CA2665678A1 - Genetic incorporation of unnatural amino acids into proteins in mammalian cells - Google Patents
Genetic incorporation of unnatural amino acids into proteins in mammalian cells Download PDFInfo
- Publication number
- CA2665678A1 CA2665678A1 CA002665678A CA2665678A CA2665678A1 CA 2665678 A1 CA2665678 A1 CA 2665678A1 CA 002665678 A CA002665678 A CA 002665678A CA 2665678 A CA2665678 A CA 2665678A CA 2665678 A1 CA2665678 A1 CA 2665678A1
- Authority
- CA
- Canada
- Prior art keywords
- trna
- amino acid
- unnatural amino
- host cell
- cell
- Prior art date
- Legal status (The legal status is an assumption and is not a legal conclusion. Google has not performed a legal analysis and makes no representation as to the accuracy of the status listed.)
- Abandoned
Links
- 150000001413 amino acids Chemical class 0.000 title claims abstract description 510
- 108090000623 proteins and genes Proteins 0.000 title claims abstract description 278
- 102000004169 proteins and genes Human genes 0.000 title claims abstract description 224
- 238000010348 incorporation Methods 0.000 title description 62
- 230000002068 genetic effect Effects 0.000 title description 59
- 210000004962 mammalian cell Anatomy 0.000 title description 54
- 238000000034 method Methods 0.000 claims abstract description 174
- 238000013519 translation Methods 0.000 claims abstract description 127
- 102000052866 Amino Acyl-tRNA Synthetases Human genes 0.000 claims abstract description 89
- 108700028939 Amino Acyl-tRNA Synthetases Proteins 0.000 claims abstract description 89
- 241000288906 Primates Species 0.000 claims abstract description 48
- 241000283984 Rodentia Species 0.000 claims abstract description 48
- 241001112695 Clostridiales Species 0.000 claims abstract description 5
- 108020004705 Codon Proteins 0.000 claims description 199
- 108091033319 polynucleotide Proteins 0.000 claims description 111
- 102000040430 polynucleotide Human genes 0.000 claims description 111
- 239000002157 polynucleotide Substances 0.000 claims description 110
- 150000007523 nucleic acids Chemical class 0.000 claims description 106
- 102000039446 nucleic acids Human genes 0.000 claims description 99
- 108020004707 nucleic acids Proteins 0.000 claims description 99
- 241000588724 Escherichia coli Species 0.000 claims description 59
- 238000004519 manufacturing process Methods 0.000 claims description 34
- 230000004044 response Effects 0.000 claims description 21
- 241000282414 Homo sapiens Species 0.000 claims description 20
- 241001442654 Percnon planissimum Species 0.000 claims description 18
- DOCYTUNUHIGJTI-QMMMGPOBSA-N (2r)-2-[(2-nitrophenyl)methylamino]-3-sulfanylpropanoic acid Chemical compound OC(=O)[C@H](CS)NCC1=CC=CC=C1[N+]([O-])=O DOCYTUNUHIGJTI-QMMMGPOBSA-N 0.000 claims description 17
- 108091028043 Nucleic acid sequence Proteins 0.000 claims description 13
- 239000002773 nucleotide Substances 0.000 claims description 12
- 125000003729 nucleotide group Chemical group 0.000 claims description 12
- 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 claims description 11
- 238000002741 site-directed mutagenesis Methods 0.000 claims description 9
- 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 claims description 8
- 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 claims description 8
- 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 claims description 8
- QHGDJQUCSGUYMF-QMMMGPOBSA-N (2s)-3-hydroxy-2-[(2-nitrophenyl)methylamino]propanoic acid Chemical compound OC[C@@H](C(O)=O)NCC1=CC=CC=C1[N+]([O-])=O QHGDJQUCSGUYMF-QMMMGPOBSA-N 0.000 claims description 8
- 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 claims description 8
- 241001425800 Pipa Species 0.000 claims description 7
- VKBLQCDGTHFOLS-NSHDSACASA-N (2s)-2-(4-benzoylanilino)propanoic acid Chemical compound C1=CC(N[C@@H](C)C(O)=O)=CC=C1C(=O)C1=CC=CC=C1 VKBLQCDGTHFOLS-NSHDSACASA-N 0.000 claims description 6
- 241000282577 Pan troglodytes Species 0.000 claims description 5
- 241000282620 Hylobates sp. Species 0.000 claims description 3
- 241000282553 Macaca Species 0.000 claims description 3
- 241000282576 Pan paniscus Species 0.000 claims description 3
- 241000282405 Pongo abelii Species 0.000 claims description 3
- 241001515942 marmosets Species 0.000 claims description 3
- 241000282575 Gorilla Species 0.000 claims description 2
- 241000288961 Saguinus imperator Species 0.000 claims description 2
- 238000012258 culturing Methods 0.000 claims description 2
- RCRODHONKLSMIF-UHFFFAOYSA-N isosuberenol Natural products O1C(=O)C=CC2=C1C=C(OC)C(CC(O)C(C)=C)=C2 RCRODHONKLSMIF-UHFFFAOYSA-N 0.000 claims description 2
- 230000004952 protein activity Effects 0.000 claims description 2
- AKVBCGQVQXPRLD-UHFFFAOYSA-N 2-aminooctanoic acid Chemical compound CCCCCCC(N)C(O)=O AKVBCGQVQXPRLD-UHFFFAOYSA-N 0.000 claims 2
- 108020004566 Transfer RNA Proteins 0.000 abstract description 197
- 102000003960 Ligases Human genes 0.000 abstract description 81
- 108090000364 Ligases Proteins 0.000 abstract description 81
- 235000001014 amino acid Nutrition 0.000 description 486
- 229940024606 amino acid Drugs 0.000 description 482
- 210000004027 cell Anatomy 0.000 description 366
- 235000018102 proteins Nutrition 0.000 description 200
- 230000014616 translation Effects 0.000 description 120
- 108090000765 processed proteins & peptides Proteins 0.000 description 103
- 102000004196 processed proteins & peptides Human genes 0.000 description 93
- 229920001184 polypeptide Polymers 0.000 description 87
- 230000001629 suppression Effects 0.000 description 56
- 230000014509 gene expression Effects 0.000 description 55
- 241000894007 species Species 0.000 description 49
- 238000001727 in vivo Methods 0.000 description 46
- 239000003550 marker Substances 0.000 description 45
- 239000000203 mixture Substances 0.000 description 39
- 239000013612 plasmid Substances 0.000 description 39
- 102000004190 Enzymes Human genes 0.000 description 38
- 108090000790 Enzymes Proteins 0.000 description 38
- 125000003275 alpha amino acid group Chemical group 0.000 description 37
- 229940088598 enzyme Drugs 0.000 description 37
- 239000005090 green fluorescent protein Substances 0.000 description 37
- 238000002703 mutagenesis Methods 0.000 description 36
- 231100000350 mutagenesis Toxicity 0.000 description 36
- 241000894006 Bacteria Species 0.000 description 33
- 108010043121 Green Fluorescent Proteins Proteins 0.000 description 33
- 102000004144 Green Fluorescent Proteins Human genes 0.000 description 33
- 238000009396 hybridization Methods 0.000 description 32
- 240000004808 Saccharomyces cerevisiae Species 0.000 description 28
- 235000014680 Saccharomyces cerevisiae Nutrition 0.000 description 28
- 108091060545 Nonsense suppressor Proteins 0.000 description 27
- 239000000523 sample Substances 0.000 description 27
- 108020004414 DNA Proteins 0.000 description 26
- 230000006870 function Effects 0.000 description 26
- 238000000338 in vitro Methods 0.000 description 26
- 238000012216 screening Methods 0.000 description 26
- 108020005038 Terminator Codon Proteins 0.000 description 25
- -1 p-acetylphenylalanyl Chemical group 0.000 description 23
- 239000013598 vector Substances 0.000 description 23
- 230000000295 complement effect Effects 0.000 description 22
- 230000000694 effects Effects 0.000 description 22
- 210000004978 chinese hamster ovary cell Anatomy 0.000 description 21
- 101150067361 Aars1 gene Proteins 0.000 description 20
- 238000006467 substitution reaction Methods 0.000 description 20
- 230000015572 biosynthetic process Effects 0.000 description 19
- 230000035772 mutation Effects 0.000 description 19
- 238000012360 testing method Methods 0.000 description 18
