ES2324608T3 - Incorporacion especifica de sitio de cetoaminoacidos en proteinas. - Google Patents
Incorporacion especifica de sitio de cetoaminoacidos en proteinas. Download PDFInfo
- Publication number
- ES2324608T3 ES2324608T3 ES03809019T ES03809019T ES2324608T3 ES 2324608 T3 ES2324608 T3 ES 2324608T3 ES 03809019 T ES03809019 T ES 03809019T ES 03809019 T ES03809019 T ES 03809019T ES 2324608 T3 ES2324608 T3 ES 2324608T3
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- Prior art keywords
- trna
- cell
- protein
- phenylalanine
- acetyl
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- C12N—MICROORGANISMS OR ENZYMES; COMPOSITIONS THEREOF; PROPAGATING, PRESERVING, OR MAINTAINING MICROORGANISMS; MUTATION OR GENETIC ENGINEERING; CULTURE MEDIA
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- 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
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- A61K38/16—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof
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- 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
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- 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
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- C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
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- C12N15/11—DNA or RNA fragments; Modified forms thereof; Non-coding nucleic acids having a biological activity
- C12N15/52—Genes encoding for enzymes or proenzymes
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- C12N9/93—Ligases (6)
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- C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
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| EP1490483B1 (en) * | 2001-04-19 | 2015-06-03 | The Scripps Research Institute | In vivo incorporation of unnatural amino acids |
| KR20050073559A (ko) | 2002-10-16 | 2005-07-14 | 더 스크립스 리서치 인스티튜트 | 당단백질 합성 |
| CN103289960B (zh) | 2003-04-17 | 2017-04-26 | 斯克利普斯研究院 | 扩展真核生物遗传密码 |
| WO2005003294A2 (en) | 2003-06-18 | 2005-01-13 | The Scripps Research Institute | Unnatural reactive amino acid genetic code additions |
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| DE602004011789T2 (de) * | 2003-07-07 | 2009-02-12 | The Scripps Research Institute, La Jolla | Zusammensetzungen der orthogonalen Lysyl-tRNA und Aminoacyl-tRNA Synthetase Paaren und ihre Verwendungen |
| WO2005038002A2 (en) | 2003-10-14 | 2005-04-28 | The Scripps Research Institute | Site-specific incorporation of redox active amino acids into proteins |
| WO2006069220A2 (en) | 2004-12-22 | 2006-06-29 | Ambrx, Inc. | Modified human growth hormone |
| BRPI0507159A (pt) | 2004-02-02 | 2007-06-26 | Ambrx Inc | polipeptìdeos em feixe de quatro hélices humanos modificados e seus usos |
| 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 |
| KR20070034512A (ko) | 2004-06-18 | 2007-03-28 | 암브룩스, 인코포레이티드 | 신규 항원-결합 폴리펩티드 및 이의 용도 |
| MX2007000728A (es) | 2004-07-21 | 2007-03-15 | Ambrx Inc | Polipeptidos biosinteticos que utilizan amino acidos no naturalmente codificados. |
| EP1794323B1 (en) | 2004-09-21 | 2014-08-06 | The Scripps Research Institute | In vivo incorporation of alkynyl amino acids into proteins in eubacteria |
| JP2008513806A (ja) * | 2004-09-22 | 2008-05-01 | ザ スクリップス リサーチ インスティテュート | Ｎｍｒ試験のための蛋白質の部位特異的標識 |
