ES2464532T3 - Métodos y composiciones para la producción de pares ortogonales de ARNt-aminoacil-ARNt sintetasa - Google Patents
Métodos y composiciones para la producción de pares ortogonales de ARNt-aminoacil-ARNt sintetasa Download PDFInfo
- Publication number
- ES2464532T3 ES2464532T3 ES09006800.8T ES09006800T ES2464532T3 ES 2464532 T3 ES2464532 T3 ES 2464532T3 ES 09006800 T ES09006800 T ES 09006800T ES 2464532 T3 ES2464532 T3 ES 2464532T3
- Authority
- ES
- Spain
- Prior art keywords
- trna
- amino acid
- synthetase
- unnatural amino
- amino acids
- 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.)
- Expired - Lifetime
Links
- 238000000034 method Methods 0.000 title claims abstract description 125
- 108090000364 Ligases Proteins 0.000 title claims description 279
- 102000003960 Ligases Human genes 0.000 title claims description 276
- 239000000203 mixture Substances 0.000 title description 23
- 238000004519 manufacturing process Methods 0.000 title description 12
- 150000001413 amino acids Chemical class 0.000 claims abstract description 432
- 241000203407 Methanocaldococcus jannaschii Species 0.000 claims abstract description 197
- 108090000765 processed proteins & peptides Proteins 0.000 claims abstract description 110
- 102000004196 processed proteins & peptides Human genes 0.000 claims abstract description 104
- 229920001184 polypeptide Polymers 0.000 claims abstract description 99
- 102000052866 Amino Acyl-tRNA Synthetases Human genes 0.000 claims abstract description 93
- 108700028939 Amino Acyl-tRNA Synthetases Proteins 0.000 claims abstract description 93
- 108020005038 Terminator Codon Proteins 0.000 claims abstract description 74
- 238000010348 incorporation Methods 0.000 claims abstract description 60
- 125000000266 alpha-aminoacyl group Chemical group 0.000 claims abstract description 24
- 108020004999 messenger RNA Proteins 0.000 claims abstract description 13
- 238000003786 synthesis reaction Methods 0.000 claims abstract description 12
- 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 claims abstract description 6
- OPOTYPXOKUZEKY-QMMMGPOBSA-N (2s)-2-nitramido-3-phenylpropanoic acid Chemical compound [O-][N+](=O)N[C@H](C(=O)O)CC1=CC=CC=C1 OPOTYPXOKUZEKY-QMMMGPOBSA-N 0.000 claims abstract description 3
- CBQJSKKFNMDLON-JTQLQIEISA-N N-acetyl-L-phenylalanine Chemical compound CC(=O)N[C@H](C(O)=O)CC1=CC=CC=C1 CBQJSKKFNMDLON-JTQLQIEISA-N 0.000 claims abstract description 3
- 239000000758 substrate Substances 0.000 claims description 37
- 238000012216 screening Methods 0.000 claims description 25
- 229940024606 amino acid Drugs 0.000 description 414
- 235000001014 amino acid Nutrition 0.000 description 414
- 108020004566 Transfer RNA Proteins 0.000 description 372
- 108090000623 proteins and genes Proteins 0.000 description 270
- 210000004027 cell Anatomy 0.000 description 231
- 102000004169 proteins and genes Human genes 0.000 description 164
- 108020004705 Codon Proteins 0.000 description 158
- 235000018102 proteins Nutrition 0.000 description 158
- 241000588724 Escherichia coli Species 0.000 description 146
- 101710146427 Probable tyrosine-tRNA ligase, cytoplasmic Proteins 0.000 description 141
- 101710107268 Tyrosine-tRNA ligase, mitochondrial Proteins 0.000 description 141
- 102000018378 Tyrosine-tRNA ligase Human genes 0.000 description 133
- 239000013612 plasmid Substances 0.000 description 110
- 108020004414 DNA Proteins 0.000 description 99
- 108091060545 Nonsense suppressor Proteins 0.000 description 96
- 150000007523 nucleic acids Chemical class 0.000 description 73
- 230000035772 mutation Effects 0.000 description 68
- 102000039446 nucleic acids Human genes 0.000 description 66
- 108020004707 nucleic acids Proteins 0.000 description 66
- 238000001727 in vivo Methods 0.000 description 60
- 230000014616 translation Effects 0.000 description 58
- 239000003550 marker Substances 0.000 description 54
- 238000013519 translation Methods 0.000 description 50
- 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 46
- 229960000723 ampicillin Drugs 0.000 description 46
- 238000009739 binding Methods 0.000 description 41
- 238000000338 in vitro Methods 0.000 description 41
- 230000027455 binding Effects 0.000 description 40
- 108020005098 Anticodon Proteins 0.000 description 39
- 230000001629 suppression Effects 0.000 description 39
- 230000000694 effects Effects 0.000 description 36
- 108010016529 Bacillus amyloliquefaciens ribonuclease Proteins 0.000 description 33
- 239000002609 medium Substances 0.000 description 33
- 238000012360 testing method Methods 0.000 description 32
- 229960004441 tyrosine Drugs 0.000 description 31
- 108010035563 Chloramphenicol O-acetyltransferase Proteins 0.000 description 29
- 229960005190 phenylalanine Drugs 0.000 description 29
- 235000002374 tyrosine Nutrition 0.000 description 29
- 108091034117 Oligonucleotide Proteins 0.000 description 28
- 238000003556 assay Methods 0.000 description 27
- 230000000875 corresponding effect Effects 0.000 description 27
- 238000009396 hybridization Methods 0.000 description 27
- 230000002163 immunogen Effects 0.000 description 27
- 240000004808 Saccharomyces cerevisiae Species 0.000 description 26
- 235000014680 Saccharomyces cerevisiae Nutrition 0.000 description 26
- 229960005091 chloramphenicol Drugs 0.000 description 26
- WIIZWVCIJKGZOK-RKDXNWHRSA-N chloramphenicol Chemical compound ClC(Cl)C(=O)N[C@H](CO)[C@H](O)C1=CC=C([N+]([O-])=O)C=C1 WIIZWVCIJKGZOK-RKDXNWHRSA-N 0.000 description 26
- 238000002703 mutagenesis Methods 0.000 description 26
- 231100000350 mutagenesis Toxicity 0.000 description 26
- OUYCCCASQSFEME-UHFFFAOYSA-N tyrosine Natural products OC(=O)C(N)CC1=CC=C(O)C=C1 OUYCCCASQSFEME-UHFFFAOYSA-N 0.000 description 26
- 239000013598 vector Substances 0.000 description 26
- 239000003795 chemical substances by application Substances 0.000 description 25
- 238000002741 site-directed mutagenesis Methods 0.000 description 25
- -1 for example Substances 0.000 description 24
- OUYCCCASQSFEME-QMMMGPOBSA-N L-tyrosine Chemical compound OC(=O)[C@@H](N)CC1=CC=C(O)C=C1 OUYCCCASQSFEME-QMMMGPOBSA-N 0.000 description 23
- GEYBMYRBIABFTA-VIFPVBQESA-N O-methyl-L-tyrosine Chemical compound COC1=CC=C(C[C@H](N)C(O)=O)C=C1 GEYBMYRBIABFTA-VIFPVBQESA-N 0.000 description 23
- 239000000523 sample Substances 0.000 description 23
- 239000002773 nucleotide Substances 0.000 description 22
- 125000003729 nucleotide group Chemical group 0.000 description 22
- 230000002068 genetic effect Effects 0.000 description 21
- 101710137500 T7 RNA polymerase Proteins 0.000 description 20
- 238000001943 fluorescence-activated cell sorting Methods 0.000 description 19
- PYMYPHUHKUWMLA-UHFFFAOYSA-N arabinose Natural products OCC(O)C(O)C(O)C=O PYMYPHUHKUWMLA-UHFFFAOYSA-N 0.000 description 18
- SRBFZHDQGSBBOR-UHFFFAOYSA-N beta-D-Pyranose-Lyxose Natural products OC1COC(O)C(O)C1O SRBFZHDQGSBBOR-UHFFFAOYSA-N 0.000 description 18
- 230000006229 amino acid addition Effects 0.000 description 17
- 239000012634 fragment Substances 0.000 description 17
- 235000008729 phenylalanine Nutrition 0.000 description 17
- 238000006467 substitution reaction Methods 0.000 description 17
- 125000001493 tyrosinyl group Chemical class [H]OC1=C([H])C([H])=C(C([H])=C1[H])C([H])([H])C([H])(N([H])[H])C(*)=O 0.000 description 17
- 102000004190 Enzymes Human genes 0.000 description 16
- 108090000790 Enzymes Proteins 0.000 description 16
- 241001302042 Methanothermobacter thermautotrophicus Species 0.000 description 16
- 241000589499 Thermus thermophilus Species 0.000 description 16
- 229940088598 enzyme Drugs 0.000 description 16
- COLNVLDHVKWLRT-UHFFFAOYSA-N phenylalanine Natural products OC(=O)C(N)CC1=CC=CC=C1 COLNVLDHVKWLRT-UHFFFAOYSA-N 0.000 description 16
- 231100000331 toxic Toxicity 0.000 description 16
- 230000002588 toxic effect Effects 0.000 description 16
- 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 16
- PEDCQBHIVMGVHV-UHFFFAOYSA-N Glycerine Chemical compound OCC(O)CO PEDCQBHIVMGVHV-UHFFFAOYSA-N 0.000 description 15
- 108010043121 Green Fluorescent Proteins Proteins 0.000 description 15
- 102000004144 Green Fluorescent Proteins Human genes 0.000 description 15
- 241000205062 Halobacterium Species 0.000 description 15
- 238000004458 analytical method Methods 0.000 description 15
- 238000004422 calculation algorithm Methods 0.000 description 15
- 230000000295 complement effect Effects 0.000 description 15
- 230000006870 function Effects 0.000 description 15
- 239000005090 green fluorescent protein Substances 0.000 description 15
- 239000002253 acid Substances 0.000 description 14
- 230000008521 reorganization Effects 0.000 description 14
- 102100024977 Glutamine-tRNA ligase Human genes 0.000 description 13
- 125000003275 alpha amino acid group Chemical group 0.000 description 13
- 230000001851 biosynthetic effect Effects 0.000 description 13
- 238000010276 construction Methods 0.000 description 13
- 238000012217 deletion Methods 0.000 description 13
- 230000037430 deletion Effects 0.000 description 13
- 239000013604 expression vector Substances 0.000 description 13
- 108010051239 glutaminyl-tRNA synthetase Proteins 0.000 description 13
- 239000007788 liquid Substances 0.000 description 13
- 241000894006 Bacteria Species 0.000 description 12
- ROHFNLRQFUQHCH-UHFFFAOYSA-N Leucine Natural products CC(C)CC(N)C(O)=O ROHFNLRQFUQHCH-UHFFFAOYSA-N 0.000 description 12
- 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 12
- 150000007513 acids Chemical class 0.000 description 12
- 238000013459 approach Methods 0.000 description 12
- PYMYPHUHKUWMLA-WDCZJNDASA-N arabinose Chemical compound OC[C@@H](O)[C@@H](O)[C@H](O)C=O PYMYPHUHKUWMLA-WDCZJNDASA-N 0.000 description 12
- 230000015572 biosynthetic process Effects 0.000 description 12
- 238000002474 experimental method Methods 0.000 description 12
- 125000000956 methoxy group Chemical group [H]C([H])([H])O* 0.000 description 12
- 108091033319 polynucleotide Proteins 0.000 description 12
- 102000040430 polynucleotide Human genes 0.000 description 12
- 230000004044 response Effects 0.000 description 12
- 230000009466 transformation Effects 0.000 description 12
- 238000005406 washing Methods 0.000 description 12
- ROHFNLRQFUQHCH-YFKPBYRVSA-N L-leucine Chemical compound CC(C)C[C@H](N)C(O)=O ROHFNLRQFUQHCH-YFKPBYRVSA-N 0.000 description 11
- 230000003115 biocidal effect Effects 0.000 description 11
- 238000011068 loading method Methods 0.000 description 11
- 238000003752 polymerase chain reaction Methods 0.000 description 11
- 239000002157 polynucleotide Substances 0.000 description 11
- 239000000126 substance Substances 0.000 description 11
- XTXGLOBWOMUGQB-VIFPVBQESA-N (2s)-2-azaniumyl-3-(3-methoxyphenyl)propanoate Chemical compound COC1=CC=CC(C[C@H](N)C(O)=O)=C1 XTXGLOBWOMUGQB-VIFPVBQESA-N 0.000 description 10
- 108091032973 (ribonucleotides)n+m Proteins 0.000 description 10
- 241000205042 Archaeoglobus fulgidus Species 0.000 description 10
- 108010021466 Mutant Proteins Proteins 0.000 description 10
- 102000008300 Mutant Proteins Human genes 0.000 description 10
- 150000002576 ketones Chemical class 0.000 description 10
- 230000008569 process Effects 0.000 description 10
- 229920000742 Cotton Polymers 0.000 description 9
- 241001302160 Escherichia coli str. K-12 substr. DH10B Species 0.000 description 9
- 239000003242 anti bacterial agent Substances 0.000 description 9
- 230000003197 catalytic effect Effects 0.000 description 9
- 238000003018 immunoassay Methods 0.000 description 9
- 238000002708 random mutagenesis Methods 0.000 description 9
- 241000196324 Embryophyta Species 0.000 description 8
- 241000193385 Geobacillus stearothermophilus Species 0.000 description 8
- COLNVLDHVKWLRT-QMMMGPOBSA-N L-phenylalanine Chemical compound OC(=O)[C@@H](N)CC1=CC=CC=C1 COLNVLDHVKWLRT-QMMMGPOBSA-N 0.000 description 8
- 108091028043 Nucleic acid sequence Proteins 0.000 description 8
- 108010029287 Threonine-tRNA ligase Proteins 0.000 description 8
- 102100034997 Threonine-tRNA ligase, mitochondrial Human genes 0.000 description 8
- 101150055766 cat gene Proteins 0.000 description 8
- 229910052739 hydrogen Inorganic materials 0.000 description 8
- 239000001257 hydrogen Substances 0.000 description 8
- 230000003993 interaction Effects 0.000 description 8
- 230000004083 survival effect Effects 0.000 description 8
- 238000013518 transcription Methods 0.000 description 8
- ZKHQWZAMYRWXGA-KQYNXXCUSA-J ATP(4-) Chemical compound C1=NC=2C(N)=NC=NC=2N1[C@@H]1O[C@H](COP([O-])(=O)OP([O-])(=O)OP([O-])([O-])=O)[C@@H](O)[C@H]1O ZKHQWZAMYRWXGA-KQYNXXCUSA-J 0.000 description 7
- ZKHQWZAMYRWXGA-UHFFFAOYSA-N Adenosine triphosphate Natural products C1=NC=2C(N)=NC=NC=2N1C1OC(COP(O)(=O)OP(O)(=O)OP(O)(O)=O)C(O)C1O ZKHQWZAMYRWXGA-UHFFFAOYSA-N 0.000 description 7
- DHMQDGOQFOQNFH-UHFFFAOYSA-N Glycine Chemical compound NCC(O)=O DHMQDGOQFOQNFH-UHFFFAOYSA-N 0.000 description 7
- ZDXPYRJPNDTMRX-VKHMYHEASA-N L-glutamine Chemical compound OC(=O)[C@@H](N)CCC(N)=O ZDXPYRJPNDTMRX-VKHMYHEASA-N 0.000 description 7
- FFEARJCKVFRZRR-BYPYZUCNSA-N L-methionine Chemical compound CSCC[C@H](N)C(O)=O FFEARJCKVFRZRR-BYPYZUCNSA-N 0.000 description 7
- 229910052799 carbon Inorganic materials 0.000 description 7
- 230000010261 cell growth Effects 0.000 description 7
- 230000008859 change Effects 0.000 description 7
- 238000006243 chemical reaction Methods 0.000 description 7
- 230000009260 cross reactivity Effects 0.000 description 7
- 230000012010 growth Effects 0.000 description 7
- 229930182817 methionine Natural products 0.000 description 7
- 230000010363 phase shift Effects 0.000 description 7
- 230000035897 transcription Effects 0.000 description 7
- 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 6
- 229920001817 Agar Polymers 0.000 description 6
- 101000787278 Arabidopsis thaliana Valine-tRNA ligase, chloroplastic/mitochondrial 2 Proteins 0.000 description 6
- 101000787296 Arabidopsis thaliana Valine-tRNA ligase, mitochondrial 1 Proteins 0.000 description 6
- 108010065272 Aspartate-tRNA ligase Proteins 0.000 description 6
- 102100026198 Aspartate-tRNA ligase, mitochondrial Human genes 0.000 description 6
- 101000787280 Dictyostelium discoideum Probable valine-tRNA ligase, mitochondrial Proteins 0.000 description 6
- XUJNEKJLAYXESH-REOHCLBHSA-N L-Cysteine Chemical compound SC[C@H](N)C(O)=O XUJNEKJLAYXESH-REOHCLBHSA-N 0.000 description 6
- QNAYBMKLOCPYGJ-REOHCLBHSA-N L-alanine Chemical compound C[C@H](N)C(O)=O QNAYBMKLOCPYGJ-REOHCLBHSA-N 0.000 description 6
- 108010004478 Phenylalanine-tRNA Ligase Proteins 0.000 description 6
- 102100029354 Phenylalanine-tRNA ligase, mitochondrial Human genes 0.000 description 6
- 241000522615 Pyrococcus horikoshii Species 0.000 description 6
- 102000013625 Valine-tRNA Ligase Human genes 0.000 description 6
- 230000010933 acylation Effects 0.000 description 6
- 238000005917 acylation reaction Methods 0.000 description 6
- 239000008272 agar Substances 0.000 description 6
- 235000004279 alanine Nutrition 0.000 description 6
- QWCKQJZIFLGMSD-UHFFFAOYSA-N alpha-aminobutyric acid Chemical compound CCC(N)C(O)=O QWCKQJZIFLGMSD-UHFFFAOYSA-N 0.000 description 6
- 230000001580 bacterial effect Effects 0.000 description 6
- 238000004113 cell culture Methods 0.000 description 6
- 230000001419 dependent effect Effects 0.000 description 6
- 230000001976 improved effect Effects 0.000 description 6
- 230000006872 improvement Effects 0.000 description 6
- 230000007246 mechanism Effects 0.000 description 6
- 239000012071 phase Substances 0.000 description 6
- 230000002829 reductive effect Effects 0.000 description 6
- ODIGIKRIUKFKHP-UHFFFAOYSA-N (n-propan-2-yloxycarbonylanilino) acetate Chemical compound CC(C)OC(=O)N(OC(C)=O)C1=CC=CC=C1 ODIGIKRIUKFKHP-UHFFFAOYSA-N 0.000 description 5
- 241000567139 Aeropyrum pernix Species 0.000 description 5
- 244000105975 Antidesma platyphyllum Species 0.000 description 5
- OKTJSMMVPCPJKN-UHFFFAOYSA-N Carbon Chemical compound [C] OKTJSMMVPCPJKN-UHFFFAOYSA-N 0.000 description 5
- 241000282414 Homo sapiens Species 0.000 description 5
- KDXKERNSBIXSRK-UHFFFAOYSA-N Lysine Natural products NCCCCC(N)C(O)=O KDXKERNSBIXSRK-UHFFFAOYSA-N 0.000 description 5
- 241000205156 Pyrococcus furiosus Species 0.000 description 5
- 238000010367 cloning Methods 0.000 description 5
- 230000000052 comparative effect Effects 0.000 description 5
- 230000001186 cumulative effect Effects 0.000 description 5
- LOKCTEFSRHRXRJ-UHFFFAOYSA-I dipotassium trisodium dihydrogen phosphate hydrogen phosphate dichloride Chemical compound P(=O)(O)(O)[O-].[K+].P(=O)(O)([O-])[O-].[Na+].[Na+].[Cl-].[K+].[Cl-].[Na+] LOKCTEFSRHRXRJ-UHFFFAOYSA-I 0.000 description 5
- 230000002255 enzymatic effect Effects 0.000 description 5
- 125000000524 functional group Chemical group 0.000 description 5
