU-UHFFFAOYSA-K thiophosphate Chemical compound [O-]P([O-])([O-])=S RYYWUUFWQRZTIU-UHFFFAOYSA-K 0.000 description 1
- NZVYCXVTEHPMHE-ZSUJOUNUSA-N thymalfasin Chemical compound CC(=O)N[C@@H](CO)C(=O)N[C@@H](CC(O)=O)C(=O)N[C@@H](C)C(=O)N[C@@H](C)C(=O)N[C@@H](C(C)C)C(=O)N[C@@H](CC(O)=O)C(=O)N[C@@H]([C@@H](C)O)C(=O)N[C@@H](CO)C(=O)N[C@@H](CO)C(=O)N[C@@H](CCC(O)=O)C(=O)N[C@@H]([C@@H](C)CC)C(=O)N[C@@H]([C@@H](C)O)C(=O)N[C@@H]([C@@H](C)O)C(=O)N[C@@H](CCCCN)C(=O)N[C@@H](CC(O)=O)C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](CCCCN)C(=O)N[C@@H](CCC(O)=O)C(=O)N[C@@H](CCCCN)C(=O)N[C@@H](CCCCN)C(=O)N[C@@H](CCC(O)=O)C(=O)N[C@@H](C(C)C)C(=O)N[C@@H](C(C)C)C(=O)N[C@@H](CCC(O)=O)C(=O)N[C@@H](CCC(O)=O)C(=O)N[C@@H](C)C(=O)N[C@@H](CCC(O)=O)C(=O)N[C@@H](CC(N)=O)C(O)=O NZVYCXVTEHPMHE-ZSUJOUNUSA-N 0.000 description 1
- 229960004231 thymalfasin Drugs 0.000 description 1
- 229940113082 thymine Drugs 0.000 description 1
- 229960000187 tissue plasminogen activator Drugs 0.000 description 1
- 231100000419 toxicity Toxicity 0.000 description 1
- 230000001988 toxicity Effects 0.000 description 1
- 238000002723 toxicity assay Methods 0.000 description 1
- 230000005026 transcription initiation Effects 0.000 description 1
- 230000001131 transforming effect Effects 0.000 description 1
- 230000009261 transgenic effect Effects 0.000 description 1
- 230000014621 translational initiation 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
- 125000001493 tyrosinyl group Chemical group [H]OC1=C([H])C([H])=C(C([H])=C1[H])C([H])([H])C([H])(N([H])[H])C(*)=O 0.000 description 1
- 108010035534 tyrosyl-leucyl-alanine Proteins 0.000 description 1
- 241001515965 unidentified phage Species 0.000 description 1
- 241001430294 unidentified retrovirus Species 0.000 description 1
- 229930195735 unsaturated hydrocarbon Natural products 0.000 description 1
- 229960005356 urokinase Drugs 0.000 description 1
- 208000007089 vaccinia Diseases 0.000 description 1
- 238000010200 validation analysis Methods 0.000 description 1
- 239000013603 viral vector Substances 0.000 description 1
- 235000019154 vitamin C Nutrition 0.000 description 1
- 239000011718 vitamin C Substances 0.000 description 1
- XLYOFNOQVPJJNP-UHFFFAOYSA-N water Substances O XLYOFNOQVPJJNP-UHFFFAOYSA-N 0.000 description 1
- JPZXHKDZASGCLU-LBPRGKRZSA-N β-(2-naphthyl)-alanine Chemical compound C1=CC=CC2=CC(C[C@H](N)C(O)=O)=CC=C21 JPZXHKDZASGCLU-LBPRGKRZSA-N 0.000 description 1
Classifications
-
- C—CHEMISTRY; METALLURGY
- C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
- C12N—MICROORGANISMS OR ENZYMES; COMPOSITIONS THEREOF; PROPAGATING, PRESERVING, OR MAINTAINING MICROORGANISMS; MUTATION OR GENETIC ENGINEERING; CULTURE MEDIA
- C12N15/00—Mutation or genetic engineering; DNA or RNA concerning genetic engineering, vectors, e.g. plasmids, or their isolation, preparation or purification; Use of hosts therefor
- C12N15/09—Recombinant DNA-technology
-
- 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
- C12N9/00—Enzymes; Proenzymes; Compositions thereof; Processes for preparing, activating, inhibiting, separating or purifying enzymes
- C12N9/10—Transferases (2.)