- 101710146427 Probable tyrosine-tRNA ligase, cytoplasmic Proteins 0.000 description 17
- 102100025336 Tyrosine-tRNA ligase, mitochondrial Human genes 0.000 description 17
- 101710107268 Tyrosine-tRNA ligase, mitochondrial Proteins 0.000 description 17
- 238000003786 synthesis reaction Methods 0.000 description 17
- 229960004441 tyrosine Drugs 0.000 description 17
- 238000003556 assay Methods 0.000 description 16
- 239000012634 fragment Substances 0.000 description 16
- 230000008569 process Effects 0.000 description 16
- 239000000758 substrate Substances 0.000 description 16
- 238000004885 tandem mass spectrometry Methods 0.000 description 16
- 235000002374 tyrosine Nutrition 0.000 description 16
- QTBSBXVTEAMEQO-UHFFFAOYSA-N Acetic acid Chemical compound CC(O)=O QTBSBXVTEAMEQO-UHFFFAOYSA-N 0.000 description 15
- OUYCCCASQSFEME-QMMMGPOBSA-N L-tyrosine Chemical compound OC(=O)[C@@H](N)CC1=CC=C(O)C=C1 OUYCCCASQSFEME-QMMMGPOBSA-N 0.000 description 15
- 238000004422 calculation algorithm Methods 0.000 description 15
- 238000001228 spectrum Methods 0.000 description 15
- 238000013518 transcription Methods 0.000 description 15
- 150000002500 ions Chemical class 0.000 description 14
- 239000000126 substance Substances 0.000 description 14
- 230000001225 therapeutic effect Effects 0.000 description 14
- 230000035897 transcription Effects 0.000 description 14
- 230000006229 amino acid addition Effects 0.000 description 13
- OUYCCCASQSFEME-UHFFFAOYSA-N tyrosine Natural products OC(=O)C(N)CC1=CC=C(O)C=C1 OUYCCCASQSFEME-UHFFFAOYSA-N 0.000 description 13
- 238000013459 approach Methods 0.000 description 12
- 230000001965 increasing effect Effects 0.000 description 12
- 230000037361 pathway Effects 0.000 description 12
- 241000206602 Eukaryota Species 0.000 description 11
- 108091005971 Wild-type GFP Proteins 0.000 description 11
- 241000193385 Geobacillus stearothermophilus Species 0.000 description 10
- 108010021466 Mutant Proteins Proteins 0.000 description 10
- 102000008300 Mutant Proteins Human genes 0.000 description 10
- 108020004485 Nonsense Codon Proteins 0.000 description 10
- 239000004098 Tetracycline Substances 0.000 description 10
- 238000004458 analytical method Methods 0.000 description 10
- 239000003795 chemical substances by application Substances 0.000 description 10
- 230000001105 regulatory effect Effects 0.000 description 10
- 229960002180 tetracycline Drugs 0.000 description 10
- 229930101283 tetracycline Natural products 0.000 description 10
- 235000019364 tetracycline Nutrition 0.000 description 10
- 150000003522 tetracyclines Chemical class 0.000 description 10
- 238000001262 western blot Methods 0.000 description 10
- WEVYAHXRMPXWCK-UHFFFAOYSA-N Acetonitrile Chemical compound CC#N WEVYAHXRMPXWCK-UHFFFAOYSA-N 0.000 description 9
- 241000203069 Archaea Species 0.000 description 9
- 108010071170 Leucine-tRNA ligase Proteins 0.000 description 9
- 102100023339 Leucine-tRNA ligase, cytoplasmic Human genes 0.000 description 9
- 102000007056 Recombinant Fusion Proteins Human genes 0.000 description 9
- 108010008281 Recombinant Fusion Proteins Proteins 0.000 description 9
- 230000003115 biocidal effect Effects 0.000 description 9
- 230000004071 biological effect Effects 0.000 description 9
- 108091032973 (ribonucleotides)n+m Proteins 0.000 description 8
- 108020005098 Anticodon Proteins 0.000 description 8
- 241000700159 Rattus Species 0.000 description 8
- 238000007792 addition Methods 0.000 description 8
- 230000006696 biosynthetic metabolic pathway Effects 0.000 description 8
- 230000001413 cellular effect Effects 0.000 description 8
- 230000008859 change Effects 0.000 description 8
- 230000001419 dependent effect Effects 0.000 description 8
- 210000005260 human cell Anatomy 0.000 description 8
- 101150066555 lacZ gene Proteins 0.000 description 8
- 239000000463 material Substances 0.000 description 8
- 108020004999 messenger RNA Proteins 0.000 description 8
- 230000004048 modification Effects 0.000 description 8
- 238000012986 modification Methods 0.000 description 8
- 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 8
- 239000000872 buffer Substances 0.000 description 7
- 238000006243 chemical reaction Methods 0.000 description 7
- 150000001875 compounds Chemical class 0.000 description 7
- 238000010276 construction Methods 0.000 description 7
- 239000012528 membrane Substances 0.000 description 7
- 230000002829 reductive effect Effects 0.000 description 7
- 241000196324 Embryophyta Species 0.000 description 6
- 241000205062 Halobacterium Species 0.000 description 6
- ZDXPYRJPNDTMRX-VKHMYHEASA-N L-glutamine Chemical compound OC(=O)[C@@H](N)CCC(N)=O ZDXPYRJPNDTMRX-VKHMYHEASA-N 0.000 description 6
- 241000699666 Mus <mouse, genus> Species 0.000 description 6
- 241000700605 Viruses Species 0.000 description 6
- 239000013592 cell lysate Substances 0.000 description 6
- 238000005516 engineering process Methods 0.000 description 6
- 230000037433 frameshift Effects 0.000 description 6
- 239000000499 gel Substances 0.000 description 6
- 239000001963 growth medium Substances 0.000 description 6
- 230000001976 improved effect Effects 0.000 description 6
- 238000004949 mass spectrometry Methods 0.000 description 6
- 238000010369 molecular cloning Methods 0.000 description 6
- 235000008729 phenylalanine Nutrition 0.000 description 6
- 230000009257 reactivity Effects 0.000 description 6
- 231100000331 toxic Toxicity 0.000 description 6
- 230000002588 toxic effect Effects 0.000 description 6
- 238000001890 transfection Methods 0.000 description 6
- 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 5
- 108020005029 5' Flanking Region Proteins 0.000 description 5
- 241000238631 Hexapoda Species 0.000 description 5
- 241000203407 Methanocaldococcus jannaschii Species 0.000 description 5
- 108091034117 Oligonucleotide Proteins 0.000 description 5
- 241000522615 Pyrococcus horikoshii Species 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
- 230000001186 cumulative effect Effects 0.000 description 5
- 238000002474 experimental method Methods 0.000 description 5
- 239000013604 expression vector Substances 0.000 description 5
- 229910052739 hydrogen Inorganic materials 0.000 description 5
- 239000001257 hydrogen Substances 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
- 238000002955 isolation Methods 0.000 description 5
- 229930182817 methionine Natural products 0.000 description 5
- 238000003752 polymerase chain reaction Methods 0.000 description 5
- 239000000047 product Substances 0.000 description 5
- 238000002708 random mutagenesis Methods 0.000 description 5
- 238000002415 sodium dodecyl sulfate polyacrylamide gel electrophoresis Methods 0.000 description 5
- 210000001519 tissue Anatomy 0.000 description 5
- UQTZMGFTRHFAAM-ZETCQYMHSA-N 3-iodo-L-tyrosine Chemical compound OC(=O)[C@@H](N)CC1=CC=C(O)C(I)=C1 UQTZMGFTRHFAAM-ZETCQYMHSA-N 0.000 description 4
- 244000105975 Antidesma platyphyllum Species 0.000 description 4
- 239000004475 Arginine Substances 0.000 description 4
- 108010016529 Bacillus amyloliquefaciens ribonuclease Proteins 0.000 description 4
- 244000063299 Bacillus subtilis Species 0.000 description 4
- 235000014469 Bacillus subtilis Nutrition 0.000 description 4
- 108010035563 Chloramphenicol O-acetyltransferase Proteins 0.000 description 4
- 241000699802 Cricetulus griseus Species 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
- 241000233866 Fungi Species 0.000 description 4
- 241000282412 Homo Species 0.000 description 4
- OAKJQQAXSVQMHS-UHFFFAOYSA-N Hydrazine Chemical compound NN OAKJQQAXSVQMHS-UHFFFAOYSA-N 0.000 description 4