- ZDXPYRJPNDTMRX-UHFFFAOYSA-N glutamine Natural products OC(=O)C(N)CCC(N)=O ZDXPYRJPNDTMRX-UHFFFAOYSA-N 0.000 description 5
- 235000004554 glutamine Nutrition 0.000 description 5
- 235000009424 haa Nutrition 0.000 description 5
- 230000002209 hydrophobic effect Effects 0.000 description 5
- 238000003780 insertion Methods 0.000 description 5
- 230000037431 insertion Effects 0.000 description 5
- 125000002496 methyl group Chemical group [H]C([H])([H])* 0.000 description 5
- 108091070501 miRNA Proteins 0.000 description 5
- 238000002823 phage display Methods 0.000 description 5
- 239000002953 phosphate buffered saline Substances 0.000 description 5
- FQRURPFZTFUXEZ-MRVPVSSYSA-N (2s)-2,3,3,3-tetrafluoro-2-(n-fluoroanilino)propanoic acid Chemical compound OC(=O)[C@](F)(C(F)(F)F)N(F)C1=CC=CC=C1 FQRURPFZTFUXEZ-MRVPVSSYSA-N 0.000 description 4
- 239000004475 Arginine Substances 0.000 description 4
- 108091035707 Consensus sequence Proteins 0.000 description 4
- 108090000626 DNA-directed RNA polymerases 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
- 241000204942 Halobacterium sp. Species 0.000 description 4
- OAKJQQAXSVQMHS-UHFFFAOYSA-N Hydrazine Chemical compound NN OAKJQQAXSVQMHS-UHFFFAOYSA-N 0.000 description 4
- ODKSFYDXXFIFQN-BYPYZUCNSA-P L-argininium(2+) Chemical compound NC(=[NH2+])NCCC[C@H]([NH3+])C(O)=O ODKSFYDXXFIFQN-BYPYZUCNSA-P 0.000 description 4
- CKLJMWTZIZZHCS-REOHCLBHSA-N L-aspartic acid Chemical compound OC(=O)[C@@H](N)CC(O)=O CKLJMWTZIZZHCS-REOHCLBHSA-N 0.000 description 4
- KDXKERNSBIXSRK-YFKPBYRVSA-N L-lysine Chemical compound NCCCC[C@H](N)C(O)=O KDXKERNSBIXSRK-YFKPBYRVSA-N 0.000 description 4
- AYFVYJQAPQTCCC-GBXIJSLDSA-N L-threonine Chemical compound C[C@@H](O)[C@H](N)C(O)=O AYFVYJQAPQTCCC-GBXIJSLDSA-N 0.000 description 4
- 241001465754 Metazoa Species 0.000 description 4
- 241000203353 Methanococcus Species 0.000 description 4
- 108020004485 Nonsense Codon Proteins 0.000 description 4
- MTCFGRXMJLQNBG-UHFFFAOYSA-N Serine Natural products OCC(N)C(O)=O MTCFGRXMJLQNBG-UHFFFAOYSA-N 0.000 description 4
- 239000004098 Tetracycline Substances 0.000 description 4
- 108010022394 Threonine synthase Proteins 0.000 description 4
- KZSNJWFQEVHDMF-UHFFFAOYSA-N Valine Natural products CC(C)C(N)C(O)=O KZSNJWFQEVHDMF-UHFFFAOYSA-N 0.000 description 4
- 125000003295 alanine group Chemical group N[C@@H](C)C(=O)* 0.000 description 4
- 229940088710 antibiotic agent Drugs 0.000 description 4
- ODKSFYDXXFIFQN-UHFFFAOYSA-N arginine Natural products OC(=O)C(N)CCCNC(N)=N ODKSFYDXXFIFQN-UHFFFAOYSA-N 0.000 description 4
- 235000009697 arginine Nutrition 0.000 description 4
- 230000008901 benefit Effects 0.000 description 4
- 230000002950 deficient Effects 0.000 description 4
- 238000001514 detection method Methods 0.000 description 4
- 102000004419 dihydrofolate reductase Human genes 0.000 description 4
- 239000001963 growth medium Substances 0.000 description 4
- 238000009630 liquid culture Methods 0.000 description 4
- 238000007899 nucleic acid hybridization Methods 0.000 description 4
- 238000001243 protein synthesis Methods 0.000 description 4
- 238000000746 purification Methods 0.000 description 4
- 230000010076 replication Effects 0.000 description 4
- 238000010187 selection method Methods 0.000 description 4
- 239000007790 solid phase Substances 0.000 description 4
- 241000894007 species Species 0.000 description 4
- 239000007858 starting material Substances 0.000 description 4
- 229960002180 tetracycline Drugs 0.000 description 4
- 229930101283 tetracycline Natural products 0.000 description 4
- 235000019364 tetracycline Nutrition 0.000 description 4
- 150000003522 tetracyclines Chemical class 0.000 description 4
- 231100000419 toxicity Toxicity 0.000 description 4
- 230000001988 toxicity Effects 0.000 description 4
- 238000011144 upstream manufacturing Methods 0.000 description 4
- 239000004474 valine Substances 0.000 description 4
- 238000011179 visual inspection Methods 0.000 description 4
- 241001244729 Apalis Species 0.000 description 3
- 241000203069 Archaea Species 0.000 description 3
- 101100392772 Caenorhabditis elegans gln-2 gene Proteins 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
- 102000004163 DNA-directed RNA polymerases Human genes 0.000 description 3
- 241000206602 Eukaryota Species 0.000 description 3
- 108700039691 Genetic Promoter Regions Proteins 0.000 description 3
- 239000004471 Glycine Substances 0.000 description 3
- 241000238631 Hexapoda Species 0.000 description 3
- 102000004310 Ion Channels Human genes 0.000 description 3
- 108090000862 Ion Channels Proteins 0.000 description 3
- DCXYFEDJOCDNAF-REOHCLBHSA-N L-asparagine Chemical compound OC(=O)[C@@H](N)CC(N)=O DCXYFEDJOCDNAF-REOHCLBHSA-N 0.000 description 3
- AGPKZVBTJJNPAG-WHFBIAKZSA-N L-isoleucine Chemical compound CC[C@H](C)[C@H](N)C(O)=O AGPKZVBTJJNPAG-WHFBIAKZSA-N 0.000 description 3
- 125000003798 L-tyrosyl group Chemical group [H]N([H])[C@]([H])(C(=O)[*])C([H])([H])C1=C([H])C([H])=C(O[H])C([H])=C1[H] 0.000 description 3
- KZSNJWFQEVHDMF-BYPYZUCNSA-N L-valine Chemical compound CC(C)[C@H](N)C(O)=O KZSNJWFQEVHDMF-BYPYZUCNSA-N 0.000 description 3
- 239000004472 Lysine Substances 0.000 description 3
- 241000124008 Mammalia Species 0.000 description 3
- 241000699670 Mus sp. Species 0.000 description 3
- 108010062374 Myoglobin Proteins 0.000 description 3
- 102000007056 Recombinant Fusion Proteins Human genes 0.000 description 3
- 108010008281 Recombinant Fusion Proteins Proteins 0.000 description 3
- 238000009825 accumulation Methods 0.000 description 3
- 125000002777 acetyl group Chemical group [H]C([H])([H])C(*)=O 0.000 description 3
- 235000008206 alpha-amino acids Nutrition 0.000 description 3
- 230000004075 alteration Effects 0.000 description 3
- 210000004899 c-terminal region Anatomy 0.000 description 3
- 230000030833 cell death Effects 0.000 description 3
- 238000012937 correction Methods 0.000 description 3
- 210000004748 cultured cell Anatomy 0.000 description 3
- 238000013461 design Methods 0.000 description 3
- 238000011161 development Methods 0.000 description 3
- 230000018109 developmental process Effects 0.000 description 3
- 238000004520 electroporation Methods 0.000 description 3
- 238000011156 evaluation Methods 0.000 description 3
- 230000005284 excitation Effects 0.000 description 3
- 238000007429 general method Methods 0.000 description 3
- 125000002887 hydroxy group Chemical group [H]O* 0.000 description 3
- 238000005462 in vivo assay Methods 0.000 description 3
- 238000011534 incubation Methods 0.000 description 3
- 239000003112 inhibitor Substances 0.000 description 3
- 239000000543 intermediate Substances 0.000 description 3
- 229960000310 isoleucine Drugs 0.000 description 3
- AGPKZVBTJJNPAG-UHFFFAOYSA-N isoleucine Natural products CCC(C)C(N)C(O)=O AGPKZVBTJJNPAG-UHFFFAOYSA-N 0.000 description 3
- 125000001449 isopropyl group Chemical group [H]C([H])([H])C([H])(*)C([H])([H])[H] 0.000 description 3
- 229930027917 kanamycin Natural products 0.000 description 3
- 229960000318 kanamycin Drugs 0.000 description 3
- SBUJHOSQTJFQJX-NOAMYHISSA-N kanamycin Chemical compound O[C@@H]1[C@@H](O)[C@H](O)[C@@H](CN)O[C@@H]1O[C@H]1[C@H](O)[C@@H](O[C@@H]2[C@@H]([C@@H](N)[C@H](O)[C@@H](CO)O2)O)[C@H](N)C[C@@H]1N SBUJHOSQTJFQJX-NOAMYHISSA-N 0.000 description 3
- 229930182823 kanamycin A Natural products 0.000 description 3
- 238000004949 mass spectrometry Methods 0.000 description 3
- 238000005259 measurement Methods 0.000 description 3
- 210000000287 oocyte Anatomy 0.000 description 3
- 239000002245 particle Substances 0.000 description 3
- 230000000704 physical effect Effects 0.000 description 3
- 229920000570 polyether Polymers 0.000 description 3
- 230000008439 repair process Effects 0.000 description 3
- 230000019491 signal transduction Effects 0.000 description 3
- RYYWUUFWQRZTIU-UHFFFAOYSA-K thiophosphate Chemical compound [O-]P([O-])([O-])=S RYYWUUFWQRZTIU-UHFFFAOYSA-K 0.000 description 3
- 238000006257 total synthesis reaction Methods 0.000 description 3
- 238000012546 transfer Methods 0.000 description 3
- 241001515965 unidentified phage Species 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
- MTCFGRXMJLQNBG-REOHCLBHSA-N (2S)-2-Amino-3-hydroxypropansäure Chemical compound OC[C@H](N)C(O)=O MTCFGRXMJLQNBG-REOHCLBHSA-N 0.000 description 2
- YTBKOFZZSHCXGJ-QRPNPIFTSA-N (2s)-2-amino-3-(4-hydroxyphenyl)propanoic acid;phenol Chemical group OC1=CC=CC=C1.OC(=O)[C@@H](N)CC1=CC=C(O)C=C1 YTBKOFZZSHCXGJ-QRPNPIFTSA-N 0.000 description 2
- 125000001622 2-naphthyl group Chemical group [H]C1=C([H])C([H])=C2C([H])=C(*)C([H])=C([H])C2=C1[H] 0.000 description 2
- 241000238421 Arthropoda Species 0.000 description 2
- DCXYFEDJOCDNAF-UHFFFAOYSA-N Asparagine Natural products OC(=O)C(N)CC(N)=O DCXYFEDJOCDNAF-UHFFFAOYSA-N 0.000 description 2
- 101710183938 Barstar Proteins 0.000 description 2
- 102100031673 Corneodesmosin Human genes 0.000 description 2
- 241000195493 Cryptophyta Species 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
- 102000004594 DNA Polymerase I Human genes 0.000 description 2
- 108010017826 DNA Polymerase I Proteins 0.000 description 2
- RTZKZFJDLAIYFH-UHFFFAOYSA-N Diethyl ether Chemical compound CCOCC RTZKZFJDLAIYFH-UHFFFAOYSA-N 0.000 description 2
- 206010059866 Drug resistance Diseases 0.000 description 2
- 102100038132 Endogenous retrovirus group K member 6 Pro protein Human genes 0.000 description 2
- 101710091045 Envelope protein Proteins 0.000 description 2
- 241000588722 Escherichia Species 0.000 description 2
- 101000740462 Escherichia coli Beta-lactamase TEM Proteins 0.000 description 2
- 108700007698 Genetic Terminator Regions Proteins 0.000 description 2
- WHUUTDBJXJRKMK-UHFFFAOYSA-N Glutamic acid Natural products OC(=O)C(N)CCC(O)=O WHUUTDBJXJRKMK-UHFFFAOYSA-N 0.000 description 2
- AVXURJPOCDRRFD-UHFFFAOYSA-N Hydroxylamine Chemical compound ON AVXURJPOCDRRFD-UHFFFAOYSA-N 0.000 description 2
- 108010058683 Immobilized Proteins Proteins 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
- 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
- 241000209510 Liliopsida Species 0.000 description 2
- 108010052285 Membrane Proteins Proteins 0.000 description 2
- 102000018697 Membrane Proteins Human genes 0.000 description 2
- 241001074903 Methanobacteria Species 0.000 description 2
- 102100030856 Myoglobin Human genes 0.000 description 2
- 108020004711 Nucleic Acid Probes Proteins 0.000 description 2
- 108091005461 Nucleic proteins Proteins 0.000 description 2
- 102000007079 Peptide Fragments Human genes 0.000 description 2
- 108010033276 Peptide Fragments Proteins 0.000 description 2
- 239000004721 Polyphenylene oxide Substances 0.000 description 2
- 108010076504 Protein Sorting Signals Proteins 0.000 description 2
- 101710188315 Protein X Proteins 0.000 description 2
- 108700008625 Reporter Genes Proteins 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
- ISAKRJDGNUQOIC-UHFFFAOYSA-N Uracil Chemical compound O=C1C=CNC(=O)N1 ISAKRJDGNUQOIC-UHFFFAOYSA-N 0.000 description 2
- 241000269370 Xenopus <genus> Species 0.000 description 2
- 239000004234 Yellow 2G Substances 0.000 description 2
- 235000019647 acidic taste Nutrition 0.000 description 2
- 230000004913 activation Effects 0.000 description 2
- 239000002671 adjuvant Substances 0.000 description 2
- 238000000246 agarose gel electrophoresis Methods 0.000 description 2
- 150000001371 alpha-amino acids Chemical class 0.000 description 2
- 125000000539 amino acid group Chemical group 0.000 description 2
- 230000000689 aminoacylating effect Effects 0.000 description 2
- 229940124277 aminobutyric acid Drugs 0.000 description 2
- 230000000844 anti-bacterial effect Effects 0.000 description 2
- 125000003118 aryl group Chemical group 0.000 description 2
- 235000009582 asparagine Nutrition 0.000 description 2
- 229960001230 asparagine Drugs 0.000 description 2
- 235000003704 aspartic acid Nutrition 0.000 description 2
- 230000003385 bacteriostatic effect Effects 0.000 description 2
- 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 2
- 230000004071 biological effect Effects 0.000 description 2
- 238000004364 calculation method Methods 0.000 description 2
- 125000003178 carboxy group Chemical group [H]OC(*)=O 0.000 description 2
- 230000003915 cell function Effects 0.000 description 2
- 238000012512 characterization method Methods 0.000 description 2
- 238000007385 chemical modification Methods 0.000 description 2
- 239000003153 chemical reaction reagent Substances 0.000 description 2
- 238000003776 cleavage reaction Methods 0.000 description 2
- 230000001427 coherent effect Effects 0.000 description 2
- 230000001332 colony forming effect Effects 0.000 description 2
- 230000009137 competitive binding Effects 0.000 description 2
- 150000001875 compounds Chemical class 0.000 description 2
- 238000007796 conventional method Methods 0.000 description 2
- 238000012258 culturing Methods 0.000 description 2
- 238000004163 cytometry Methods 0.000 description 2
- 210000000805 cytoplasm Anatomy 0.000 description 2
- 230000003247 decreasing effect Effects 0.000 description 2
- 230000007547 defect Effects 0.000 description 2
- XPPKVPWEQAFLFU-UHFFFAOYSA-J diphosphate(4-) Chemical group [O-]P([O-])(=O)OP([O-])([O-])=O XPPKVPWEQAFLFU-UHFFFAOYSA-J 0.000 description 2
- 235000011180 diphosphates Nutrition 0.000 description 2
- 238000005516 engineering process Methods 0.000 description 2
- 238000006911 enzymatic reaction Methods 0.000 description 2
- 241001233957 eudicotyledons Species 0.000 description 2
- 210000003527 eukaryotic cell Anatomy 0.000 description 2
- BTCSSZJGUNDROE-UHFFFAOYSA-N gamma-aminobutyric acid Chemical compound NCCCC(O)=O BTCSSZJGUNDROE-UHFFFAOYSA-N 0.000 description 2
- 235000013922 glutamic acid Nutrition 0.000 description 2
- 239000004220 glutamic acid Substances 0.000 description 2
- 150000002308 glutamine derivatives Chemical class 0.000 description 2
- 235000014304 histidine Nutrition 0.000 description 2
- 238000002744 homologous recombination Methods 0.000 description 2
- 230000006801 homologous recombination Effects 0.000 description 2
- 230000028993 immune response Effects 0.000 description 2
- 230000006698 induction Effects 0.000 description 2
- 208000015181 infectious disease Diseases 0.000 description 2
- 239000003999 initiator Substances 0.000 description 2
- 150000002500 ions Chemical class 0.000 description 2
- 125000000959 isobutyl group Chemical group [H]C([H])([H])C([H])(C([H])([H])[H])C([H])([H])* 0.000 description 2
- 238000002955 isolation Methods 0.000 description 2
- 101150066555 lacZ gene Proteins 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
- 230000000670 limiting effect Effects 0.000 description 2
- 239000011159 matrix material Substances 0.000 description 2
- 239000012528 membrane Substances 0.000 description 2
- 239000002184 metal Substances 0.000 description 2
- 229910052751 metal Inorganic materials 0.000 description 2
- 244000005700 microbiome Species 0.000 description 2
- 238000000520 microinjection Methods 0.000 description 2
- 230000004048 modification Effects 0.000 description 2
- 238000012986 modification Methods 0.000 description 2
- 238000010369 molecular cloning Methods 0.000 description 2
- 125000000449 nitro group Chemical group [O-][N+](*)=O 0.000 description 2
- 239000002853 nucleic acid probe Substances 0.000 description 2
- 235000015097 nutrients Nutrition 0.000 description 2
- 238000005457 optimization Methods 0.000 description 2
- VLTRZXGMWDSKGL-UHFFFAOYSA-N perchloric acid Chemical compound OCl(=O)(=O)=O VLTRZXGMWDSKGL-UHFFFAOYSA-N 0.000 description 2
- 210000001322 periplasm Anatomy 0.000 description 2
- 230000029553 photosynthesis Effects 0.000 description 2
- 238000010672 photosynthesis Methods 0.000 description 2
- 239000002243 precursor Substances 0.000 description 2
- 125000002924 primary amino group Chemical group [H]N([H])* 0.000 description 2
- 125000001500 prolyl group Chemical class [H]N1C([H])(C(=O)[*])C([H])([H])C([H])([H])C1([H])[H] 0.000 description 2
- 230000004853 protein function Effects 0.000 description 2
- 238000011158 quantitative evaluation Methods 0.000 description 2
- 230000009257 reactivity Effects 0.000 description 2
- 238000005215 recombination Methods 0.000 description 2
- 230000006798 recombination Effects 0.000 description 2
- 238000011084 recovery Methods 0.000 description 2
- 108091008146 restriction endonucleases Proteins 0.000 description 2
- 102200024032 rs369610897 Human genes 0.000 description 2
- 230000007017 scission Effects 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
- 229940055619 selenocysteine Drugs 0.000 description 2
- 230000035945 sensitivity Effects 0.000 description 2
- 238000012163 sequencing technique Methods 0.000 description 2
- 239000007787 solid Substances 0.000 description 2
