JP2000515366A - 新規化合物 - Google Patents
新規化合物Info
- Publication number
- JP2000515366A JP2000515366A JP09537452A JP53745297A JP2000515366A JP 2000515366 A JP2000515366 A JP 2000515366A JP 09537452 A JP09537452 A JP 09537452A JP 53745297 A JP53745297 A JP 53745297A JP 2000515366 A JP2000515366 A JP 2000515366A
- Authority
- JP
- Japan
- Prior art keywords
- polypeptide
- polynucleotide
- asns
- seq
- dna
- Prior art date
- Legal status (The legal status is an assumption and is not a legal conclusion. Google has not performed a legal analysis and makes no representation as to the accuracy of the status listed.)
- Pending
Links
- 150000001875 compounds Chemical class 0.000 title claims abstract description 28
- 108090000765 processed proteins & peptides Proteins 0.000 claims abstract description 185
- 102000004196 processed proteins & peptides Human genes 0.000 claims abstract description 180
- 229920001184 polypeptide Polymers 0.000 claims abstract description 175
- 101150014732 asnS gene Proteins 0.000 claims abstract description 89
- 238000000034 method Methods 0.000 claims abstract description 62
- 108091033319 polynucleotide Proteins 0.000 claims description 127
- 102000040430 polynucleotide Human genes 0.000 claims description 127
- 239000002157 polynucleotide Substances 0.000 claims description 126
- 108090000623 proteins and genes Proteins 0.000 claims description 59
- 108020004414 DNA Proteins 0.000 claims description 50
- 239000012634 fragment Substances 0.000 claims description 38
- 125000003275 alpha amino acid group Chemical group 0.000 claims description 33
- 210000004027 cell Anatomy 0.000 claims description 33
- 241000193998 Streptococcus pneumoniae Species 0.000 claims description 28
- 125000003729 nucleotide group Chemical group 0.000 claims description 27
- 229940031000 streptococcus pneumoniae Drugs 0.000 claims description 27
- 239000002773 nucleotide Substances 0.000 claims description 26
- 239000005557 antagonist Substances 0.000 claims description 21
- 108091032973 (ribonucleotides)n+m Proteins 0.000 claims description 19
- 150000001413 amino acids Chemical class 0.000 claims description 19
- 230000014509 gene expression Effects 0.000 claims description 19
- 239000013598 vector Substances 0.000 claims description 19
- FWMNVWWHGCHHJJ-SKKKGAJSSA-N 4-amino-1-[(2r)-6-amino-2-[[(2r)-2-[[(2r)-2-[[(2r)-2-amino-3-phenylpropanoyl]amino]-3-phenylpropanoyl]amino]-4-methylpentanoyl]amino]hexanoyl]piperidine-4-carboxylic acid Chemical compound C([C@H](C(=O)N[C@H](CC(C)C)C(=O)N[C@H](CCCCN)C(=O)N1CCC(N)(CC1)C(O)=O)NC(=O)[C@H](N)CC=1C=CC=CC=1)C1=CC=CC=C1 FWMNVWWHGCHHJJ-SKKKGAJSSA-N 0.000 claims description 18
- 230000028993 immune response Effects 0.000 claims description 18
- 201000010099 disease Diseases 0.000 claims description 17
- 208000037265 diseases, disorders, signs and symptoms Diseases 0.000 claims description 17
- 230000000694 effects Effects 0.000 claims description 15
- 108091028043 Nucleic acid sequence Proteins 0.000 claims description 14
- 150000007523 nucleic acids Chemical group 0.000 claims description 13
- 238000004519 manufacturing process Methods 0.000 claims description 12
- 230000003993 interaction Effects 0.000 claims description 11
- 241000124008 Mammalia Species 0.000 claims description 10
- 102000039446 nucleic acids Human genes 0.000 claims description 9
- 108020004707 nucleic acids Proteins 0.000 claims description 9
- 210000001744 T-lymphocyte Anatomy 0.000 claims description 6
- 230000001939 inductive effect Effects 0.000 claims description 6
- 230000000295 complement effect Effects 0.000 claims description 5
- 241001465754 Metazoa Species 0.000 claims description 4
- 239000002253 acid Substances 0.000 claims description 4
- 238000001727 in vivo Methods 0.000 claims description 4
- 230000005764 inhibitory process Effects 0.000 claims description 3
- 230000004044 response Effects 0.000 claims description 3
- 238000012258 culturing Methods 0.000 claims 1
- 150000004676 glycans Chemical class 0.000 claims 1
- 229920001282 polysaccharide Polymers 0.000 claims 1
- 239000005017 polysaccharide Substances 0.000 claims 1
- 238000012216 screening Methods 0.000 abstract description 9
- 230000000844 anti-bacterial effect Effects 0.000 abstract description 5
- 238000010188 recombinant method Methods 0.000 abstract description 3
- 102000004169 proteins and genes Human genes 0.000 description 42
- 239000000203 mixture Substances 0.000 description 34
- 208000015181 infectious disease Diseases 0.000 description 21
- 230000027455 binding Effects 0.000 description 19
- 238000003556 assay Methods 0.000 description 12
- 230000001580 bacterial effect Effects 0.000 description 11
- 238000009472 formulation Methods 0.000 description 11
- 201000009906 Meningitis Diseases 0.000 description 10
- 239000000523 sample Substances 0.000 description 10
- 102000003924 Asparagine-tRNA ligases Human genes 0.000 description 9
- 108090000314 Asparagine-tRNA ligases Proteins 0.000 description 9
- 239000000556 agonist Substances 0.000 description 9
- 239000000758 substrate Substances 0.000 description 9
- 241000282412 Homo Species 0.000 description 8
- 241000282414 Homo sapiens Species 0.000 description 8
- 239000000427 antigen Substances 0.000 description 8
- 238000009396 hybridization Methods 0.000 description 8
- 238000010561 standard procedure Methods 0.000 description 8
- 102000004190 Enzymes Human genes 0.000 description 7
- 108090000790 Enzymes Proteins 0.000 description 7
- 239000003242 anti bacterial agent Substances 0.000 description 7
- 108091007433 antigens Proteins 0.000 description 7
- 102000036639 antigens Human genes 0.000 description 7
- 230000015572 biosynthetic process Effects 0.000 description 7
- 239000002299 complementary DNA Substances 0.000 description 7
- 239000003446 ligand Substances 0.000 description 7
- 125000002924 primary amino group Chemical group [H]N([H])* 0.000 description 7
- 238000012163 sequencing technique Methods 0.000 description 7
- 229960005486 vaccine Drugs 0.000 description 7
- 208000031729 Bacteremia Diseases 0.000 description 6
- 208000035143 Bacterial infection Diseases 0.000 description 6
- 241000588724 Escherichia coli Species 0.000 description 6
- LFQSCWFLJHTTHZ-UHFFFAOYSA-N Ethanol Chemical compound CCO LFQSCWFLJHTTHZ-UHFFFAOYSA-N 0.000 description 6
- 238000007792 addition Methods 0.000 description 6
- 125000000539 amino acid group Chemical group 0.000 description 6
- 208000022362 bacterial infectious disease Diseases 0.000 description 6
- 210000001175 cerebrospinal fluid Anatomy 0.000 description 6
- 238000012217 deletion Methods 0.000 description 6
- 230000037430 deletion Effects 0.000 description 6
- 238000005755 formation reaction Methods 0.000 description 6
- 230000002163 immunogen Effects 0.000 description 6
- 239000003112 inhibitor Substances 0.000 description 6
- 230000004048 modification Effects 0.000 description 6
- 238000012986 modification Methods 0.000 description 6