- 108090000723 Insulin-Like Growth Factor I Proteins 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
- 229930182816 L-glutamine Natural products 0.000 description 4
- COLNVLDHVKWLRT-QMMMGPOBSA-N L-phenylalanine Chemical compound OC(=O)[C@@H](N)CC1=CC=CC=C1 COLNVLDHVKWLRT-QMMMGPOBSA-N 0.000 description 4
- 241001465754 Metazoa Species 0.000 description 4
- 108020004711 Nucleic Acid Probes Proteins 0.000 description 4
- ISAKRJDGNUQOIC-UHFFFAOYSA-N Uracil Chemical compound O=C1C=CNC(=O)N1 ISAKRJDGNUQOIC-UHFFFAOYSA-N 0.000 description 4
- 235000004279 alanine Nutrition 0.000 description 4
- 125000000539 amino acid group Chemical group 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
- 230000001851 biosynthetic effect Effects 0.000 description 4
- 229930189065 blasticidin Natural products 0.000 description 4
- 230000003197 catalytic effect Effects 0.000 description 4
- 239000003153 chemical reaction reagent Substances 0.000 description 4
- 230000002255 enzymatic effect Effects 0.000 description 4
- 229940126864 fibroblast growth factor Drugs 0.000 description 4
- 239000012737 fresh medium Substances 0.000 description 4
- 150000002308 glutamine derivatives Chemical class 0.000 description 4
- 235000009424 haa Nutrition 0.000 description 4
- 238000001294 liquid chromatography-tandem mass spectrometry Methods 0.000 description 4
- 125000001360 methionine group Chemical group N[C@@H](CCSC)C(=O)* 0.000 description 4
- 239000002853 nucleic acid probe Substances 0.000 description 4
- COLNVLDHVKWLRT-UHFFFAOYSA-N phenylalanine Natural products OC(=O)C(N)CC1=CC=CC=C1 COLNVLDHVKWLRT-UHFFFAOYSA-N 0.000 description 4
- 229960005190 phenylalanine Drugs 0.000 description 4
- 239000013641 positive control Substances 0.000 description 4
- 239000002243 precursor Substances 0.000 description 4
- 125000002924 primary amino group Chemical group [H]N([H])* 0.000 description 4
- 238000000746 purification Methods 0.000 description 4
- 102000005962 receptors Human genes 0.000 description 4
- 108020003175 receptors Proteins 0.000 description 4
- 230000006798 recombination Effects 0.000 description 4
- 238000005215 recombination Methods 0.000 description 4
- 238000011160 research Methods 0.000 description 4
- 239000002904 solvent Substances 0.000 description 4
- 125000001424 substituent group Chemical group 0.000 description 4
- 230000002103 transcriptional effect Effects 0.000 description 4
- 241000282693 Cercopithecidae 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
- 108010014303 DNA-directed DNA polymerase Proteins 0.000 description 3
- 102000016928 DNA-directed DNA polymerase Human genes 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
- 102100039620 Granulocyte-macrophage colony-stimulating factor Human genes 0.000 description 3
- 102100034221 Growth-regulated alpha protein Human genes 0.000 description 3
- 241000204933 Haloferax volcanii Species 0.000 description 3
- 102000007625 Hirudins Human genes 0.000 description 3
- 108010007267 Hirudins Proteins 0.000 description 3
- 241001272567 Hominoidea Species 0.000 description 3
- 101000611183 Homo sapiens Tumor necrosis factor Proteins 0.000 description 3
- 108010002352 Interleukin-1 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
- ROHFNLRQFUQHCH-YFKPBYRVSA-N L-leucine Chemical compound CC(C)C[C@H](N)C(O)=O ROHFNLRQFUQHCH-YFKPBYRVSA-N 0.000 description 3
- 241000288903 Lemuridae Species 0.000 description 3
- ROHFNLRQFUQHCH-UHFFFAOYSA-N Leucine Natural products CC(C)CC(N)C(O)=O ROHFNLRQFUQHCH-UHFFFAOYSA-N 0.000 description 3
- 241000124008 Mammalia 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
- 241000288935 Platyrrhini Species 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
- 102000013275 Somatomedins Human genes 0.000 description 3
- 241000168914 Strepsirrhini Species 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
- 102000004142 Trypsin Human genes 0.000 description 3
- 108090000631 Trypsin Proteins 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
- 210000004102 animal cell Anatomy 0.000 description 3
- 125000003118 aryl group Chemical group 0.000 description 3
- 229960001230 asparagine Drugs 0.000 description 3
- 210000004671 cell-free system Anatomy 0.000 description 3
- 230000007541 cellular toxicity Effects 0.000 description 3
- 238000010367 cloning Methods 0.000 description 3
- XUJNEKJLAYXESH-UHFFFAOYSA-N cysteine Natural products SCC(N)C(O)=O XUJNEKJLAYXESH-UHFFFAOYSA-N 0.000 description 3
- 235000018417 cysteine Nutrition 0.000 description 3
- 238000012217 deletion Methods 0.000 description 3
- 230000037430 deletion Effects 0.000 description 3
- 238000010790 dilution Methods 0.000 description 3
- 239000012895 dilution Substances 0.000 description 3
- 241001493065 dsRNA viruses Species 0.000 description 3
- 238000001425 electrospray ionisation time-of-flight mass spectrometry Methods 0.000 description 3
- 230000007613 environmental effect Effects 0.000 description 3
- 210000003527 eukaryotic cell Anatomy 0.000 description 3
- 238000001943 fluorescence-activated cell sorting Methods 0.000 description 3
- 238000003306 harvesting Methods 0.000 description 3
- 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 3
- 229940006607 hirudin Drugs 0.000 description 3
- 230000006801 homologous recombination Effects 0.000 description 3
- 238000002744 homologous recombination Methods 0.000 description 3
- 238000011534 incubation Methods 0.000 description 3
- 230000001939 inductive effect Effects 0.000 description 3
- 230000002757 inflammatory effect Effects 0.000 description 3
- 238000001819 mass spectrum Methods 0.000 description 3
- 239000011159 matrix material Substances 0.000 description 3
- 238000012269 metabolic engineering Methods 0.000 description 3
- 244000005700 microbiome Species 0.000 description 3
- NCGWKCHAJOUDHQ-UHFFFAOYSA-N n,n-diethylethanamine;formic acid Chemical compound OC=O.OC=O.CCN(CC)CC NCGWKCHAJOUDHQ-UHFFFAOYSA-N 0.000 description 3
- 210000001672 ovary Anatomy 0.000 description 3
- TVIDEEHSOPHZBR-AWEZNQCLSA-N para-(benzoyl)-phenylalanine Chemical compound C1=CC(C[C@H](N)C(O)=O)=CC=C1C(=O)C1=CC=CC=C1 TVIDEEHSOPHZBR-AWEZNQCLSA-N 0.000 description 3
- 239000002245 particle Substances 0.000 description 3
- 229920000570 polyether Polymers 0.000 description 3
- 230000010076 replication Effects 0.000 description 3
- 108091008146 restriction endonucleases Proteins 0.000 description 3
- 210000003705 ribosome Anatomy 0.000 description 3
- 230000035945 sensitivity Effects 0.000 description 3
- 230000000392 somatic effect Effects 0.000 description 3
- 239000003053 toxin Substances 0.000 description 3
- 231100000765 toxin Toxicity 0.000 description 3
- 108700012359 toxins Proteins 0.000 description 3
- 230000001960 triggered effect Effects 0.000 description 3
- 239000012588 trypsin Substances 0.000 description 3
- 102000003298 tumor necrosis factor receptor Human genes 0.000 description 3
- 238000011179 visual inspection Methods 0.000 description 3
- XLYOFNOQVPJJNP-UHFFFAOYSA-N water Substances O XLYOFNOQVPJJNP-UHFFFAOYSA-N 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
- 108020005065 3' Flanking Region Proteins 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
- LDCYZAJDBXYCGN-VIFPVBQESA-N 5-hydroxy-L-tryptophan Chemical compound C1=C(O)C=C2C(C[C@H](N)C(O)=O)=CNC2=C1 LDCYZAJDBXYCGN-VIFPVBQESA-N 0.000 description 2
- 229940000681 5-hydroxytryptophan Drugs 0.000 description 2
- 229920000936 Agarose Polymers 0.000 description 2
- 102000007698 Alcohol dehydrogenase Human genes 0.000 description 2
- 108010021809 Alcohol dehydrogenase Proteins 0.000 description 2
- 241000205042 Archaeoglobus fulgidus 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
- 241000193830 Bacillus <bacterium> Species 0.000 description 2