- 239000000243 solution Substances 0.000 description 2
- 108010068698 spleen exonuclease Proteins 0.000 description 2
- 125000001424 substituent group Chemical group 0.000 description 2
- 235000000346 sugar Nutrition 0.000 description 2
- 230000001225 therapeutic effect Effects 0.000 description 2
- 108010074429 thiolsubtilisins Proteins 0.000 description 2
- 210000001519 tissue Anatomy 0.000 description 2
- 238000002054 transplantation Methods 0.000 description 2
- 239000013603 viral vector Substances 0.000 description 2
- KNWCDYSKJSREAQ-VKHMYHEASA-N (2s)-1,3-oxazolidine-2-carboxylic acid Chemical compound OC(=O)[C@H]1NCCO1 KNWCDYSKJSREAQ-VKHMYHEASA-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
- 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
- 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
- NEMHIKRLROONTL-QMMMGPOBSA-N (2s)-2-azaniumyl-3-(4-azidophenyl)propanoate Chemical compound OC(=O)[C@@H](N)CC1=CC=C(N=[N+]=[N-])C=C1 NEMHIKRLROONTL-QMMMGPOBSA-N 0.000 description 1
- CYHRSNOITZHLJN-NSHDSACASA-N (2s)-2-azaniumyl-3-(4-propan-2-ylphenyl)propanoate Chemical compound CC(C)C1=CC=C(C[C@H](N)C(O)=O)C=C1 CYHRSNOITZHLJN-NSHDSACASA-N 0.000 description 1
- YTLYLLTVENPWFT-UPHRSURJSA-N (Z)-3-aminoacrylic acid Chemical compound N\C=C/C(O)=O YTLYLLTVENPWFT-UPHRSURJSA-N 0.000 description 1
- 238000004293 19F NMR spectroscopy Methods 0.000 description 1
- RNAMYOYQYRYFQY-UHFFFAOYSA-N 2-(4,4-difluoropiperidin-1-yl)-6-methoxy-n-(1-propan-2-ylpiperidin-4-yl)-7-(3-pyrrolidin-1-ylpropoxy)quinazolin-4-amine Chemical compound N1=C(N2CCC(F)(F)CC2)N=C2C=C(OCCCN3CCCC3)C(OC)=CC2=C1NC1CCN(C(C)C)CC1 RNAMYOYQYRYFQY-UHFFFAOYSA-N 0.000 description 1
- QKNYBSVHEMOAJP-UHFFFAOYSA-N 2-amino-2-(hydroxymethyl)propane-1,3-diol;hydron;chloride Chemical compound Cl.OCC(N)(CO)CO QKNYBSVHEMOAJP-UHFFFAOYSA-N 0.000 description 1
- 125000003903 2-propenyl group Chemical group [H]C([*])([H])C([H])=C([H])[H] 0.000 description 1
- 102100039217 3-ketoacyl-CoA thiolase, peroxisomal Human genes 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
- ATVJXMYDOSMEPO-UHFFFAOYSA-N 3-prop-2-enoxyprop-1-ene Chemical group C=CCOCC=C ATVJXMYDOSMEPO-UHFFFAOYSA-N 0.000 description 1
- YXDGRBPZVQPESQ-QMMMGPOBSA-N 4-[(2s)-2-amino-2-carboxyethyl]benzoic acid Chemical compound OC(=O)[C@@H](N)CC1=CC=C(C(O)=O)C=C1 YXDGRBPZVQPESQ-QMMMGPOBSA-N 0.000 description 1
- XWHHYOYVRVGJJY-UHFFFAOYSA-N 4-fluorophenylalanine Chemical compound OC(=O)C(N)CC1=CC=C(F)C=C1 XWHHYOYVRVGJJY-UHFFFAOYSA-N 0.000 description 1
- PZNQZSRPDOEBMS-QMMMGPOBSA-N 4-iodo-L-phenylalanine Chemical compound OC(=O)[C@@H](N)CC1=CC=C(I)C=C1 PZNQZSRPDOEBMS-QMMMGPOBSA-N 0.000 description 1
- XFGVJLGVINCWDP-UHFFFAOYSA-N 5,5,5-trifluoroleucine Chemical compound FC(F)(F)C(C)CC(N)C(O)=O XFGVJLGVINCWDP-UHFFFAOYSA-N 0.000 description 1
- 241000023308 Acca Species 0.000 description 1
- 229930024421 Adenine Natural products 0.000 description 1
- 108010088751 Albumins Proteins 0.000 description 1
- 102000009027 Albumins Human genes 0.000 description 1
- 102000007698 Alcohol dehydrogenase Human genes 0.000 description 1
- 108010021809 Alcohol dehydrogenase Proteins 0.000 description 1
- 101100366707 Arabidopsis thaliana SSL11 gene 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
- 241000283690 Bos taurus Species 0.000 description 1
- 108091003079 Bovine Serum Albumin Proteins 0.000 description 1
- 102100025570 Cancer/testis antigen 1 Human genes 0.000 description 1
- 239000004215 Carbon black (E152) Substances 0.000 description 1
- 102000014914 Carrier Proteins Human genes 0.000 description 1
- 108010078791 Carrier Proteins Proteins 0.000 description 1
- 229920001661 Chitosan Polymers 0.000 description 1
- 108010000898 Chorismate mutase Proteins 0.000 description 1
- 241000223782 Ciliophora Species 0.000 description 1
- 241000938605 Crocodylia Species 0.000 description 1
- 101000702579 Crotalus durissus terrificus Snaclec crotocetin Proteins 0.000 description 1
- 102100026398 Cyclic AMP-responsive element-binding protein 3 Human genes 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
- 229930195713 D-glutamate Natural products 0.000 description 1
- KDXKERNSBIXSRK-RXMQYKEDSA-N D-lysine Chemical compound NCCCC[C@@H](N)C(O)=O KDXKERNSBIXSRK-RXMQYKEDSA-N 0.000 description 1
- HMFHBZSHGGEWLO-SOOFDHNKSA-N D-ribofuranose Chemical compound OC[C@H]1OC(O)[C@H](O)[C@@H]1O HMFHBZSHGGEWLO-SOOFDHNKSA-N 0.000 description 1
- 102000053602 DNA Human genes 0.000 description 1
- 239000003155 DNA primer Substances 0.000 description 1
- 230000004568 DNA-binding Effects 0.000 description 1
- 102000016928 DNA-directed DNA polymerase Human genes 0.000 description 1
- 108010014303 DNA-directed DNA polymerase Proteins 0.000 description 1
- 102000016911 Deoxyribonucleases Human genes 0.000 description 1
- 108010053770 Deoxyribonucleases Proteins 0.000 description 1
- 108010074124 Escherichia coli Proteins Proteins 0.000 description 1
- 241001524679 Escherichia virus M13 Species 0.000 description 1
- 108060002716 Exonuclease Proteins 0.000 description 1
- 102000034286 G proteins Human genes 0.000 description 1
- 108091006027 G proteins Proteins 0.000 description 1
- 108010015514 Glutamate-tRNA ligase Proteins 0.000 description 1
- 108010010369 HIV Protease 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
- 241000282412 Homo Species 0.000 description 1
- 101100153048 Homo sapiens ACAA1 gene Proteins 0.000 description 1
- 101000963424 Homo sapiens Acetyl-CoA carboxylase 1 Proteins 0.000 description 1
- 101000856237 Homo sapiens Cancer/testis antigen 1 Proteins 0.000 description 1
- 101000855520 Homo sapiens Cyclic AMP-responsive element-binding protein 3 Proteins 0.000 description 1
- 101000871088 Homo sapiens G-protein coupled receptor 3 Proteins 0.000 description 1
- 101000582320 Homo sapiens Neurogenic differentiation factor 6 Proteins 0.000 description 1
- UFHFLCQGNIYNRP-UHFFFAOYSA-N Hydrogen Chemical compound [H][H] UFHFLCQGNIYNRP-UHFFFAOYSA-N 0.000 description 1
- 102000008394 Immunoglobulin Fragments Human genes 0.000 description 1
- 108010021625 Immunoglobulin Fragments Proteins 0.000 description 1
- 229910021578 Iron(III) chloride Inorganic materials 0.000 description 1
- 229930194542 Keto Natural products 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
- HNDVDQJCIGZPNO-YFKPBYRVSA-N L-histidine Chemical compound OC(=O)[C@@H](N)CC1=CN=CN1 HNDVDQJCIGZPNO-YFKPBYRVSA-N 0.000 description 1
- LRQKBLKVPFOOQJ-YFKPBYRVSA-N L-norleucine Chemical compound CCCC[C@H]([NH3+])C([O-])=O LRQKBLKVPFOOQJ-YFKPBYRVSA-N 0.000 description 1
- GUBGYTABKSRVRQ-QKKXKWKRSA-N Lactose Natural products OC[C@H]1O[C@@H](O[C@H]2[C@H](O)[C@@H](O)C(O)O[C@@H]2CO)[C@H](O)[C@@H](O)[C@H]1O GUBGYTABKSRVRQ-QKKXKWKRSA-N 0.000 description 1
- 241000254158 Lampyridae Species 0.000 description 1
- 108010071170 Leucine-tRNA ligase Proteins 0.000 description 1
- 102100023342 Leucine-tRNA ligase, mitochondrial Human genes 0.000 description 1
- 108060001084 Luciferase Proteins 0.000 description 1
- NPPQSCRMBWNHMW-UHFFFAOYSA-N Meprobamate Chemical compound NC(=O)OCC(C)(CCC)COC(N)=O NPPQSCRMBWNHMW-UHFFFAOYSA-N 0.000 description 1
- 108010003060 Methionine-tRNA ligase Proteins 0.000 description 1
- 102000004587 Methionine-tRNA ligase Human genes 0.000 description 1
- 241000191938 Micrococcus luteus Species 0.000 description 1
- 241000243190 Microsporidia Species 0.000 description 1
- 102000016943 Muramidase Human genes 0.000 description 1
- 108010014251 Muramidase Proteins 0.000 description 1
- 108010062010 N-Acetylmuramoyl-L-alanine Amidase Proteins 0.000 description 1
- 102100030589 Neurogenic differentiation factor 6 Human genes 0.000 description 1
- 108010079246 OMPA outer membrane proteins Proteins 0.000 description 1
- PEMUHKUIQHFMTH-UHFFFAOYSA-N P-Bromo-DL-phenylalanine Chemical compound OC(=O)C(N)CC1=CC=C(Br)C=C1 PEMUHKUIQHFMTH-UHFFFAOYSA-N 0.000 description 1
- 238000012408 PCR amplification Methods 0.000 description 1
- 101100366562 Panax ginseng SS12 gene Proteins 0.000 description 1
- 108020002230 Pancreatic Ribonuclease Proteins 0.000 description 1
- 102000005891 Pancreatic ribonuclease Human genes 0.000 description 1
- 239000002202 Polyethylene glycol Substances 0.000 description 1
- 102000017033 Porins Human genes 0.000 description 1
- 108010013381 Porins Proteins 0.000 description 1
- ONIBWKKTOPOVIA-UHFFFAOYSA-N Proline Natural products OC(=O)C1CCCN1 ONIBWKKTOPOVIA-UHFFFAOYSA-N 0.000 description 1
- 102100026126 Proline-tRNA ligase Human genes 0.000 description 1
- 102220477048 Protein C-ets-1_F130S_mutation Human genes 0.000 description 1
- 229940096437 Protein S Drugs 0.000 description 1
- 230000004570 RNA-binding Effects 0.000 description 1
- 108020004511 Recombinant DNA Proteins 0.000 description 1
- 108010083644 Ribonucleases Proteins 0.000 description 1
- 102000006382 Ribonucleases Human genes 0.000 description 1
- PYMYPHUHKUWMLA-LMVFSUKVSA-N Ribose Natural products OC[C@@H](O)[C@@H](O)[C@@H](O)C=O PYMYPHUHKUWMLA-LMVFSUKVSA-N 0.000 description 1
- 241000791876 Selene Species 0.000 description 1
- RJFAYQIBOAGBLC-BYPYZUCNSA-N Selenium-L-methionine Chemical compound C[Se]CC[C@H](N)C(O)=O RJFAYQIBOAGBLC-BYPYZUCNSA-N 0.000 description 1
- RJFAYQIBOAGBLC-UHFFFAOYSA-N Selenomethionine Natural products C[Se]CCC(N)C(O)=O RJFAYQIBOAGBLC-UHFFFAOYSA-N 0.000 description 1
- 238000012300 Sequence Analysis Methods 0.000 description 1
- 108010051611 Signal Recognition Particle Proteins 0.000 description 1
- 102000013598 Signal recognition particle Human genes 0.000 description 1
- 108020004682 Single-Stranded DNA Proteins 0.000 description 1
- FAPWRFPIFSIZLT-UHFFFAOYSA-M Sodium chloride Chemical compound [Na+].[Cl-] FAPWRFPIFSIZLT-UHFFFAOYSA-M 0.000 description 1
- 108010090804 Streptavidin Proteins 0.000 description 1
- 108090000787 Subtilisin Proteins 0.000 description 1
- 102220607206 Succinate dehydrogenase [ubiquinone] cytochrome b small subunit, mitochondrial_E93K_mutation Human genes 0.000 description 1
- AYFVYJQAPQTCCC-UHFFFAOYSA-N Threonine Natural products CC(O)C(N)C(O)=O AYFVYJQAPQTCCC-UHFFFAOYSA-N 0.000 description 1
- 239000004473 Threonine Substances 0.000 description 1
- 102100034298 Tyrosine-tRNA ligase, cytoplasmic Human genes 0.000 description 1
- 241000700605 Viruses Species 0.000 description 1
- 108010031318 Vitronectin Proteins 0.000 description 1
- 238000002835 absorbance Methods 0.000 description 1
- 230000004308 accommodation Effects 0.000 description 1
- 108020002494 acetyltransferase Proteins 0.000 description 1
- 102000005421 acetyltransferase Human genes 0.000 description 1
- 230000003213 activating effect Effects 0.000 description 1
- 125000002252 acyl group Chemical group 0.000 description 1
- 239000000654 additive Substances 0.000 description 1
- 230000000996 additive effect Effects 0.000 description 1
- 229960000643 adenine Drugs 0.000 description 1
- UDMBCSSLTHHNCD-KQYNXXCUSA-N adenosine 5'-monophosphate Chemical compound C1=NC=2C(N)=NC=NC=2N1[C@@H]1O[C@H](COP(O)(O)=O)[C@@H](O)[C@H]1O UDMBCSSLTHHNCD-KQYNXXCUSA-N 0.000 description 1
- GFFGJBXGBJISGV-UHFFFAOYSA-N adenyl group Chemical group N1=CN=C2N=CNC2=C1N GFFGJBXGBJISGV-UHFFFAOYSA-N 0.000 description 1
- 230000002411 adverse Effects 0.000 description 1
- 150000001294 alanine derivatives Chemical class 0.000 description 1
- 150000001299 aldehydes Chemical class 0.000 description 1
- 125000002009 alkene group Chemical group 0.000 description 1
- 125000003342 alkenyl group Chemical group 0.000 description 1
- 150000001345 alkine derivatives Chemical class 0.000 description 1
- 125000000217 alkyl group Chemical group 0.000 description 1
- 125000000304 alkynyl group Chemical group 0.000 description 1
- HMFHBZSHGGEWLO-UHFFFAOYSA-N alpha-D-Furanose-Ribose Natural products OCC1OC(O)C(O)C1O HMFHBZSHGGEWLO-UHFFFAOYSA-N 0.000 description 1
- 150000001370 alpha-amino acid derivatives Chemical class 0.000 description 1
- 150000001408 amides Chemical group 0.000 description 1
- 150000001412 amines Chemical class 0.000 description 1
- 125000003277 amino group Chemical group 0.000 description 1
- 229940067621 aminobutyrate Drugs 0.000 description 1
- 230000003698 anagen phase Effects 0.000 description 1
- 210000004102 animal cell Anatomy 0.000 description 1
- 108700003859 araC Genes Proteins 0.000 description 1
- 101150044616 araC gene Proteins 0.000 description 1
- 125000004429 atom Chemical group 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
- 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
- 150000001615 biotins Chemical class 0.000 description 1
- 230000000903 blocking effect Effects 0.000 description 1
- 238000006664 bond formation reaction Methods 0.000 description 1
- ZADPBFCGQRWHPN-UHFFFAOYSA-N boronic acid Chemical compound OBO ZADPBFCGQRWHPN-UHFFFAOYSA-N 0.000 description 1
- 229940098773 bovine serum albumin Drugs 0.000 description 1
- 150000005693 branched-chain amino acids Chemical class 0.000 description 1
- 239000000872 buffer Substances 0.000 description 1
- 150000001720 carbohydrates Chemical class 0.000 description 1
- 235000014633 carbohydrates Nutrition 0.000 description 1
- 238000012219 cassette mutagenesis Methods 0.000 description 1
- 230000001413 cellular effect Effects 0.000 description 1
- 230000006364 cellular survival Effects 0.000 description 1
- 125000003636 chemical group Chemical group 0.000 description 1
- 210000000349 chromosome Anatomy 0.000 description 1
- 239000013599 cloning vector Substances 0.000 description 1
- 230000001447 compensatory effect Effects 0.000 description 1
- 238000012875 competitive assay Methods 0.000 description 1
- 239000000470 constituent Substances 0.000 description 1
- 238000011109 contamination Methods 0.000 description 1
- 230000001276 controlling effect Effects 0.000 description 1
- 230000002596 correlated effect Effects 0.000 description 1
- 230000008878 coupling Effects 0.000 description 1
- 238000010168 coupling process Methods 0.000 description 1
- 238000005859 coupling reaction Methods 0.000 description 1
- 238000004132 cross linking Methods 0.000 description 1
- 239000003431 cross linking reagent Substances 0.000 description 1
- 230000037029 cross reaction Effects 0.000 description 1
- 125000004093 cyano group Chemical group *C#N 0.000 description 1
- 125000004122 cyclic group Chemical group 0.000 description 1
- XUJNEKJLAYXESH-UHFFFAOYSA-N cysteine Natural products SCC(N)C(O)=O XUJNEKJLAYXESH-UHFFFAOYSA-N 0.000 description 1
- 235000018417 cysteine Nutrition 0.000 description 1
- 230000007423 decrease Effects 0.000 description 1
- 238000009795 derivation Methods 0.000 description 1
- 238000001212 derivatisation Methods 0.000 description 1
- 239000003599 detergent Substances 0.000 description 1
- 230000029087 digestion Effects 0.000 description 1
- 230000012361 double-strand break repair Effects 0.000 description 1
- 239000003814 drug Substances 0.000 description 1
- 229940079593 drug Drugs 0.000 description 1
- 238000009510 drug design Methods 0.000 description 1
- 238000002330 electrospray ionisation mass spectrometry Methods 0.000 description 1
- 230000007613 environmental effect Effects 0.000 description 1
- 230000007515 enzymatic degradation Effects 0.000 description 1
- 230000007247 enzymatic mechanism Effects 0.000 description 1
- 230000009144 enzymatic modification Effects 0.000 description 1
- 150000002148 esters Chemical class 0.000 description 1
- ZMMJGEGLRURXTF-UHFFFAOYSA-N ethidium bromide Chemical compound [Br-].C12=CC(N)=CC=C2C2=CC=C(N)C=C2[N+](CC)=C1C1=CC=CC=C1 ZMMJGEGLRURXTF-UHFFFAOYSA-N 0.000 description 1
- 229960005542 ethidium bromide Drugs 0.000 description 1
- 230000007717 exclusion Effects 0.000 description 1
- 102000013165 exonuclease Human genes 0.000 description 1
- 238000010195 expression analysis Methods 0.000 description 1
- 239000013613 expression plasmid Substances 0.000 description 1
- 230000004438 eyesight Effects 0.000 description 1
- 238000000684 flow cytometry Methods 0.000 description 1
- 238000002866 fluorescence resonance energy transfer Methods 0.000 description 1
- ZHNUHDYFZUAESO-UHFFFAOYSA-N formamide Substances NC=O ZHNUHDYFZUAESO-UHFFFAOYSA-N 0.000 description 1
- 238000006062 fragmentation reaction Methods 0.000 description 1
- 230000004927 fusion Effects 0.000 description 1
- 239000000499 gel Substances 0.000 description 1
- 229960002743 glutamine Drugs 0.000 description 1
- 102000005396 glutamine synthetase Human genes 0.000 description 1
- 108020002326 glutamine synthetase Proteins 0.000 description 1
- 230000013595 glycosylation Effects 0.000 description 1
- 238000006206 glycosylation reaction Methods 0.000 description 1
- 125000001475 halogen functional group Chemical group 0.000 description 1
- 229960002897 heparin Drugs 0.000 description 1
- 229920000669 heparin Polymers 0.000 description 1