- 230000035772 mutation Effects 0.000 description 6
- 239000002243 precursor Substances 0.000 description 6
- 210000001519 tissue Anatomy 0.000 description 6
- 238000011282 treatment Methods 0.000 description 6
- 235000014469 Bacillus subtilis Nutrition 0.000 description 5
- 206010010741 Conjunctivitis Diseases 0.000 description 5
- 108091034117 Oligonucleotide Proteins 0.000 description 5
- 206010033078 Otitis media Diseases 0.000 description 5
- 206010035664 Pneumonia Diseases 0.000 description 5
- 206010052428 Wound Diseases 0.000 description 5
- 208000027418 Wounds and injury Diseases 0.000 description 5
- 125000003178 carboxy group Chemical group [H]OC(*)=O 0.000 description 5
- 206010014665 endocarditis Diseases 0.000 description 5
- 230000002068 genetic effect Effects 0.000 description 5
- 238000003780 insertion Methods 0.000 description 5
- 230000037431 insertion Effects 0.000 description 5
- 230000001404 mediated effect Effects 0.000 description 5
- 201000009890 sinusitis Diseases 0.000 description 5
- 239000000126 substance Substances 0.000 description 5
- 238000006467 substitution reaction Methods 0.000 description 5
- 244000063299 Bacillus subtilis Species 0.000 description 4
- 241000894006 Bacteria Species 0.000 description 4
- 108091026890 Coding region Proteins 0.000 description 4
- 102000053602 DNA Human genes 0.000 description 4
- 239000013543 active substance Substances 0.000 description 4
- 230000003321 amplification Effects 0.000 description 4
- 229940088710 antibiotic agent Drugs 0.000 description 4
- 239000000969 carrier Substances 0.000 description 4
- 239000006071 cream Substances 0.000 description 4
- 238000011161 development Methods 0.000 description 4
- 230000018109 developmental process Effects 0.000 description 4
- 229920000140 heteropolymer Polymers 0.000 description 4
- 229910052739 hydrogen Inorganic materials 0.000 description 4
- 239000001257 hydrogen Substances 0.000 description 4
- 125000004435 hydrogen atom Chemical group [H]* 0.000 description 4
- 238000002347 injection Methods 0.000 description 4
- 239000007924 injection Substances 0.000 description 4
- 108020004999 messenger RNA Proteins 0.000 description 4
- 238000010369 molecular cloning Methods 0.000 description 4
- 238000003199 nucleic acid amplification method Methods 0.000 description 4
- 239000013612 plasmid Substances 0.000 description 4
- 238000012545 processing Methods 0.000 description 4
- 230000000069 prophylactic effect Effects 0.000 description 4
- 238000000746 purification Methods 0.000 description 4
- 238000011160 research Methods 0.000 description 4
- 238000003757 reverse transcription PCR Methods 0.000 description 4
- 230000001225 therapeutic effect Effects 0.000 description 4
- 206010014568 Empyema Diseases 0.000 description 3
- 241000206602 Eukaryota Species 0.000 description 3
- 102000010834 Extracellular Matrix Proteins Human genes 0.000 description 3
- 108010037362 Extracellular Matrix Proteins Proteins 0.000 description 3
- PEDCQBHIVMGVHV-UHFFFAOYSA-N Glycerine Chemical compound OCC(O)CO PEDCQBHIVMGVHV-UHFFFAOYSA-N 0.000 description 3
- 102000003960 Ligases Human genes 0.000 description 3
- 108090000364 Ligases Proteins 0.000 description 3
- 102000007056 Recombinant Fusion Proteins Human genes 0.000 description 3
- 108010008281 Recombinant Fusion Proteins Proteins 0.000 description 3
- 102000006382 Ribonucleases Human genes 0.000 description 3
- 108010083644 Ribonucleases Proteins 0.000 description 3
- FAPWRFPIFSIZLT-UHFFFAOYSA-M Sodium chloride Chemical compound [Na+].[Cl-] FAPWRFPIFSIZLT-UHFFFAOYSA-M 0.000 description 3
- 108020004566 Transfer RNA Proteins 0.000 description 3
- 239000002671 adjuvant Substances 0.000 description 3
- 230000000692 anti-sense effect Effects 0.000 description 3
- 230000004071 biological effect Effects 0.000 description 3
- 239000013611 chromosomal DNA Substances 0.000 description 3
- 125000004122 cyclic group Chemical group 0.000 description 3
- 238000001514 detection method Methods 0.000 description 3
- 230000004927 fusion Effects 0.000 description 3
- 108020001507 fusion proteins Proteins 0.000 description 3
- 102000037865 fusion proteins Human genes 0.000 description 3
- 230000005847 immunogenicity Effects 0.000 description 3
- 230000001965 increasing effect Effects 0.000 description 3
- 238000002955 isolation Methods 0.000 description 3
- 150000002632 lipids Chemical class 0.000 description 3
- 239000000463 material Substances 0.000 description 3
- 244000005700 microbiome Species 0.000 description 3
- 239000002674 ointment Substances 0.000 description 3
- 244000052769 pathogen Species 0.000 description 3
- 230000001717 pathogenic effect Effects 0.000 description 3
- 230000004481 post-translational protein modification Effects 0.000 description 3
- 230000008569 process Effects 0.000 description 3
- 230000002829 reductive effect Effects 0.000 description 3
- 150000003384 small molecules Chemical class 0.000 description 3
- 239000000243 solution Substances 0.000 description 3
- 238000001890 transfection Methods 0.000 description 3
- 230000014616 translation Effects 0.000 description 3
- 102000040650 (ribonucleotides)n+m Human genes 0.000 description 2
- 108091003079 Bovine Serum Albumin Proteins 0.000 description 2
- ZHNUHDYFZUAESO-UHFFFAOYSA-N Formamide Chemical compound NC=O ZHNUHDYFZUAESO-UHFFFAOYSA-N 0.000 description 2
- 102000005720 Glutathione transferase Human genes 0.000 description 2
- 108010070675 Glutathione transferase Proteins 0.000 description 2
- 108010054477 Immunoglobulin Fab Fragments Proteins 0.000 description 2
- 102000001706 Immunoglobulin Fab Fragments Human genes 0.000 description 2
- 206010071699 Infectious pleural effusion Diseases 0.000 description 2
- 240000004808 Saccharomyces cerevisiae Species 0.000 description 2
- 238000012300 Sequence Analysis Methods 0.000 description 2
- 241000194017 Streptococcus Species 0.000 description 2
- 241000700605 Viruses Species 0.000 description 2
- 230000009471 action Effects 0.000 description 2
- 239000000654 additive Substances 0.000 description 2
- 238000001042 affinity chromatography Methods 0.000 description 2
- 230000006229 amino acid addition Effects 0.000 description 2
- 238000004458 analytical method Methods 0.000 description 2
- 230000000890 antigenic effect Effects 0.000 description 2
- 230000003385 bacteriostatic effect Effects 0.000 description 2
- 230000003115 biocidal effect Effects 0.000 description 2
- 210000004369 blood Anatomy 0.000 description 2
- 239000008280 blood Substances 0.000 description 2
- 229940098773 bovine serum albumin Drugs 0.000 description 2
- 239000001506 calcium phosphate Substances 0.000 description 2
- 229910000389 calcium phosphate Inorganic materials 0.000 description 2
- 235000011010 calcium phosphates Nutrition 0.000 description 2
- 230000001413 cellular effect Effects 0.000 description 2
- 230000008859 change Effects 0.000 description 2
- 239000003153 chemical reaction reagent Substances 0.000 description 2
