MXPA03009566A - Metodos y composicion para la produccion de pares trna-aminoaciltrna sintetasa ortogonales. - Google Patents
Metodos y composicion para la produccion de pares trna-aminoaciltrna sintetasa ortogonales.Info
- Publication number
- MXPA03009566A MXPA03009566A MXPA03009566A MXPA03009566A MXPA03009566A MX PA03009566 A MXPA03009566 A MX PA03009566A MX PA03009566 A MXPA03009566 A MX PA03009566A MX PA03009566 A MXPA03009566 A MX PA03009566A MX PA03009566 A MXPA03009566 A MX PA03009566A
- Authority
- MX
- Mexico
- Prior art keywords
- trna
- amino acid
- organism
- screening
- codon
- Prior art date
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- C12P13/00—Preparation of nitrogen-containing organic compounds
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- 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
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Applications Claiming Priority (3)
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| US28503001P | 2001-04-19 | 2001-04-19 | |
| US35551402P | 2002-02-06 | 2002-02-06 | |
| PCT/US2002/012635 WO2002086075A2 (en) | 2001-04-19 | 2002-04-19 | Methods and composition for the production of orthoganal trna-aminoacyltrna synthetase pairs |
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| MXPA03009566A true MXPA03009566A (es) | 2004-12-06 |
Family
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| MXPA03009563A MXPA03009563A (es) | 2001-04-19 | 2002-04-19 | Incorporacion in vivo de aminoacidos no naturales. |
| MXPA03009566A MXPA03009566A (es) | 2001-04-19 | 2002-04-19 | Metodos y composicion para la produccion de pares trna-aminoaciltrna sintetasa ortogonales. |
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| MXPA03009563A MXPA03009563A (es) | 2001-04-19 | 2002-04-19 | Incorporacion in vivo de aminoacidos no naturales. |
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| IL (7) | IL158419A0 (enExample) |
| MX (2) | MXPA03009563A (enExample) |
| WO (2) | WO2002085923A2 (enExample) |
Families Citing this family (429)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| EP1490483B1 (en) * | 2001-04-19 | 2015-06-03 | The Scripps Research Institute | In vivo incorporation of unnatural amino acids |
| 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 |
| CA2493798A1 (en) * | 2002-07-25 | 2004-02-05 | Mds Proteomics Inc. | Improved 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 |
| DK1578949T3 (da) | 2002-10-16 | 2009-07-27 | Scripps Research Inst | Stedspecifik optagelse af keto-aminnosyrer hos proteiner |
| KR20050073559A (ko) * | 2002-10-16 | 2005-07-14 | 더 스크립스 리서치 인스티튜트 | 당단백질 합성 |
| EP1583816A4 (en) * | 2002-12-22 | 2007-06-13 | Scripps Research Inst | PROTEIN ARRAYS |
| JP4903036B2 (ja) | 2003-01-06 | 2012-03-21 | アンジオケム・インコーポレーテッド | 血液脳関門を通過する担体としてのアプロチニンおよび類似体 |
| 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 |
| 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 |
| 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) |
| WO2005003294A2 (en) | 2003-06-18 | 2005-01-13 | The Scripps Research Institute | Unnatural reactive amino acid genetic code additions |
| WO2005007870A2 (en) * | 2003-07-07 | 2005-01-27 | The Scripps Research Institute | COMPOSITIONS OF ORTHOGONAL LEUCYL-tRNA AND AMINOACYL-tRNA SYNTHETASE PAIRS AND USES THEREOF |
| 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 |
| 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 |
| EP1668114B1 (en) | 2003-08-18 | 2009-11-04 | The Regents of the University of California | Polypeptide display libraries and methods of making and using thereof |
| WO2005038002A2 (en) * | 2003-10-14 | 2005-04-28 | The Scripps Research Institute | Site-specific incorporation of redox active amino acids into proteins |
| JP2007530013A (ja) * | 2003-12-12 | 2007-11-01 | コンジュゴン インコーポレーティッド | 緻密に調節された遺伝子発現のためのシステム |