- C12N9/1025—Acyltransferases (2.3)
- C12N9/104—Aminoacyltransferases (2.3.2)
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K14/00—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof
- C07K14/195—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from bacteria
-
- 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
- C12N15/63—Introduction of foreign genetic material using vectors; Vectors; Use of hosts therefor; Regulation of expression
- C12N15/67—General methods for enhancing the expression
-
- 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
- C12N15/63—Introduction of foreign genetic material using vectors; Vectors; Use of hosts therefor; Regulation of expression
- C12N15/74—Vectors or expression systems specially adapted for prokaryotic hosts other than E. coli, e.g. Lactobacillus, Micromonospora
-
- 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
- C12N9/00—Enzymes; Proenzymes; Compositions thereof; Processes for preparing, activating, inhibiting, separating or purifying enzymes
- C12N9/93—Ligases (6)
-
- C—CHEMISTRY; METALLURGY
- C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
- C12P—FERMENTATION OR ENZYME-USING PROCESSES TO SYNTHESISE A DESIRED CHEMICAL COMPOUND OR COMPOSITION OR TO SEPARATE OPTICAL ISOMERS FROM A RACEMIC MIXTURE
- C12P21/00—Preparation of peptides or proteins
- C12P21/02—Preparation of peptides or proteins having a known sequence of two or more amino acids, e.g. glutathione
-
- C—CHEMISTRY; METALLURGY
- C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
- C12P—FERMENTATION OR ENZYME-USING PROCESSES TO SYNTHESISE A DESIRED CHEMICAL COMPOUND OR COMPOSITION OR TO SEPARATE OPTICAL ISOMERS FROM A RACEMIC MIXTURE
- C12P21/00—Preparation of peptides or proteins
- C12P21/06—Preparation of peptides or proteins produced by the hydrolysis of a peptide bond, e.g. hydrolysate products
Landscapes
- Life Sciences & Earth Sciences (AREA)
- Health & Medical Sciences (AREA)
- Chemical & Material Sciences (AREA)
- Genetics & Genomics (AREA)
- Organic Chemistry (AREA)
- Engineering & Computer Science (AREA)
- Zoology (AREA)
- Wood Science & Technology (AREA)
- Bioinformatics & Cheminformatics (AREA)
- Biotechnology (AREA)
- General Engineering & Computer Science (AREA)
- General Health & Medical Sciences (AREA)
- Biochemistry (AREA)
- Molecular Biology (AREA)
- Biomedical Technology (AREA)
- Microbiology (AREA)
- Biophysics (AREA)
- Medicinal Chemistry (AREA)
- Plant Pathology (AREA)
- Physics & Mathematics (AREA)
- Proteomics, Peptides & Aminoacids (AREA)
- Chemical Kinetics & Catalysis (AREA)
- General Chemical & Material Sciences (AREA)
- Gastroenterology & Hepatology (AREA)
- Micro-Organisms Or Cultivation Processes Thereof (AREA)
- Preparation Of Compounds By Using Micro-Organisms (AREA)
- Peptides Or Proteins (AREA)
Applications Claiming Priority (5)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| US78327206P | 2006-03-16 | 2006-03-16 | |