- 238000004587 chromatography analysis Methods 0.000 description 2
- 230000002759 chromosomal effect Effects 0.000 description 2
- 238000010367 cloning Methods 0.000 description 2
- 238000004590 computer program Methods 0.000 description 2
- 238000002405 diagnostic procedure Methods 0.000 description 2
- 239000003814 drug Substances 0.000 description 2
- 239000003937 drug carrier Substances 0.000 description 2
- 230000004064 dysfunction Effects 0.000 description 2
- 229920001519 homopolymer Polymers 0.000 description 2
- 210000000987 immune system Anatomy 0.000 description 2
- 230000036039 immunity Effects 0.000 description 2
- 230000003053 immunization Effects 0.000 description 2
- 238000002649 immunization Methods 0.000 description 2
- 238000002513 implantation Methods 0.000 description 2
- 108010045069 keyhole-limpet hemocyanin Proteins 0.000 description 2
- 239000006210 lotion Substances 0.000 description 2
- 239000003550 marker Substances 0.000 description 2
- 229910052751 metal Chemical group 0.000 description 2
- 239000002184 metal Chemical group 0.000 description 2
- 230000000813 microbial effect Effects 0.000 description 2
- 210000003205 muscle Anatomy 0.000 description 2
- 229930014626 natural product Natural products 0.000 description 2
- 239000006225 natural substrate Substances 0.000 description 2
- 230000036961 partial effect Effects 0.000 description 2
- 230000026731 phosphorylation Effects 0.000 description 2
- 238000006366 phosphorylation reaction Methods 0.000 description 2
- 230000010399 physical interaction Effects 0.000 description 2
- 238000002360 preparation method Methods 0.000 description 2
- 238000011321 prophylaxis Methods 0.000 description 2
- 238000001243 protein synthesis Methods 0.000 description 2
- 108091008146 restriction endonucleases Proteins 0.000 description 2
- 102220240796 rs553605556 Human genes 0.000 description 2
- 230000028327 secretion Effects 0.000 description 2
- 210000003491 skin Anatomy 0.000 description 2
- 239000011780 sodium chloride Substances 0.000 description 2
- 239000002904 solvent Substances 0.000 description 2
- 238000001356 surgical procedure Methods 0.000 description 2
- 238000003786 synthesis reaction Methods 0.000 description 2
- 230000000451 tissue damage Effects 0.000 description 2
- 231100000827 tissue damage Toxicity 0.000 description 2
- 238000010361 transduction Methods 0.000 description 2
- 230000026683 transduction Effects 0.000 description 2
- 238000013519 translation Methods 0.000 description 2
- QORWJWZARLRLPR-UHFFFAOYSA-H tricalcium bis(phosphate) Chemical compound [Ca+2].[Ca+2].[Ca+2].[O-]P([O-])([O-])=O.[O-]P([O-])([O-])=O QORWJWZARLRLPR-UHFFFAOYSA-H 0.000 description 2
- YNJBWRMUSHSURL-UHFFFAOYSA-N trichloroacetic acid Chemical compound OC(=O)C(Cl)(Cl)Cl YNJBWRMUSHSURL-UHFFFAOYSA-N 0.000 description 2
- 241001515965 unidentified phage Species 0.000 description 2
- 230000002792 vascular Effects 0.000 description 2
- 238000005406 washing Methods 0.000 description 2
- XLYOFNOQVPJJNP-UHFFFAOYSA-N water Substances O XLYOFNOQVPJJNP-UHFFFAOYSA-N 0.000 description 2
- ALSTYHKOOCGGFT-KTKRTIGZSA-N (9Z)-octadecen-1-ol Chemical compound CCCCCCCC\C=C/CCCCCCCCO ALSTYHKOOCGGFT-KTKRTIGZSA-N 0.000 description 1
- MINDHVHHQZYEEK-UHFFFAOYSA-N (E)-(2S,3R,4R,5S)-5-[(2S,3S,4S,5S)-2,3-epoxy-5-hydroxy-4-methylhexyl]tetrahydro-3,4-dihydroxy-(beta)-methyl-2H-pyran-2-crotonic acid ester with 9-hydroxynonanoic acid Natural products CC(O)C(C)C1OC1CC1C(O)C(O)C(CC(C)=CC(=O)OCCCCCCCCC(O)=O)OC1 MINDHVHHQZYEEK-UHFFFAOYSA-N 0.000 description 1
- ODHCTXKNWHHXJC-VKHMYHEASA-N 5-oxo-L-proline Chemical compound OC(=O)[C@@H]1CCC(=O)N1 ODHCTXKNWHHXJC-VKHMYHEASA-N 0.000 description 1
- 230000005730 ADP ribosylation Effects 0.000 description 1
- 108700028369 Alleles Proteins 0.000 description 1
- 102000052866 Amino Acyl-tRNA Synthetases Human genes 0.000 description 1
- 108700028939 Amino Acyl-tRNA Synthetases Proteins 0.000 description 1
- 241000228212 Aspergillus Species 0.000 description 1
- 241000972773 Aulopiformes Species 0.000 description 1
- 241000193830 Bacillus <bacterium> Species 0.000 description 1
- 102100026189 Beta-galactosidase Human genes 0.000 description 1
- 102000014914 Carrier Proteins Human genes 0.000 description 1
- 108010078791 Carrier Proteins Proteins 0.000 description 1
- 241000282693 Cercopithecidae Species 0.000 description 1
- 108010047041 Complementarity Determining Regions Proteins 0.000 description 1
- 102000004127 Cytokines Human genes 0.000 description 1
- 108090000695 Cytokines Proteins 0.000 description 1
- LEVWYRKDKASIDU-QWWZWVQMSA-N D-cystine Chemical compound OC(=O)[C@H](N)CSSC[C@@H](N)C(O)=O LEVWYRKDKASIDU-QWWZWVQMSA-N 0.000 description 1
- 238000001712 DNA sequencing Methods 0.000 description 1
- 108010014303 DNA-directed DNA polymerase Proteins 0.000 description 1
- 102000016928 DNA-directed DNA polymerase Human genes 0.000 description 1
- 229920002307 Dextran Polymers 0.000 description 1
- 241000255581 Drosophila <fruit fly, genus> Species 0.000 description 1
- 238000012286 ELISA Assay Methods 0.000 description 1
- 241000196324 Embryophyta Species 0.000 description 1
- 108060002716 Exonuclease Proteins 0.000 description 1
- 241000700662 Fowlpox virus Species 0.000 description 1
- 241000287828 Gallus gallus Species 0.000 description 1
- WQZGKKKJIJFFOK-GASJEMHNSA-N Glucose Natural products OC[C@H]1OC(O)[C@H](O)[C@@H](O)[C@@H]1O WQZGKKKJIJFFOK-GASJEMHNSA-N 0.000 description 1
- 108060003393 Granulin Proteins 0.000 description 1
- HVLSXIKZNLPZJJ-TXZCQADKSA-N HA peptide Chemical compound C([C@@H](C(=O)N[C@@H](CC(O)=O)C(=O)N[C@@H](C(C)C)C(=O)N1[C@@H](CCC1)C(=O)N[C@@H](CC(O)=O)C(=O)N[C@@H](CC=1C=CC(O)=CC=1)C(=O)N[C@@H](C)C(O)=O)NC(=O)[C@H]1N(CCC1)C(=O)[C@@H](N)CC=1C=CC(O)=CC=1)C1=CC=C(O)C=C1 HVLSXIKZNLPZJJ-TXZCQADKSA-N 0.000 description 1
- 241000606768 Haemophilus influenzae Species 0.000 description 1
- SQUHHTBVTRBESD-UHFFFAOYSA-N Hexa-Ac-myo-Inositol Natural products CC(=O)OC1C(OC(C)=O)C(OC(C)=O)C(OC(C)=O)C(OC(C)=O)C1OC(C)=O SQUHHTBVTRBESD-UHFFFAOYSA-N 0.000 description 1
- 241000238631 Hexapoda Species 0.000 description 1
- 108010093488 His-His-His-His-His-His Proteins 0.000 description 1
- 108060003951 Immunoglobulin Proteins 0.000 description 1
- 229930010555 Inosine Natural products 0.000 description 1
- UGQMRVRMYYASKQ-KQYNXXCUSA-N Inosine Chemical compound O[C@@H]1[C@H](O)[C@@H](CO)O[C@H]1N1C2=NC=NC(O)=C2N=C1 UGQMRVRMYYASKQ-KQYNXXCUSA-N 0.000 description 1
- 108091092195 Intron Proteins 0.000 description 1
- 102000029793 Isoleucine-tRNA ligase Human genes 0.000 description 1
- 108700040464 Isoleucine-tRNA ligases Proteins 0.000 description 1
- 108090001090 Lectins Proteins 0.000 description 1
- 102000004856 Lectins Human genes 0.000 description 1
- 108090001030 Lipoproteins Proteins 0.000 description 1
- 102000004895 Lipoproteins Human genes 0.000 description 1
- 108010052285 Membrane Proteins Proteins 0.000 description 1