| BRPI0417801A (pt) | 2003-12-18 | 2007-04-10 | Scripps Research Inst | incorporação seletiva de 5-hidroxitriptofano em proteìnas de células mamìferas |
| BRPI0507159A (pt) * | 2004-02-02 | 2007-06-26 | Ambrx Inc | polipeptìdeos em feixe de quatro hélices humanos modificados e seus usos |
| WO2006069220A2 (en) | 2004-12-22 | 2006-06-29 | Ambrx, Inc. | Modified human growth hormone |
| 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 |
| US20080274110A1 (en) * | 2004-04-09 | 2008-11-06 | Shuji Ozaki | Cell Death-Inducing Agents |
| 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 |
| KR20070034512A (ko) * | 2004-06-18 | 2007-03-28 | 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 |
| AU2005269716B2 (en) | 2004-07-20 | 2011-01-27 | Genentech, Inc. | Inhibitors of angiopoietin-like 4 protein, combinations, and their use |
| 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 |
| AU2005295351A1 (en) * | 2004-10-18 | 2006-04-27 | Codon Devices, Inc. | Methods for assembly of high fidelity synthetic polynucleotides |
| US20070122817A1 (en) * | 2005-02-28 | 2007-05-31 | George Church | Methods for assembly of high fidelity synthetic polynucleotides |
| EP1809758A4 (en) | 2004-10-20 | 2009-04-01 | Scripps Research Inst | LOCAL IN VIVO INSTALLATION OF N-ACETYLGALACTOSAMINE AMINO ACIDS IN EU BACTERIA |
| AU2011204773B2 (en) * | 2004-10-27 | 2012-02-02 | The Scripps Research Institute | Orthogonal translation components for the in vivo incorporation of unnatural amino acids |
| AU2005330514B2 (en) * | 2004-10-27 | 2011-05-12 | The Scripps Research Institute | Orthogonal translation components for the in vivo incorporation of unnatural amino acids |
| HUE026826T2 (en) | 2004-10-29 | 2016-07-28 | Ratiopharm Gmbh | Modeling 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 |
| GB2438982A (en) | 2004-12-22 | 2007-12-12 | Ambrx Inc | Compostions containing, methods involving, and uses of non-natural amino acids and polypeptides |
| AU2013205030B2 (en) * | 2004-12-22 | 2016-05-12 | Ambrx, Inc. | Compositions containing, methods involving, and uses of non-natural amino acids and polypeptides |
| 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 |
| 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 |
| 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 |
| EP1871795A4 (en) | 2005-04-08 | 2010-03-31 | Biogenerix Ag | COMPOSITIONS AND METHOD FOR PRODUCING GLYCOSYLATION MUTANTS OF A PROTEASE-RESISTANT HUMAN GROWTH HORMONE |
| 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 |
| WO2006132969A2 (en) * | 2005-06-03 | 2006-12-14 | Ambrx, Inc. | Incorporation of non-naturally encoded amino acids into proteins |
| WO2006133088A2 (en) * | 2005-06-03 | 2006-12-14 | Ambrx, Inc. | Improved human interferon molecules and their uses |
| EP1908482B1 (en) * | 2005-06-10 | 2017-09-06 | Chugai Seiyaku Kabushiki Kaisha | Stabilizer for protein preparation comprising meglumine and use thereof |
| US20070004041A1 (en) * | 2005-06-30 | 2007-01-04 | Codon Devices, Inc. | Heirarchical assembly methods for genome engineering |
| WO2007009229A1 (en) | 2005-07-15 | 2007-01-25 | Angiochem Inc. | Use of aprotinin polypeptides as carriers in pharmaceutical conjugates |
| DE602006017703D1 (de) * | 2005-07-15 | 2010-12-02 | Medical Res Council London | Zusammensetzungen und verfahren in verbindung mit orthogonalen ribosomen-mrna-paaren |
| US8008453B2 (en) | 2005-08-12 | 2011-08-30 | Amgen Inc. | Modified Fc molecules |
| JP4829969B2 (ja) | 2005-08-18 | 2011-12-07 | アンブルックス，インコーポレイテッド | ｔＲＮＡ組成物、およびその使用 |
| AU2006284651C1 (en) | 2005-08-31 | 2013-09-12 | The Regents Of The University Of California | Cellular libraries of peptide sequences (CLiPS) and methods of using the same |