| US60/783,272 | 2006-03-16 | ||
| US86145606P | 2006-11-28 | 2006-11-28 | |
| US60/861,456 | 2006-11-28 | ||
| PCT/US2007/006382 WO2007109035A2 (en) | 2006-03-16 | 2007-03-13 | Genetically programmed expression of proteins containing the unnatural amino acid phenylselenocysteine |
Publications (1)
| Publication Number | Publication Date |
|---|---|
| CA2638772A1 true CA2638772A1 (en) | 2007-09-27 |
Family
ID=38522926
Family Applications (1)
| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| CA002638772A Abandoned CA2638772A1 (en) | 2006-03-16 | 2007-03-13 | Genetically programmed expression of proteins containing the unnatural amino acid phenylselenocysteine |
Country Status (12)
| Country | Link |
|---|---|
| US (3) | US8217145B2 (enExample) |
| EP (1) | EP1994165B1 (enExample) |
| JP (1) | JP5249194B2 (enExample) |
| KR (1) | KR20080113226A (enExample) |
| CN (1) | CN101405401B (enExample) |
| AU (1) | AU2007227592B2 (enExample) |
| BR (1) | BRPI0709603A2 (enExample) |
| CA (1) | CA2638772A1 (enExample) |
| IL (1) | IL193722A0 (enExample) |
| MX (1) | MX2008011669A (enExample) |
| RU (1) | RU2464315C2 (enExample) |
| WO (1) | WO2007109035A2 (enExample) |
Families Citing this family (33)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| EP1456360B1 (en) * | 2001-04-19 | 2015-06-03 | The Scripps Research Institute | Methods and composition for the production of orthoganal trna-aminoacyltrna synthetase pairs |
| SG160203A1 (en) * | 2002-10-16 | 2010-04-29 | Scripps Research Inst | Glycoprotein synthesis |
| CN101223272B (zh) | 2003-04-17 | 2013-04-03 | 斯克利普斯研究院 | 扩展真核生物遗传密码 |
| EP1649004A4 (en) | 2003-07-07 | 2008-04-09 | Scripps Research Inst | COMPOSITIONS WITH PAIRS OF ORTHOGONAL LYSYL-TRNA AND AMINOACYL-TRNA-SYNTHETASE AND USES THEREOF |
| EP1807515A4 (en) * | 2004-10-27 | 2008-06-18 | Scripps Research Inst | Orthogonal translation components for the in vivo incorporation of unnatural amino acids |
| AU2007223830A1 (en) * | 2006-03-09 | 2007-09-13 | The Scripps Research Institute | System for the expression of orthogonal translation components in eubacterial host cells |
| EP1994165B1 (en) | 2006-03-16 | 2014-11-05 | The Scripps Research Institute | Genetically programmed expression of proteins containing the unnatural amino acid phenylselenocysteine |
| AU2007267950B2 (en) * | 2006-05-23 | 2012-08-16 | The Scripps Research Institute | Genetically encoded fluorescent coumarin amino acids |
| US8114627B2 (en) | 2006-09-21 | 2012-02-14 | The Scripps Research Institute | Genetically programmed expression of selectively sulfated proteins in eubacteria |
| RU2009112104A (ru) | 2006-10-18 | 2010-11-27 | Зе Скрипс Ресеч Инститьют (Us) | Генетическое встраивание не встречающихся в природе аминокислот в белки клеток млекопитающих |
| WO2009055616A2 (en) | 2007-10-25 | 2009-04-30 | The Scripps Research Institute | Genetic incorporation of 3-aminotyrosine into reductases |