- 125000000623 heterocyclic group Chemical group 0.000 description 1
- HNDVDQJCIGZPNO-UHFFFAOYSA-N histidine Natural products OC(=O)C(N)CC1=CN=CN1 HNDVDQJCIGZPNO-UHFFFAOYSA-N 0.000 description 1
- 150000002411 histidines Chemical class 0.000 description 1
- 229930195733 hydrocarbon Natural products 0.000 description 1
- 150000002430 hydrocarbons Chemical class 0.000 description 1
- 230000003301 hydrolyzing effect Effects 0.000 description 1
- 238000005286 illumination Methods 0.000 description 1
- 150000002466 imines Chemical class 0.000 description 1
- 238000001597 immobilized metal affinity chromatography Methods 0.000 description 1
- 230000003053 immunization Effects 0.000 description 1
- 238000002649 immunization Methods 0.000 description 1
- 238000010324 immunological assay Methods 0.000 description 1
- 238000012750 in vivo screening Methods 0.000 description 1
- 230000005764 inhibitory process Effects 0.000 description 1
- 230000000977 initiatory effect Effects 0.000 description 1
- 230000010354 integration Effects 0.000 description 1
- 230000003834 intracellular effect Effects 0.000 description 1
- RBTARNINKXHZNM-UHFFFAOYSA-K iron trichloride Chemical compound Cl[Fe](Cl)Cl RBTARNINKXHZNM-UHFFFAOYSA-K 0.000 description 1
- 125000000468 ketone group Chemical group 0.000 description 1
- 238000002372 labelling Methods 0.000 description 1
- 238000011005 laboratory method Methods 0.000 description 1
- 239000008101 lactose Substances 0.000 description 1
- 231100000518 lethal Toxicity 0.000 description 1
- 230000001665 lethal effect Effects 0.000 description 1
- 239000003446 ligand Substances 0.000 description 1
- 229960000274 lysozyme Drugs 0.000 description 1
- 239000004325 lysozyme Substances 0.000 description 1
- 235000010335 lysozyme Nutrition 0.000 description 1
- 239000000463 material Substances 0.000 description 1
- 230000001404 mediated effect Effects 0.000 description 1
- 238000002844 melting Methods 0.000 description 1
- 230000008018 melting Effects 0.000 description 1
- 230000037353 metabolic pathway Effects 0.000 description 1
- 150000002741 methionine derivatives Chemical class 0.000 description 1
- 125000001360 methionine group Chemical group N[C@@H](CCSC)C(=O)* 0.000 description 1
- 230000002906 microbiologic effect Effects 0.000 description 1
- 230000033607 mismatch repair Effects 0.000 description 1
- 238000001823 molecular biology technique Methods 0.000 description 1
- 231100000219 mutagenic Toxicity 0.000 description 1
- 230000003505 mutagenic effect Effects 0.000 description 1
- 210000002569 neuron Anatomy 0.000 description 1
- 239000012038 nucleophile Substances 0.000 description 1
- 239000002777 nucleoside Substances 0.000 description 1
- 150000003833 nucleoside derivatives Chemical class 0.000 description 1
- 210000000056 organ Anatomy 0.000 description 1
- 239000003960 organic solvent Substances 0.000 description 1
- 230000003647 oxidation Effects 0.000 description 1
- 238000007254 oxidation reaction Methods 0.000 description 1
- 230000001590 oxidative effect Effects 0.000 description 1
- 229910052760 oxygen Inorganic materials 0.000 description 1
- 238000004806 packaging method and process Methods 0.000 description 1
- 238000012856 packing Methods 0.000 description 1
- 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 1
- 230000035515 penetration Effects 0.000 description 1
- 238000010647 peptide synthesis reaction Methods 0.000 description 1
- 150000002994 phenylalanines Chemical class 0.000 description 1
- XHTJLMYQJHCUPE-UHFFFAOYSA-N phosphanylphosphonic acid Chemical compound OP(O)(P)=O XHTJLMYQJHCUPE-UHFFFAOYSA-N 0.000 description 1
- 239000008363 phosphate buffer Substances 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
- 125000002743 phosphorus functional group Chemical group 0.000 description 1
- 230000026731 phosphorylation Effects 0.000 description 1
- 238000006366 phosphorylation reaction Methods 0.000 description 1
- BZQFBWGGLXLEPQ-REOHCLBHSA-N phosphoserine Chemical compound OC(=O)[C@@H](N)COP(O)(O)=O BZQFBWGGLXLEPQ-REOHCLBHSA-N 0.000 description 1
- 238000007747 plating Methods 0.000 description 1
- 229920002401 polyacrylamide Polymers 0.000 description 1
- 229920002647 polyamide Polymers 0.000 description 1
- 229920001223 polyethylene glycol Polymers 0.000 description 1
- 229920000642 polymer Polymers 0.000 description 1
- 239000013641 positive control Substances 0.000 description 1
- 230000004481 post-translational protein modification Effects 0.000 description 1
- 239000000843 powder Substances 0.000 description 1
- 238000002360 preparation method Methods 0.000 description 1
- 108010080502 preprolactin Proteins 0.000 description 1
- 239000013615 primer Substances 0.000 description 1
- 238000012545 processing Methods 0.000 description 1
- 210000001236 prokaryotic cell Anatomy 0.000 description 1
- 230000012846 protein folding Effects 0.000 description 1
- 230000009145 protein modification Effects 0.000 description 1
- 210000001938 protoplast Anatomy 0.000 description 1
- 238000011002 quantification Methods 0.000 description 1
- 230000002285 radioactive effect Effects 0.000 description 1
- 102000016914 ras Proteins Human genes 0.000 description 1
- 239000011541 reaction mixture Substances 0.000 description 1
- 210000003370 receptor cell Anatomy 0.000 description 1
- 102000005962 receptors Human genes 0.000 description 1
- 230000000306 recurrent effect Effects 0.000 description 1
- 238000000611 regression analysis Methods 0.000 description 1
- 238000011160 research Methods 0.000 description 1
- 238000012552 review Methods 0.000 description 1
- 108010066533 ribonuclease S Proteins 0.000 description 1
- 210000003705 ribosome Anatomy 0.000 description 1
- 210000004358 rod cell outer segment Anatomy 0.000 description 1
- 102220046326 rs587782837 Human genes 0.000 description 1
- QSHGUCSTWRSQAF-FJSLEGQWSA-N s-peptide Chemical group C([C@@H](C(=O)N[C@@H](CC(O)=O)C(=O)N[C@@H]([C@@H](C)CC)C(=O)N[C@@H](CC(N)=O)C(=O)N[C@@H](CC=1C=CC(OS(O)(=O)=O)=CC=1)C(=O)N[C@@H](CC=1C=CC(O)=CC=1)C(=O)N[C@@H]([C@@H](C)O)C(=O)N[C@@H](CO)C(=O)N[C@@H](CCC(O)=O)C(=O)N1[C@@H](CCC1)C(=O)N[C@@H](CO)C(=O)N[C@@H](CCC(N)=O)C(=O)N[C@@H](CCCCN)C(O)=O)NC(=O)[C@@H](NC(=O)[C@H]1N(CCC1)C(=O)[C@H](CO)NC(=O)[C@H](CO)NC(=O)[C@@H](NC(=O)[C@H](CCC(N)=O)NC(=O)[C@H](CC=1C=CC(O)=CC=1)NC(=O)[C@H](CC(O)=O)NC(=O)[C@@H](N)CCSC)C(C)C)[C@@H](C)CC)C1=CC=C(OS(O)(=O)=O)C=C1 QSHGUCSTWRSQAF-FJSLEGQWSA-N 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
- 238000003345 scintillation counting Methods 0.000 description 1
- 229960002718 selenomethionine Drugs 0.000 description 1
- 238000002864 sequence alignment Methods 0.000 description 1
- 150000003354 serine derivatives Chemical class 0.000 description 1
- 239000013605 shuttle vector Substances 0.000 description 1
- 235000020183 skimmed milk Nutrition 0.000 description 1
- 239000011780 sodium chloride Substances 0.000 description 1
- 239000002904 solvent Substances 0.000 description 1
- 230000000087 stabilizing effect Effects 0.000 description 1
- 238000007619 statistical method Methods 0.000 description 1
- 230000004936 stimulating effect Effects 0.000 description 1
- 125000003107 substituted aryl group Chemical group 0.000 description 1
- 150000008163 sugars Chemical class 0.000 description 1
- 125000000446 sulfanediyl group Chemical group *S* 0.000 description 1
- 125000000472 sulfonyl group Chemical group *S(*)(=O)=O 0.000 description 1
- 229910052717 sulfur Inorganic materials 0.000 description 1
- 230000008093 supporting effect Effects 0.000 description 1
- 238000010189 synthetic method Methods 0.000 description 1
- 125000003396 thiol group Chemical group [H]S* 0.000 description 1
- 150000003573 thiols Chemical class 0.000 description 1
- DZLNHFMRPBPULJ-UHFFFAOYSA-N thioproline Chemical compound OC(=O)C1CSCN1 DZLNHFMRPBPULJ-UHFFFAOYSA-N 0.000 description 1
- 229950001139 timonacic Drugs 0.000 description 1
- 230000005026 transcription initiation Effects 0.000 description 1
- 230000005030 transcription termination Effects 0.000 description 1
- 238000010361 transduction Methods 0.000 description 1
- 230000026683 transduction Effects 0.000 description 1
- 238000011426 transformation method Methods 0.000 description 1
- 230000009261 transgenic effect Effects 0.000 description 1
- 230000007704 transition Effects 0.000 description 1
- 230000014621 translational initiation Effects 0.000 description 1
- 238000011282 treatment Methods 0.000 description 1
- YLJLTSVBCXYTQK-VKHMYHEASA-N trifluoro-L-methionine Chemical compound OC(=O)[C@@H](N)CCSC(F)(F)F YLJLTSVBCXYTQK-VKHMYHEASA-N 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
- 238000002211 ultraviolet spectrum Methods 0.000 description 1
- 229930195735 unsaturated hydrocarbon Natural products 0.000 description 1
- 229940035893 uracil Drugs 0.000 description 1
- 125000002987 valine group Chemical group [H]N([H])C([H])(C(*)=O)C([H])(C([H])([H])[H])C([H])([H])[H] 0.000 description 1
- 230000035899 viability Effects 0.000 description 1
- 230000000007 visual effect Effects 0.000 description 1
- 238000002424 x-ray crystallography Methods 0.000 description 1
- 210000005253 yeast cell Anatomy 0.000 description 1
Classifications
-
- 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
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P43/00—Drugs for specific purposes, not provided for in groups A61P1/00-A61P41/00
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P7/00—Drugs for disorders of the blood or the extracellular fluid
-
- 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
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K14/00—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof
- C07K14/435—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from animals; from humans
- C07K14/475—Growth factors; Growth regulators
- C07K14/505—Erythropoietin [EPO]
-
- C—CHEMISTRY; METALLURGY
- C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
- C12N—MICROORGANISMS OR ENZYMES; COMPOSITIONS THEREOF; PROPAGATING, PRESERVING, OR MAINTAINING MICROORGANISMS; MUTATION OR GENETIC ENGINEERING; CULTURE MEDIA
- C12N15/00—Mutation or genetic engineering; DNA or RNA concerning genetic engineering, vectors, e.g. plasmids, or their isolation, preparation or purification; Use of hosts therefor
- C12N15/09—Recombinant DNA-technology
- C12N15/63—Introduction of foreign genetic material using vectors; Vectors; Use of hosts therefor; Regulation of expression
- C12N15/67—General methods for enhancing the expression
-
- C—CHEMISTRY; METALLURGY
- C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
- C12N—MICROORGANISMS OR ENZYMES; COMPOSITIONS THEREOF; PROPAGATING, PRESERVING, OR MAINTAINING MICROORGANISMS; MUTATION OR GENETIC ENGINEERING; CULTURE MEDIA
- C12N9/00—Enzymes; Proenzymes; Compositions thereof; Processes for preparing, activating, inhibiting, separating or purifying enzymes
- C12N9/93—Ligases (6)
-
- C—CHEMISTRY; METALLURGY
- C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
- C12P—FERMENTATION OR ENZYME-USING PROCESSES TO SYNTHESISE A DESIRED CHEMICAL COMPOUND OR COMPOSITION OR TO SEPARATE OPTICAL ISOMERS FROM A RACEMIC MIXTURE
- C12P13/00—Preparation of nitrogen-containing organic compounds
-
- 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
- C12P13/00—Preparation of nitrogen-containing organic compounds
- C12P13/005—Amino acids other than alpha- or beta amino acids, e.g. gamma amino acids
-
- 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
- C12P13/00—Preparation of nitrogen-containing organic compounds
- C12P13/04—Alpha- or beta- amino acids
-
- 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
- C12P13/00—Preparation of nitrogen-containing organic compounds
- C12P13/04—Alpha- or beta- amino acids
- C12P13/22—Tryptophan; Tyrosine; Phenylalanine; 3,4-Dihydroxyphenylalanine
-
- 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
- C12P19/00—Preparation of compounds containing saccharide radicals
- C12P19/26—Preparation of nitrogen-containing carbohydrates
-
- 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
- Chemical & Material Sciences (AREA)
- Organic Chemistry (AREA)
- Life Sciences & Earth Sciences (AREA)
- Health & Medical Sciences (AREA)
- Engineering & Computer Science (AREA)
- Zoology (AREA)
- Wood Science & Technology (AREA)
- Genetics & Genomics (AREA)
- Bioinformatics & Cheminformatics (AREA)
- General Health & Medical Sciences (AREA)
- Biochemistry (AREA)
- General Engineering & Computer Science (AREA)
- Biotechnology (AREA)
- Microbiology (AREA)
- General Chemical & Material Sciences (AREA)
- Chemical Kinetics & Catalysis (AREA)
- Molecular Biology (AREA)
- Medicinal Chemistry (AREA)
- Proteomics, Peptides & Aminoacids (AREA)
- Biomedical Technology (AREA)
- Biophysics (AREA)
- Gastroenterology & Hepatology (AREA)
- Physics & Mathematics (AREA)
- Toxicology (AREA)
- Plant Pathology (AREA)
- Nuclear Medicine, Radiotherapy & Molecular Imaging (AREA)
- Veterinary Medicine (AREA)
- Public Health (AREA)
- Animal Behavior & Ethology (AREA)
- Pharmacology & Pharmacy (AREA)
- Diabetes (AREA)
- Hematology (AREA)
- Micro-Organisms Or Cultivation Processes Thereof (AREA)
- Preparation Of Compounds By Using Micro-Organisms (AREA)
- Enzymes And Modification Thereof (AREA)
- Medicines That Contain Protein Lipid Enzymes And Other Medicines (AREA)
- Measuring Or Testing Involving Enzymes Or Micro-Organisms (AREA)
- Organic Low-Molecular-Weight Compounds And Preparation Thereof (AREA)
- Peptides Or Proteins (AREA)
Applications Claiming Priority (4)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| US28503001P | 2001-04-19 | 2001-04-19 | |
| US285030P | 2001-04-19 | ||
| US35551402P | 2002-02-06 | 2002-02-06 | |
| US355514P | 2002-02-06 |
Publications (1)
| Publication Number | Publication Date |
|---|---|
| ES2464532T3 true ES2464532T3 (es) | 2014-06-03 |
Family
ID=26962950
Family Applications (1)
| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| ES09006800.8T Expired - Lifetime ES2464532T3 (es) | 2001-04-19 | 2002-04-19 | Métodos y composiciones para la producción de pares ortogonales de ARNt-aminoacil-ARNt sintetasa |
Country Status (11)
| Country | Link |
|---|---|
| US (19) | US7083970B2 (https=) |
| EP (5) | EP2322631B1 (https=) |
| JP (7) | JP2005502322A (https=) |
| AU (2) | AU2002256292C1 (https=) |
| CA (2) | CA2444098C (https=) |
| DK (4) | DK1456360T3 (https=) |
| ES (1) | ES2464532T3 (https=) |
| HK (1) | HK1203558A1 (https=) |
| IL (7) | IL158419A0 (https=) |
| MX (2) | MXPA03009566A (https=) |
| WO (2) | WO2002085923A2 (https=) |
Families Citing this family (440)
| 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 |
| WO2003033521A1 (en) | 2001-10-16 | 2003-04-24 | Massachusetts Institute Of Technology | Inppressor trna system in mammalian cells for the introduction of unnatural amino acids in polypeptides. |
| US20030148391A1 (en) * | 2002-01-24 | 2003-08-07 | Salafsky Joshua S. | Method using a nonlinear optical technique for detection of interactions involving a conformational change |
| US7112435B1 (en) | 2002-08-07 | 2006-09-26 | Ambit Biosciences Corporation | Uncoupling of DNA insert propagation and expression of protein for phage display |
| US20040038273A1 (en) * | 2002-06-17 | 2004-02-26 | Whitehead Institute For Biomedical Research | Bifunctional tRNA for in vitro selection |
| US20040161795A1 (en) * | 2002-07-25 | 2004-08-19 | Mds Proteomics Inc. | Systems and methods for analysis of protein post-translational modification |
| US7833741B2 (en) * | 2002-08-07 | 2010-11-16 | Ambit Biosciences Corporation | Uncoupling of DNA insert propagation and expression of protein for phage display |
| US7897381B2 (en) * | 2002-08-07 | 2011-03-01 | Ambit Biosciences Corporation | Uncoupling of DNA insert propagation and expression of protein for phage display |
| US7563600B2 (en) | 2002-09-12 | 2009-07-21 | Combimatrix Corporation | Microarray synthesis and assembly of gene-length polynucleotides |
| 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. |
| WO2004058946A2 (en) | 2002-12-22 | 2004-07-15 | The Scripps Research Institute | Protein arrays |
| BRPI0406647A (pt) | 2003-01-06 | 2005-12-06 | Angiochem Inc | Método para transportar um composto através da barreira sanguìnea do cérebro |
| US7772188B2 (en) | 2003-01-28 | 2010-08-10 | Ironwood Pharmaceuticals, Inc. | Methods and compositions for the treatment of gastrointestinal disorders |
| JP2006180701A (ja) * | 2003-02-10 | 2006-07-13 | Institute Of Physical & Chemical Research | チロシルtRNA合成酵素の変異体及びその作製方法 |
| WO2004094593A2 (en) | 2003-04-17 | 2004-11-04 | The Scripps Research Institute | Expanding the eukaryotic genetic code |
| AU2013201487B2 (en) * | 2003-04-17 | 2014-09-18 | The Scripps Research Institute | Expanding the eukaryotic genetic code |