| 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 |
| CA2633524A1 (en) | 2005-12-22 | 2007-07-05 | Pacific Biosciences Of California, Inc. | Polymerases for nucleotide analogue incorporation |
| CA2632832A1 (en) * | 2005-12-30 | 2007-07-12 | Ambrx, Inc. | Compositions containing, methods involving, and uses of non-natural amino acids and polypeptides |
| CN101384711A (zh) * | 2006-01-19 | 2009-03-11 | Ambrx公司 | 具有经调节的免疫原性的非天然氨基酸多肽 |
| US20070178554A1 (en) * | 2006-02-01 | 2007-08-02 | Nima Shiva | Orthogonal Aminoacyl Synthetase-tRNA Pairs for Incorporating Unnatural Amino Acids Into Proteins |
| WO2007090198A2 (en) * | 2006-02-01 | 2007-08-09 | 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 |
| JP5808882B2 (ja) * | 2006-03-03 | 2015-11-10 | カリフォルニア インスティテュート オブ テクノロジー | 分子へのアミノ酸の部位特異的な組み込み |
| 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 |
| US20080096819A1 (en) * | 2006-05-02 | 2008-04-24 | Allozyne, Inc. | Amino acid substituted molecules |
| US7632492B2 (en) | 2006-05-02 | 2009-12-15 | Allozyne, Inc. | Modified human interferon-β polypeptides |
| BRPI0711811A2 (pt) * | 2006-05-23 | 2011-12-06 | Scripps Research Inst | aminoácidos de cumarina fluorescente geneticamente codificados |
| JO2968B1 (en) * | 2006-06-09 | 2016-03-15 | نوفارتيس ايه جي | Polypeptides are a stable insulin-like growth factor |
| ATE533846T1 (de) * | 2006-06-28 | 2011-12-15 | Riken | Seprs-mutante und verfahren zur stellengerichteten einführung von phosphoserin in protein unter verwendung davon |
| EP2035554B1 (en) * | 2006-06-29 | 2013-04-24 | The Board of Trustees of The Leland Stanford Junior University | Cell-free synthesis of proteins containing unnatural amino acids |
| TW200808351A (en) * | 2006-07-13 | 2008-02-16 | Chugai Pharmaceutical Co Ltd | Cell death-inducing agents |
| 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 |
| ES2465473T3 (es) | 2006-09-08 | 2014-06-05 | Ambrx, Inc. | Transcripción de arnt supresor en células de vertebrado |
| AU2013202770B2 (en) * | 2006-09-08 | 2015-08-20 | Ambrx, Inc. | Modified human plasma polypeptide or Fc scaffolds and their uses |
| CA2662752C (en) * | 2006-09-08 | 2016-04-12 | Ambrx, Inc. | Site specific incorporation of non-natural amino acids by vertebrate cells |
| AU2012203737B2 (en) * | 2006-09-08 | 2014-06-19 | 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 |
| US20080166766A1 (en) | 2006-10-18 | 2008-07-10 | The Scripps Research Institute | Genetic incorporation of unnatural amino acids into proteins in mammalian cells |
| JP2010510794A (ja) | 2006-11-28 | 2010-04-08 | ハナル ファーマシューティカル カンパニー リミテッド | 修飾型エリスロポエチンポリペプチド及びこの治療用用途 |
| EP1936340A1 (en) * | 2006-12-21 | 2008-06-25 | Koninklijke Philips Electronics N.V. | Sub wavelength aperture |
| WO2008103618A1 (en) * | 2007-02-22 | 2008-08-28 | University Of Utah Research Foundation | Synthesis of novel xylosides and potential uses thereof |
| 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 |
| 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 |
| US8183037B2 (en) * | 2007-04-13 | 2012-05-22 | The Salk Institute For Biological Studies | Methods of genetically encoding unnatural amino acids in eukaryotic cells using orthogonal tRNA/synthetase pairs |
| WO2008137471A2 (en) * | 2007-05-02 | 2008-11-13 | Ambrx, Inc. | Modified interferon beta polypeptides and their uses |
| 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 |
| JP5546451B2 (ja) | 2007-06-04 | 2014-07-09 | シナジー ファーマシューティカルズ インコーポレイテッド | 胃腸の障害、炎症、癌および他の障害の処置に有用なグアニル酸シクラーゼのアゴニスト |
| US20100120694A1 (en) | 2008-06-04 | 2010-05-13 | 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 |
| US20110178029A1 (en) * | 2007-09-14 | 2011-07-21 | Ambrx, Inc. | Modified Human Apolipoprotein A-1 and Their Uses |