- 102000018697 Membrane Proteins Human genes 0.000 description 1
- 241000699660 Mus musculus Species 0.000 description 1
- 241000699670 Mus sp. Species 0.000 description 1
- 238000000636 Northern blotting Methods 0.000 description 1
- 101710163270 Nuclease Proteins 0.000 description 1
- 108020005187 Oligonucleotide Probes Proteins 0.000 description 1
- 108010038807 Oligopeptides Proteins 0.000 description 1
- 102000015636 Oligopeptides Human genes 0.000 description 1
- 108700026244 Open Reading Frames Proteins 0.000 description 1
- 206010034133 Pathogen resistance Diseases 0.000 description 1
- 102000004022 Protein-Tyrosine Kinases Human genes 0.000 description 1
- 108090000412 Protein-Tyrosine Kinases Proteins 0.000 description 1
- 241000700159 Rattus Species 0.000 description 1
- 108700008625 Reporter Genes Proteins 0.000 description 1
- AUNGANRZJHBGPY-SCRDCRAPSA-N Riboflavin Chemical compound OC[C@@H](O)[C@@H](O)[C@@H](O)CN1C=2C=C(C)C(C)=CC=2N=C2C1=NC(=O)NC2=O AUNGANRZJHBGPY-SCRDCRAPSA-N 0.000 description 1
- 229940124639 Selective inhibitor Drugs 0.000 description 1
- 108020004682 Single-Stranded DNA Proteins 0.000 description 1
- 241000256248 Spodoptera Species 0.000 description 1
- 241000295644 Staphylococcaceae Species 0.000 description 1
- 108091081024 Start codon Proteins 0.000 description 1
- 241000187747 Streptomyces Species 0.000 description 1
- 241000701093 Suid alphaherpesvirus 1 Species 0.000 description 1
- 241000700618 Vaccinia virus Species 0.000 description 1
- 241000251539 Vertebrata <Metazoa> Species 0.000 description 1
- 206010048038 Wound infection Diseases 0.000 description 1
- 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 1
- 230000021736 acetylation Effects 0.000 description 1
- 238000006640 acetylation reaction Methods 0.000 description 1
- 238000003916 acid precipitation Methods 0.000 description 1
- 230000004913 activation Effects 0.000 description 1
- 230000010933 acylation Effects 0.000 description 1
- 238000005917 acylation reaction Methods 0.000 description 1
- 230000000996 additive effect Effects 0.000 description 1
- 230000002411 adverse Effects 0.000 description 1
- 239000000443 aerosol Substances 0.000 description 1
- 230000032683 aging Effects 0.000 description 1
- 230000009435 amidation Effects 0.000 description 1
- 238000007112 amidation reaction Methods 0.000 description 1
- BFNBIHQBYMNNAN-UHFFFAOYSA-N ammonium sulfate Chemical compound N.N.OS(O)(=O)=O BFNBIHQBYMNNAN-UHFFFAOYSA-N 0.000 description 1
- 229910052921 ammonium sulfate Inorganic materials 0.000 description 1
- 238000012870 ammonium sulfate precipitation Methods 0.000 description 1
- 235000011130 ammonium sulphate Nutrition 0.000 description 1
- 239000003708 ampul Substances 0.000 description 1
- 210000004102 animal cell Anatomy 0.000 description 1
- 238000010171 animal model Methods 0.000 description 1
- 238000005571 anion exchange chromatography Methods 0.000 description 1
- 150000001450 anions Chemical class 0.000 description 1
- 239000004599 antimicrobial Substances 0.000 description 1
- 239000003963 antioxidant agent Substances 0.000 description 1
- 239000007900 aqueous suspension Substances 0.000 description 1
- 230000010516 arginylation Effects 0.000 description 1
- 230000010065 bacterial adhesion Effects 0.000 description 1
- 230000008952 bacterial invasion Effects 0.000 description 1
- 230000008901 benefit Effects 0.000 description 1
- WQZGKKKJIJFFOK-VFUOTHLCSA-N beta-D-glucose Chemical compound OC[C@H]1O[C@@H](O)[C@H](O)[C@@H](O)[C@@H]1O WQZGKKKJIJFFOK-VFUOTHLCSA-N 0.000 description 1
- 108010005774 beta-Galactosidase Proteins 0.000 description 1
- 230000008827 biological function Effects 0.000 description 1
- 210000001124 body fluid Anatomy 0.000 description 1
- 239000010839 body fluid Substances 0.000 description 1
- 238000006664 bond formation reaction Methods 0.000 description 1
- 210000000988 bone and bone Anatomy 0.000 description 1
- 239000000872 buffer Substances 0.000 description 1
- 239000007975 buffered saline Substances 0.000 description 1
- 210000004899 c-terminal region Anatomy 0.000 description 1
- 210000000845 cartilage Anatomy 0.000 description 1
- 230000015556 catabolic process Effects 0.000 description 1
- 238000005277 cation exchange chromatography Methods 0.000 description 1
- 238000004113 cell culture Methods 0.000 description 1
- 210000002421 cell wall Anatomy 0.000 description 1
- 108091092356 cellular DNA Proteins 0.000 description 1
- 230000007969 cellular immunity Effects 0.000 description 1
- 238000012512 characterization method Methods 0.000 description 1
- 238000007385 chemical modification Methods 0.000 description 1
- 238000006243 chemical reaction Methods 0.000 description 1
- 239000003795 chemical substances by application Substances 0.000 description 1
- 235000013330 chicken meat Nutrition 0.000 description 1
- 238000003776 cleavage reaction Methods 0.000 description 1
- 238000000975 co-precipitation Methods 0.000 description 1
- 238000012875 competitive assay Methods 0.000 description 1
- 230000001010 compromised effect Effects 0.000 description 1
- 230000021615 conjugation Effects 0.000 description 1
- 210000002808 connective tissue Anatomy 0.000 description 1
- 239000012050 conventional carrier Substances 0.000 description 1
- 238000007796 conventional method Methods 0.000 description 1
- 229960003067 cystine Drugs 0.000 description 1
- 210000001151 cytotoxic T lymphocyte Anatomy 0.000 description 1
- 230000003247 decreasing effect Effects 0.000 description 1
- 238000006731 degradation reaction Methods 0.000 description 1
- 230000003111 delayed effect Effects 0.000 description 1
- 238000002716 delivery method Methods 0.000 description 1
- 230000017858 demethylation Effects 0.000 description 1
- 238000010520 demethylation reaction Methods 0.000 description 1
- 229960002086 dextran Drugs 0.000 description 1
- 229960000633 dextran sulfate Drugs 0.000 description 1
- 239000008121 dextrose Substances 0.000 description 1
- 238000003745 diagnosis Methods 0.000 description 1
- 238000000502 dialysis Methods 0.000 description 1
- 230000029087 digestion Effects 0.000 description 1
- 239000006185 dispersion Substances 0.000 description 1
- 229940079593 drug Drugs 0.000 description 1
- 239000003221 ear drop Substances 0.000 description 1
- 229940047652 ear drops Drugs 0.000 description 1
- 238000004520 electroporation Methods 0.000 description 1
- 238000005538 encapsulation Methods 0.000 description 1
- 210000002472 endoplasmic reticulum Anatomy 0.000 description 1
- 238000005516 engineering process Methods 0.000 description 1
- 238000012869 ethanol precipitation Methods 0.000 description 1
- 102000013165 exonuclease Human genes 0.000 description 1
- 238000002474 experimental method Methods 0.000 description 1
- 238000000605 extraction Methods 0.000 description 1
- 239000003889 eye drop Substances 0.000 description 1
- 229940012356 eye drops Drugs 0.000 description 1
- 239000003885 eye ointment Substances 0.000 description 1