- 241000283690 Bos taurus Species 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
- 108010029697 CD40 Ligand Proteins 0.000 description 2
- 102100032937 CD40 ligand Human genes 0.000 description 2
- 102000003952 Caspase 3 Human genes 0.000 description 2
- 108090000397 Caspase 3 Proteins 0.000 description 2
- 108010071942 Colony-Stimulating Factors Proteins 0.000 description 2
- 241000195493 Cryptophyta Species 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
- FDKWRPBBCBCIGA-UWTATZPHSA-N D-Selenocysteine Natural products [Se]C[C@@H](N)C(O)=O FDKWRPBBCBCIGA-UWTATZPHSA-N 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
- 241000283073 Equus caballus Species 0.000 description 2
- 241000186394 Eubacterium Species 0.000 description 2
- 102000002464 Galactosidases Human genes 0.000 description 2
- 108010093031 Galactosidases Proteins 0.000 description 2
- 108010015514 Glutamate-tRNA ligase Proteins 0.000 description 2
- 102000001888 Glutamate-tRNA ligase Human genes 0.000 description 2
- WHUUTDBJXJRKMK-UHFFFAOYSA-N Glutamic acid Natural products OC(=O)C(N)CCC(O)=O WHUUTDBJXJRKMK-UHFFFAOYSA-N 0.000 description 2
- DHMQDGOQFOQNFH-UHFFFAOYSA-N Glycine Chemical compound NCC(O)=O DHMQDGOQFOQNFH-UHFFFAOYSA-N 0.000 description 2
- 102000003886 Glycoproteins Human genes 0.000 description 2
- 108090000288 Glycoproteins Proteins 0.000 description 2
- 108090000100 Hepatocyte Growth Factor Proteins 0.000 description 2
- 102100021866 Hepatocyte growth factor Human genes 0.000 description 2
- 101001069921 Homo sapiens Growth-regulated alpha protein 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
- 108010002350 Interleukin-2 Proteins 0.000 description 2
- 108010063738 Interleukins Proteins 0.000 description 2
- 102000015696 Interleukins Human genes 0.000 description 2
- XUJNEKJLAYXESH-REOHCLBHSA-N L-Cysteine Chemical compound SC[C@H](N)C(O)=O XUJNEKJLAYXESH-REOHCLBHSA-N 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
- HNDVDQJCIGZPNO-YFKPBYRVSA-N L-histidine Chemical compound OC(=O)[C@@H](N)CC1=CN=CN1 HNDVDQJCIGZPNO-YFKPBYRVSA-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
- FFEARJCKVFRZRR-BYPYZUCNSA-N L-methionine Chemical compound CSCC[C@H](N)C(O)=O FFEARJCKVFRZRR-BYPYZUCNSA-N 0.000 description 2
- 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 2
- ZKZBPNGNEQAJSX-REOHCLBHSA-N L-selenocysteine Chemical compound [SeH]C[C@H](N)C(O)=O ZKZBPNGNEQAJSX-REOHCLBHSA-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
- 102000003820 Lipoxygenases Human genes 0.000 description 2
- 108090000128 Lipoxygenases Proteins 0.000 description 2
- KDXKERNSBIXSRK-UHFFFAOYSA-N Lysine Natural products NCCCCC(N)C(O)=O KDXKERNSBIXSRK-UHFFFAOYSA-N 0.000 description 2
- 239000004472 Lysine Substances 0.000 description 2
- 241001302042 Methanothermobacter thermautotrophicus Species 0.000 description 2
- 241000699660 Mus musculus Species 0.000 description 2
- 238000000636 Northern blotting Methods 0.000 description 2
- 108091005461 Nucleic proteins Proteins 0.000 description 2
- 108700020796 Oncogene Proteins 0.000 description 2
- 102000043276 Oncogene Human genes 0.000 description 2
- 241001502095 Pan troglodytes verus Species 0.000 description 2
- 102000035195 Peptidases Human genes 0.000 description 2
- 108091005804 Peptidases Proteins 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
- 241000700161 Rattus rattus Species 0.000 description 2
- 241000555745 Sciuridae Species 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
- 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
- 230000021736 acetylation Effects 0.000 description 2
- 238000006640 acetylation reaction Methods 0.000 description 2
- 239000002253 acid Substances 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
- 239000003242 anti bacterial agent Substances 0.000 description 2
- 235000009582 asparagine Nutrition 0.000 description 2
- 238000003149 assay kit Methods 0.000 description 2
- 239000012298 atmosphere Substances 0.000 description 2
- 230000008901 benefit Effects 0.000 description 2
- 229910052799 carbon Inorganic materials 0.000 description 2
- 125000003178 carboxy group Chemical group [H]OC(*)=O 0.000 description 2
- 239000006143 cell culture medium Substances 0.000 description 2
- 230000030833 cell death Effects 0.000 description 2
- 230000010261 cell growth Effects 0.000 description 2
- 210000002421 cell wall Anatomy 0.000 description 2
- 230000004700 cellular uptake Effects 0.000 description 2
- WHTVZRBIWZFKQO-UHFFFAOYSA-N chloroquine Chemical compound ClC1=CC=C2C(NC(C)CCCN(CC)CC)=CC=NC2=C1 WHTVZRBIWZFKQO-UHFFFAOYSA-N 0.000 description 2
- 210000000349 chromosome Anatomy 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
- 238000004132 cross linking Methods 0.000 description 2
- 239000013078 crystal Substances 0.000 description 2
- 125000000151 cysteine group Chemical group N[C@@H](CS)C(=O)* 0.000 description 2
- 230000002950 deficient Effects 0.000 description 2
- 238000013461 design Methods 0.000 description 2
- 238000001514 detection method Methods 0.000 description 2
- 108010048367 enhanced green fluorescent protein Proteins 0.000 description 2
- 239000003623 enhancer Substances 0.000 description 2
- 238000002073 fluorescence micrograph Methods 0.000 description 2
- 238000013467 fragmentation Methods 0.000 description 2
- 238000006062 fragmentation reaction Methods 0.000 description 2
- BTCSSZJGUNDROE-UHFFFAOYSA-N gamma-aminobutyric acid Chemical compound NCCCC(O)=O BTCSSZJGUNDROE-UHFFFAOYSA-N 0.000 description 2
- 108091008053 gene clusters Proteins 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
- 238000004128 high performance liquid chromatography Methods 0.000 description 2
- HNDVDQJCIGZPNO-UHFFFAOYSA-N histidine Natural products OC(=O)C(N)CC1=CN=CN1 HNDVDQJCIGZPNO-UHFFFAOYSA-N 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
- 230000006698 induction 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
- 230000010354 integration Effects 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
- 238000005040 ion trap Methods 0.000 description 2
- JEIPFZHSYJVQDO-UHFFFAOYSA-N iron(III) oxide Inorganic materials O=[Fe]O[Fe]=O JEIPFZHSYJVQDO-UHFFFAOYSA-N 0.000 description 2
- YOBAEOGBNPPUQV-UHFFFAOYSA-N iron;trihydrate Chemical compound O.O.O.[Fe].[Fe] YOBAEOGBNPPUQV-UHFFFAOYSA-N 0.000 description 2
- 229960000310 isoleucine Drugs 0.000 description 2
- AGPKZVBTJJNPAG-UHFFFAOYSA-N isoleucine Natural products CCC(C)C(N)C(O)=O AGPKZVBTJJNPAG-UHFFFAOYSA-N 0.000 description 2
- 125000000468 ketone group Chemical group 0.000 description 2
- 238000011005 laboratory method Methods 0.000 description 2
- 125000001909 leucine group Chemical group [H]N(*)C(C(*)=O)C([H])([H])C(C([H])([H])[H])C([H])([H])[H] 0.000 description 2
- 239000003446 ligand Substances 0.000 description 2
- 230000000670 limiting effect Effects 0.000 description 2
- 150000002632 lipids Chemical class 0.000 description 2
- 238000005259 measurement Methods 0.000 description 2
- 230000007246 mechanism Effects 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
- 239000002184 metal Substances 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
- LDCYZAJDBXYCGN-UHFFFAOYSA-N oxitriptan Natural products C1=C(O)C=C2C(CC(N)C(O)=O)=CNC2=C1 LDCYZAJDBXYCGN-UHFFFAOYSA-N 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
- 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
- 150000003148 prolines Chemical class 0.000 description 2
- 238000001243 protein synthesis Methods 0.000 description 2
- 230000017854 proteolysis Effects 0.000 description 2
- 108091007054 readthrough proteins Proteins 0.000 description 2
- 229940055619 selenocysteine Drugs 0.000 description 2