| US9249408B2 (en) * | 2007-11-02 | 2016-02-02 | The Scripps Research Institute | Directed evolution using proteins comprising unnatural amino acids |
| WO2009059056A2 (en) * | 2007-11-02 | 2009-05-07 | The Scripps Research Institute | A genetically encoded boronate amino acid |
| AU2008335778B2 (en) * | 2007-12-11 | 2014-04-10 | The Scripps Research Institute | In vivo unnatural amino acid expression in the methylotrophic yeast Pichia pastoris |
| WO2009086497A2 (en) * | 2007-12-28 | 2009-07-09 | Ardell David H | Genetic encryption |
| CA2710683A1 (en) | 2008-01-03 | 2009-07-16 | Verenium Corporation | Transferases and oxidoreductases, nucleic acids encoding them and methods for making and using them |
| AU2009210677A1 (en) * | 2008-02-08 | 2009-08-13 | The Scripps Research Institute | Breaking immunological tolerance with a genetically encoded unnatural amino acid |
| US20090197339A1 (en) * | 2008-12-10 | 2009-08-06 | The Scripps Research Institute | In vivo unnatural amino acid expression in the methylotrophic yeast pichia pastoris |
| US8637306B2 (en) | 2008-12-10 | 2014-01-28 | The Scripps Research Institute | Production of carrier-peptide conjugates using chemically reactive unnatural amino acids |
| US8658394B2 (en) * | 2011-02-02 | 2014-02-25 | Waterstone Pharmaceuticals | Methods, cells and systems for incorporating non-canonical amino acids into proteins |
| CN103215235B (zh) * | 2012-01-18 | 2014-11-05 | 中国科学院生物物理研究所 | 3-咪唑基酪氨酸翻译系统及其应用 |
| CN103571804B (zh) * | 2012-08-10 | 2015-08-12 | 中国科学院生物物理研究所 | 3-吡唑基酪氨酸翻译系统及其应用 |
| KR102018863B1 (ko) | 2012-10-12 | 2019-09-05 | 서트로 바이오파마, 인크. | 개선된 발현을 위해 박테리아 추출물 중 선택 단백질의 단백질분해 불활성화 |
| CN103820410B (zh) * | 2012-11-16 | 2016-03-30 | 中国科学院生物物理研究所 | 3-甲硫酪氨酸翻译系统及其应用 |
| CN104004723B (zh) * | 2013-02-22 | 2016-08-17 | 中国科学院生物物理研究所 | 3,5-二氟代酪氨酸翻译系统及其应用 |
| CN104059891B (zh) * | 2013-03-22 | 2016-08-17 | 中国科学院生物物理研究所 | 8-羟基喹啉丙氨酸翻译系统及其应用 |
| JP6822839B2 (ja) * | 2013-09-13 | 2021-01-27 | ザ・スクリップス・リサーチ・インスティテュート | 修飾された治療剤、及びその組成物 |
| US10039809B2 (en) | 2013-12-18 | 2018-08-07 | The California Institute For Biomedical Research | Modified therapeutic agents, stapled peptide lipid conjugates, and compositions thereof |
| DK3458074T3 (da) * | 2016-05-16 | 2024-07-29 | Univ Texas | COMPOSITIONS FOR THE DELIVERY OF tRNA AS NANOPARTICLES AND METHODS OF USE THEREWITH |
| KR102747205B1 (ko) | 2016-12-29 | 2024-12-31 | 일루미나, 인코포레이티드 | 세포 구획 내의 생체분자에 대한 직교 접근 및 그의 태그부착을 위한 분석 시스템 |
| CN114644581B (zh) * | 2021-01-04 | 2024-07-16 | 北京惠大生物科技有限公司 | 含芳基硫酚或芳基硒酚经修饰的氨基酸、重组蛋白及其生物合成方法及应用 |
| KR20240032010A (ko) | 2021-06-09 | 2024-03-08 | 더 스크립스 리서치 인스티튜트 | 장기 지속형 이중 gip/glp-1 펩타이드 접합체 및 사용 방법 |
| CN118389493B (zh) * | 2024-05-10 | 2025-04-11 | 北京大学 | 一种定点修饰的工程化tRNA及其应用 |
Family Cites Families (22)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| KR20030097604A (ko) * | 1992-07-13 | 2003-12-31 | 유카리언, 인코포레이티드 | 세포의 세포내 구획으로 지질화된 면역글로불린을전달하기 위한 조성물, 지질화된 단백질 및 지질화된 항체 |