- 230000022244 formylation Effects 0.000 description 1
- 238000006170 formylation reaction Methods 0.000 description 1
- 230000006870 function Effects 0.000 description 1
- 230000002538 fungal effect Effects 0.000 description 1
- 230000006251 gamma-carboxylation Effects 0.000 description 1
- 239000000499 gel Substances 0.000 description 1
- 230000007614 genetic variation Effects 0.000 description 1
- 238000003205 genotyping method Methods 0.000 description 1
- 150000003278 haem Chemical group 0.000 description 1
- 210000003709 heart valve Anatomy 0.000 description 1
- 238000004128 high performance liquid chromatography Methods 0.000 description 1
- 210000004408 hybridoma Anatomy 0.000 description 1
- 238000004191 hydrophobic interaction chromatography Methods 0.000 description 1
- 238000012872 hydroxylapatite chromatography Methods 0.000 description 1
- 230000033444 hydroxylation Effects 0.000 description 1
- 238000005805 hydroxylation reaction Methods 0.000 description 1
- 102000018358 immunoglobulin Human genes 0.000 description 1
- 230000003308 immunostimulating effect Effects 0.000 description 1
- 239000007943 implant Substances 0.000 description 1
- 230000001976 improved effect Effects 0.000 description 1
- 238000010348 incorporation Methods 0.000 description 1
- 239000012678 infectious agent Substances 0.000 description 1
- 230000002401 inhibitory effect Effects 0.000 description 1
- 230000000977 initiatory effect Effects 0.000 description 1
- 239000007972 injectable composition Substances 0.000 description 1
- 238000011081 inoculation Methods 0.000 description 1
- 229960003786 inosine Drugs 0.000 description 1
- CDAISMWEOUEBRE-GPIVLXJGSA-N inositol Chemical compound O[C@H]1[C@H](O)[C@@H](O)[C@H](O)[C@H](O)[C@@H]1O CDAISMWEOUEBRE-GPIVLXJGSA-N 0.000 description 1
- 229960000367 inositol Drugs 0.000 description 1
- 239000000543 intermediate Substances 0.000 description 1
- 230000026045 iodination Effects 0.000 description 1
- 238000006192 iodination reaction Methods 0.000 description 1
- 238000011005 laboratory method Methods 0.000 description 1
- 239000002523 lectin Substances 0.000 description 1
- 239000002502 liposome Substances 0.000 description 1
- 239000007788 liquid Substances 0.000 description 1
- 238000011068 loading method Methods 0.000 description 1
- 210000004698 lymphocyte Anatomy 0.000 description 1
- 210000004962 mammalian cell Anatomy 0.000 description 1
- 210000005075 mammary gland Anatomy 0.000 description 1
- 201000001441 melanoma Diseases 0.000 description 1
- 238000002844 melting Methods 0.000 description 1
- 230000008018 melting Effects 0.000 description 1
- 210000004379 membrane Anatomy 0.000 description 1
- 239000012528 membrane Substances 0.000 description 1
- MYWUZJCMWCOHBA-VIFPVBQESA-N methamphetamine Chemical compound CN[C@@H](C)CC1=CC=CC=C1 MYWUZJCMWCOHBA-VIFPVBQESA-N 0.000 description 1
- 230000011987 methylation Effects 0.000 description 1
- 238000007069 methylation reaction Methods 0.000 description 1
- 238000000520 microinjection Methods 0.000 description 1
- 239000011859 microparticle Substances 0.000 description 1
- 210000000214 mouth Anatomy 0.000 description 1
- 239000002324 mouth wash Substances 0.000 description 1
- 210000004400 mucous membrane Anatomy 0.000 description 1
- 229960003128 mupirocin Drugs 0.000 description 1
- 229930187697 mupirocin Natural products 0.000 description 1
- DDHVILIIHBIMQU-YJGQQKNPSA-L mupirocin calcium hydrate Chemical group O.O.[Ca+2].C[C@H](O)[C@H](C)[C@@H]1O[C@H]1C[C@@H]1[C@@H](O)[C@@H](O)[C@H](C\C(C)=C\C(=O)OCCCCCCCCC([O-])=O)OC1.C[C@H](O)[C@H](C)[C@@H]1O[C@H]1C[C@@H]1[C@@H](O)[C@@H](O)[C@H](C\C(C)=C\C(=O)OCCCCCCCCC([O-])=O)OC1 DDHVILIIHBIMQU-YJGQQKNPSA-L 0.000 description 1
- 238000002703 mutagenesis Methods 0.000 description 1
- 231100000350 mutagenesis Toxicity 0.000 description 1
- 230000007498 myristoylation Effects 0.000 description 1
- 239000003883 ointment base Substances 0.000 description 1
- XMLQWXUVTXCDDL-UHFFFAOYSA-N oleyl alcohol Natural products CCCCCCC=CCCCCCCCCCCO XMLQWXUVTXCDDL-UHFFFAOYSA-N 0.000 description 1
- 229940055577 oleyl alcohol Drugs 0.000 description 1
- 229940046166 oligodeoxynucleotide Drugs 0.000 description 1
- 239000002751 oligonucleotide probe Substances 0.000 description 1
- 238000011275 oncology therapy Methods 0.000 description 1
- 210000000056 organ Anatomy 0.000 description 1
- 230000000399 orthopedic effect Effects 0.000 description 1
- 230000002018 overexpression Effects 0.000 description 1
- 230000003647 oxidation Effects 0.000 description 1
- 238000007254 oxidation reaction Methods 0.000 description 1
- 238000007911 parenteral administration Methods 0.000 description 1
- 239000002245 particle Substances 0.000 description 1
- 230000007170 pathology Effects 0.000 description 1
- 230000035515 penetration Effects 0.000 description 1
- 238000010647 peptide synthesis reaction Methods 0.000 description 1
- 210000001322 periplasm Anatomy 0.000 description 1
- 238000002823 phage display Methods 0.000 description 1
- 239000008194 pharmaceutical composition Substances 0.000 description 1
- 239000000546 pharmaceutical excipient Substances 0.000 description 1
- 229940080469 phosphocellulose Drugs 0.000 description 1
- 230000008488 polyadenylation Effects 0.000 description 1
- 102000054765 polymorphisms of proteins Human genes 0.000 description 1
- 230000001323 posttranslational effect Effects 0.000 description 1
- 230000013823 prenylation Effects 0.000 description 1
- 239000003755 preservative agent Substances 0.000 description 1
- 230000002265 prevention Effects 0.000 description 1
- 230000003449 preventive effect Effects 0.000 description 1
- 230000001681 protective effect Effects 0.000 description 1
- 238000000159 protein binding assay Methods 0.000 description 1
- 230000009145 protein modification Effects 0.000 description 1
- 230000002797 proteolythic effect Effects 0.000 description 1
- 229940043131 pyroglutamate Drugs 0.000 description 1
- 230000006340 racemization Effects 0.000 description 1
- 230000002285 radioactive effect Effects 0.000 description 1
- 238000003127 radioimmunoassay Methods 0.000 description 1
- 239000011541 reaction mixture Substances 0.000 description 1
- 230000008929 regeneration Effects 0.000 description 1
- 238000011069 regeneration method Methods 0.000 description 1
- 230000001105 regulatory effect Effects 0.000 description 1
- 230000010076 replication Effects 0.000 description 1
- 230000004043 responsiveness Effects 0.000 description 1
- 230000001177 retroviral effect Effects 0.000 description 1
- 238000007363 ring formation reaction Methods 0.000 description 1
- 102220201851 rs143406017 Human genes 0.000 description 1
- 235000019515 salmon Nutrition 0.000 description 1
- 230000007017 scission Effects 0.000 description 1
- CDAISMWEOUEBRE-UHFFFAOYSA-N scyllo-inosotol Natural products OC1C(O)C(O)C(O)C(O)C1O CDAISMWEOUEBRE-UHFFFAOYSA-N 0.000 description 1
- 230000003248 secreting effect Effects 0.000 description 1