- 235000016491 selenocysteine Nutrition 0.000 description 2
- ZKZBPNGNEQAJSX-UHFFFAOYSA-N selenocysteine Natural products [SeH]CC(N)C(O)=O ZKZBPNGNEQAJSX-UHFFFAOYSA-N 0.000 description 2
- 238000012163 sequencing technique Methods 0.000 description 2
- 210000002966 serum Anatomy 0.000 description 2
- 230000019491 signal transduction Effects 0.000 description 2
- 239000000243 solution Substances 0.000 description 2
- 238000010561 standard procedure Methods 0.000 description 2
- 239000006228 supernatant Substances 0.000 description 2
- 125000003396 thiol group Chemical group [H]S* 0.000 description 2
- RWQNBRDOKXIBIV-UHFFFAOYSA-N thymine Chemical compound CC1=CNC(=O)NC1=O RWQNBRDOKXIBIV-UHFFFAOYSA-N 0.000 description 2
- 108091006106 transcriptional activators Proteins 0.000 description 2
- 238000012546 transfer Methods 0.000 description 2
- 238000003146 transient transfection Methods 0.000 description 2
- 230000012863 translational readthrough Effects 0.000 description 2
- 241001515965 unidentified phage Species 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
- 239000003643 water by type 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
- 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
- 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
- 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
- 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
- 101000997963 Aequorea victoria Green fluorescent protein Proteins 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
- 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
- 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
- VHUUQVKOLVNVRT-UHFFFAOYSA-N Ammonium hydroxide Chemical compound [NH4+].[OH-] VHUUQVKOLVNVRT-UHFFFAOYSA-N 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
- 101000640990 Arabidopsis thaliana Tryptophan-tRNA ligase, chloroplastic/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
- BTBUEUYNUDRHOZ-UHFFFAOYSA-N Borate Chemical compound [O-]B([O-])[O-] BTBUEUYNUDRHOZ-UHFFFAOYSA-N 0.000 description 1
- 101000583086 Bunodosoma granuliferum Delta-actitoxin-Bgr2b Proteins 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
- 102000001902 CC Chemokines Human genes 0.000 description 1
- 108010040471 CC Chemokines Proteins 0.000 description 1
- 101150013553 CD40 gene Proteins 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
- 241000288950 Callithrix jacchus Species 0.000 description 1
- 241000222120 Candida <Saccharomycetales> Species 0.000 description 1
- 241000282465 Canis Species 0.000 description 1
- 241000283707 Capra 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
- 241000282552 Chlorocebus aethiops Species 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
- 101100007328 Cocos nucifera COS-1 gene Proteins 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
- 241000699800 Cricetinae 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
- 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
- 108010017826 DNA Polymerase I Proteins 0.000 description 1
- 102000004594 DNA Polymerase I Human genes 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
- 239000006144 Dulbecco’s modified Eagle's medium Substances 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
- 101150066002 GFP gene 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
- 241000224466 Giardia Species 0.000 description 1
- 102000004547 Glucosylceramidase Human genes 0.000 description 1
- 108010017544 Glucosylceramidase Proteins 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
- 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
- 241000282578 Gorilla gorilla gorilla Species 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
- 108050002220 Green fluorescent protein, GFP Proteins 0.000 description 1
- 108010051696 Growth Hormone Proteins 0.000 description 1
- 101150009006 HIS3 gene Proteins 0.000 description 1
- 101710088172 HTH-type transcriptional regulator RipA 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
- 102000006947 Histones Human genes 0.000 description 1
- 108010033040 Histones Proteins 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
- 101000871017 Homo sapiens Growth factor receptor-bound protein 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
- 102000002265 Human Growth Hormone Human genes 0.000 description 1
- 108010000521 Human Growth Hormone Proteins 0.000 description 1
- 239000000854 Human Growth Hormone Substances 0.000 description 1
- 102000008100 Human Serum Albumin Human genes 0.000 description 1
- 108091006905 Human Serum Albumin 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
- 108010002386 Interleukin-3 Proteins 0.000 description 1
- 108090000978 Interleukin-4 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
- 108090001007 Interleukin-8 Proteins 0.000 description 1
- 108010002335 Interleukin-9 Proteins 0.000 description 1
- 102000004310 Ion Channels Human genes 0.000 description 1
- 108090000862 Ion Channels 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
- KDXKERNSBIXSRK-YFKPBYRVSA-N L-lysine Chemical compound NCCCC[C@H](N)C(O)=O KDXKERNSBIXSRK-YFKPBYRVSA-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
- 239000006142 Luria-Bertani Agar 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
- 102000017737 Lysine-tRNA Ligase Human genes 0.000 description 1
- 108010092041 Lysine-tRNA Ligase Proteins 0.000 description 1
- 241000282566 Macaca arctoides Species 0.000 description 1
- 241000282567 Macaca fascicularis Species 0.000 description 1
- 241000282560 Macaca mulatta Species 0.000 description 1
- 241000282559 Macaca sylvanus Species 0.000 description 1
- 102100027754 Mast/stem cell growth factor receptor Kit Human genes 0.000 description 1
- 240000008821 Menyanthes trifoliata Species 0.000 description 1
- 235000011779 Menyanthes trifoliata Nutrition 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
- 101710135898 Myc proto-oncogene protein Proteins 0.000 description 1
- 102100038895 Myc proto-oncogene protein Human genes 0.000 description 1
- 241000204031 Mycoplasma Species 0.000 description 1
- 231100000678 Mycotoxin Toxicity 0.000 description 1
- 102100030856 Myoglobin Human genes 0.000 description 1
- 108010062374 Myoglobin Proteins 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
- 239000000020 Nitrocellulose Substances 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
- 102000004140 Oncostatin M Human genes 0.000 description 1
- 108090000630 Oncostatin M 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
- 241000282579 Pan Species 0.000 description 1
- 241001502102 Pan troglodytes schweinfurthii Species 0.000 description 1
- 241000282520 Papio Species 0.000 description 1
- 241000282516 Papio anubis Species 0.000 description 1
- 241000862462 Papio sp. Species 0.000 description 1
- 241001504519 Papio ursinus Species 0.000 description 1
- 108090000445 Parathyroid hormone Proteins 0.000 description 1
- 102000003982 Parathyroid hormone Human genes 0.000 description 1
- 241001494479 Pecora Species 0.000 description 1
- 108700019535 Phosphoprotein Phosphatases Proteins 0.000 description 1
- 102000045595 Phosphoprotein Phosphatases Human genes 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
- 239000002202 Polyethylene glycol Substances 0.000 description 1
- 241000282407 Pongo pygmaeus pygmaeus Species 0.000 description 1
- ONIBWKKTOPOVIA-UHFFFAOYSA-N Proline Natural products OC(=O)C1CCCN1 ONIBWKKTOPOVIA-UHFFFAOYSA-N 0.000 description 1
- 229940124158 Protease/peptidase inhibitor Drugs 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
- 239000012083 RIPA buffer Substances 0.000 description 1
- 102000014450 RNA Polymerase III Human genes 0.000 description 1