| AU2008310912A1 (en) * | 2007-10-08 | 2009-04-16 | Synthetic Genomics, Inc. | System and method for producing synthetic microorganisms capable of translating proteins containing non-standard amino acids |
| KR20100088618A (ko) * | 2007-10-25 | 2010-08-09 | 더 스크립스 리서치 인스티튜트 | 리덕타제 내로의 3-아미노티로신의 유전적 도입 |
| ES2560532T3 (es) | 2007-11-02 | 2016-02-19 | Novartis Ag | Moléculas y métodos de modulación de la proteína 6 relacionada con el receptor de lipoproteína de baja densidad (LRP6) |
| BRPI0819092A2 (pt) * | 2007-11-02 | 2014-10-14 | Scripps Research Inst | Evolução direcionada usando proteínas que compreendem aminoácidos não naturais. |
| US20090148887A1 (en) * | 2007-11-02 | 2009-06-11 | The Scripps Research Institute | 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 |
| KR101656107B1 (ko) * | 2007-11-20 | 2016-09-08 | 암브룩스, 인코포레이티드 | 변형된 인슐린 폴리펩티드 및 이의 용도 |
| CN105647824A (zh) * | 2007-12-11 | 2016-06-08 | 斯克利普斯研究院 | 甲基营养酵母菌巴斯德毕赤酵母中的体内非天然氨基酸表达 |
| WO2009088949A1 (en) | 2008-01-03 | 2009-07-16 | Verenium Corporation | Transferases and oxidoreductases, nucleic acids encoding them and methods for making and using them |
| JP2011511778A (ja) * | 2008-01-30 | 2011-04-14 | 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 | エステルに基づいたペプチドプロドラッグ |
| CA2712606A1 (en) | 2008-02-08 | 2009-08-13 | Ambrx, Inc. | Modified leptin polypeptides and their uses |
| KR20100125290A (ko) * | 2008-02-08 | 2010-11-30 | 더 스크립스 리서치 인스티튜트 | 유전적으로 코딩된 비천연 아미노산에 의한 면역 내성의 파괴 |
| US20110015345A1 (en) * | 2008-03-19 | 2011-01-20 | Ambrx, Inc. | Modified FGF-23 Polypeptides and Their Uses |
| WO2009117726A2 (en) * | 2008-03-21 | 2009-09-24 | The Regents Of The University Of California | High-sensitive fluorescent energy transfer assay using fluorescent amino acids and fluoresent proteins |
| EP2604280A3 (en) | 2008-03-27 | 2013-10-16 | ZymoGenetics, Inc. | Compositions and methods for inhibiting PDGFRBETA and VEGF-A |
| AU2009251883B2 (en) | 2008-03-31 | 2014-09-11 | Pacific Biosciences Of California, Inc. | Generation of modified polymerases for improved accuracy in single molecule sequencing |
| MX2010011957A (es) | 2008-05-02 | 2011-03-04 | Novartis Ag Star | Moleculas de union basadas en fibronectina mejoradas y usos de las mismas. |
| 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 |
| JP5988580B2 (ja) | 2008-06-30 | 2016-09-07 | エスバテック − ア ノバルティス カンパニー エルエルシー | 機能性ポリペプチド |
| CN104800147A (zh) * | 2008-07-10 | 2015-07-29 | 德勒尼克斯治疗股份公司 | 用于大分子的增强的递送的方法和组合物 |
| 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 |
| 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 |
| US9182406B2 (en) | 2008-08-04 | 2015-11-10 | Biodesy, Inc. | Nonlinear optical detection of molecules comprising an unnatural amino acid possessing a hyperpolarizability |
| JP2012500284A (ja) * | 2008-08-19 | 2012-01-05 | フェリング ベスローテン フェンノートシャップ | ペプチド性ｐｔｈ受容体アゴニスト |
| 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 |
| WO2010043047A1 (en) | 2008-10-15 | 2010-04-22 | Angiochem Inc. | Conjugates of glp-1 agonists and uses thereof |
| CA2742043C (en) | 2008-10-24 | 2014-11-25 | Irm Llc | Biosynthetically generated pyrroline-carboxy-lysine and site specific protein modifications via chemical derivatization of pyrroline-carboxy-lysine and pyrrolysine residues |
| US9914754B2 (en) | 2008-12-05 | 2018-03-13 | Angiochem Inc. | Conjugates of neurotensin or neurotensin analogs and uses thereof |
| US8637306B2 (en) * | 2008-12-10 | 2014-01-28 | The Scripps Research Institute | Production of carrier-peptide conjugates using chemically reactive unnatural amino acids |
| US20090197339A1 (en) * | 2008-12-10 | 2009-08-06 | The Scripps Research Institute | In vivo unnatural amino acid expression in the methylotrophic yeast pichia pastoris |
| AU2009327267A1 (en) | 2008-12-17 | 2011-07-14 | Angiochem, Inc. | Membrane type-1 matrix metalloprotein inhibitors and uses thereof |