| EP1456360B1 (en) * | 2001-04-19 | 2015-06-03 | The Scripps Research Institute | Methods and composition for the production of orthoganal trna-aminoacyltrna synthetase pairs |
| AU2003277373B2 (en) * | 2002-10-16 | 2009-05-07 | The Scripps Research Institute | Site specific incorporation of keto amino acids into proteins |
| SG160203A1 (en) * | 2002-10-16 | 2010-04-29 | Scripps Research Inst | Glycoprotein synthesis |
| CA2508939A1 (en) | 2002-12-22 | 2004-07-15 | The Scripps Research Institute | Protein arrays |
| CN101223272B (zh) | 2003-04-17 | 2013-04-03 | 斯克利普斯研究院 | 扩展真核生物遗传密码 |
| JP5275566B2 (ja) | 2003-06-18 | 2013-08-28 | ザ スクリプス リサーチ インスティチュート | 反応性非天然アミノ酸遺伝コード付加 |
| EP1704242A4 (en) | 2003-07-07 | 2008-06-18 | Scripps Research Inst | COMPOSITIONS WITH PAIRS OF ORTHOGONAL LEUCYL-TRNA AND AMINOACYL-TRNA-SYNTHETASE AND USES THEREOF |
| EP1649004A4 (en) | 2003-07-07 | 2008-04-09 | Scripps Research Inst | COMPOSITIONS WITH PAIRS OF ORTHOGONAL LYSYL-TRNA AND AMINOACYL-TRNA-SYNTHETASE AND USES THEREOF |
| EP1658366A4 (en) | 2003-07-07 | 2006-08-09 | Scripps Research Inst | COMPOSITIONS OF ORTHOGONAL GLUTAMYL-TRNA AND AMINOACYL-TRNA-SYNTHETASEPAARES AND THEIR USES |
| CN1942579B (zh) * | 2003-10-14 | 2013-06-26 | 斯克利普斯研究院 | 将氧化还原活性氨基酸位点特异地掺入蛋白质 |
| CA2549830A1 (en) * | 2003-12-18 | 2006-01-05 | The Scripps Research Institute | Selective incorporation of 5-hyroxytryptophan into proteins in mammalian cells |
| US20050287639A1 (en) | 2004-05-17 | 2005-12-29 | California Institute Of Technology | Methods of incorporating amino acid analogs into proteins |
| JP2008500050A (ja) | 2004-05-25 | 2008-01-10 | ザ スクリップス リサーチ インスティテュート | 結晶構造決定のための重原子含有非天然アミノ酸の部位特異的蛋白質組込み |
| ES2666693T3 (es) | 2004-09-21 | 2018-05-07 | The Scripps Research Institute | Incorporación in vivo de alquinil aminoácidos a proteínas en eubacterias |
| US20090181858A1 (en) | 2004-09-21 | 2009-07-16 | The Scripps Research Institute | Adding photoregulated amino acids to the genetic code |
| EP1794312A4 (en) | 2004-09-22 | 2009-08-12 | Scripps Research Inst | LOCAL LABELING OF PROTEINS FOR NMR STUDIES |
| US20080064059A1 (en) | 2004-10-20 | 2008-03-13 | Scripps Research Institute | In Vivo Site-Specific Incorporation of N-Acetyl-Galactosamine Amino Acids in Eubacteria |
| EP1807515A4 (en) | 2004-10-27 | 2008-06-18 | Scripps Research Inst | Orthogonal translation components for the in vivo incorporation of unnatural amino acids |
| CA2624290A1 (en) * | 2005-10-12 | 2007-04-26 | Scripps Research Institute | Selective posttranslational modification of phage-displayed polypeptides |
| AU2007223830A1 (en) | 2006-03-09 | 2007-09-13 | The Scripps Research Institute | System for the expression of orthogonal translation components in eubacterial host cells |
| EP1994165B1 (en) | 2006-03-16 | 2014-11-05 | The Scripps Research Institute | Genetically programmed expression of proteins containing the unnatural amino acid phenylselenocysteine |