- 108010078067 RNA Polymerase III 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
- 241000700157 Rattus norvegicus Species 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
- 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
- 241000288960 Saguinus oedipus Species 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
- 102000012479 Serine Proteases Human genes 0.000 description 1
- 108010022999 Serine Proteases Proteins 0.000 description 1
- 108010056088 Somatostatin Proteins 0.000 description 1
- 102000005157 Somatostatin Human genes 0.000 description 1
- 102100038803 Somatotropin 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
- 241000282898 Sus scrofa Species 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
- 101710150448 Transcriptional regulator Myc Proteins 0.000 description 1
- 102220602924 Transmembrane protein 184A_Y37V_mutation Human genes 0.000 description 1
- 241000224526 Trichomonas Species 0.000 description 1
- 241000209140 Triticum Species 0.000 description 1
- 235000021307 Triticum Nutrition 0.000 description 1
- 241000223104 Trypanosoma Species 0.000 description 1
- 102000002501 Tryptophan-tRNA Ligase Human genes 0.000 description 1
- 108060008682 Tumor Necrosis Factor Proteins 0.000 description 1
- 102000000852 Tumor Necrosis Factor-alpha Human genes 0.000 description 1
- 102100040245 Tumor necrosis factor receptor superfamily member 5 Human genes 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
- 125000002252 acyl group Chemical group 0.000 description 1
- 230000006978 adaptation Effects 0.000 description 1
- 239000000853 adhesive Substances 0.000 description 1
- 230000001070 adhesive effect Effects 0.000 description 1
- 238000001261 affinity purification Methods 0.000 description 1
- 238000000246 agarose gel electrophoresis Methods 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
- 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
- 150000001370 alpha-amino acid derivatives Chemical class 0.000 description 1
- 102000005922 amidase Human genes 0.000 description 1
- 150000001408 amides Chemical group 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
- 239000000908 ammonium hydroxide Substances 0.000 description 1
- 239000012491 analyte Substances 0.000 description 1
- 238000000137 annealing Methods 0.000 description 1
- 230000002587 anti-hemolytic effect Effects 0.000 description 1
- 108010082685 antiarrhythmic peptide Proteins 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
- 230000006907 apoptotic process Effects 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
- 125000000852 azido group Chemical group *N=[N+]=[N-] 0.000 description 1
- 210000003719 b-lymphocyte Anatomy 0.000 description 1
- 244000052616 bacterial pathogen Species 0.000 description 1
- 238000007630 basic procedure Methods 0.000 description 1
- 239000011324 bead Substances 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
- 230000031018 biological processes and functions Effects 0.000 description 1
- 230000033228 biological regulation 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
- 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
- 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
- 150000001720 carbohydrates Chemical group 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
- 230000034303 cell budding Effects 0.000 description 1
- 238000004113 cell culture Methods 0.000 description 1
- 230000024245 cell differentiation Effects 0.000 description 1
- 230000009134 cell regulation Effects 0.000 description 1
- 238000012512 characterization method Methods 0.000 description 1
- 239000003638 chemical reducing agent Substances 0.000 description 1
- 229960003677 chloroquine Drugs 0.000 description 1
- 238000003776 cleavage reaction Methods 0.000 description 1
- 239000013599 cloning vector Substances 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
- 125000004122 cyclic group Chemical group 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
- 238000009795 derivation Methods 0.000 description 1
- 238000011033 desalting Methods 0.000 description 1
- 239000003599 detergent Substances 0.000 description 1
- 238000001784 detoxification Methods 0.000 description 1
- 238000011161 development Methods 0.000 description 1
- 230000018109 developmental process Effects 0.000 description 1
- 229950006137 dexfosfoserine Drugs 0.000 description 1
- 230000029087 digestion Effects 0.000 description 1
- 239000002934 diuretic Substances 0.000 description 1
- 230000012361 double-strand break repair Effects 0.000 description 1
- 239000003814 drug Substances 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
- 239000000975 dye Substances 0.000 description 1
- 238000004520 electroporation Methods 0.000 description 1
- 238000010828 elution Methods 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
- 230000007717 exclusion Effects 0.000 description 1
- 239000002095 exotoxin Substances 0.000 description 1
- 231100000776 exotoxin Toxicity 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
- 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
- 231100000221 frame shift mutation induction Toxicity 0.000 description 1
- 238000002546 full scan Methods 0.000 description 1
- 125000000524 functional group Chemical group 0.000 description 1
- 230000002496 gastric effect Effects 0.000 description 1
- 238000007429 general method Methods 0.000 description 1
- 229930195712 glutamate Natural products 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
- 238000009499 grossing Methods 0.000 description 1
- 230000012010 growth Effects 0.000 description 1
- 125000001475 halogen functional group Chemical group 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
- 102000054653 human GRB2 Human genes 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
- 230000002458 infectious effect Effects 0.000 description 1
- 206010022000 influenza Diseases 0.000 description 1
- 230000002401 inhibitory effect Effects 0.000 description 1
- 239000003999 initiator Substances 0.000 description 1
- 230000000977 initiatory effect Effects 0.000 description 1
- 229940125396 insulin Drugs 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
- 125000001449 isopropyl group Chemical group [H]C([H])([H])C([H])(*)C([H])([H])[H] 0.000 description 1
- 210000003292 kidney cell Anatomy 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
- 235000019421 lipase Nutrition 0.000 description 1
- 239000007788 liquid Substances 0.000 description 1
- 238000004895 liquid chromatography mass spectrometry Methods 0.000 description 1
- 239000006194 liquid suspension Substances 0.000 description 1
- 238000011068 loading method Methods 0.000 description 1
- 238000004020 luminiscence type Methods 0.000 description 1
- 101150109301 lys2 gene Proteins 0.000 description 1
- 239000012139 lysis buffer Substances 0.000 description 1
- 229920002521 macromolecule Polymers 0.000 description 1
- 238000002844 melting Methods 0.000 description 1
- 230000008018 melting Effects 0.000 description 1
- 229910021645 metal ion Inorganic materials 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
- 108091005601 modified peptides Proteins 0.000 description 1
- 102000035118 modified proteins Human genes 0.000 description 1
- 108091005573 modified proteins Proteins 0.000 description 1
- 238000012544 monitoring process Methods 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
- 230000001452 natriuretic effect Effects 0.000 description 1
- 239000013642 negative control Substances 0.000 description 1
- 210000002569 neuron Anatomy 0.000 description 1
- 125000006502 nitrobenzyl group Chemical group 0.000 description 1
- 229920001220 nitrocellulos Polymers 0.000 description 1