| AU2009335715B2 (en) | 2008-12-19 | 2016-09-15 | Indiana University Research And Technology Corporation | Amide-based insulin prodrugs |
| CA2747195A1 (en) * | 2008-12-19 | 2010-07-15 | Indiana University Research And Technology Corporation | Dipeptide linked medicinal agents |
| 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 |
| US8481485B2 (en) | 2008-12-19 | 2013-07-09 | Indiana University Research And Technology Corporation | Insulin analogs |
| WO2010096394A2 (en) | 2009-02-17 | 2010-08-26 | Redwood Biosciences, 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 |
| US20100310576A1 (en) * | 2009-03-31 | 2010-12-09 | Adams Ryan A | COMPOSITIONS AND METHODS COMPRISING ASPARTYL-tRNA SYNTHETASES HAVING NON-CANONICAL BIOLOGICAL ACTIVITIES |
| ES2729261T3 (es) | 2009-04-20 | 2019-10-31 | Angiochem Inc | Tratamiento del cáncer de ovario utilizando un agente anticancerígeno conjugado con un análogo de Angiopep-2 |
| US9243253B2 (en) | 2009-05-11 | 2016-01-26 | Pfenex, Inc. | Production of recombinant proteins utilizing non-antibiotic selection methods and the incorporation of non-natural amino acids therein |
| MX338775B (es) | 2009-06-04 | 2016-05-02 | Novartis Ag | Metodos para identificacion de sitios para conjugacion de igg. |
| WO2011000095A1 (en) | 2009-07-02 | 2011-01-06 | 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 |
| WO2011056502A1 (en) | 2009-10-26 | 2011-05-12 | Genentech, Inc. | Bone morphogenetic protein receptor type ii compositions and methods of use |
| 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 |
| 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 |
| CN102640001A (zh) | 2009-11-05 | 2012-08-15 | 诺瓦提斯公司 | 预测纤维化进展的生物标记物 |
| PE20121707A1 (es) | 2009-12-21 | 2012-12-17 | Ambrx Inc | Polipeptidos de somatotropina bovina modificados y sus usos |
| BR112012015597A2 (pt) | 2009-12-21 | 2017-01-31 | Ambrx Inc | peptídeos de somatotropina suínos modificados e seus usos |
| US9051593B2 (en) | 2009-12-21 | 2015-06-09 | Trustees Of Dartmouth College | Recombinant prokaryotes and use thereof for production of O-glycosylated proteins |
| EP2528615B1 (en) | 2010-01-27 | 2020-05-13 | 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 |
| JP6066900B2 (ja) | 2010-04-26 | 2017-01-25 | エータイアー ファーマ， インコーポレイテッド | システイニル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 |
| ES2638311T3 (es) | 2010-04-27 | 2017-10-19 | Atyr Pharma, Inc. | Descubrimiento innovador de composiciones terapéuticas, diagnósticas y de anticuerpos relacionadas con fragmentos de proteína de treonil ARNt sintetasas |
| US8961960B2 (en) | 2010-04-27 | 2015-02-24 | Atyr Pharma, Inc. | Innovative discovery of therapeutic, diagnostic, and antibody compositions related to protein fragments of isoleucyl tRNA synthetases |
| JP6008837B2 (ja) | 2010-04-28 | 2016-10-19 | エータイアー ファーマ， インコーポレイテッド | アラニル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 |
| US8986680B2 (en) | 2010-04-29 | 2015-03-24 | Atyr Pharma, Inc. | Innovative discovery of therapeutic, diagnostic, and antibody compositions related to protein fragments of Asparaginyl tRNA synthetases |
| WO2011139907A2 (en) | 2010-04-29 | 2011-11-10 | Atyr Pharma, Inc. | Innovative discovery of therapeutic, diagnostic, and antibody compositions related to protein fragments of valyl trna synthetases |
| 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 |
| AU2011248227B2 (en) | 2010-05-03 | 2016-12-01 | Pangu Biopharma Limited | Innovative discovery of therapeutic, diagnostic, and antibody compositions related to protein fragments of phenylalanyl-alpha-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 |
| 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 |
| JP6008843B2 (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 | グルタミル−プロリル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 |