| WO2004110964A2 (en) * | 2003-06-16 | 2004-12-23 | Nuevolution A/S | Encoded molecules by translation (emt) |
| 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 |
| DE602004023956D1 (de) * | 2003-08-18 | 2009-12-17 | Univ California | Polypeptid-display-bibliotheken und verfahren zur herstellung und verwendung davon |
| 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 |
| WO2005072092A2 (en) * | 2003-12-12 | 2005-08-11 | Conjugon, Inc. | Systems for tightly regulated gene expression |
| 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 |
| CA2558749A1 (en) * | 2004-02-27 | 2005-09-29 | President And Fellows Of Harvard College | Polynucleotide synthesis |
| FR2868081A1 (fr) * | 2004-03-23 | 2005-09-30 | Libragen Sa | Methode d'identification de famille de voie metabolique par selection positive |
| US20050260711A1 (en) * | 2004-03-30 | 2005-11-24 | Deepshikha Datta | Modulating pH-sensitive binding using non-natural amino acids |
| EP1757686A4 (en) * | 2004-04-09 | 2008-03-12 | Chugai Pharmaceutical Co Ltd | Cell death inducer |
| US20050287639A1 (en) | 2004-05-17 | 2005-12-29 | California Institute Of Technology | Methods of incorporating amino acid analogs into proteins |
| 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 |
| US20060008844A1 (en) * | 2004-06-17 | 2006-01-12 | Avidia Research Institute | c-Met kinase binding proteins |
| KR101699142B1 (ko) | 2004-06-18 | 2017-01-23 | 암브룩스, 인코포레이티드 | 신규 항원-결합 폴리펩티드 및 이의 용도 |
| CN1968712B (zh) * | 2004-06-18 | 2012-05-16 | Ambrx公司 | 新颖抗原结合多肽和其用途 |
| WO2006014729A2 (en) | 2004-07-20 | 2006-02-09 | Genentech, Inc. | Inhibitors of angiopoietin-like 4 protein, combinations, and their use |
| JP2008507280A (ja) * | 2004-07-21 | 2008-03-13 | アンブレツクス・インコーポレイテツド | 非天然コードアミノ酸を用いた生合成ポリペプチド |
| CA2580840A1 (en) * | 2004-09-21 | 2006-03-30 | The Scripps Research Institute | In vivo incorporation of alkynyl amino acids into proteins in eubacteria |
| US20080171317A1 (en) * | 2004-09-22 | 2008-07-17 | The Scripps Research Institute | Site-Specific Labeling of Proteins for Nmr Studies |
| US20070122817A1 (en) * | 2005-02-28 | 2007-05-31 | George Church | Methods for assembly of high fidelity synthetic polynucleotides |
| EP1812598A1 (en) * | 2004-10-18 | 2007-08-01 | Codon Devices, Inc. | Methods for assembly of high fidelity synthetic polynucleotides |
| 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 |
| AU2011204773B2 (en) * | 2004-10-27 | 2012-02-02 | The Scripps Research Institute | Orthogonal translation components for the in vivo incorporation of unnatural amino acids |
| US20080176790A1 (en) | 2004-10-29 | 2008-07-24 | Defrees Shawn | Remodeling and Glycopegylation of Fibroblast Growth Factor (Fgf) |
| US20060134748A1 (en) * | 2004-11-20 | 2006-06-22 | Rajbhandary Uttam | Orthogonal suppressor tRNAs and aminoacyl-tRNA synthetases and uses thereof |
| JPWO2006054807A1 (ja) * | 2004-11-22 | 2008-06-05 | 国立大学法人岐阜大学 | ミトコンドリア蛋白質を用いる、非天然アミノ酸を蛋白質に部位特異的に導入する方法及びtRNAの効率的調製方法 |
| CN102732588B (zh) * | 2004-12-22 | 2015-01-07 | Ambrx公司 | 氨酰基-tRNA合成酶的组合物及其用途 |
| US7816320B2 (en) | 2004-12-22 | 2010-10-19 | Ambrx, Inc. | Formulations of human growth hormone comprising a non-naturally encoded amino acid at position 35 |
| AU2013205042B2 (en) * | 2004-12-22 | 2016-05-12 | Ambrx, Inc. | Compositions containing, methods involving, and uses of non-natural amino acids and polypeptides |
| EP1828224B1 (en) * | 2004-12-22 | 2016-04-06 | Ambrx, Inc. | Compositions containing, methods involving, and uses of non-natural amino acids and polypeptides |
| JP2008525473A (ja) | 2004-12-22 | 2008-07-17 | アンブレツクス・インコーポレイテツド | 修飾されたヒト成長ホルモン |
| GB2438760A (en) * | 2004-12-22 | 2007-12-05 | Ambrx Inc | Methods for expression and purification of recombinant human growth hormone |
| PA8660701A1 (es) | 2005-02-04 | 2006-09-22 | Pfizer Prod Inc | Agonistas de pyy y sus usos |
| US7723069B2 (en) * | 2005-04-05 | 2010-05-25 | Yale University | Site specific incorporation of phosphoserine into polypeptides using phosphoseryl-tRNA synthetase |
| US20070154992A1 (en) | 2005-04-08 | 2007-07-05 | Neose Technologies, Inc. | Compositions and methods for the preparation of protease resistant human growth hormone glycosylation mutants |
| US8293517B2 (en) * | 2005-05-11 | 2012-10-23 | Wayne State University | Methods and compositions for the identification of antibiotics that are not susceptible to antibiotic resistance in Pseudomonas aeruginosa |
| WO2006133089A2 (en) * | 2005-06-03 | 2006-12-14 | Ambrx, Inc. | Improved human interferon molecules and their uses |
| JP2008541766A (ja) * | 2005-06-03 | 2008-11-27 | アンブレツクス・インコーポレイテツド | タンパク質中への天然にコードされないアミノ酸の取り込み |
| KR101367544B1 (ko) * | 2005-06-10 | 2014-02-26 | 추가이 세이야쿠 가부시키가이샤 | 메글루민을 함유하는 단백질 제제의 안정화제, 및 그의이용 |
| US20070004041A1 (en) * | 2005-06-30 | 2007-01-04 | Codon Devices, Inc. | Heirarchical assembly methods for genome engineering |
| EP2361979A3 (en) * | 2005-07-15 | 2011-11-09 | Medical Research Council | Compositions and methods relating to orthogonal ribosome mRNA pairs |
| JP5436856B2 (ja) | 2005-07-15 | 2014-03-05 | アンジオケム インコーポレーティッド | 薬学的複合体における担体としてのアプロチニンポリペプチドの使用 |
| US8008453B2 (en) | 2005-08-12 | 2011-08-30 | Amgen Inc. | Modified Fc molecules |
| MX2008002149A (es) | 2005-08-18 | 2008-04-22 | Ambrx Inc | Composiciones de arnt y sus usos. |
| EP2535346B1 (en) | 2005-08-31 | 2017-08-02 | The Regents of The University of California | Cellular libraries of peptide sequences (CLiPS) and methods of using the same |
| US8367588B2 (en) * | 2005-10-12 | 2013-02-05 | The Scripps Research Institute | Selective posttranslational modification of phage-displayed polypeptides |
| EP1951890A4 (en) | 2005-11-16 | 2009-06-24 | Ambrx Inc | PROCESSES AND COMPOSITIONS WITH NON-NATURAL AMINO ACIDS |
| DK1968635T3 (en) | 2005-12-14 | 2014-12-15 | Ambrx Inc | Compositions and Methods of, and uses of non-natural amino acids and polypeptides |
| US8921086B2 (en) | 2005-12-22 | 2014-12-30 | Pacific Biosciences Of California, Inc. | Polymerases for nucleotide analogue incorporation |
| AU2006332809A1 (en) * | 2005-12-30 | 2007-07-12 | Ambrx, Inc. | Compositions containing, methods involving, and uses of non-natural amino acids and polypeptides |
| AU2007215566A1 (en) * | 2006-01-19 | 2007-08-23 | Ambrx, Inc. | Non-natural amino acid polypeptides having modulated immunogenicity |
| US20070178554A1 (en) * | 2006-02-01 | 2007-08-02 | Nima Shiva | Orthogonal Aminoacyl Synthetase-tRNA Pairs for Incorporating Unnatural Amino Acids Into Proteins |
| US20090081669A1 (en) * | 2006-02-01 | 2009-03-26 | Encode Bio, Inc. | Fluorescent Assays Using Orthogonal tRNA - Aminoacyl Synthetase Pairs |
| WO2007092475A2 (en) * | 2006-02-06 | 2007-08-16 | Franklin And Marshall College | Site-specific incorporation of fluorinated amino acids into proteins |
| AU2007224019A1 (en) * | 2006-03-03 | 2007-09-13 | California Institute Of Technology | Site-specific incorporation of amino acids into molecules |
| 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 |
| EP2444499A3 (en) | 2006-05-02 | 2012-05-09 | Allozyne, Inc. | Amino acid substituted molecules |
| US20080096819A1 (en) * | 2006-05-02 | 2008-04-24 | Allozyne, Inc. | Amino acid substituted molecules |
| US7807411B2 (en) * | 2006-05-23 | 2010-10-05 | The Scripps Research Institute | Genetically encoded fluorescent coumarin amino acids |
| CL2007001614A1 (es) * | 2006-06-09 | 2008-08-08 | Novartis Ag | Polipeptido que comprende una proteina del precursor del factor de crecimiento tipo insulina, igf-1 humana, en la cual la escision del peptido e mediante una proteasa se reduce a traves de la modificacion de la proteina del precursor; y su uso para t |
| WO2008001947A1 (en) * | 2006-06-28 | 2008-01-03 | Riken | MUTANT SepRS, AND METHOD FOR SITE-SPECIFIC INTRODUCTION OF PHOSPHOSERINE INTO PROTEIN BY USING THE SAME |
| DK2035554T3 (da) * | 2006-06-29 | 2013-06-17 | Univ Leland Stanford Junior | Celle-fri syntese af proteiner indeholdende ikke-naturlige aminosyrer |
| CN101517075A (zh) * | 2006-07-13 | 2009-08-26 | 中外制药株式会社 | 细胞死亡诱导剂 |
| CN106008699A (zh) * | 2006-09-08 | 2016-10-12 | Ambrx公司 | 经修饰的人类血浆多肽或Fc骨架和其用途 |
| MX2009002460A (es) * | 2006-09-08 | 2009-03-20 | Ambrx Inc | Arnt supresor hibrido para celulas de vertebrados. |
| EP2064333B1 (en) | 2006-09-08 | 2014-02-26 | Ambrx, Inc. | Suppressor trna transcription in vertebrate cells |
| EP2064316B1 (en) * | 2006-09-08 | 2012-01-25 | Ambrx, Inc. | Site specific incorporation of non-natural amino acids by vertebrate cells |
| AU2013202770B2 (en) * | 2006-09-08 | 2015-08-20 | Ambrx, Inc. | Modified human plasma polypeptide or Fc scaffolds and their uses |
| AU2012203737B2 (en) * | 2006-09-08 | 2014-06-19 | Ambrx, Inc. | Modified human plasma polypeptide or Fc scaffolds and their uses |
| EP2052083B1 (en) | 2006-09-21 | 2014-01-08 | The Scripps Research Institute | Genetically programmed expression of selectively sulfated proteins in eubacteria |
| JP2010506591A (ja) | 2006-10-18 | 2010-03-04 | ザ スクリップス リサーチ インスティテュート | 哺乳動物細胞中の蛋白質への非天然アミノ酸の遺伝的組込み |
| CN101678079B (zh) | 2006-11-28 | 2013-12-25 | 韩诺生物制约株式会社 | 修饰的促红细胞生成素多肽及其治疗用途 |
| EP1936340A1 (en) * | 2006-12-21 | 2008-06-25 | Koninklijke Philips Electronics N.V. | Sub wavelength aperture |
| EP2112928A4 (en) * | 2007-02-22 | 2014-01-08 | Univ Utah Res Found | SYNTHESIS OF NOVEL XYLOSIDES AND ITS POSSIBLE USES |
| CL2008000719A1 (es) * | 2007-03-12 | 2008-09-05 | Univ Tokushima Chugai Seiyaku | Agente terapeutico para cancer resistente a agentes quimioterapeuticos que comprende un anticuerpo que reconoce hla de clase i como ingrediente activo; composicion farmaceutica que comprende dicho anticuerpo; y metodo para tratar cancer resistente a |
| CA2682147C (en) | 2007-03-30 | 2017-08-08 | Ambrx, Inc. | Modified fgf-21 polypeptides and their uses |
| WO2008127900A1 (en) * | 2007-04-13 | 2008-10-23 | The Salk Institute For Biological Studies | Methods of genetically encoding unnatural amino acids in eukaryotic cells using orthogonal trna/synthetase pairs |
| MX2009011870A (es) * | 2007-05-02 | 2009-11-12 | Ambrx Inc | Polipeptidos de interferon beta modificados y usos de los mismos. |
| US9365634B2 (en) | 2007-05-29 | 2016-06-14 | Angiochem Inc. | Aprotinin-like polypeptides for delivering agents conjugated thereto to tissues |
| US8969514B2 (en) | 2007-06-04 | 2015-03-03 | Synergy Pharmaceuticals, Inc. | Agonists of guanylate cyclase useful for the treatment of hypercholesterolemia, atherosclerosis, coronary heart disease, gallstone, obesity and other cardiovascular diseases |
| EP2527360B1 (en) | 2007-06-04 | 2015-10-28 | Synergy Pharmaceuticals Inc. | Agonists of guanylate cyclase useful for the treatment of gastrointestinal disorders, inflammation, cancer and other disorders |
| US8293685B2 (en) | 2007-07-26 | 2012-10-23 | The Regents Of The University Of California | Methods for enhancing bacterial cell display of proteins and peptides |
| CA2707840A1 (en) * | 2007-08-20 | 2009-02-26 | Allozyne, Inc. | Amino acid substituted molecules |
| WO2009036460A2 (en) * | 2007-09-14 | 2009-03-19 | Ambrx, Inc. | Modified human apolipoprotein a-i polypeptides and their uses |
| EP2217700A4 (en) * | 2007-10-08 | 2011-02-16 | Synthetic Genomics Inc | SYSTEM AND METHOD FOR PRODUCING SYNTHETIC MICROORGANISMS CAPABLE OF TRANSLATING PROTEINS CONTAINING NON-STANDARD AMINO ACIDS |
| MX2010004464A (es) | 2007-10-25 | 2010-06-07 | Scripps Research Inst | Incorporacion genetica de 3-aminotirosina a reductasas. |
| WO2009059056A2 (en) * | 2007-11-02 | 2009-05-07 | The Scripps Research Institute | A genetically encoded boronate amino acid |
| KR20100091170A (ko) | 2007-11-02 | 2010-08-18 | 노파르티스 아게 | 저밀도-지단백질 수용체-관련 단백질 6 (lrp6)을 조정하기 위한 분자 및 방법 |
| US9150849B2 (en) | 2007-11-02 | 2015-10-06 | The Scripps Research Institute | Directed evolution using proteins comprising unnatural amino acids |
| WO2009064416A2 (en) * | 2007-11-15 | 2009-05-22 | The Scripps Research Institute | Genetic incorporation of an alpha-hydroxy acid into proteins to generate ester backbone linkages at defined sites |
| MX2010005317A (es) | 2007-11-20 | 2010-06-02 | Ambrx Inc | Polipeptidos de insulina modificados y sus usos. |
| AU2008335778B2 (en) * | 2007-12-11 | 2014-04-10 | The Scripps Research Institute | In vivo unnatural amino acid expression in the methylotrophic yeast Pichia pastoris |
| CA2710683A1 (en) | 2008-01-03 | 2009-07-16 | Verenium Corporation | Transferases and oxidoreductases, nucleic acids encoding them and methods for making and using them |
| AU2009210570B2 (en) * | 2008-01-30 | 2014-11-20 | Indiana University Research And Technology Corporation | Ester-based insulin prodrugs |
| NZ586947A (en) | 2008-02-08 | 2012-11-30 | Ambrx Inc | Modified leptin polypeptides and their uses |
| CN101970005A (zh) * | 2008-02-08 | 2011-02-09 | 斯克利普斯研究院 | 用遗传编码的非天然氨基酸打破免疫耐受 |
| US20110015345A1 (en) * | 2008-03-19 | 2011-01-20 | Ambrx, Inc. | Modified FGF-23 Polypeptides and Their Uses |
| US8940506B2 (en) * | 2008-03-21 | 2015-01-27 | The Regents Of The University Of California | High-sensitive fluorescent energy transfer assay using fluoresent amino acids and fluorescent proteins |
| WO2009120922A2 (en) | 2008-03-27 | 2009-10-01 | Zymogenetics, Inc. | Compositions and methods for inhibiting pdgfrbeta and vegf-a |
| WO2009145820A2 (en) | 2008-03-31 | 2009-12-03 | Pacific Biosciences Of California, Inc. | Generation of modified polymerases for improved accuracy in single molecule sequencing |
| PL2274331T3 (pl) | 2008-05-02 | 2014-04-30 | Novartis Ag | Ulepszone cząsteczki wiążące oparte na fibronektynie i ich zastosowanie |
| EP2810951B1 (en) | 2008-06-04 | 2017-03-15 | Synergy Pharmaceuticals Inc. | Agonists of guanylate cyclase useful for the treatment of gastrointestinal disorders, inflammation, cancer and other disorders |
| KR101784231B1 (ko) | 2008-06-20 | 2017-11-08 | 노파르티스 아게 | 응집이 감소된 면역글로불린 |
| US8404471B2 (en) | 2008-06-26 | 2013-03-26 | Atyr Pharma, Inc. | Compositions and methods comprising glycyl-tRNA synthetases having non-canonical biological activities |
| WO2010006454A2 (en) | 2008-06-30 | 2010-01-21 | Esbatech, An Alcon Biomedical Research Unit Llc | Functionalized polypeptides |
| MX2011000009A (es) | 2008-07-10 | 2011-08-15 | Esbatech Alcon Biomed Res Unit | Metodos y composiciones para la administracion mejorada de macromoleculas. |
| EP3241839B1 (en) | 2008-07-16 | 2019-09-04 | Bausch Health Ireland Limited | Agonists of guanylate cyclase useful for the treatment of gastrointestinal, inflammation, cancer and other disorders |
| PT2318029T (pt) | 2008-07-23 | 2018-01-10 | Ambrx Inc | Polipéptidos de g-csf bovino modificados e suas utilizações |
| US9182406B2 (en) | 2008-08-04 | 2015-11-10 | Biodesy, Inc. | Nonlinear optical detection of molecules comprising an unnatural amino acid possessing a hyperpolarizability |
| WO2010022171A1 (en) * | 2008-08-19 | 2010-02-25 | Ferring International Center S.A. | Peptidic pth receptor agonists |
| PE20110480A1 (es) | 2008-09-26 | 2011-07-01 | Ambrx Inc | Microorganismos y vacunas dependientes de replicacion de aminoacidos no naturales |
| MX2011003272A (es) | 2008-09-26 | 2011-04-28 | Ambrx Inc | Polipeptidos de eritropoyetina animal modificados y sus usos. |
| BRPI0920209A2 (pt) | 2008-10-15 | 2015-12-22 | Angiochem Inc | conjugados de agonistas de glp-1 e usos dos mesmos |
| BRPI0919932A8 (pt) | 2008-10-24 | 2018-02-06 | Novartis Ag | Pirrolina-carbóxi-lisina gerada biossinteticamente, bem como processo para preparar método para derivatizar uma proteína |
| CA2745524C (en) | 2008-12-05 | 2020-06-09 | Angiochem Inc. | Conjugates of neurotensin or neurotensin analogs and uses thereof |
| US20090197339A1 (en) * | 2008-12-10 | 2009-08-06 | The Scripps Research Institute | In vivo unnatural amino acid expression in the methylotrophic yeast pichia pastoris |
| CN102307905B (zh) | 2008-12-10 | 2015-11-25 | 斯克利普斯研究院 | 利用化学反应性非天然氨基酸产生载体-肽偶联物 |
| WO2010069074A1 (en) | 2008-12-17 | 2010-06-24 | Universite Du Quebec A Montreal | Membrane type-1 matrix metalloprotein inhibitors and uses thereof |
| CN102300580A (zh) * | 2008-12-19 | 2011-12-28 | 印第安纳大学研究及科技有限公司 | 二肽连接的药剂 |
| WO2010080609A1 (en) | 2008-12-19 | 2010-07-15 | Indiana University Research And Technology Corporation | Amide-based insulin prodrugs |
| WO2010080606A1 (en) | 2008-12-19 | 2010-07-15 | Indiana University Research And Technology Corporation | Insulin analogs |
| CN102325539A (zh) | 2008-12-19 | 2012-01-18 | 印第安纳大学研究及科技有限公司 | 基于酰胺的胰高血糖素超家族肽前药 |
| US9238878B2 (en) | 2009-02-17 | 2016-01-19 | Redwood Bioscience, Inc. | Aldehyde-tagged protein-based drug carriers and methods of use |
| WO2010099477A2 (en) | 2009-02-27 | 2010-09-02 | Atyr Pharma, Inc. | Polypeptide structural motifs associated with cell signaling activity |