| EP1809758A4 (en) | 2004-10-20 | 2009-04-01 | Scripps Research Inst | LOCAL IN VIVO INSTALLATION OF N-ACETYLGALACTOSAMINE AMINO ACIDS IN EU BACTERIA |
| AU2005330514B2 (en) | 2004-10-27 | 2011-05-12 | The Scripps Research Institute | Orthogonal translation components for the in vivo incorporation of unnatural amino acids |
| CA2590429C (en) | 2004-12-22 | 2014-10-07 | Ambrx, Inc. | Compositions of aminoacyl-trna synthetase and uses thereof |
| CA2594561C (en) | 2004-12-22 | 2014-12-23 | Ambrx, Inc. | Formulations of human growth hormone comprising a non-naturally encoded amino acid |
| US8080391B2 (en) | 2004-12-22 | 2011-12-20 | Ambrx, Inc. | Process of producing non-naturally encoded amino acid containing high conjugated to a water soluble polymer |
| GB2438982A (en) | 2004-12-22 | 2007-12-12 | Ambrx Inc | Compostions containing, methods involving, and uses of non-natural amino acids and polypeptides |
| WO2006133088A2 (en) | 2005-06-03 | 2006-12-14 | Ambrx, Inc. | Improved human interferon molecules and their uses |
| US20090306023A1 (en) * | 2005-06-29 | 2009-12-10 | Ramirez Jose E | Stable organic peroxide compositions |
| CA2624290A1 (en) * | 2005-10-12 | 2007-04-26 | Scripps Research Institute | Selective posttranslational modification of phage-displayed polypeptides |
| JP2009520949A (ja) | 2005-11-16 | 2009-05-28 | アンブルックス，インコーポレイテッド | 非天然アミノ酸を含んでいる組成物および方法 |
| EP1968635B1 (en) | 2005-12-14 | 2014-09-17 | Ambrx, Inc. | Compositions containing, methods involving, and uses of non-natural amino acids and polypeptides |
| WO2007092475A2 (en) * | 2006-02-06 | 2007-08-16 | Franklin And Marshall College | Site-specific incorporation of fluorinated amino acids into proteins |
| CA2638763A1 (en) * | 2006-03-09 | 2007-09-13 | The Scripps Research Institute | System for the expression of orthogonal translation components in eubacterial host cells |
| JP5249194B2 (ja) * | 2006-03-16 | 2013-07-31 | ザ スクリプス リサーチ インスティチュート | 非天然アミノ酸フェニルセレノシステインを含有するタンパク質の遺伝的にプログラムされた発現 |
| BRPI0711811A2 (pt) * | 2006-05-23 | 2011-12-06 | Scripps Research Inst | aminoácidos de cumarina fluorescente geneticamente codificados |
| ES2465473T3 (es) | 2006-09-08 | 2014-06-05 | Ambrx, Inc. | Transcripción de arnt supresor en células de vertebrado |
| PT2061878E (pt) * | 2006-09-08 | 2014-04-22 | Ambrx Inc | Supressor híbrido arnt para células de vertebrados |
| WO2008030558A2 (en) | 2006-09-08 | 2008-03-13 | Ambrx, Inc. | Modified human plasma polypeptide or fc scaffolds and their uses |
| CA2663052A1 (en) | 2006-09-21 | 2008-03-27 | The Scripps Research Institute | Genetically programmed expression of selectively sulfated proteins in eubacteria |
| WO2008049034A1 (en) * | 2006-10-17 | 2008-04-24 | Zymera, Inc. | System for assays of aminotranferase |
| US20080166766A1 (en) | 2006-10-18 | 2008-07-10 | The Scripps Research Institute | Genetic incorporation of unnatural amino acids into proteins in mammalian cells |
| GB0623974D0 (en) | 2006-11-30 | 2007-01-10 | Medical Res Council | Evolved orthogonal ribosomes |
| JP2010523084A (ja) | 2007-03-30 | 2010-07-15 | アンブルックス，インコーポレイテッド | 修飾ｆｇｆ−２１ポリペプチド |
| WO2008137471A2 (en) | 2007-05-02 | 2008-11-13 | Ambrx, Inc. | Modified interferon beta polypeptides and their uses |
| KR101656107B1 (ko) | 2007-11-20 | 2016-09-08 | 암브룩스, 인코포레이티드 | 변형된 인슐린 폴리펩티드 및 이의 용도 |
| CA2712606A1 (en) | 2008-02-08 | 2009-08-13 | Ambrx, Inc. | Modified leptin polypeptides and their uses |