-
2007
- 2007-03-13 EP EP07753037.6A patent/EP1994165B1/en not_active Not-in-force
- 2007-03-13 RU RU2008135114/10A patent/RU2464315C2/ru not_active IP Right Cessation
- 2007-03-13 MX MX2008011669A patent/MX2008011669A/es active IP Right Grant
- 2007-03-13 CN CN2007800092529A patent/CN101405401B/zh not_active Expired - Fee Related
- 2007-03-13 JP JP2009500449A patent/JP5249194B2/ja not_active Expired - Fee Related
- 2007-03-13 AU AU2007227592A patent/AU2007227592B2/en not_active Ceased
- 2007-03-13 KR KR1020087024575A patent/KR20080113226A/ko not_active Ceased
- 2007-03-13 WO PCT/US2007/006382 patent/WO2007109035A2/en not_active Ceased
- 2007-03-13 US US12/225,261 patent/US8217145B2/en active Active
- 2007-03-13 BR BRPI0709603-8A patent/BRPI0709603A2/pt not_active Application Discontinuation
- 2007-03-13 CA CA002638772A patent/CA2638772A1/en not_active Abandoned
- 2007-03-13 US US11/724,039 patent/US7790847B2/en active Active
-
2008
- 2008-08-27 IL IL193722A patent/IL193722A0/en unknown
-
2012
- 2012-06-08 US US13/492,240 patent/US8394605B2/en not_active Expired - Fee Related
Also Published As
| Publication number | Publication date |
|---|---|
| CN101405401A (zh) | 2009-04-08 |
| EP1994165A2 (en) | 2008-11-26 |
| WO2007109035A3 (en) | 2008-10-16 |
| MX2008011669A (es) | 2008-09-22 |
| EP1994165B1 (en) | 2014-11-05 |
| RU2008135114A (ru) | 2010-04-27 |
| US7790847B2 (en) | 2010-09-07 |
| JP5249194B2 (ja) | 2013-07-31 |
| WO2007109035A2 (en) | 2007-09-27 |
| US8394605B2 (en) | 2013-03-12 |
| CN101405401B (zh) | 2013-03-27 |
| US20070238152A1 (en) | 2007-10-11 |
| BRPI0709603A2 (pt) | 2011-07-19 |
| US20120282668A1 (en) | 2012-11-08 |
| RU2464315C2 (ru) | 2012-10-20 |
| JP2009529877A (ja) | 2009-08-27 |
| IL193722A0 (en) | 2011-08-01 |
| US20090209000A1 (en) | 2009-08-20 |
| KR20080113226A (ko) | 2008-12-29 |
| AU2007227592A1 (en) | 2007-09-27 |
| US8217145B2 (en) | 2012-07-10 |
| AU2007227592B2 (en) | 2011-11-24 |
| EP1994165A4 (en) | 2012-11-07 |
Similar Documents
| Publication | Publication Date | Title |
|---|---|---|
| AU2007227592B2 (en) | Genetically programmed expression of proteins containing the unnatural amino acid phenylselenocysteine | |
| AU2005286722B2 (en) | In vivo incorporation of alkynyl amino acids into proteins in eubacteria | |
| US8114654B2 (en) | Site-specific incorporation of redox active amino acids into proteins | |
| US9624485B2 (en) | Genetic incorporation of unnatural amino acids into proteins in mammalian cells | |
| US8361770B2 (en) | Genetically programmed expression of selectively sulfated proteins in Eubacteria | |
| CA2638763A1 (en) | System for the expression of orthogonal translation components in eubacterial host cells | |
| AU2007267950B2 (en) | Genetically encoded fluorescent coumarin amino acids |
Legal Events
| Date | Code | Title | Description |
|---|---|---|---|
| EEER | Examination request | ||
| FZDE | Discontinued |
Effective date: 20141010 |