- 238000004904 shortening Methods 0.000 description 1
- 238000002791 soaking Methods 0.000 description 1
- 239000001509 sodium citrate Substances 0.000 description 1
- 239000001488 sodium phosphate Substances 0.000 description 1
- 229910000162 sodium phosphate Inorganic materials 0.000 description 1
- 230000000087 stabilizing effect Effects 0.000 description 1
- 239000007858 starting material Substances 0.000 description 1
- 230000001954 sterilising effect Effects 0.000 description 1
- 238000004659 sterilization and disinfection Methods 0.000 description 1
- 230000004936 stimulating effect Effects 0.000 description 1
- 210000002784 stomach Anatomy 0.000 description 1
- 230000006585 stringent response Effects 0.000 description 1
- 230000019635 sulfation Effects 0.000 description 1
- 238000005670 sulfation reaction Methods 0.000 description 1
- 230000004083 survival effect Effects 0.000 description 1
- 239000000375 suspending agent Substances 0.000 description 1
- 230000002194 synthesizing effect Effects 0.000 description 1
- 238000010189 synthetic method Methods 0.000 description 1
- 230000009885 systemic effect Effects 0.000 description 1
- 238000002560 therapeutic procedure Methods 0.000 description 1
- 230000003685 thermal hair damage Effects 0.000 description 1
- 239000002562 thickening agent Substances 0.000 description 1
- 230000000699 topical effect Effects 0.000 description 1
- 239000012049 topical pharmaceutical composition Substances 0.000 description 1
- 231100000419 toxicity Toxicity 0.000 description 1
- 230000001988 toxicity Effects 0.000 description 1
- 230000002110 toxicologic effect Effects 0.000 description 1
- 231100000759 toxicological effect Toxicity 0.000 description 1
- 238000011830 transgenic mouse model Methods 0.000 description 1
- 230000032258 transport Effects 0.000 description 1
- HRXKRNGNAMMEHJ-UHFFFAOYSA-K trisodium citrate Chemical compound [Na+].[Na+].[Na+].[O-]C(=O)CC(O)(CC([O-])=O)C([O-])=O HRXKRNGNAMMEHJ-UHFFFAOYSA-K 0.000 description 1
- 229940038773 trisodium citrate Drugs 0.000 description 1
- RYFMWSXOAZQYPI-UHFFFAOYSA-K trisodium phosphate Chemical compound [Na+].[Na+].[Na+].[O-]P([O-])([O-])=O RYFMWSXOAZQYPI-UHFFFAOYSA-K 0.000 description 1
- 238000010798 ubiquitination Methods 0.000 description 1
- 230000034512 ubiquitination Effects 0.000 description 1
- 241000701161 unidentified adenovirus Species 0.000 description 1
- 241000701447 unidentified baculovirus Species 0.000 description 1
- 241001430294 unidentified retrovirus Species 0.000 description 1
- 210000003708 urethra Anatomy 0.000 description 1
- 230000002485 urinary effect Effects 0.000 description 1
- 238000002255 vaccination Methods 0.000 description 1
- 230000003612 virological effect Effects 0.000 description 1
- 238000001262 western blot Methods 0.000 description 1
- 239000003357 wound healing promoting agent Substances 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
- 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)
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P31/00—Antiinfectives, i.e. antibiotics, antiseptics, chemotherapeutics
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P31/00—Antiinfectives, i.e. antibiotics, antiseptics, chemotherapeutics
- A61P31/04—Antibacterial agents
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P37/00—Drugs for immunological or allergic disorders
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P37/00—Drugs for immunological or allergic disorders
- A61P37/02—Immunomodulators
- A61P37/04—Immunostimulants
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K14/00—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof
- C07K14/195—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from bacteria
- C07K14/315—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from bacteria from Streptococcus (G), e.g. Enterococci
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K14/00—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof
- C07K14/195—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from bacteria
- C07K14/315—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from bacteria from Streptococcus (G), e.g. Enterococci
- C07K14/3153—Streptokinase
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K14/00—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof
- C07K14/195—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from bacteria
- C07K14/315—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from bacteria from Streptococcus (G), e.g. Enterococci
- C07K14/3156—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from bacteria from Streptococcus (G), e.g. Enterococci from Streptococcus pneumoniae (Pneumococcus)
-
- G—PHYSICS
- G01—MEASURING; TESTING
- G01N—INVESTIGATING OR ANALYSING MATERIALS BY DETERMINING THEIR CHEMICAL OR PHYSICAL PROPERTIES
- G01N33/00—Investigating or analysing materials by specific methods not covered by groups G01N1/00 - G01N31/00
- G01N33/48—Biological material, e.g. blood, urine; Haemocytometers
- G01N33/50—Chemical analysis of biological material, e.g. blood, urine; Testing involving biospecific ligand binding methods; Immunological testing
- G01N33/53—Immunoassay; Biospecific binding assay; Materials therefor
- G01N33/569—Immunoassay; Biospecific binding assay; Materials therefor for microorganisms, e.g. protozoa, bacteria, viruses
- G01N33/56911—Bacteria
- G01N33/56944—Streptococcus
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61K—PREPARATIONS FOR MEDICAL, DENTAL OR TOILETRY PURPOSES
- A61K39/00—Medicinal preparations containing antigens or antibodies
- A61K2039/51—Medicinal preparations containing antigens or antibodies comprising whole cells, viruses or DNA/RNA
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61K—PREPARATIONS FOR MEDICAL, DENTAL OR TOILETRY PURPOSES
- A61K38/00—Medicinal preparations containing peptides
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61K—PREPARATIONS FOR MEDICAL, DENTAL OR TOILETRY PURPOSES
- A61K39/00—Medicinal preparations containing antigens or antibodies
Landscapes
- Health & Medical Sciences (AREA)
- Chemical & Material Sciences (AREA)
- Life Sciences & Earth Sciences (AREA)
- Organic Chemistry (AREA)
- General Health & Medical Sciences (AREA)
- Medicinal Chemistry (AREA)
- Engineering & Computer Science (AREA)
- Molecular Biology (AREA)
- Genetics & Genomics (AREA)
- Biochemistry (AREA)
- Immunology (AREA)
- Biophysics (AREA)
- Proteomics, Peptides & Aminoacids (AREA)
- Gastroenterology & Hepatology (AREA)
- Biomedical Technology (AREA)
- Bioinformatics & Cheminformatics (AREA)
- General Chemical & Material Sciences (AREA)
- Chemical Kinetics & Catalysis (AREA)
- Nuclear Medicine, Radiotherapy & Molecular Imaging (AREA)
- Pharmacology & Pharmacy (AREA)
- Animal Behavior & Ethology (AREA)
- Public Health (AREA)
- Veterinary Medicine (AREA)
- Urology & Nephrology (AREA)
- Hematology (AREA)
- Zoology (AREA)
- Biotechnology (AREA)