| NZ591235A (en) | 2008-07-23 | 2012-07-27 | Ambrx Inc | Modified bovine g-csf polypeptides comprising non natural amino acid and their uses treating infections such as mastitis |
| BRPI0919403A2 (pt) | 2008-09-26 | 2017-09-26 | Ambrx Inc | polipeptídeos modificados de eritropoetina animal e seus usos |
| DK2337846T3 (en) | 2008-09-26 | 2018-03-12 | Ambrx Inc | NON-NATURAL AMINO ACID REPLICATION DEPENDENT MICROORGANISMS AND VACCINES |
| WO2011073738A1 (en) | 2009-12-14 | 2011-06-23 | Metabolic Explorer | Use of inducible promoters in the production of methionine |
| BR112012015597A2 (pt) | 2009-12-21 | 2017-01-31 | Ambrx Inc | peptídeos de somatotropina suínos modificados e seus usos |
| PE20121707A1 (es) | 2009-12-21 | 2012-12-17 | Ambrx Inc | Polipeptidos de somatotropina bovina modificados y sus usos |
| KR101963460B1 (ko) | 2010-08-17 | 2019-03-28 | 암브룩스, 인코포레이티드 | 변형된 릴랙신 폴리펩타이드 및 그것의 용도 |
| US9567386B2 (en) | 2010-08-17 | 2017-02-14 | Ambrx, Inc. | Therapeutic uses of modified relaxin polypeptides |
| AR083006A1 (es) | 2010-09-23 | 2013-01-23 | Lilly Co Eli | Formulaciones para el factor estimulante de colonias de granulocitos (g-csf) bovino y variantes de las mismas |
| 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 |
| UY35368A (es) | 2013-03-08 | 2014-10-31 | Irm Llc | Péptidos y composiciones para el tratamiento de daño articular |
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| WO2016004024A1 (en) | 2014-07-02 | 2016-01-07 | Sutro Biopharma, Inc. | High growth capacity auxotrophic escherichia coli and methods of use |
| CN107108710B (zh) | 2014-10-24 | 2022-02-15 | 百时美施贵宝公司 | 修饰的fgf-21多肽及其用途 |
| CN114656483A (zh) | 2014-12-04 | 2022-06-24 | 细胞基因公司 | 生物分子共轭物 |
| US9744624B2 (en) * | 2015-06-17 | 2017-08-29 | Kinsus Interconnect Technology Corp. | Method for manufacturing circuit board |
| IL266361B2 (en) | 2016-11-14 | 2024-02-01 | Novartis Ag | Methods and preparations for the treatment of cartilage damage and arthritis |
| US11339209B2 (en) | 2016-11-14 | 2022-05-24 | Novartis Ag | Compositions, methods, and therapeutic uses related to fusogenic protein minion |
| MX2019008449A (es) | 2017-02-08 | 2019-09-09 | Bristol Myers Squibb Co | Polipetidos de relaxina modificada que comprenden un mejorador farmacocinetico y sus usos. |
| 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 |
| EP4598586A1 (en) | 2022-10-07 | 2025-08-13 | Ambrx, Inc. | Drug linkers and antibody conjugates thereof |
| WO2024091824A1 (en) | 2022-10-26 | 2024-05-02 | Ada Forsyth Institute, Inc. | Differentiation and reprogramming of chondrocyte |
| KR20250134670A (ko) | 2023-01-16 | 2025-09-11 | 암브룩스, 인코포레이티드 | 항-cd70 항체-약물 접합체 |
| WO2024178310A1 (en) | 2023-02-23 | 2024-08-29 | Ambrx, Inc. | Trop2-directed antibody-drug conjugates and uses thereof |
| WO2024241086A1 (en) | 2023-05-24 | 2024-11-28 | Ambrx, Inc. | Pegylated bovine interferon lambda and methods of use thereof |
| WO2025041055A1 (en) | 2023-08-22 | 2025-02-27 | Ambrx, Inc. | Anti-psma adc conjugate compositions and methods of use thereof |
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| JPH11504218A (ja) | 1995-04-24 | 1999-04-20 | クロマゾーム コーポレーション | 新規代謝経路の生成およびスクリーニングのための方法 |
| 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 |
| EP1490483B1 (en) * | 2001-04-19 | 2015-06-03 | The Scripps Research Institute | In vivo incorporation of unnatural amino acids |
| KR20050073559A (ko) * | 2002-10-16 | 2005-07-14 | 더 스크립스 리서치 인스티튜트 | 당단백질 합성 |
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