| CN102449143B (zh) | 2009-03-31 | 2017-11-14 | Atyr医药公司 | 包含具有非常规生物活性的天冬氨酰‑tRNA合成酶的组合物和方法 |
| WO2010121379A1 (en) | 2009-04-20 | 2010-10-28 | Angiochem Inc | Treatment of ovarian cancer using an anticancer agent conjugated to an angiopep-2 analog |
| WO2010132341A2 (en) | 2009-05-11 | 2010-11-18 | Pfenex, Inc. | Production of recombinant proteins utilizing non-antibiotic selection methods and the incorporation of non-natural amino acids therein |
| CA2763935A1 (en) | 2009-06-04 | 2010-12-09 | Novartis Ag | Methods for identification of sites for igg conjugation |
| AU2010268726A1 (en) | 2009-07-02 | 2012-01-19 | Angiochem Inc. | Multimeric peptide conjugates and uses thereof |
| US20110054019A1 (en) * | 2009-09-01 | 2011-03-03 | Pedro Anastacio Serrano-Ojeda | Cancer Starvation Therapy |
| US10292956B2 (en) | 2009-09-01 | 2019-05-21 | Serbig Pharmaceutics Corp. | Cancer starvation therapy |
| EP2311947A1 (en) * | 2009-10-14 | 2011-04-20 | Ludwig-Maximilians-Universität München | Protein synthesis via click chemistry |
| WO2011056494A1 (en) | 2009-10-26 | 2011-05-12 | Genentech, Inc. | Activin receptor-like kinase-1 antagonist and vegfr3 antagonist combinations |
| WO2011056497A1 (en) | 2009-10-26 | 2011-05-12 | Genentech, Inc. | Activin receptor type iib compositions and methods of use |
| WO2011056502A1 (en) | 2009-10-26 | 2011-05-12 | Genentech, Inc. | Bone morphogenetic protein receptor type ii compositions and methods of use |
| WO2011051327A2 (en) | 2009-10-30 | 2011-05-05 | Novartis Ag | Small antibody-like single chain proteins |
| WO2011051466A1 (en) | 2009-11-02 | 2011-05-05 | Novartis Ag | Anti-idiotypic fibronectin-based binding molecules and uses thereof |
| EP2496944A2 (en) | 2009-11-05 | 2012-09-12 | Novartis AG | Biomarkers predictive of progression of fibrosis |
| WO2011078987A1 (en) | 2009-12-21 | 2011-06-30 | Trustees Of Dartmouth College | Recombinant prokaryotes and use thereof for production of o-glycosylated proteins |
| JP2013515081A (ja) | 2009-12-21 | 2013-05-02 | アンブルックス,インコーポレイテッド | 修飾されているブタのソマトトロピンポリペプチドおよびそれらの使用 |
| NZ600361A (en) | 2009-12-21 | 2014-06-27 | Ambrx Inc | Modified bovine somatotropin polypeptides and their uses |
| WO2011094445A1 (en) | 2010-01-27 | 2011-08-04 | Massachusetts Institute Of Technology | Engineered polypeptide agents for targeted broad spectrum influenza neutralization |
| WO2011092233A1 (en) | 2010-01-29 | 2011-08-04 | Novartis Ag | Yeast mating to produce high-affinity combinations of fibronectin-based binders |
| JP2013519869A (ja) | 2010-02-10 | 2013-05-30 | ノバルティス アーゲー | 筋肉成長のための方法および化合物 |
| US8674064B2 (en) * | 2010-03-03 | 2014-03-18 | Onkologix Ltd | Immunogenic compositions against human progastrin peptides |
| US8464858B2 (en) | 2010-03-12 | 2013-06-18 | Cabin Creek Inc. | Conveyor belt scraper and system for the same |
| WO2011119771A2 (en) * | 2010-03-23 | 2011-09-29 | The Salk Institute For Biological Studies | Methods and compositions for detecting protein modifications |
| US8980253B2 (en) | 2010-04-26 | 2015-03-17 | Atyr Pharma, Inc. | Innovative discovery of therapeutic, diagnostic, and antibody compositions related to protein fragments of cysteinyl-tRNA synthetase |
| EP2563382B1 (en) | 2010-04-27 | 2017-06-07 | aTyr Pharma, Inc. | Innovative discovery of therapeutic, diagnostic, and antibody compositions related to protein fragments of threonyl trna synthetases |
| CA2797362C (en) | 2010-04-27 | 2020-12-08 | Atyr Pharma, Inc. | Innovative discovery of therapeutic, diagnostic, and antibody compositions related to protein fragments of isoleucyl trna synthetases |
| WO2011139853A2 (en) | 2010-04-28 | 2011-11-10 | Atyr Pharma, Inc. | Innovative discovery of therapeutic, diagnostic, and antibody compositions related to protein fragments of alanyl trna synthetases |
| CA2797374C (en) | 2010-04-29 | 2021-02-16 | Pangu Biopharma Limited | Innovative discovery of therapeutic, diagnostic, and antibody compositions related to protein fragments of asparaginyl trna synthetases |
| CA2797393C (en) | 2010-04-29 | 2020-03-10 | Pangu Biopharma Limited | Innovative discovery of therapeutic, diagnostic, and antibody compositions related to protein fragments of valyl trna synthetases |
| US8961961B2 (en) | 2010-05-03 | 2015-02-24 | a Tyr Pharma, Inc. | Innovative discovery of therapeutic, diagnostic, and antibody compositions related protein fragments of arginyl-tRNA synthetases |
| CN103096912A (zh) | 2010-05-03 | 2013-05-08 | Atyr医药公司 | 与苯丙氨酰-α-tRNA合成酶的蛋白片段相关的治疗、诊断和抗体组合物的创新发现 |
| CA2797799C (en) | 2010-05-03 | 2020-12-08 | Atyr Pharma, Inc. | Innovative discovery of therapeutic, diagnostic, and antibody compositions related to protein fragments of seryl-trna synthetases |
| CN103140233B (zh) | 2010-05-03 | 2017-04-05 | Atyr 医药公司 | 与甲硫氨酰‑tRNA合成酶的蛋白片段相关的治疗、诊断和抗体组合物的发现 |
| US9062301B2 (en) | 2010-05-04 | 2015-06-23 | Atyr Pharma, Inc. | Innovative discovery of therapeutic, diagnostic, and antibody compositions related to protein fragments of glutamyl-prolyl-tRNA synthetases |
| JP6008844B2 (ja) | 2010-05-04 | 2016-10-19 | エータイアー ファーマ, インコーポレイテッド | p38MULTI−tRNA合成酵素複合体のタンパク質フラグメントに関連した治療用、診断用および抗体組成物の革新的発見 |
| EP2568996B1 (en) | 2010-05-14 | 2017-10-04 | aTyr Pharma, Inc. | Therapeutic, diagnostic, and antibody compositions related to protein fragments of phenylalanyl-beta-trna synthetases |
| CN103096914B (zh) | 2010-05-17 | 2015-08-12 | Atyr医药公司 | 与亮氨酰-tRNA合成酶的蛋白片段相关的治疗、诊断和抗体组合物的创新发现 |
| CA2800375C (en) * | 2010-05-27 | 2021-03-09 | Atyr Pharma, Inc. | Innovative discovery of therapeutic, diagnostic, and antibody compositions related to protein fragments of glutaminyl-trna synthetases |
| EP2575857B1 (en) | 2010-06-01 | 2018-01-24 | aTyr Pharma, Inc. | Innovative discovery of therapeutic, diagnostic, and antibody compositions related to protein fragments of lysyl-trna synthetases |
| US9340790B2 (en) | 2010-06-16 | 2016-05-17 | Riken | Method for constructing recombinant bacterium for producing non-native protein, and utilization of same |
| EP2582719B1 (en) | 2010-06-16 | 2016-08-10 | Indiana University Research and Technology Corporation | Single chain insulin agonists exhibiting high activity at the insulin receptor |
| RU2580317C2 (ru) | 2010-06-24 | 2016-04-10 | Индиана Юниверсити Рисерч Энд Текнолоджи Корпорейшн | Пептидные пролекарства, принадлежащие к суперсемейству амид-содержащих глюкагонов |
| JP5912112B2 (ja) | 2010-06-24 | 2016-04-27 | インディアナ ユニバーシティー リサーチ アンド テクノロジー コーポレーションIndiana University Research And Technology Corporation | アミド系インスリンプロドラッグ |
| US20130202576A1 (en) * | 2010-07-12 | 2013-08-08 | Pangu Biopharma Limited | Innovative discovery of therapeutic, diagnostic, and antibody compositions related to protein fragments of histidyl-trna synthetases |
| EP2593125B1 (en) | 2010-07-12 | 2017-11-01 | aTyr Pharma, Inc. | Innovative discovery of therapeutic, diagnostic, and antibody compositions related to protein fragments of glycyl-trna synthetases |
| WO2012009289A2 (en) * | 2010-07-12 | 2012-01-19 | Atyr Pharma, Inc. | Innovative discovery of therapeutic, diagnostic, and antibody compositions related to protein fragments of aspartyl-trna synthetases |
| US8999321B2 (en) | 2010-07-12 | 2015-04-07 | Atyr Pharma, Inc. | Innovative discovery of therapeutic, diagnostic, and antibody compositions related to protein fragments of glycyl-tRNA synthetases |
| MA34521B1 (fr) | 2010-08-17 | 2013-09-02 | Ambrx Inc | Polypeptides de relaxine modifiés et leurs utilisations |
| US9567386B2 (en) | 2010-08-17 | 2017-02-14 | Ambrx, Inc. | Therapeutic uses of modified relaxin polypeptides |
| AU2011293294B2 (en) | 2010-08-25 | 2016-03-24 | Pangu Biopharma Limited | Innovative discovery of therapeutic, diagnostic, and antibody compositions related to protein fragments of Tyrosyl-tRNA synthetases |
| JP6173911B2 (ja) | 2010-09-10 | 2017-08-09 | メディミューン リミテド | 抗体誘導体 |
| US9616097B2 (en) | 2010-09-15 | 2017-04-11 | Synergy Pharmaceuticals, Inc. | Formulations of guanylate cyclase C agonists and methods of use |
| TWI480288B (zh) | 2010-09-23 | 2015-04-11 | Lilly Co Eli | 牛顆粒細胞群落刺激因子及其變體之調配物 |
| CA2812795C (en) | 2010-10-06 | 2021-08-31 | Atyr Pharma, Inc. | Innovative discovery of therapeutic, diagnostic, and antibody compositions related protein fragments of tryptophanyl trna synthetases |
| US9090928B2 (en) | 2010-10-07 | 2015-07-28 | Yale University | Site-specific incorporation of phosphoserine into proteins in Escherichia coli |
| US9023791B2 (en) | 2010-11-19 | 2015-05-05 | Novartis Ag | Fibroblast growth factor 21 mutations |
| AU2012205301B2 (en) | 2011-01-14 | 2017-01-05 | Redwood Bioscience, Inc. | Aldehyde-tagged immunoglobulin polypeptides and method of use thereof |
| DK2670767T3 (en) | 2011-02-03 | 2018-03-26 | European Molecular Biology Laboratory | Non-naturally occurring amino acids comprising a cyclooctynyl or transcyclooctynyl analog group and uses thereof |
| US9428789B2 (en) | 2011-03-21 | 2016-08-30 | Biodesy, Inc. | Classification of kinase inhibitors using nonlinear optical techniques |
| US20140249090A1 (en) * | 2011-04-01 | 2014-09-04 | Max-Planck-Gesellschaft zur Förderung der Wissenschaft e.V. | Peptides and pharmaceutical compositions for use in the treatment by nasal administration of patients suffering from anxiety and sleep disorders |
| EP2694095B1 (en) | 2011-04-05 | 2018-03-07 | Longevity Biotech, Inc. | Compositions comprising glucagon analogs and methods of making and using the same |
| KR20140037105A (ko) | 2011-05-27 | 2014-03-26 | 암브룩스, 인코포레이티드 | 비-천연 아미노산 연결된 돌라스타틴 유도체를 함유하는 조성물, 이를 수반하는 방법, 및 용도 |
| KR102356286B1 (ko) | 2011-05-27 | 2022-02-08 | 암브룩스, 인코포레이티드 | 비-천연 아미노산 연결된 돌라스타틴 유도체를 함유하는 조성물, 이를 수반하는 방법, 및 용도 |
| WO2013009868A1 (en) | 2011-07-11 | 2013-01-17 | Yale University | Compositions and methods for making selenocysteine containing polypeptides |
| US11788111B2 (en) | 2011-07-11 | 2023-10-17 | Yale University | Compositions and methods for making selenocysteine containing polypeptides |
| US10876142B2 (en) | 2011-07-11 | 2020-12-29 | Yale University | Compositions and methods for making selenocysteine containing polypeptides |
| US10240158B2 (en) | 2011-07-11 | 2019-03-26 | Yale University | Compositions and methods for making selenocysteine containing polypeptides |
| CN102888387B (zh) * | 2011-07-21 | 2015-03-18 | 中国科学院生物物理研究所 | 3-氯代酪氨酸翻译系统及其应用 |
| JP6261500B2 (ja) | 2011-07-22 | 2018-01-17 | プレジデント アンド フェローズ オブ ハーバード カレッジ | ヌクレアーゼ切断特異性の評価および改善 |
| CN102925427B (zh) * | 2011-08-08 | 2014-01-22 | 中国科学院生物物理研究所 | 丙烯酰赖氨酸翻译系统及其应用 |
| US9714419B2 (en) | 2011-08-09 | 2017-07-25 | Atyr Pharma, Inc. | PEGylated tyrosyl-tRNA synthetase polypeptides |
| TW201315742A (zh) | 2011-09-26 | 2013-04-16 | Novartis Ag | 治療代謝病症之雙功能蛋白質 |
| WO2013068874A1 (en) | 2011-11-11 | 2013-05-16 | Pfizer Inc. | Antibody-drug conjugates |
| US9822353B2 (en) | 2011-12-06 | 2017-11-21 | Atyr Pharma, Inc. | PEGylated aspartyl-tRNA synthetase polypeptides |
| US9816084B2 (en) | 2011-12-06 | 2017-11-14 | Atyr Pharma, Inc. | Aspartyl-tRNA synthetases |
| US9573987B2 (en) | 2011-12-20 | 2017-02-21 | Indiana University Research And Technology Corporation | CTP-based insulin analogs for treatment of diabetes |
| TWI787670B (zh) | 2011-12-28 | 2022-12-21 | 日商中外製藥股份有限公司 | 具有環狀部之胜肽化合物及其醫藥組成物 |
| WO2013115926A2 (en) | 2011-12-29 | 2013-08-08 | Atyr Pharma, Inc. | Aspartyl-trna synthetase-fc conjugates |
| US9395358B2 (en) | 2012-02-05 | 2016-07-19 | Biodesy, Inc. | Methods for detecting allosteric modulators of protein |
| MX356107B (es) | 2012-02-16 | 2018-05-15 | Atyr Pharma Inc | Histidil-arnt sintetasas para tratar enfermedades autoinmunes e inflamatorias. |
| HK1207970A1 (en) | 2012-05-10 | 2016-02-19 | Massachusetts Institute Of Technology | Agents for influenza neutralization |
| US10800856B2 (en) | 2012-06-07 | 2020-10-13 | Ambrx, Inc. | Prostate-specific membrane antigen antibody drug conjugates |
| PL2859017T3 (pl) | 2012-06-08 | 2019-07-31 | Sutro Biopharma, Inc. | Przeciwciała zawierające swoiste dla miejsca, niewystępujące naturalnie reszty aminokwasowe, sposoby ich wytwarzania i sposoby ich zastosowania |
| SG11201408494UA (en) | 2012-06-19 | 2015-02-27 | Ambrx Inc | Anti-cd70 antibody drug conjugates |
| WO2014004639A1 (en) | 2012-06-26 | 2014-01-03 | Sutro Biopharma, Inc. | Modified fc proteins comprising site-specific non-natural amino acid residues, conjugates of the same, methods of their preparation and methods of their use |
| CN103571804B (zh) * | 2012-08-10 | 2015-08-12 | 中国科学院生物物理研究所 | 3-吡唑基酪氨酸翻译系统及其应用 |
| EP2887966B1 (en) | 2012-08-22 | 2018-07-18 | The Government of the United States of America as represented by The Secretary of the Department of Health and Human Services | Engineered anthrax lethal toxin for targeted delivery |
| WO2014035364A2 (en) * | 2012-08-27 | 2014-03-06 | Empire Technology Development Llc | Gelatin alkyd peptides and uses thereof |
| HRP20220455T1 (hr) | 2012-08-31 | 2022-05-27 | Sutro Biopharma, Inc. | Modificirane aminokiseline koje sadrže azid grupu |
| SG10201702387YA (en) | 2012-09-24 | 2017-04-27 | Medimmune Ltd | Cell lines |
| AU2013323669B2 (en) | 2012-09-26 | 2018-03-01 | Indiana University Research And Technology Corporation | Insulin analog dimers |
| CN102875733B (zh) * | 2012-10-25 | 2014-06-11 | 西安科技大学 | 具有仿细胞外层膜结构的纳米颗粒及其制备方法 |
| US20140120116A1 (en) | 2012-10-26 | 2014-05-01 | The Chinese University Of Hong Kong | Treatment of cancer using smad3 inhibitor |
| UY35144A (es) | 2012-11-20 | 2014-06-30 | Novartis Ag | Miméticos lineales sintéticos de apelina para el tratamiento de insuficiencia cardiaca |
| JP6499080B2 (ja) | 2012-12-18 | 2019-04-10 | ノバルティス アーゲー | 安定化されたインスリン様成長因子ポリペプチド |
| WO2014116730A2 (en) | 2013-01-23 | 2014-07-31 | The Board Of Trustees Of The Leland Stanford Junior University | Stabilized hepatitis b core polypeptide |
| US9545446B2 (en) | 2013-02-25 | 2017-01-17 | Synergy Pharmaceuticals, Inc. | Agonists of guanylate cyclase and their uses |
| US9255255B2 (en) | 2013-03-04 | 2016-02-09 | The Board Of Trustees Of The Leland Stanford Junior University | Synthesis of linear and branched polymers of polypeptides through direct conjugation |
| JO3564B1 (ar) | 2013-03-08 | 2020-07-05 | Novartis Ag | ببتيدات وتركيبات لعلاج ضرر المفاصل |
| WO2014158900A1 (en) | 2013-03-14 | 2014-10-02 | Indiana University Research And Technology Corporation | Insulin-incretin conjugates |
| CN105378075B (zh) | 2013-03-15 | 2022-04-05 | Atyr 医药公司 | 组氨酰-trna合成酶-fc缀合物 |
| WO2014145654A1 (en) | 2013-03-15 | 2014-09-18 | The Trustees Of The University Of Pennsylvania | Method for the site-specific covalent cross-linking of antibodies to surfaces |
| CA2905435A1 (en) | 2013-03-15 | 2014-09-25 | Synergy Pharmaceuticals Inc. | Compositions useful for the treatment of gastrointestinal disorders |
| CA2905438A1 (en) | 2013-03-15 | 2014-09-25 | Synergy Pharmaceuticals Inc. | Agonists of guanylate cyclase and their uses |
| US9789164B2 (en) | 2013-03-15 | 2017-10-17 | Longevity Biotech, Inc. | Peptides comprising non-natural amino acids and methods of making and using the same |
| WO2014146575A1 (en) | 2013-03-19 | 2014-09-25 | Beijing Shenogen Pharma Group Ltd. | Antibodies and methods for treating estrogen receptor-associated diseases |
| SI3004138T1 (sl) | 2013-06-05 | 2024-07-31 | Bausch Health Ireland Limited | Ultra čisti agonisti gvanilat ciklaze C, postopek za njihovo pripravo in uporabo |
| KR101568336B1 (ko) | 2013-07-02 | 2015-11-12 | 서강대학교산학협력단 | 목적 단백질의 돌연변이체를 생성하는 세포, 상기 세포의 제조 방법, 및 상기 세포를 이용한 목적 단백질의 돌연변이체의 제조 방법 |
| ES2865473T3 (es) | 2013-07-10 | 2021-10-15 | Sutro Biopharma Inc | Anticuerpos que comprenden múltiples residuos de aminoácidos no naturales sitio-específicos, métodos para su preparación y métodos de uso |
| US10005838B2 (en) | 2013-07-19 | 2018-06-26 | The Regents Of The University Of California | Milk fat globule epidermal growth factor 8 regulates fatty acid uptake |
| CN105705167A (zh) | 2013-07-25 | 2016-06-22 | 诺华股份有限公司 | 合成的apelin多肽的生物缀合物 |
| MX2016001020A (es) | 2013-07-25 | 2016-08-03 | Novartis Ag | Polipeptidos ciclicos para el tratamiento de insuficiencia cardiaca. |
| US20150044192A1 (en) | 2013-08-09 | 2015-02-12 | President And Fellows Of Harvard College | Methods for identifying a target site of a cas9 nuclease |
| KR102456567B1 (ko) | 2013-08-09 | 2022-10-19 | 알데릭스, 인코포레이티드 | 인산염 수송을 억제하기 위한 화합물 및 방법 |
| US9359599B2 (en) | 2013-08-22 | 2016-06-07 | President And Fellows Of Harvard College | Engineered transcription activator-like effector (TALE) domains and uses thereof |
| US10011649B2 (en) | 2013-08-26 | 2018-07-03 | Arizona Board Of Regents On Behalf Of Arizona State University | High affinity synbodies for influenza |