- Microbiology (AREA)
- Wood Science & Technology (AREA)
- Communicable Diseases (AREA)
- Pathology (AREA)
- Tropical Medicine & Parasitology (AREA)
- Virology (AREA)
- Cell Biology (AREA)
- Oncology (AREA)
- Pulmonology (AREA)
- Food Science & Technology (AREA)
- Physics & Mathematics (AREA)
- Analytical Chemistry (AREA)
- General Physics & Mathematics (AREA)
Applications Claiming Priority (3)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| GBGB9607993.4A GB9607993D0 (en) | 1996-04-18 | 1996-04-18 | Novel compounds |
| GB9607993.4 | 1996-04-18 | ||
| PCT/US1997/006879 WO1997038719A1 (en) | 1996-04-18 | 1997-04-18 | Novel compounds |
Publications (1)
| Publication Number | Publication Date |
|---|---|
| JP2000515366A true JP2000515366A (ja) | 2000-11-21 |
Family
ID=10792237
Family Applications (6)
| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| JP09537430A Pending JP2000510688A (ja) | 1996-04-18 | 1997-04-18 | ストレプトコッカス・ニューモニアエのアスパルチルｔＲＮＡシンセターゼ |
| JP09537450A Pending JP2000509975A (ja) | 1996-04-18 | 1997-04-18 | 新規化合物 |
| JP09537428A Pending JP2000515724A (ja) | 1996-04-18 | 1997-04-18 | 新規化合物 |
| JP9537451A Pending JP2000509264A (ja) | 1996-04-18 | 1997-04-18 | ストレプトコッカス・ニューモニアエのヒスチジルｔＲＮＡシンセターゼ |
| JP09537452A Pending JP2000515366A (ja) | 1996-04-18 | 1997-04-18 | 新規化合物 |
| JP9537449A Pending JP2000509263A (ja) | 1996-04-18 | 1997-04-18 | 新規化合物 |
Family Applications Before (4)
| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| JP09537430A Pending JP2000510688A (ja) | 1996-04-18 | 1997-04-18 | ストレプトコッカス・ニューモニアエのアスパルチルｔＲＮＡシンセターゼ |
| JP09537450A Pending JP2000509975A (ja) | 1996-04-18 | 1997-04-18 | 新規化合物 |
| JP09537428A Pending JP2000515724A (ja) | 1996-04-18 | 1997-04-18 | 新規化合物 |
| JP9537451A Pending JP2000509264A (ja) | 1996-04-18 | 1997-04-18 | ストレプトコッカス・ニューモニアエのヒスチジルｔＲＮＡシンセターゼ |
Family Applications After (1)
| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| JP9537449A Pending JP2000509263A (ja) | 1996-04-18 | 1997-04-18 | 新規化合物 |
Country Status (5)
| Country | Link |
|---|---|
| US (9) | US5747313A (enExample) |
| EP (6) | EP0909181A4 (enExample) |
| JP (6) | JP2000510688A (enExample) |
| GB (1) | GB9607993D0 (enExample) |
| WO (6) | WO1997038719A1 (enExample) |
Families Citing this family (47)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| US5834276A (en) * | 1996-04-18 | 1998-11-10 | Smithkline Beecham Corporation | Asparaginyl TRNA synthetase polynucleotides of streptococcus |
| US5795758A (en) * | 1997-04-18 | 1998-08-18 | Smithkline Beecham Corporation | DNA encoding histidyl tRNA synthetase variant from Streptococcus pneumoniae |
| US5858720A (en) * | 1997-07-23 | 1999-01-12 | Smithkline Beecham Corporation | Hiss |
| US5882892A (en) | 1997-07-23 | 1999-03-16 | Smithkline Beecham Corporation | Asps |
| EP0916728A1 (en) * | 1997-10-17 | 1999-05-19 | Smithkline Beecham Corporation | Phenyl alanyl tRNA synthetase [EC 6.1.1.20] alpha subunit family, pheS (alpha), from Streptococcus pneumoniae |
| EP1040200A4 (en) | 1997-11-25 | 2005-04-20 | Gen Hospital Corp | NUCLEOTIDE SEQUENCES ASSOCIATED WITH VIRULENCE AND USES THEREOF |
| JP2002516078A (ja) * | 1998-05-28 | 2002-06-04 | スミスクライン・ビーチャム・コーポレイション | ａｃｐＳ |
| US6245539B1 (en) | 1998-10-06 | 2001-06-12 | Board Of Trustees Operating Michigan State University | Human asparaginyl-tRNA synthetase DNA |
| WO2001040332A1 (en) | 1999-11-29 | 2001-06-07 | Daikin Industries, Ltd. | Fluororesin material lowly permeable to liquid chemical |
| US7112716B2 (en) | 2000-04-06 | 2006-09-26 | The General Hospital Corporation | Methods for screening and identifying host pathogen defense genes |
| WO2009152247A2 (en) | 2008-06-11 | 2009-12-17 | Atyr Pharma, Inc | Thrombopoietic activity of tyrosyl-trna synthetase polypeptides |
| WO2009158649A1 (en) | 2008-06-26 | 2009-12-30 | Atyr Pharma, Inc. | Compositions and methods comprising glycyl-trna synthetases having non-canonical biological activities |
| WO2010099477A2 (en) | 2009-02-27 | 2010-09-02 | Atyr Pharma, Inc. | Polypeptide structural motifs associated with cell signaling activity |
| DK3255146T3 (da) | 2009-03-16 | 2019-08-19 | Pangu Biopharma Ltd | Præparater og fremgangsmåder omfattende histidyl-tRNA-synthetasesplejsningsvarianter med ikke-kanoniske biologiske aktiviteter |
| JP5848236B2 (ja) | 2009-03-31 | 2016-01-27 | エータイアー ファーマ， インコーポレイテッド | 非標準的な生物活性を有するアスパルチルｔＲＮＡ合成酵素を含む組成物および方法 |
| US8828395B2 (en) | 2009-12-11 | 2014-09-09 | Atyr Pharma, Inc. | Antibodies that bind tyrosyl-tRNA synthetases |
| ES2535951T3 (es) | 2009-12-11 | 2015-05-19 | Atyr Pharma, Inc. | Histidil ARNt sintetasas para reducir la inflamación |
| CA2797093C (en) | 2010-04-26 | 2019-10-29 | Atyr Pharma, Inc. | Innovative discovery of therapeutic, diagnostic, and antibody compositions related to protein fragments of cysteinyl-trna synthetase |
| EP2563381B1 (en) | 2010-04-27 | 2017-08-09 | aTyr Pharma, Inc. | Innovative discovery of therapeutic, diagnostic, and antibody compositions related to protein fragments of isoleucyl trna synthetases |
| CN108165537A (zh) | 2010-04-27 | 2018-06-15 | Atyr医药公司 | 与苏氨酰-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 |
| CN103097524B (zh) | 2010-04-28 | 2016-08-03 | Atyr医药公司 | 与丙氨酰-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 |
| JP5991963B2 (ja) | 2010-04-29 | 2016-09-14 | エータイアー ファーマ， インコーポレイテッド | バリルｔＲＮＡ合成酵素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 |
| US9068177B2 (en) | 2010-04-29 | 2015-06-30 | Atyr Pharma, Inc | Innovative discovery of therapeutic, diagnostic, and antibody compositions related to protein fragments of glutaminyl-tRNA synthetases |
| CN103097523B (zh) | 2010-04-29 | 2016-09-28 | Atyr医药公司 | 与天冬酰胺酰-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 |
| 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 |
| JP6008840B2 (ja) | 2010-05-03 | 2016-10-19 | エータイアー ファーマ， インコーポレイテッド | フェニルアラニルαｔＲＮＡ合成酵素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 |
| JP6008841B2 (ja) | 2010-05-03 | 2016-10-19 | エータイアー ファーマ， インコーポレイテッド | メチオニルｔＲＮＡ合成酵素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 |
| WO2011139988A2 (en) | 2010-05-03 | 2011-11-10 | Atyr Pharma, Inc. | Innovative discovery of therapeutic, diagnostic, and antibody compositions related to protein fragments of seryl-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 |
| 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 |
| JP6396656B2 (ja) | 2010-05-14 | 2018-09-26 | エータイアー ファーマ， インコーポレイテッド | フェニルアラニルβｔＲＮＡ合成酵素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 |
| US9034598B2 (en) | 2010-05-17 | 2015-05-19 | Atyr Pharma, Inc. | Innovative discovery of therapeutic, diagnostic, and antibody compositions related to protein fragments of leucyl-tRNA synthetases |
| US8962560B2 (en) | 2010-06-01 | 2015-02-24 | Atyr Pharma Inc. | Innovative discovery of therapeutic, diagnostic, and antibody compositions related to protein fragments of Lysyl-tRNA synthetases |