| EP2566499B1 (en) | 2010-05-04 | 2017-01-25 | aTyr Pharma, Inc. | Innovative discovery of therapeutic, diagnostic, and antibody compositions related to protein fragments of p38 multi-trna synthetase complex |
| 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 |
| AU2011256366C1 (en) | 2010-05-17 | 2017-06-15 | Pangu Biopharma Limited | Innovative discovery of therapeutic, diagnostic, and antibody compositions related to protein fragments of leucyl-tRNA synthetases |
| CN103096913B (zh) | 2010-05-27 | 2017-07-18 | Atyr 医药公司 | 与谷氨酰胺酰‑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 |
| CA2800281C (en) | 2010-06-01 | 2021-01-12 | Atyr Pharma, Inc. | Innovative discovery of therapeutic, diagnostic, and antibody compositions related to protein fragments of lysyl-trna synthetases |
| EP2584037B1 (en) * | 2010-06-16 | 2016-08-10 | Riken | Method for constructing recombinant bacterium for producing non-native protein, and utilization of same |
| AU2011268327B2 (en) | 2010-06-16 | 2016-02-25 | 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 |
| US8946147B2 (en) | 2010-06-24 | 2015-02-03 | Indiana University Research And Technology Corporation | Amide-based insulin prodrugs |
| 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 |
| CA2804278C (en) * | 2010-07-12 | 2021-07-13 | Atyr Pharma, Inc. | Innovative discovery of therapeutic, diagnostic, and antibody compositions related to protein fragments of aspartyl-trna synthetases |
| CA2804416C (en) * | 2010-07-12 | 2020-04-28 | Atyr Pharma, Inc. | Innovative discovery of therapeutic, diagnostic, and antibody compositions related to protein fragments of glycyl-trna synthetases |
| KR20130102534A (ko) | 2010-07-12 | 2013-09-17 | 에이티와이알 파마, 인코포레이티드 | 히스티딜trna 합성효소의 단백질 단편에 관련된 치료적, 진단적, 및 항체 조성물의 혁신적 발견 |
| US9567386B2 (en) | 2010-08-17 | 2017-02-14 | Ambrx, Inc. | Therapeutic uses of modified relaxin polypeptides |
| KR101963460B1 (ko) | 2010-08-17 | 2019-03-28 | 암브룩스, 인코포레이티드 | 변형된 릴랙신 폴리펩타이드 및 그것의 용도 |
| JP5964304B2 (ja) * | 2010-08-25 | 2016-08-03 | エータイアー ファーマ， インコーポレイテッド | チロシル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 |
| EP2640745B1 (en) | 2010-09-10 | 2018-11-07 | MedImmune Limited | Bivalent and bispecific anti-il6/anti-il23 antibodies |
| US9616097B2 (en) | 2010-09-15 | 2017-04-11 | Synergy Pharmaceuticals, Inc. | Formulations of guanylate cyclase C agonists and methods of use |
| 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 |
| EP2624857B1 (en) | 2010-10-06 | 2017-08-02 | aTyr Pharma, Inc. | Innovative discovery of therapeutic, diagnostic, and antibody compositions related to 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 |
| US9540438B2 (en) | 2011-01-14 | 2017-01-10 | Redwood Bioscience, Inc. | Aldehyde-tagged immunoglobulin polypeptides and methods of use thereof |
| US9085514B2 (en) | 2011-02-03 | 2015-07-21 | Embl | Unnatural amino acids comprising a cyclooctynyl or trans-cyclooctenyl analog group and uses thereof |
| CA2831136A1 (en) | 2011-03-21 | 2012-09-27 | Biodesy, Llc | Classification of kinase inhibitors using nonlinear optical techniques |
| EP2694083A2 (en) * | 2011-04-01 | 2014-02-12 | Max-Planck-Gesellschaft zur Förderung der Wissenschaften e.V. | Peptides and pharmaceutical compositions for use in the treatment by nasal administration of patients suffering from anxiety and sleep disorders |
| DK2694095T3 (en) | 2011-04-05 | 2018-05-28 | Longevity Biotech Inc | COMPOSITIONS COMPREHENSIVE GLUCAGON ANALOGS AND METHODS FOR PREPARING AND USING THE SAME |
| ES2898854T3 (es) | 2011-05-27 | 2022-03-09 | Ambrx Inc | Composiciones que contienen, métodos que implican, y usos de derivados de dolastatina enlazados con aminoácidos no naturales |