- 239000002777 nucleoside Substances 0.000 description 1
- 150000003833 nucleoside derivatives Chemical class 0.000 description 1
- 229940046166 oligodeoxynucleotide Drugs 0.000 description 1
- 239000011022 opal Substances 0.000 description 1
- 210000000056 organ Anatomy 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
- 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
- 239000000137 peptide hydrolase inhibitor 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
- 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
- 230000008635 plant growth Effects 0.000 description 1
- 102000005162 pleiotrophin Human genes 0.000 description 1
- 230000001402 polyadenylating effect Effects 0.000 description 1
- 229920001223 polyethylene glycol Polymers 0.000 description 1
- 229920000166 polytrimethylene carbonate Polymers 0.000 description 1
- 231100000683 possible toxicity Toxicity 0.000 description 1
- 229960003387 progesterone Drugs 0.000 description 1
- 239000000186 progesterone Substances 0.000 description 1
- 235000013930 proline Nutrition 0.000 description 1
- 238000003498 protein array Methods 0.000 description 1
- 108060006633 protein kinase Proteins 0.000 description 1
- 230000001698 pyrogenic effect Effects 0.000 description 1
- 238000012205 qualitative assay Methods 0.000 description 1
- 238000011002 quantification Methods 0.000 description 1
- 150000003254 radicals Chemical class 0.000 description 1
- 230000002285 radioactive effect Effects 0.000 description 1
- 238000010814 radioimmunoprecipitation assay Methods 0.000 description 1
- 239000000376 reactant Substances 0.000 description 1
- 238000003259 recombinant expression Methods 0.000 description 1
- 108010054624 red fluorescent protein Proteins 0.000 description 1
- 230000009467 reduction Effects 0.000 description 1
- 230000022532 regulation of transcription, DNA-dependent 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
- 230000032537 response to toxin Effects 0.000 description 1
- 238000004366 reverse phase liquid chromatography Methods 0.000 description 1
- 238000010839 reverse transcription Methods 0.000 description 1
- 238000012552 review Methods 0.000 description 1
- 108020004418 ribosomal RNA Proteins 0.000 description 1
- 238000007363 ring formation reaction Methods 0.000 description 1
- 102200006540 rs121913530 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
- 230000007017 scission Effects 0.000 description 1
- 239000013605 shuttle vector Substances 0.000 description 1
- 230000011664 signaling Effects 0.000 description 1
- 150000003384 small molecules Chemical class 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
- 108010068698 spleen exonuclease Proteins 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
- 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
- 108091005994 sulfated proteins Proteins 0.000 description 1
- 231100000617 superantigen Toxicity 0.000 description 1
- 229960003604 testosterone 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
- 238000006257 total synthesis reaction Methods 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
- 239000012096 transfection reagent Substances 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
- 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
- 239000013603 viral vector Substances 0.000 description 1
- 235000019154 vitamin C Nutrition 0.000 description 1
- 239000011718 vitamin C Substances 0.000 description 1
- 238000005406 washing Methods 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
- C12N15/11—DNA or RNA fragments; Modified forms thereof; Non-coding nucleic acids having a biological activity
- C12N15/52—Genes encoding for enzymes or proenzymes
-
- 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
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K14/00—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof
-
- 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
- C12N5/00—Undifferentiated human, animal or plant cells, e.g. cell lines; Tissues; Cultivation or maintenance thereof; Culture media therefor
- C12N5/10—Cells modified by introduction of foreign genetic material
-
- 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
Landscapes
- Life Sciences & Earth Sciences (AREA)
- Health & Medical Sciences (AREA)
- Chemical & Material Sciences (AREA)
- Organic Chemistry (AREA)
- Engineering & Computer Science (AREA)
- Genetics & Genomics (AREA)
- Wood Science & Technology (AREA)
- Zoology (AREA)
- Bioinformatics & Cheminformatics (AREA)
- Biotechnology (AREA)
- General Health & Medical Sciences (AREA)
- General Engineering & Computer Science (AREA)
- Biochemistry (AREA)
- Molecular Biology (AREA)
- Microbiology (AREA)
- Biomedical Technology (AREA)
- Proteomics, Peptides & Aminoacids (AREA)
- Medicinal Chemistry (AREA)
- Chemical Kinetics & Catalysis (AREA)
- General Chemical & Material Sciences (AREA)
- Biophysics (AREA)
- Plant Pathology (AREA)
- Physics & Mathematics (AREA)
- Gastroenterology & Hepatology (AREA)
- Cell Biology (AREA)
- Micro-Organisms Or Cultivation Processes Thereof (AREA)
- Preparation Of Compounds By Using Micro-Organisms (AREA)
Applications Claiming Priority (5)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| US85300806P | 2006-10-18 | 2006-10-18 | |
| US60/853,008 | 2006-10-18 | ||
| US92345807P | 2007-04-12 | 2007-04-12 | |
| US60/923,458 | 2007-04-12 | ||
| PCT/US2007/022232 WO2008073184A2 (en) | 2006-10-18 | 2007-10-17 | Genetic incorporation of unnatural amino acids into proteins in mammalian cells |
Publications (1)
| Publication Number | Publication Date |
|---|---|
| CA2665678A1 true CA2665678A1 (en) | 2008-06-19 |
Family
ID=39512252
Family Applications (1)
| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| CA002665678A Abandoned CA2665678A1 (en) | 2006-10-18 | 2007-10-17 | Genetic incorporation of unnatural amino acids into proteins in mammalian cells |
Country Status (12)
| Country | Link |
|---|---|
| US (2) | US20080166766A1 (https=) |
| EP (1) | EP2069481A4 (https=) |
| JP (1) | JP2010506591A (https=) |
| KR (1) | KR20090094812A (https=) |
| CN (1) | CN101535338A (https=) |
| AU (1) | AU2007333010A1 (https=) |
| BR (1) | BRPI0718389A2 (https=) |
| CA (1) | CA2665678A1 (https=) |
| IL (1) | IL197917A0 (https=) |
| MX (1) | MX2009004043A (https=) |
| RU (1) | RU2009112104A (https=) |
| WO (1) | WO2008073184A2 (https=) |
Cited By (1)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| CN114134141A (zh) * | 2021-11-03 | 2022-03-04 | 浙江大学 | 一种引入非天然氨基酸的嵌合体苯丙氨酸翻译系统及其构建方法 |
Families Citing this family (24)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| US7083970B2 (en) * | 2001-04-19 | 2006-08-01 | The Scripps Research Institute | Methods and compositions for the production of orthogonal tRNA-aminoacyl tRNA synthetase pairs |
| MXPA05003978A (es) * | 2002-10-16 | 2005-06-22 | Scripps Research Inst | Sintesis de glicoproteinas. |
| WO2004094593A2 (en) | 2003-04-17 | 2004-11-04 | The Scripps Research Institute | Expanding the eukaryotic genetic code |
| WO2005019415A2 (en) | 2003-07-07 | 2005-03-03 | The Scripps Research Institute | Compositions of orthogonal lysyl-trna and aminoacyl-trna synthetase pairs and uses thereof |
| WO2010114615A2 (en) * | 2009-04-03 | 2010-10-07 | The Scripps Research Institute | A facile system for encoding unnatural amino acids in mammalian cells |
| CN103328648B (zh) * | 2010-12-03 | 2015-11-25 | 国立大学法人东京大学 | 具有稳定的二级结构的肽和肽库以及它们的制造方法 |
| DE102010056289A1 (de) | 2010-12-24 | 2012-06-28 | Geneart Ag | Verfahren zur Herstellung von Leseraster-korrekten Fragment-Bibliotheken |
| SG10201702387YA (en) * | 2012-09-24 | 2017-04-27 | Medimmune Ltd | Cell lines |