| JP5991973B2 (ja) | 2010-07-12 | 2016-09-14 | エータイアー ファーマ， インコーポレイテッド | アスパルチルｔＲＮＡ合成酵素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 |
| EP2593126B1 (en) | 2010-07-12 | 2017-09-20 | aTyr Pharma, Inc. | Innovative discovery of therapeutic, diagnostic, and antibody compositions related to protein fragments of histidyl-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 |
| AU2011289831C1 (en) | 2010-07-12 | 2017-06-15 | Pangu Biopharma Limited | Innovative discovery of therapeutic, diagnostic, and antibody compositions related to protein fragments of glycyl-tRNA synthetases |
| 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 |
| AU2011311956C1 (en) | 2010-10-06 | 2017-06-15 | Pangu Biopharma Limited | Innovative discovery of therapeutic, diagnostic, and antibody compositions related protein fragments of tryptophanyl tRNA synthetases |
| WO2013022982A2 (en) | 2011-08-09 | 2013-02-14 | Atyr Pharma, Inc. | Pegylated tyrosyl-trna synthetase polypeptides |
| US9816084B2 (en) | 2011-12-06 | 2017-11-14 | Atyr Pharma, Inc. | Aspartyl-tRNA synthetases |
| WO2013086228A1 (en) | 2011-12-06 | 2013-06-13 | Atyr Pharma, Inc. | Pegylated aspartyl-trna synthetase polypeptides |
| EP2797959A4 (en) | 2011-12-29 | 2015-08-26 | Atyr Pharma Inc | ASPARTYL-tRNA synthetase FC CONJUGATES |
| AU2013221317B2 (en) | 2012-02-16 | 2017-07-06 | Pangu Biopharma Limited | Histidyl-tRNA synthetases for treating autoimmune and inflammatory diseases |
| CA2907046C (en) | 2013-03-15 | 2021-04-20 | Atyr Pharma, Inc. | Histidyl-trna synthetase-fc conjugates |
| WO2018195338A1 (en) | 2017-04-20 | 2018-10-25 | Atyr Pharma, Inc. | Compositions and methods for treating lung inflammation |
| EP4085919A3 (en) | 2017-07-21 | 2023-02-08 | Novartis AG | Compositions and methods to treat cancer |
Family Cites Families (6)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| AU6958194A (en) * | 1993-05-28 | 1994-12-20 | Massachusetts Institute Of Technology | Trna binding-dependent inhibition of microbial pathogen growth |
| AU5552396A (en) * | 1995-04-21 | 1996-11-07 | Human Genome Sciences, Inc. | Nucleotide sequence of the haemophilus influenzae rd genome, fragments thereof, and uses thereof |
| US6737248B2 (en) * | 1996-01-05 | 2004-05-18 | Human Genome Sciences, Inc. | Staphylococcus aureus polynucleotides and sequences |
| EP1300468A3 (en) * | 1996-01-19 | 2004-02-04 | Smithkline Beecham Plc | TRNA synthetase |
| WO1997026348A1 (en) * | 1996-01-19 | 1997-07-24 | Smithkline Beecham Plc | ASPARAGINYL tRNA SYNTHETASE OF STAPHYLOCOCCUS AUREUS |
| US6420135B1 (en) * | 1996-10-31 | 2002-07-16 | Human Genome Sciences, Inc. | Streptococcus pneumoniae polynucleotides and sequences |
-
1996
- 1996-04-18 GB GBGB9607993.4A patent/GB9607993D0/en active Pending
-
1997
- 1997-04-18 EP EP97922434A patent/EP0909181A4/en not_active Withdrawn
- 1997-04-18 US US08/844,055 patent/US5747313A/en not_active Expired - Fee Related
- 1997-04-18 JP JP09537430A patent/JP2000510688A/ja active Pending
- 1997-04-18 WO PCT/US1997/006879 patent/WO1997038719A1/en not_active Ceased
- 1997-04-18 JP JP09537450A patent/JP2000509975A/ja active Pending
- 1997-04-18 WO PCT/US1997/006877 patent/WO1997039017A1/en not_active Ceased
- 1997-04-18 US US08/844,280 patent/US5747315A/en not_active Expired - Fee Related
- 1997-04-18 US US08/844,154 patent/US5827708A/en not_active Expired - Fee Related
- 1997-04-18 JP JP09537428A patent/JP2000515724A/ja active Pending
- 1997-04-18 EP EP97921302A patent/EP0904280A4/en not_active Withdrawn
- 1997-04-18 US US08/843,521 patent/US5753479A/en not_active Expired - Lifetime
- 1997-04-18 EP EP97918764A patent/EP0894006A4/en not_active Withdrawn
- 1997-04-18 JP JP9537451A patent/JP2000509264A/ja active Pending
- 1997-04-18 EP EP97921361A patent/EP0904281A4/en not_active Withdrawn
- 1997-04-18 JP JP09537452A patent/JP2000515366A/ja active Pending
- 1997-04-18 JP JP9537449A patent/JP2000509263A/ja active Pending
- 1997-04-18 EP EP97918806A patent/EP0904104A4/en not_active Withdrawn
- 1997-04-18 WO PCT/US1997/006638 patent/WO1997039014A1/en not_active Ceased
- 1997-04-18 WO PCT/US1997/006634 patent/WO1997038717A1/en not_active Ceased
- 1997-04-18 WO PCT/US1997/006876 patent/WO1997038722A1/en not_active Ceased
- 1997-04-18 US US08/844,086 patent/US5866390A/en not_active Expired - Lifetime
- 1997-04-18 WO PCT/US1997/006875 patent/WO1997039022A1/en not_active Ceased
- 1997-04-18 EP EP97923452A patent/EP0951469A1/en not_active Withdrawn
-
1998
- 1998-01-14 US US09/006,849 patent/US6071731A/en not_active Expired - Fee Related
- 1998-01-23 US US09/012,871 patent/US6200787B1/en not_active Expired - Fee Related
- 1998-02-03 US US09/018,211 patent/US6048716A/en not_active Expired - Lifetime
- 1998-07-30 US US09/126,192 patent/US6040163A/en not_active Expired - Fee Related
Also Published As
| Publication number | Publication date |
|---|---|
| US6200787B1 (en) | 2001-03-13 |
| US5827708A (en) | 1998-10-27 |
| US6048716A (en) | 2000-04-11 |
| EP0904280A4 (en) | 1999-10-20 |
| EP0904104A4 (en) | 1999-11-03 |
| US5747315A (en) | 1998-05-05 |
| EP0904281A1 (en) | 1999-03-31 |
| EP0904281A4 (en) | 2000-01-12 |
| EP0951469A4 (enExample) | 1999-11-03 |
| US5866390A (en) | 1999-02-02 |
| EP0894006A1 (en) | 1999-02-03 |
| US6071731A (en) | 2000-06-06 |
| WO1997038717A1 (en) | 1997-10-23 |
| JP2000515724A (ja) | 2000-11-28 |
| US6040163A (en) | 2000-03-21 |
| WO1997038719A1 (en) | 1997-10-23 |
| JP2000509263A (ja) | 2000-07-25 |
| EP0904104A1 (en) | 1999-03-31 |
| EP0951469A1 (en) | 1999-10-27 |
| US5753479A (en) | 1998-05-19 |
| US5747313A (en) | 1998-05-05 |
| GB9607993D0 (en) | 1996-06-19 |
| WO1997038722A1 (en) | 1997-10-23 |
| EP0909181A4 (en) | 1999-11-03 |
| WO1997039022A1 (en) | 1997-10-23 |
| EP0894006A4 (en) | 1999-11-24 |
| JP2000510688A (ja) | 2000-08-22 |
| JP2000509975A (ja) | 2000-08-08 |
| EP0904280A1 (en) | 1999-03-31 |
| WO1997039014A1 (en) | 1997-10-23 |
| EP0909181A1 (en) | 1999-04-21 |
| JP2000509264A (ja) | 2000-07-25 |
| WO1997039017A1 (en) | 1997-10-23 |
Similar Documents
| Publication | Publication Date | Title |
|---|---|---|
| JP2000515366A (ja) | 新規化合物 | |
| JP2001519651A (ja) | 新規化合物 | |
| JP2000512487A (ja) | 新規化合物 | |
| JPH11137280A (ja) | 新規ｈｉｓＳ | |
| JP2002142784A (ja) | 新規ｈｉｓＳ | |
| JPH11127878A (ja) | 新規ＲａｔＡ | |
| JPH11215990A (ja) | 新規ｐｈｅＳ | |
| JP2002504304A (ja) | ｒｉｂＨ | |
| JP2000512485A (ja) | 新規化合物 | |
| JP2000509261A (ja) | 新規化合物 | |
| JPH1198993A (ja) | 新規化合物 | |
| JP2001504682A (ja) | 新規化合物 | |
| JP2000509260A (ja) | ストレプトコッカス・ニューモニアエのイソロイシルｔＲＮＡシンセターゼ | |
| JP2002247994A (ja) | 新規ＲａｔＢ | |
| JP2001521371A (ja) | ストレプトコッカス・ニューモニアエのチロシルｔＲＮＡシンセターゼ | |
| JP2000509984A (ja) | 新規化合物 | |
| JP2000508543A (ja) | ストレプトコッカス・ニューモニアエのメチオニルｔＲＮＡシンセターゼ | |
| JP2001509682A (ja) | 新規ストレプトコッカスｅｒｓ | |
| JPH11187887A (ja) | 新規ＬｙｓＳ | |
| JP2002504312A (ja) | ｒｉｂＢ | |
| JP2000510335A (ja) | 新規化合物 | |
| JP2002253274A (ja) | 新規化合物 | |
| JPH11262392A (ja) | 新規ＭｕｒＥ | |
| JP2002504310A (ja) | ｒｉｂＡ | |
| JP2002247995A (ja) | 新規ｆｆｈ |