| US9526784B2 (en) | 2013-09-06 | 2016-12-27 | President And Fellows Of Harvard College | Delivery system for functional nucleases |
| US9340799B2 (en) | 2013-09-06 | 2016-05-17 | President And Fellows Of Harvard College | MRNA-sensing switchable gRNAs |
| US9388430B2 (en) | 2013-09-06 | 2016-07-12 | President And Fellows Of Harvard College | Cas9-recombinase fusion proteins and uses thereof |
| CN106061494A (zh) | 2013-10-10 | 2016-10-26 | 辛纳吉制药公司 | 可用于治疗阿片样物质诱导的功能障碍的鸟苷酸环化酶的激动剂 |
| EP3055298B1 (en) | 2013-10-11 | 2020-04-29 | Sutro Biopharma, Inc. | Modified amino acids comprising tetrazine functional groups, methods of preparation, and methods of their use |
| EP3057605A1 (en) | 2013-10-18 | 2016-08-24 | Novartis AG | Methods of treating diabetes and related disorders |
| US20150165054A1 (en) | 2013-12-12 | 2015-06-18 | President And Fellows Of Harvard College | Methods for correcting caspase-9 point mutations |
| CA2936615C (en) | 2014-01-14 | 2023-06-13 | European Molecular Biology Laboratory | Multiple cycloaddition reactions for labeling of molecules |
| WO2015120287A2 (en) | 2014-02-06 | 2015-08-13 | Yale University | Compositions and methods of use thereof for making polypeptides with many instances of nonstandard amino acids |
| CA2947605A1 (en) | 2014-05-13 | 2015-11-19 | Bioatla, Llc | Conditionally active biological proteins |
| US10588980B2 (en) | 2014-06-23 | 2020-03-17 | Novartis Ag | Fatty acids and their use in conjugation to biomolecules |
| EP3157942B1 (en) | 2014-06-23 | 2020-06-17 | Novartis AG | Site specific protein modifications |
| US10316322B2 (en) | 2014-07-02 | 2019-06-11 | Sutro Biopharma, Inc. | High growth capacity auxotrophic Escherichia coli and methods of use |
| ES3047792T3 (en) | 2014-07-14 | 2025-12-04 | Univ California | Crispr/cas transcriptional modulation |
| WO2016022363A2 (en) | 2014-07-30 | 2016-02-11 | President And Fellows Of Harvard College | Cas9 proteins including ligand-dependent inteins |
| WO2016036916A1 (en) | 2014-09-03 | 2016-03-10 | Bioatla, Llc | Discovering and producing conditionally active biologic proteins in the same eukaryotic cell production hosts |
| WO2016049174A1 (en) | 2014-09-24 | 2016-03-31 | Indiana University Research And Technology Corporation | Lipidated amide-based insulin prodrugs |
| ES2822994T3 (es) | 2014-09-24 | 2021-05-05 | Univ Indiana Res & Tech Corp | Conjugados de incretina-insulina |
| US11408007B2 (en) | 2014-09-26 | 2022-08-09 | Yale University | Compositions and methods for biocontainment of microorganisms |
| SMT202100388T1 (it) | 2014-10-24 | 2021-09-14 | Bristol Myers Squibb Co | Polipeptidi fgf-21 modificati e loro usi |
| WO2016090157A1 (en) | 2014-12-04 | 2016-06-09 | Celgene Corporation | Biomolecule conjugates |
| EP3237906B8 (en) | 2014-12-23 | 2020-10-28 | Bluelight Therapeutics, Inc. | Attachment of proteins to interfaces for use in nonlinear optical detection |
| SE538541C2 (en) * | 2015-01-19 | 2016-09-13 | Fogelstrand Per | Method for preparing a biological sample for use in an immunolabeling process |
| CN107209176B (zh) | 2015-01-21 | 2020-08-14 | 克罗姆尼贡公司 | 免疫标记复合物的形成方法及用途 |
| CR20170338A (es) | 2015-01-23 | 2017-09-12 | Novartis Ag | Conjugados de ácidos grasos y apelina sintética con mayor vida media |
| WO2016123578A1 (en) | 2015-01-30 | 2016-08-04 | The Regents Of The University Of California | Protein delivery in primary hematopoietic cells |
| DK3269809T3 (da) | 2015-03-13 | 2022-09-12 | Chugai Pharmaceutical Co Ltd | MODIFICERET AMINOACYL-tRNA-SYNTETASE OG ANVENDELSE DERAF |
| US10483262B2 (en) * | 2015-05-15 | 2019-11-19 | Taiwan Semiconductor Manufacturing Co., Ltd. | Dual nitride stressor for semiconductor device and method of manufacturing |
| JP6618534B2 (ja) * | 2015-06-09 | 2019-12-11 | 国立研究開発法人産業技術総合研究所 | アミノ酸修飾核酸とその利用 |
| DK3307326T3 (da) | 2015-06-15 | 2020-10-19 | Angiochem Inc | Fremgangsmåder til behandling af leptomeningeal karcinomatose |
| WO2017009750A1 (en) | 2015-07-10 | 2017-01-19 | The Hong Kong University Of Science And Technology | Methods and compositions for treating neurodegenerative and neuroinflammatory conditions |
| EP3359191A4 (en) | 2015-10-05 | 2019-05-29 | Merck Sharp & Dohme Corp. | ANTIBODY PEPTIDE CONJUGATES WITH AGONISTEACTIVITY ON GLUCAGON RECEPTORS AND GLUCAGON-LIKE PEPTIDE-1 |
| JP7109784B2 (ja) | 2015-10-23 | 2022-08-01 | プレジデント アンド フェローズ オブ ハーバード カレッジ | 遺伝子編集のための進化したCas9蛋白質 |
| CN108367053A (zh) | 2015-12-22 | 2018-08-03 | 诺华股份有限公司 | 使用生长分化因子15(gdf-15)治疗或改善代谢性疾病的方法 |
| KR102844773B1 (ko) | 2015-12-23 | 2025-08-13 | 암젠 인크 | 위 억제 펩티드 수용체 (gipr)에 대한 결합 단백질을 glp-1 효능제와 조합하여 사용하여 대사 장애를 치료하거나 개선시키는 방법 |
| CN106929482A (zh) * | 2015-12-31 | 2017-07-07 | 北京大学 | 定点突变的流感病毒、其活疫苗及其制备方法和应用 |
| WO2017123634A1 (en) | 2016-01-11 | 2017-07-20 | Synergy Pharmaceuticals, Inc. | Formulations and methods for treating ulcerative colitis |
| SG11201806419RA (en) | 2016-01-27 | 2018-08-30 | Sutro Biopharma Inc | Anti-cd74 antibody conjugates, compositions comprising anti-cd74 antibody conjugates and methods of using anti-cd74 antibody conjugates |
| AU2017257504A1 (en) | 2016-04-26 | 2018-10-25 | R.P. Scherer Technologies, Llc | Antibody conjugates and methods of making and using the same |
| WO2017196891A1 (en) | 2016-05-09 | 2017-11-16 | Biodesy, Inc. | Methods and devices for detection of peripheral membrane protein interactions using nonlinear optical techniques |
| EP3465204B1 (en) * | 2016-05-25 | 2023-08-02 | Kromnigon AB | Method for preparing a biological sample for use in an immunolabeling process |
| EP3471759A1 (en) | 2016-06-15 | 2019-04-24 | Novartis AG | Methods for treating disease using inhibitors of bone morphogenetic protein 6 (bmp6) |
| KR102547316B1 (ko) | 2016-08-03 | 2023-06-23 | 프레지던트 앤드 펠로우즈 오브 하바드 칼리지 | 아데노신 핵염기 편집제 및 그의 용도 |
| US11661590B2 (en) | 2016-08-09 | 2023-05-30 | President And Fellows Of Harvard College | Programmable CAS9-recombinase fusion proteins and uses thereof |
| US11542509B2 (en) | 2016-08-24 | 2023-01-03 | President And Fellows Of Harvard College | Incorporation of unnatural amino acids into proteins using base editing |
| EP3526320A1 (en) | 2016-10-14 | 2019-08-21 | President and Fellows of Harvard College | Aav delivery of nucleobase editors |
| EP3309260A1 (en) | 2016-10-14 | 2018-04-18 | European Molecular Biology Laboratory | Archaeal pyrrolysyl trna synthetases for orthogonal use |
| EP3538546B1 (en) | 2016-11-14 | 2025-01-08 | Novartis AG | Compositions, methods, and therapeutic uses related to fusogenic protein minion |
| CN109963579A (zh) | 2016-11-14 | 2019-07-02 | 诺华股份有限公司 | 用于治疗软骨损伤和关节炎的方法和组合物 |
| TWI788318B (zh) | 2016-12-19 | 2023-01-01 | 美商寬騰矽公司 | 用於定序反應之聚合酶 |
| WO2018119359A1 (en) | 2016-12-23 | 2018-06-28 | President And Fellows Of Harvard College | Editing of ccr5 receptor gene to protect against hiv infection |
| ES3024474T3 (en) | 2016-12-30 | 2025-06-04 | Vaxcyte Inc | Polypeptide-antigen conjugates with non-natural amino acids |
| US11951165B2 (en) | 2016-12-30 | 2024-04-09 | Vaxcyte, Inc. | Conjugated vaccine carrier proteins |
| BR112019014588A2 (pt) | 2017-01-17 | 2020-02-18 | Amgen Inc. | Método de tratamento ou amenização de distúrbios metabólicos usando agonistas do receptor de glp-1 conjugados a antagonistas para receptor do peptídeo inibidor gástrico (gipr) |
| US12391971B2 (en) | 2017-01-31 | 2025-08-19 | Chugai Seiyaku Kabushiki Kaisha | Method for synthesizing peptides in cell-free translation system |
| JP2020506948A (ja) | 2017-02-07 | 2020-03-05 | ザ リージェンツ オブ ザ ユニバーシティ オブ カリフォルニア | ハプロ不全のための遺伝子治療 |
| CN110637027B (zh) | 2017-02-08 | 2024-08-30 | 百时美施贵宝公司 | 包含药代动力学增强子的修饰的松弛素多肽及其用途 |
| EP3592853A1 (en) | 2017-03-09 | 2020-01-15 | President and Fellows of Harvard College | Suppression of pain by gene editing |
| JP2020510038A (ja) | 2017-03-09 | 2020-04-02 | プレジデント アンド フェローズ オブ ハーバード カレッジ | がんワクチン |
| JP2020510439A (ja) | 2017-03-10 | 2020-04-09 | プレジデント アンド フェローズ オブ ハーバード カレッジ | シトシンからグアニンへの塩基編集因子 |
| CA3057192A1 (en) | 2017-03-23 | 2018-09-27 | President And Fellows Of Harvard College | Nucleobase editors comprising nucleic acid programmable dna binding proteins |
| EP3381932A1 (en) | 2017-03-28 | 2018-10-03 | Technische Universität Berlin | Modified mussel proteins, uses thereof and related compounds |
| CN110536694A (zh) | 2017-04-20 | 2019-12-03 | Atyr 医药公司 | 用于治疗肺部炎症的组合物和方法 |
| WO2018209320A1 (en) | 2017-05-12 | 2018-11-15 | President And Fellows Of Harvard College | Aptazyme-embedded guide rnas for use with crispr-cas9 in genome editing and transcriptional activation |
| EP3630977B1 (en) | 2017-06-02 | 2024-02-21 | Ambrx, Inc. | Methods and compositions for promoting non-natural amino acid-containing protein production |
| WO2018225851A1 (ja) | 2017-06-09 | 2018-12-13 | 中外製薬株式会社 | N-置換アミノ酸を含むペプチドの合成方法 |
| CN110831969B (zh) | 2017-06-20 | 2024-06-21 | 安进公司 | 使用抑胃肽受体(gipr)结合蛋白与glp-1激动剂的组合治疗或改善代谢障碍的方法 |
| MX2019015544A (es) | 2017-06-21 | 2020-07-28 | Amgen Inc | Metodo para tratar o mejorar trastornos metabolicos con proteinas de fusion de agonistas del receptor de glp-1/proteinas de union antagonistas para el receptor peptidico inhibidor gastrico (gipr). |
| AU2018300069C1 (en) | 2017-07-11 | 2025-11-20 | Synthorx, Inc. | Incorporation of unnatural nucleotides and methods thereof |
| KR101956042B1 (ko) * | 2017-07-13 | 2019-03-08 | 서강대학교산학협력단 | 표적 단백질 내 l-디하이드록시페닐알라닌의 도입 방법 |
| US20200207859A1 (en) | 2017-07-26 | 2020-07-02 | Sutro Biopharma, Inc. | Methods of using anti-cd74 antibodies and antibody conjugates in treatment of t-cell lymphoma |
| WO2019023680A1 (en) | 2017-07-28 | 2019-01-31 | President And Fellows Of Harvard College | METHODS AND COMPOSITIONS FOR EVOLUTION OF BASIC EDITORS USING PHAGE-ASSISTED CONTINUOUS EVOLUTION (PACE) |
| WO2019028419A1 (en) | 2017-08-03 | 2019-02-07 | Synthorx, Inc. | CYTOKINE CONJUGATES FOR THE TREATMENT OF PROLIFERATIVE AND INFECTIOUS DISEASES |
| EP3676376B1 (en) | 2017-08-30 | 2025-01-15 | President and Fellows of Harvard College | High efficiency base editors comprising gam |
| TW201920249A (zh) | 2017-09-07 | 2019-06-01 | 美商信號生物製藥公司 | 具有結合位點之t細胞調節多聚體多肽及其使用方法 |
| JP7423513B2 (ja) | 2017-09-18 | 2024-01-29 | ストロ バイオファーマ インコーポレーテッド | 抗葉酸受容体α抗体コンジュゲート及びその使用 |
| KR20250107288A (ko) | 2017-10-16 | 2025-07-11 | 더 브로드 인스티튜트, 인코퍼레이티드 | 아데노신 염기 편집제의 용도 |
| WO2019118949A1 (en) | 2017-12-15 | 2019-06-20 | The Broad Institute, Inc. | Systems and methods for predicting repair outcomes in genetic engineering |
| EP3725796A4 (en) | 2017-12-15 | 2021-09-15 | Chugai Seiyaku Kabushiki Kaisha | METHOD FOR MANUFACTURING PEPTIDE AND METHOD FOR PROCESSING BASES |
| KR20210005172A (ko) | 2018-05-01 | 2021-01-13 | 암브룩스, 인코포레이티드 | 항체 발현을 최적화하는 방법 |
| EP3797160A1 (en) | 2018-05-23 | 2021-03-31 | The Broad Institute Inc. | Base editors and uses thereof |
| WO2019237119A1 (en) | 2018-06-08 | 2019-12-12 | The United States Of America As Represented By The Secretary Of The Department Of Health And Human Services | New compositions and detection methods for onchocerca volvulus infection |
| US12522807B2 (en) | 2018-07-09 | 2026-01-13 | The Broad Institute, Inc. | RNA programmable epigenetic RNA modifiers and uses thereof |
| CN112673109A (zh) * | 2018-09-07 | 2021-04-16 | 免疫医疗有限责任公司 | 细胞选择方法 |
| HRP20240016T1 (hr) | 2018-09-11 | 2024-03-29 | Ambrx, Inc. | Konjugati polipeptida interleukina-2 i njihove uporabe |
| JP2022500454A (ja) | 2018-09-17 | 2022-01-04 | ストロ バイオファーマ インコーポレーテッド | 抗葉酸受容体抗体コンジュゲートによる併用療法 |
| WO2020082057A1 (en) | 2018-10-19 | 2020-04-23 | Ambrx, Inc. | Interleukin-10 polypeptide conjugates, dimers thereof, and their uses |
| WO2020092453A1 (en) | 2018-10-29 | 2020-05-07 | The Broad Institute, Inc. | Nucleobase editors comprising geocas9 and uses thereof |
| US11325978B2 (en) | 2018-11-06 | 2022-05-10 | The United States Of America, As Represented By The Secretary Of The Department Of Health And Human Services | Compositions and methods for treating beta-globinopathies |
| EP3878836B1 (en) | 2018-11-07 | 2025-07-23 | Chugai Seiyaku Kabushiki Kaisha | O-substituted serine derivative production method |
| JP7568510B2 (ja) | 2018-11-30 | 2024-10-16 | 中外製薬株式会社 | ペプチド化合物、またはアミド化合物の脱保護法および固相反応における脱樹脂方法、並びにペプチド化合物の製造方法 |
| US12351837B2 (en) | 2019-01-23 | 2025-07-08 | The Broad Institute, Inc. | Supernegatively charged proteins and uses thereof |
| KR20260039812A (ko) | 2019-02-06 | 2026-03-20 | 신톡스, 인크. | Il-2 콘쥬게이트 및 이의 사용 방법 |
| JP7695885B2 (ja) | 2019-02-12 | 2025-06-19 | アンブルックス,インコーポレイテッド | 抗体-tlrアゴニストコンジュゲートを含有する組成物、その方法、及び使用 |
| EP3696189A1 (en) | 2019-02-14 | 2020-08-19 | European Molecular Biology Laboratory | Means and methods for preparing engineered target proteins by genetic code expansion in a target protein selective manner |
| WO2020169658A2 (en) | 2019-02-20 | 2020-08-27 | Novo Nordisk A/S | Aminoacyl-trna synthetases and uses hereof |
| CN113785058B (zh) * | 2019-03-04 | 2024-12-24 | 得克萨斯A&M大学系统 | 制作和利用琥珀专性的噬菌体展示文库的方法 |
| KR20210139366A (ko) | 2019-03-15 | 2021-11-22 | 추가이 세이야쿠 가부시키가이샤 | 방향족 아미노산 유도체의 제조 방법 |
| JP7657726B2 (ja) | 2019-03-19 | 2025-04-07 | ザ ブロード インスティテュート,インコーポレーテッド | 編集ヌクレオチド配列を編集するための方法および組成物 |
| US12473543B2 (en) | 2019-04-17 | 2025-11-18 | The Broad Institute, Inc. | Adenine base editors with reduced off-target effects |
| EP3962951A1 (en) | 2019-05-03 | 2022-03-09 | Sutro Biopharma, Inc. | Anti-bcma antibody conjugates |
| US12258304B2 (en) | 2019-05-20 | 2025-03-25 | Albert Einstein College Of Medicine | Compounds and methods for treatment of bacterial infections |
| EP3980057A1 (en) | 2019-06-04 | 2022-04-13 | Institut Curie | Methods of producing shiga toxin b-subunit (stxb) monomers and oligomers, and uses thereof |
| WO2020247803A2 (en) | 2019-06-07 | 2020-12-10 | Massachusetts Institute Of Technology | Frameshift suppressor trna compositions and methods of use |
| CN114269749B (zh) | 2019-06-10 | 2024-10-01 | 苏特罗生物制药公司 | 5H-吡咯并[3,2-d]嘧啶-2,4-二氨基化合物及其抗体偶联物 |
| EP3983410A1 (en) | 2019-06-17 | 2022-04-20 | Sutro Biopharma, Inc. | 1-(4-(aminomethyl)benzyl)-2-butyl-2h-pyrazolo[3,4-c]quinolin-4-amine derivatives and related compounds as toll-like receptor (tlr) 7/8 agonists, as well as antibody drug conjugates thereof for use in cancer therapy and diagnosis |
| EP3976771A1 (en) | 2019-06-28 | 2022-04-06 | Quantum-si Incorporated | Polymerizing enzymes for sequencing reactions |
| AU2020361533A1 (en) | 2019-10-08 | 2022-04-28 | Trustees Of Boston College | Proteins containing multiple, different unnatural amino acids and methods of making and using such proteins |
| TW202128996A (zh) * | 2019-10-10 | 2021-08-01 | 美商史基普研究協會 | 用於活體內合成非天然多肽的組合物及方法 |
| US12435330B2 (en) | 2019-10-10 | 2025-10-07 | The Broad Institute, Inc. | Methods and compositions for prime editing RNA |
| KR20220080101A (ko) * | 2019-10-15 | 2022-06-14 | 트러스티스 오브 보스톤 칼리지 | 향상된 비천연 아미노산 혼입을 위한 키메라 열안정성 아미노아실-tRNA 합성효소 |
| US11149280B2 (en) | 2019-10-29 | 2021-10-19 | Yale University | Engineering organisms resistant to viruses and horizontally transferred genetic elements |
| US20220389466A1 (en) * | 2019-11-05 | 2022-12-08 | Nitro Biosciences, Inc. | Biosynthesis of para-nitro-l-phenylalanine |
| PE20221323A1 (es) | 2019-11-07 | 2022-09-09 | Chugai Pharmaceutical Co Ltd | Compuesto de peptidos ciclicos que tiene accion inhibidora de kras |
| CN115260313B (zh) | 2019-12-31 | 2023-07-18 | 北京质肽生物医药科技有限公司 | Glp-1和gdf15的融合蛋白以及其缀合物 |
| EP4084819A1 (en) | 2020-01-03 | 2022-11-09 | The United States of America, as represented by the Secretary, Department of Health and Human Services | Tnap locally administered for promoting periodontal health |
| CN115322794B (zh) | 2020-01-11 | 2025-09-19 | 北京质肽生物医药科技有限公司 | Glp-1和fgf21的融合蛋白的缀合物 |
| WO2021165968A1 (en) * | 2020-02-20 | 2021-08-26 | B. G. Negev Technologies And Applications Ltd., At Ben-Gurion University | Mutant aminoacyl-trna synthetases |
| EP3868882A1 (en) | 2020-02-21 | 2021-08-25 | European Molecular Biology Laboratory | Archaeal pyrrolysyl trna synthetases for orthogonal use |
| US20230095053A1 (en) | 2020-03-03 | 2023-03-30 | Sutro Biopharma, Inc. | Antibodies comprising site-specific glutamine tags, methods of their preparation and methods of their use |
| WO2021183832A1 (en) | 2020-03-11 | 2021-09-16 | Ambrx, Inc. | Interleukin-2 polypeptide conjugates and methods of use thereof |
| CN111302975A (zh) * | 2020-03-30 | 2020-06-19 | 滨海吉尔多肽有限公司 | 一种n-叔丁氧羰基-o-烯丙基-l-酪氨酸的制备方法 |
| AR121891A1 (es) | 2020-04-22 | 2022-07-20 | Merck Sharp & Dohme | CONJUGADOS DE INTERLEUCINA 2 HUMANA SESGADOS AL DÍMERO DEL RECEPTOR DE INTERLEUCINA 2 bgᶜ Y CONJUGADOS CON UN POLÍMERO HIDROSOLUBLE NO PEPTÍDICO |
| US12351850B2 (en) | 2020-04-30 | 2025-07-08 | Sutro Biopharma, Inc. | Methods of producing full-length antibodies using E. coli |
| EP4146665A1 (en) | 2020-05-05 | 2023-03-15 | Genentech, Inc. | Systems and methods for tyrosinase-mediated site-specific protein conjugation |