| BR112015022641B1 (pt) * | 2013-03-15 | 2023-02-28 | Medimmune Limited | Construção de dna e processo de preparação de uma proteína-alvo |
| CN109295025B (zh) * | 2014-09-03 | 2021-04-02 | 中国科学院生物物理研究所 | 酪氨酸类似物翻译系统和基因编码的蛋白质光致电子转移荧光传感器蛋白家族 |
| CN105400816A (zh) * | 2015-11-24 | 2016-03-16 | 深圳市第二人民医院 | 用于膀胱癌检测的逻辑与门基因线路的构建方法 |
| GB201600512D0 (en) | 2016-01-12 | 2016-02-24 | Univ York | Recombinant protein production |
| CN112725282A (zh) * | 2016-01-27 | 2021-04-30 | 北京大学 | 携带正交tRNA/氨酰tRNA合成酶的稳定细胞系的构建 |
| CN110520522A (zh) | 2017-02-17 | 2019-11-29 | 鲁比厄斯治疗法股份有限公司 | 功能化红系细胞 |
| EP3630977B1 (en) * | 2017-06-02 | 2024-02-21 | Ambrx, Inc. | Methods and compositions for promoting non-natural amino acid-containing protein production |
| JP2020522263A (ja) | 2017-06-06 | 2020-07-30 | キンドレッド バイオサイエンシズ インコーポレイテッド | 獣医学的使用のためのエリスロポエチンおよびアナログ |
| JP2021520828A (ja) | 2018-04-19 | 2021-08-26 | キンドレッド バイオサイエンシズ インコーポレイテッド | 医療用の変異体アスパラギナーゼポリペプチド |
| CN112673109A (zh) * | 2018-09-07 | 2021-04-16 | 免疫医疗有限责任公司 | 细胞选择方法 |
| US12565646B2 (en) | 2019-06-21 | 2026-03-03 | Trustees Of Boston College | Enhanced platforms for unnatural amino acid incorporation in mammalian cells |
| CN114729334A (zh) * | 2019-08-08 | 2022-07-08 | 布里克生物公司 | 用于非天然氨基酸的位点特异性掺入的氨酰tRNA合成酶和细胞系 |
| KR20220080101A (ko) * | 2019-10-15 | 2022-06-14 | 트러스티스 오브 보스톤 칼리지 | 향상된 비천연 아미노산 혼입을 위한 키메라 열안정성 아미노아실-tRNA 합성효소 |
| US20230069218A1 (en) * | 2019-12-12 | 2023-03-02 | Chugai Seiyaku Kabushiki Kaisha | Method for producing peptide containing non-natural amino acid |
| CN113388654A (zh) * | 2021-06-04 | 2021-09-14 | 清华大学 | 一种基于线形模板无细胞体系非天然氨基酸嵌入方法 |
| CN119662697B (zh) * | 2024-12-20 | 2026-03-27 | 天津大学 | 缺失基因的酿酒酵母及在利用非天然氨基酸修饰蛋白质中的应用 |
Family Cites Families (23)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| US7083970B2 (en) | 2001-04-19 | 2006-08-01 | The Scripps Research Institute | Methods and compositions for the production of orthogonal tRNA-aminoacyl tRNA synthetase pairs |
| MXPA05003978A (es) | 2002-10-16 | 2005-06-22 | Scripps Research Inst | Sintesis de glicoproteinas. |
| ES2324608T3 (es) | 2002-10-16 | 2009-08-11 | The Scripps Research Institute | Incorporacion especifica de sitio de cetoaminoacidos en proteinas. |
| WO2004039989A1 (ja) * | 2002-10-31 | 2004-05-13 | Riken | 非天然型アミノ酸組み込みタンパク質の発現方法 |
| WO2004058946A2 (en) | 2002-12-22 | 2004-07-15 | The Scripps Research Institute | Protein arrays |
| JP2006517802A (ja) * | 2003-02-14 | 2006-08-03 | バイオジェン・アイデック・エムエイ・インコーポレイテッド | 外来性分子の一過性の発現もしくは安定な発現のための発現カセットおよび発現ベクター |
| WO2004094593A2 (en) | 2003-04-17 | 2004-11-04 | The Scripps Research Institute | Expanding the eukaryotic genetic code |
| 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 |
| WO2005019415A2 (en) | 2003-07-07 | 2005-03-03 | The Scripps Research Institute | Compositions of orthogonal lysyl-trna and aminoacyl-trna synthetase pairs and uses thereof |
| US20060160175A1 (en) | 2003-07-07 | 2006-07-20 | The Scripps Research Institute | Compositions of orthogonal leucyl-trna and aminoacyl-trna synthetase pairs and uses thereof |
| WO2005007624A2 (en) | 2003-07-07 | 2005-01-27 | The Scripps Research Institute | Compositions of orthogonal glutamyl-trna and aminoacyl trna synthetase pairs and uses thereof |
| JP5657850B2 (ja) | 2003-10-14 | 2015-01-21 | ザ スクリプス リサーチ インスティテュート | 酸化還元機能性アミノ酸のタンパク質への部位特異的組み入れ |
| AU2004321117B2 (en) | 2003-12-18 | 2010-09-02 | The Scripps Research Institute | Selective incorporation of 5-hydroxytryptophan into proteins in mammalian cells |
| EP2327724A3 (en) * | 2004-02-02 | 2011-07-27 | Ambrx, Inc. | Modified human growth hormone polypeptides and their uses |
| AU2005248392A1 (en) | 2004-05-25 | 2005-12-08 | Irm, Llc | Site specific incorporation of heavy atom-containing unnatural amino acids into proteins for crystal structure determination |
| CA2580840A1 (en) | 2004-09-21 | 2006-03-30 | The Scripps Research Institute | In vivo incorporation of alkynyl amino acids into proteins in eubacteria |
| US20090181858A1 (en) * | 2004-09-21 | 2009-07-16 | The Scripps Research Institute | Adding photoregulated amino acids to the genetic code |
| US20080171317A1 (en) | 2004-09-22 | 2008-07-17 | The Scripps Research Institute | Site-Specific Labeling of Proteins for Nmr Studies |
| JP2008516637A (ja) | 2004-10-20 | 2008-05-22 | ザ スクリップス リサーチ インスティテュート | 真正細菌へのｎ−アセチルガラクトサミンアミノ酸のインビボ部位特異的組込み |
| EP1807515A4 (en) | 2004-10-27 | 2008-06-18 | Scripps Research Inst | Orthogonal translation components for the in vivo incorporation of unnatural amino acids |
| US8367588B2 (en) | 2005-10-12 | 2013-02-05 | The Scripps Research Institute | Selective posttranslational modification of phage-displayed polypeptides |
| US7960141B2 (en) | 2006-03-09 | 2011-06-14 | The Scripps Research Institute | Systems for the expression of orthogonal translation components in eubacterial host cells |
| KR20080113226A (ko) | 2006-03-16 | 2008-12-29 | 더 스크립스 리서치 인스티튜트 | 비천연 아미노산 페닐셀레노시스테인을 함유하는 단백질의 유전자적으로 프로그램된 발현 |
-
2007
- 2007-10-17 JP JP2009533372A patent/JP2010506591A/ja active Pending
- 2007-10-17 WO PCT/US2007/022232 patent/WO2008073184A2/en not_active Ceased
- 2007-10-17 EP EP07870795A patent/EP2069481A4/en not_active Withdrawn
- 2007-10-17 CA CA002665678A patent/CA2665678A1/en not_active Abandoned
- 2007-10-17 CN CNA2007800390157A patent/CN101535338A/zh active Pending
- 2007-10-17 US US11/975,351 patent/US20080166766A1/en not_active Abandoned
- 2007-10-17 AU AU2007333010A patent/AU2007333010A1/en not_active Abandoned
- 2007-10-17 KR KR1020097009346A patent/KR20090094812A/ko not_active Ceased
- 2007-10-17 MX MX2009004043A patent/MX2009004043A/es not_active Application Discontinuation
- 2007-10-17 US US12/311,545 patent/US9624485B2/en not_active Expired - Fee Related
- 2007-10-17 BR BRPI0718389-5A patent/BRPI0718389A2/pt not_active IP Right Cessation
- 2007-10-17 RU RU2009112104/10A patent/RU2009112104A/ru not_active Application Discontinuation
-
2009
- 2009-04-05 IL IL197917A patent/IL197917A0/en unknown
Cited By (2)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| CN114134141A (zh) * | 2021-11-03 | 2022-03-04 | 浙江大学 | 一种引入非天然氨基酸的嵌合体苯丙氨酸翻译系统及其构建方法 |
| CN114134141B (zh) * | 2021-11-03 | 2024-01-30 | 杭州嵌化合生医药科技有限公司 | 一种引入非天然氨基酸的嵌合体苯丙氨酸翻译系统及其构建方法 |
Also Published As
| Publication number | Publication date |
|---|---|
| EP2069481A4 (en) | 2010-01-06 |
| KR20090094812A (ko) | 2009-09-08 |
| IL197917A0 (en) | 2011-08-01 |
| WO2008073184A2 (en) | 2008-06-19 |
| EP2069481A2 (en) | 2009-06-17 |
| RU2009112104A (ru) | 2010-11-27 |
| US20100021963A1 (en) | 2010-01-28 |
| BRPI0718389A2 (pt) | 2012-04-10 |
| AU2007333010A1 (en) | 2008-06-19 |
| MX2009004043A (es) | 2009-04-27 |
| JP2010506591A (ja) | 2010-03-04 |
| US20080166766A1 (en) | 2008-07-10 |
| US9624485B2 (en) | 2017-04-18 |
| CN101535338A (zh) | 2009-09-16 |
| WO2008073184A3 (en) | 2008-11-27 |
Similar Documents
| Publication | Publication Date | Title |
|---|---|---|
| US9624485B2 (en) | Genetic incorporation of unnatural amino acids into proteins in mammalian cells | |
| US8394605B2 (en) | Genetically programmed expression of proteins containing the unnatural amino acid phenylselenocysteine | |
| US7960141B2 (en) | Systems for the expression of orthogonal translation components in eubacterial host cells | |
| US7811801B2 (en) | Site-specific incorporation of redox active amino acids into proteins | |
| US7824893B2 (en) | In vivo incorporation of alkynyl amino acids into proteins in eubacteria | |
| US7807411B2 (en) | Genetically encoded fluorescent coumarin amino acids |
Legal Events
| Date | Code | Title | Description |
|---|---|---|---|
| EEER | Examination request | ||
| FZDE | Discontinued |
Effective date: 20141017 |