| US9796754B2 (en) | 2011-05-27 | 2017-10-24 | Ambrx, Inc. | Compositions containing, methods involving, and uses of non-natural amino acid linked dolastatin derivatives |
| 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 |
| US9464288B2 (en) | 2011-07-11 | 2016-10-11 | 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 |
| WO2013066438A2 (en) | 2011-07-22 | 2013-05-10 | President And Fellows Of Harvard College | Evaluation and improvement of nuclease cleavage specificity |
| 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 |
| US9458214B2 (en) | 2011-09-26 | 2016-10-04 | Novartis Ag | Dual function fibroblast growth factor 21 proteins |
| WO2013068874A1 (en) | 2011-11-11 | 2013-05-16 | Pfizer Inc. | Antibody-drug conjugates |
| 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 |
| BR112014015156A2 (pt) | 2011-12-20 | 2020-10-27 | Indiana University Research And Technology Corporation | análogos de insulina à base de ctp, seus métodos de produção e uso no tratamento de hiperglicemia, bem como sequência de ácido nucleico e célula hospedeira |
| TWI579296B (zh) | 2011-12-28 | 2017-04-21 | Chugai Pharmaceutical Co Ltd | Cyclization of Peptide Compounds |
| CA2858613A1 (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 |
| JP6170077B2 (ja) | 2012-02-16 | 2017-07-26 | エータイアー ファーマ， インコーポレイテッド | 自己免疫および炎症疾患を処置するためのヒスチジルｔＲＮＡ合成酵素 |
| CN109265541A (zh) | 2012-05-10 | 2019-01-25 | 麻省理工学院 | 流感中和药剂 |
| EP2858676B1 (en) | 2012-06-07 | 2019-03-13 | Ambrx, Inc. | Prostate-specific membrane antigen antibody drug conjugates |
| SG11201408161RA (en) | 2012-06-08 | 2015-01-29 | Sutro Biopharma Inc | Antibodies comprising site-specific non-natural amino acid residues, methods of their preparation and methods of their use |
| KR102190832B1 (ko) | 2012-06-19 | 2020-12-15 | 암브룩스, 인코포레이티드 | 항cd70 항체 약물 컨쥬게이트 |
| EP3135690A1 (en) | 2012-06-26 | 2017-03-01 | 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 |
| AU2013305744B2 (en) | 2012-08-22 | 2017-06-01 | 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 |
| US8859735B2 (en) | 2012-08-27 | 2014-10-14 | Empire Technology Development Llc | Gelatin alkyd peptides and uses thereof |
| ES2728864T3 (es) | 2012-08-31 | 2019-10-29 | Sutro Biopharma Inc | Aminoácidos modificados que comprenden un grupo azido |
| BR112015006368B1 (pt) | 2012-09-24 | 2022-02-08 | Medimmune Limited | Processo para produção de linha celular eucariótica estável |
| CN108383902A (zh) | 2012-09-26 | 2018-08-10 | 印第安纳大学研究及科技有限公司 | 胰岛素类似物二聚体 |
| 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 |
| EP3626735A1 (en) | 2012-12-18 | 2020-03-25 | Novartis AG | Stabilized insulin-like growth factor polypeptides |
| EP2948469A4 (en) | 2013-01-23 | 2016-11-02 | Univ Leland Stanford Junior | STABILIZED HEPATITIS B CORE POLYPEPTIDE |
| EP3718557A3 (en) | 2013-02-25 | 2020-10-21 | Bausch Health Ireland Limited | Guanylate cyclase receptor agonist sp-333 for use in colonic cleansing |
| 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 |
| UY35368A (es) | 2013-03-08 | 2014-10-31 | Irm Llc | Péptidos y composiciones para el tratamiento de daño articular |
| WO2014158900A1 (en) | 2013-03-14 | 2014-10-02 | Indiana University Research And Technology Corporation | Insulin-incretin conjugates |
| HK1220696A1 (zh) | 2013-03-15 | 2017-05-12 | Bausch Health Ireland Limited | 鸟苷酸环化酶激动剂及其用途 |
| 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 |
| ES2708565T3 (es) | 2013-03-15 | 2019-04-10 | Atyr Pharma Inc | Conjugados de Fc-histidil-ARNt sintetasa |
| EP2968469A4 (en) | 2013-03-15 | 2016-08-31 | Longevity Biotech Inc | PEPTIDES COMPRISING NON-ENDOGENIC AMINO ACIDS AND METHODS OF MAKING AND USING SAME |
| AU2014235209B2 (en) | 2013-03-15 | 2018-06-14 | Bausch Health Ireland Limited | Guanylate cyclase receptor agonists combined with other drugs |