| DE112021002672T5 (de) | 2020-05-08 | 2023-04-13 | President And Fellows Of Harvard College | Vefahren und zusammensetzungen zum gleichzeitigen editieren beider stränge einer doppelsträngigen nukleotid-zielsequenz |
| JP2023526546A (ja) | 2020-05-22 | 2023-06-21 | 武田薬品工業株式会社 | コロナウイルス疾患の合併症の治療及び診断のための、adamts13組成物及び方法 |
| EP4199968A1 (en) | 2020-08-20 | 2023-06-28 | Ambrx, Inc. | Antibody-tlr agonist conjugates, methods and uses thereof |
| CA3192331A1 (en) * | 2020-09-14 | 2022-03-17 | Sutro Biopharma, Inc. | Method for large scale production of antibodies using a cell-free protein synthesis system |
| CN114729060B (zh) | 2020-09-30 | 2022-11-25 | 北京质肽生物医药科技有限公司 | 多肽缀合物和使用方法 |
| US20250161471A1 (en) | 2021-04-03 | 2025-05-22 | Feng Tian | Anti-her2 antibody-drug conjugates and uses thereof |
| US20230016731A1 (en) * | 2021-05-21 | 2023-01-19 | The Regents Of The University Of California | Affinity purification sequencing |
| US20230181754A1 (en) | 2021-07-09 | 2023-06-15 | Bright Peak Therapeutics Ag | Modified checkpoint inhibitors and uses thereof |
| WO2023281479A1 (en) | 2021-07-09 | 2023-01-12 | Bright Peak Therapeutics Ag | Checkpoint inhibitors conjugated to il-2, and uses thereof |
| US20230201365A1 (en) | 2021-07-09 | 2023-06-29 | Bright Peak Therapeutics Ag | Modified cd20 antibodies and uses thereof |
| US20230201364A1 (en) | 2021-07-09 | 2023-06-29 | Bright Peak Therapeutics Ag | Antibody conjugates and manufacture thereof |
| WO2023281485A1 (en) | 2021-07-09 | 2023-01-12 | Bright Peak Therapeutics Ag | Modified il-2 polypeptides for treatment of inflammatory and autoimmune diseases |
| US12606598B2 (en) | 2021-07-12 | 2026-04-21 | Bactoclear Holdings PTE, Ltd. | Chimeric klebicins |
| JP2024532537A (ja) | 2021-09-06 | 2024-09-05 | ヴェラクサ バイオテック ゲーエムベーハー | 真核生物における遺伝暗号の拡張のための新規アミノアシルtRNA合成酵素変異体 |
| WO2023044431A2 (en) * | 2021-09-17 | 2023-03-23 | Absci Corporation | Composition of transfer rnas and use in production of proteins containing non-standard amino acids |
| WO2023069816A2 (en) | 2021-09-20 | 2023-04-27 | The Broad Institute, Inc. | Compositions and methods for multiplex decoding of quadruplet codons |
| JP2024539139A (ja) | 2021-10-20 | 2024-10-28 | シンセカイン インコーポレイテッド | ヘテロ二量体fcサイトカインおよびその使用 |
| WO2023081167A2 (en) | 2021-11-02 | 2023-05-11 | The Regents Of The University Of California | P-selectin mutants and modulation of integrin-mediated signaling |
| CA3238627A1 (en) | 2021-11-25 | 2023-06-01 | Christine Kohler | Improved antibody-payload conjugates (apcs) prepared by site-specific conjugation utilizing genetic code expansion |
| ES3039688T3 (en) | 2021-11-25 | 2025-10-23 | Veraxa Biotech Gmbh | Improved antibody-payload conjugates (apcs) prepared by site-specific conjugation utilizing genetic code expansion |
| KR20240119102A (ko) | 2021-12-08 | 2024-08-06 | 유럽피안 몰레큘러 바이올로지 래보러토리 | 표적화 접합체의 제조를 위한 친수성 테트라진-관능화 페이로드 |
| WO2023146807A1 (en) | 2022-01-25 | 2023-08-03 | The Regents Of The University Of California | Vegf mutants and modulation of integrin-mediated signaling |
| JP2025508823A (ja) | 2022-02-23 | 2025-04-10 | ブライト ピーク セラピューティクス エージー | 免疫抗原特異的il-18免疫サイトカイン及びその使用 |
| WO2023161857A1 (en) | 2022-02-23 | 2023-08-31 | Bright Peak Therapeutics Ag | Bifunctional cytokine compositions |
| EP4323413A4 (en) | 2022-03-30 | 2025-10-15 | Beijing Ql Biopharmaceutical Co Ltd | LIQUID PHARMACEUTICAL COMPOSITIONS OF POLYPEPTIDE CONJUGATES AND METHODS OF USE THEREOF |
| KR20250043602A (ko) | 2022-06-30 | 2025-03-28 | 서트로 바이오파마, 인크. | 항-ror1 항체 및 항체 접합체, 항-ror1 항체 또는 항체 접합체를 포함하는 조성물, 및 항-ror1 항체 및 항체 접합체의 제조 및 사용 방법 |
| CN116376851A (zh) * | 2022-08-25 | 2023-07-04 | 凯莱英医药集团(天津)股份有限公司 | 氨酰tRNA合酶突变体及其应用 |
| NL2033185B1 (en) | 2022-09-29 | 2024-04-08 | Stichting Vu | Compounds for rna stabilisation and delivery |
| JP2025535713A (ja) | 2022-10-07 | 2025-10-28 | アンブレツクス・インコーポレイテツド | 薬物リンカー及びその抗体コンジュゲート |
| WO2024091824A1 (en) | 2022-10-26 | 2024-05-02 | Ada Forsyth Institute, Inc. | Differentiation and reprogramming of chondrocyte |
| CN120380161A (zh) * | 2022-12-31 | 2025-07-25 | 康码(上海)生物科技有限公司 | 一种用于插入非天然氨基酸的体外无细胞蛋白质合成体系、方法及应用 |
| WO2024150175A1 (en) | 2023-01-11 | 2024-07-18 | Bright Peak Therapeutics Ag | Conditionally activated proteins and methods of use |
| AU2024209360A1 (en) | 2023-01-16 | 2025-09-04 | Ambrx, Inc. | Anti-cd70 antibody-drug conjugates |
| WO2024178310A1 (en) | 2023-02-23 | 2024-08-29 | Ambrx, Inc. | Trop2-directed antibody-drug conjugates and uses thereof |
| WO2024211306A1 (en) | 2023-04-03 | 2024-10-10 | Sutro Biopharma, Inc. | Rf1 ko e. coli strains |
| WO2024241086A1 (en) | 2023-05-24 | 2024-11-28 | Ambrx, Inc. | Pegylated bovine interferon lambda and methods of use thereof |
| AU2024300552A1 (en) | 2023-07-27 | 2026-01-29 | Veraxa Biotech Gmbh | Hydrophilic trans-cyclooctene (hytco) compounds, constructs and conjugates containing the same |
| IL326709A (en) | 2023-08-22 | 2026-04-01 | Ambrx Inc | Anti-PSMA ADC conjugate compositions and methods of using them |
| WO2025041102A1 (en) | 2023-08-23 | 2025-02-27 | Bright Peak Therapeutics Ag | Targeted immune activation with il-18 immunocytokines |
| WO2025041101A1 (en) | 2023-08-23 | 2025-02-27 | Bright Peak Therapeutics Ag | Activatable il-18 immunocytokines and uses thereof |
| WO2025080711A1 (en) | 2023-10-13 | 2025-04-17 | Sutro Biopharma, Inc. | Dual payload antibody drug conjugates |
| AU2024358957A1 (en) | 2023-10-13 | 2026-04-02 | Sutro Biopharma, Inc. | Anti-tissue factor antibodies and antibody conjugates, compositions comprising anti-tissue factor antibodies or antibody conjugates, and methods of making and using anti-tissue factor antibodies and antibody conjugates |
| WO2025176699A1 (en) | 2024-02-20 | 2025-08-28 | LenioBio GmbH | A system and method for cell-free unnatural amino acid incorporation |
| TW202602923A (zh) | 2024-02-29 | 2026-01-16 | 美商安進公司 | 升糖素受體促效劑及與葡萄糖依賴性促胰島素多肽拮抗劑之軛合物 |
| WO2025199030A1 (en) | 2024-03-18 | 2025-09-25 | Amgen Inc. | Glp-1 receptor agonists and their medical use |
| EP4644408A1 (en) | 2024-04-19 | 2025-11-05 | The Chinese University of Hong Kong Office of Research and Knowledge Transfer Services (ORKTS) | Polyethylenimine-modified cry proteins and their use |
| WO2025257694A1 (en) | 2024-06-10 | 2025-12-18 | Università Degli Studi Di Torino | Cell differentiation through multimodal tuning of gene expression |
| WO2025257695A1 (en) | 2024-06-10 | 2025-12-18 | Università Degli Studi Di Torino | Growth factor-free stem cell expansion and differentiation |
| WO2026043823A2 (en) | 2024-08-19 | 2026-02-26 | Sutro Biopharma, Inc. | Antibodies comprising site-specific non-natural amino acid residues, methods of preparation and uses thereof |
| WO2026069134A1 (en) | 2024-09-26 | 2026-04-02 | Bright Peak Therapeutics Ag | Human therapy with il-18 immunocytokines |
| WO2026080688A1 (en) | 2024-10-09 | 2026-04-16 | Sutro Biopharma, Inc. | Dual mechanism of action payload antibody drug conjugates |
| WO2026080697A1 (en) | 2024-10-09 | 2026-04-16 | Sutro Biopharma, Inc. | Antibody conjugates with high payload to antibody ratios, compositions comprising the same, and methods of their use |
Family Cites Families (49)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| CH652145A5 (de) | 1982-01-22 | 1985-10-31 | Sandoz Ag | Verfahren zur in vitro-herstellung von hybridomen welche humane monoklonale antikoerper erzeugen. |
| US4634666A (en) | 1984-01-06 | 1987-01-06 | The Board Of Trustees Of The Leland Stanford Junior University | Human-murine hybridoma fusion partner |
| US5001065A (en) | 1987-05-27 | 1991-03-19 | Cetus Corporation | Human cell line and triomas, antibodies, and transformants derived therefrom |
| DE9115660U1 (de) * | 1991-12-18 | 1992-07-30 | Aventis Research & Technologies GmbH & Co KG, 65929 Frankfurt | L-Phenylalanyl-tRNA-Synthetase mit erweiterter Substratselektivität aus Mikroorganismen |
| KR100501838B1 (ko) | 1995-04-24 | 2005-07-21 | 큐비스트 파마슈티컬즈 인코포레이티드 | 새로운 대사 경로를 만들고 이를 스크리닝하는 방법 |
| US5958672A (en) | 1995-07-18 | 1999-09-28 | Diversa Corporation | Protein activity screening of clones having DNA from uncultivated microorganisms |
| US5756316A (en) | 1995-11-02 | 1998-05-26 | Genencor International, Inc. | Molecular cloning by multimerization of plasmids |
| US6238884B1 (en) | 1995-12-07 | 2001-05-29 | Diversa Corporation | End selection in directed evolution |
| US5783431A (en) | 1996-04-24 | 1998-07-21 | Chromaxome Corporation | Methods for generating and screening novel metabolic pathways |
| US6706504B1 (en) * | 1996-11-12 | 2004-03-16 | The Scripps Research Institute | Tissue type plasminogen activator (t-PA) variants: compositions and methods of use |
| 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 |
| DE10151556A1 (de) * | 2001-10-23 | 2003-04-30 | Bosch Gmbh Robert | Vorrichtung zum Öffnen und Schließen eines beweglichen Teils |
| ITTO20020441A1 (it) * | 2002-05-24 | 2003-11-24 | Telecom Italia Lab Spa | Metodo per determinare l'installazione di costo minimo per le apparecchiature di una rete fissa di telecomunicazione. |
| ES2324608T3 (es) * | 2002-10-16 | 2009-08-11 | The Scripps Research Institute | Incorporacion especifica de sitio de cetoaminoacidos en proteinas. |
| MXPA05003978A (es) * | 2002-10-16 | 2005-06-22 | Scripps Research Inst | Sintesis de glicoproteinas. |
| WO2004058946A2 (en) * | 2002-12-22 | 2004-07-15 | The Scripps Research Institute | Protein arrays |
| 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 |
| 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 |
| 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 |
| 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 |
| 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 |
| FR2888097B1 (fr) * | 2005-07-06 | 2007-10-05 | Oreal | Dispositif de conditionnement et d'application comportant un organe d'essorage |
| 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 |
| US7807411B2 (en) | 2006-05-23 | 2010-10-05 | The Scripps Research Institute | Genetically encoded fluorescent coumarin amino acids |
| US7421795B2 (en) * | 2006-08-04 | 2008-09-09 | Seagate Technology Llc | Sapphire alignment fixture |
| EP2052083B1 (en) * | 2006-09-21 | 2014-01-08 | The Scripps Research Institute | Genetically programmed expression of selectively sulfated proteins in eubacteria |
| JP2010506591A (ja) * | 2006-10-18 | 2010-03-04 | ザ スクリップス リサーチ インスティテュート | 哺乳動物細胞中の蛋白質への非天然アミノ酸の遺伝的組込み |
| TWI334126B (en) * | 2007-07-17 | 2010-12-01 | Au Optronics Corp | Voltage adjusting circuit, method, and display apparatus having the same |
| JP4978419B2 (ja) * | 2007-10-23 | 2012-07-18 | 富士ゼロックス株式会社 | 光送受信モジュール |
| MX2010004464A (es) * | 2007-10-25 | 2010-06-07 | Scripps Research Inst | Incorporacion genetica de 3-aminotirosina a reductasas. |
| US9150849B2 (en) * | 2007-11-02 | 2015-10-06 | The Scripps Research Institute | Directed evolution using proteins comprising unnatural amino acids |
| WO2009059056A2 (en) | 2007-11-02 | 2009-05-07 | The Scripps Research Institute | A genetically encoded boronate amino acid |
| WO2009064416A2 (en) | 2007-11-15 | 2009-05-22 | The Scripps Research Institute | Genetic incorporation of an alpha-hydroxy acid into proteins to generate ester backbone linkages at defined sites |
| US8218509B2 (en) * | 2008-01-15 | 2012-07-10 | Apple Inc. | Dynamic allocation of communication resources in a wireless system |
| CN101970005A (zh) * | 2008-02-08 | 2011-02-09 | 斯克利普斯研究院 | 用遗传编码的非天然氨基酸打破免疫耐受 |
| WO2009151491A2 (en) | 2008-02-27 | 2009-12-17 | The Scripps Research Institute | In vivo incorporation of an unnatural amino acid comprising a 1,2-aminothiol group |
| US20090197339A1 (en) * | 2008-12-10 | 2009-08-06 | The Scripps Research Institute | In vivo unnatural amino acid expression in the methylotrophic yeast pichia pastoris |
| CN102307905B (zh) * | 2008-12-10 | 2015-11-25 | 斯克利普斯研究院 | 利用化学反应性非天然氨基酸产生载体-肽偶联物 |
| WO2010114615A2 (en) | 2009-04-03 | 2010-10-07 | The Scripps Research Institute | A facile system for encoding unnatural amino acids in mammalian cells |
-
2002
- 2002-04-19 US US10/126,931 patent/US7083970B2/en not_active Expired - Lifetime
- 2002-04-19 DK DK02731454.1T patent/DK1456360T3/en active
- 2002-04-19 EP EP10182672.5A patent/EP2322631B1/en not_active Expired - Lifetime
- 2002-04-19 EP EP02725743.5A patent/EP1490483B1/en not_active Expired - Lifetime
- 2002-04-19 MX MXPA03009566A patent/MXPA03009566A/es active IP Right Grant
- 2002-04-19 DK DK10182672.5T patent/DK2322631T3/en active
- 2002-04-19 DK DK09006800.8T patent/DK2128246T3/da active
- 2002-04-19 MX MXPA03009563A patent/MXPA03009563A/es active IP Right Grant
- 2002-04-19 ES ES09006800.8T patent/ES2464532T3/es not_active Expired - Lifetime
- 2002-04-19 EP EP09006800.8A patent/EP2128246B1/en not_active Expired - Lifetime
- 2002-04-19 EP EP14167479.6A patent/EP2796546B1/en not_active Expired - Lifetime
- 2002-04-19 CA CA2444098A patent/CA2444098C/en not_active Expired - Lifetime
- 2002-04-19 IL IL15841902A patent/IL158419A0/xx unknown
- 2002-04-19 JP JP2002583449A patent/JP2005502322A/ja active Pending
- 2002-04-19 EP EP02731454.1A patent/EP1456360B1/en not_active Expired - Lifetime
- 2002-04-19 IL IL15841802A patent/IL158418A0/xx active IP Right Grant
- 2002-04-19 JP JP2002583590A patent/JP2004537984A/ja active Pending
- 2002-04-19 WO PCT/US2002/012465 patent/WO2002085923A2/en not_active Ceased
- 2002-04-19 WO PCT/US2002/012635 patent/WO2002086075A2/en not_active Ceased
- 2002-04-19 US US10/126,927 patent/US7045337B2/en not_active Expired - Lifetime
- 2002-04-19 CA CA2443757A patent/CA2443757C/en not_active Expired - Lifetime
- 2002-04-19 DK DK02725743.5T patent/DK1490483T3/en active
- 2002-04-19 AU AU2002256292A patent/AU2002256292C1/en not_active Expired
- 2002-04-19 AU AU2002303431A patent/AU2002303431C1/en not_active Expired
-
2003
- 2003-10-15 IL IL158419A patent/IL158419A/en active IP Right Grant
-
2004
- 2004-12-01 US US11/002,387 patent/US7713721B2/en not_active Expired - Lifetime
- 2004-12-10 US US11/009,635 patent/US8183012B2/en not_active Expired - Fee Related
- 2004-12-17 US US11/017,550 patent/US20050250183A1/en not_active Abandoned
-
2005
- 2005-10-18 US US11/254,161 patent/US7368275B2/en not_active Expired - Lifetime
- 2005-10-18 US US11/254,170 patent/US7354761B2/en not_active Expired - Lifetime
-
2006
- 2006-10-18 US US11/583,551 patent/US7638300B2/en not_active Expired - Lifetime
-
2007
- 2007-05-04 US US11/800,455 patent/US7915025B2/en not_active Expired - Fee Related
- 2007-10-26 US US11/978,156 patent/US8173392B2/en not_active Expired - Fee Related
- 2007-10-26 US US11/978,221 patent/US8173364B2/en not_active Expired - Fee Related
- 2007-10-26 US US11/978,217 patent/US20110027867A1/en not_active Abandoned
- 2007-10-26 US US11/978,157 patent/US20090068717A1/en not_active Abandoned
- 2007-10-26 US US11/978,188 patent/US8114648B2/en not_active Expired - Fee Related
- 2007-10-26 US US11/978,154 patent/US8012739B2/en not_active Expired - Fee Related
- 2007-10-26 US US11/978,108 patent/US8030074B2/en not_active Expired - Fee Related
- 2007-11-22 IL IL187588A patent/IL187588A/en active IP Right Grant
- 2007-11-29 IL IL187775A patent/IL187775A0/en active IP Right Grant
-
2008
- 2008-11-06 JP JP2008285996A patent/JP2009132704A/ja active Pending
- 2008-11-06 JP JP2008285997A patent/JP2009077731A/ja active Pending
-
2009
- 2009-01-26 IL IL196714A patent/IL196714A/en active IP Right Grant
- 2009-01-28 IL IL196762A patent/IL196762A/en active IP Right Grant
-
2010
- 2010-09-21 JP JP2010211248A patent/JP5766925B2/ja not_active Expired - Lifetime
-
2011
- 2011-06-15 US US13/161,335 patent/US20120101006A1/en not_active Abandoned
- 2011-08-02 US US13/196,829 patent/US20120202243A1/en not_active Abandoned
-
2012
- 2012-05-18 US US13/475,792 patent/US9163271B2/en not_active Expired - Fee Related
-
2013
- 2013-07-26 JP JP2013156012A patent/JP6239888B2/ja not_active Expired - Lifetime
-
2015
- 2015-04-29 HK HK15104166.3A patent/HK1203558A1/en unknown
-
2016
- 2016-02-08 JP JP2016021701A patent/JP6294368B2/ja not_active Expired - Lifetime
Also Published As
Similar Documents
| Publication | Publication Date | Title |
|---|---|---|
| ES2464532T3 (es) | Métodos y composiciones para la producción de pares ortogonales de ARNt-aminoacil-ARNt sintetasa | |
| AU2002303431A1 (en) | Methods and composition for the production of orthoganal tRNA-aminoacyltRNA synthetase pairs | |
| AU2007251897B2 (en) | Methods and compositions for the production of orthoganal tRNA-aminoacyltRNA synthetase pairs | |
| AU2008200780B2 (en) | In vivo incorporation of unnatural amino acids | |
| HK1065065B (en) | Methods and composition for the production of orthoganal trna-aminoacyltrna synthetase pairs |