| JP6574754B2 (ja) | 2013-03-19 | 2019-09-11 | ベイジン シェノゲン ファーマ グループ リミテッド | エストロゲン受容体関連疾患を処置するための抗体及び方法 |
| EP4424697A3 (en) | 2013-06-05 | 2024-12-25 | Bausch Health Ireland Limited | Ultra-pure agonists of guanylate cyclase c, method of making and using same |
| 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 |
| ES2658039T3 (es) | 2013-07-10 | 2018-03-08 | Sutro Biopharma, Inc. | Anticuerpos que comprenden múltiples residuos de aminoácidos no naturales sitio-específicos, métodos para su preparación y métodos de uso |
| EP3021942A4 (en) | 2013-07-19 | 2017-04-19 | The Regents of The University of California | Milk fat globule epidermal growth factor 8 regulates fatty acid uptake |
| TW201518323A (zh) | 2013-07-25 | 2015-05-16 | Novartis Ag | 合成ａｐｅｌｉｎ多肽之生物結合物 |
| SG11201600211XA (en) | 2013-07-25 | 2016-02-26 | Novartis Ag | Cyclic polypeptides for the treatment of heart failure |
| US20150044192A1 (en) | 2013-08-09 | 2015-02-12 | President And Fellows Of Harvard College | Methods for identifying a target site of a cas9 nuclease |
| JP6694385B2 (ja) | 2013-08-09 | 2020-05-13 | アーデリクス，インコーポレーテッド | リン酸塩輸送阻害のための化合物及び方法 |
| US9359599B2 (en) | 2013-08-22 | 2016-06-07 | President And Fellows Of Harvard College | Engineered transcription activator-like effector (TALE) domains and uses thereof |
| WO2015031268A1 (en) | 2013-08-26 | 2015-03-05 | Arizona Board Of Regents On Behalf Of Arizona State University | High affinity synbodies for influenza |
| 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 |
| US9737604B2 (en) | 2013-09-06 | 2017-08-22 | President And Fellows Of Harvard College | Use of cationic lipids to deliver CAS9 |
| EA201690732A1 (ru) | 2013-10-10 | 2016-12-30 | Синерджи Фармасьютикалз, Инк. | Агонисты гуанилатциклазы, используемые для лечения индуцированных опиоидами дисфункций |
| 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 |
| WO2015057908A1 (en) | 2013-10-18 | 2015-04-23 | Novartis Ag | Methods of treating diabetes and related disorders |
| US11053481B2 (en) | 2013-12-12 | 2021-07-06 | President And Fellows Of Harvard College | Fusions of Cas9 domains and nucleic acid-editing domains |
| EP3094977B1 (en) | 2014-01-14 | 2018-08-22 | 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 |
| WO2016004024A1 (en) | 2014-07-02 | 2016-01-07 | Sutro Biopharma, Inc. | High growth capacity auxotrophic escherichia coli and methods of use |
| US11254933B2 (en) | 2014-07-14 | 2022-02-22 | The Regents Of The University Of California | CRISPR/Cas transcriptional modulation |
| AU2015298571B2 (en) | 2014-07-30 | 2020-09-03 | President And Fellows Of Harvard College | Cas9 proteins including ligand-dependent inteins |
| US10513699B2 (en) | 2014-09-03 | 2019-12-24 | Bioatla, Llc | Discovering and producing conditionally active biologic proteins in the same eukaryotic cell production hosts |
| JP6657230B2 (ja) | 2014-09-24 | 2020-03-04 | インディアナ ユニヴァーシティ リサーチ アンド テクノロジー コーポレイション | インクレチン−インスリンコンジュゲート |
| ES2947409T3 (es) | 2014-09-24 | 2023-08-08 | Univ Indiana Res & Tech Corp | Profármacos de insulina a base de amida lipídica |
| WO2016073079A2 (en) | 2014-09-26 | 2016-05-12 | Yale University | Compositions and methods for biocontainment of microorganisms |
| 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 |
| 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 |
| AU2016209968B2 (en) | 2015-01-23 | 2018-11-29 | Novartis Ag | Synthetic apelin fatty acid conjugates with improved half-life |
| ES2880473T5 (es) | 2015-01-30 | 2024-05-09 | Univ California | Suministro de proteínas en células hematopoyéticas primarias |
| EP3269809B1 (en) | 2015-03-13 | 2022-07-27 | Chugai Seiyaku Kabushiki Kaisha | MODIFIED AMINOACYL-tRNA SYNTHETASE AND USE THEREOF |
| US10483262B2 (en) * | 2015-05-15 | 2019-11-19 | Taiwan Semiconductor Manufacturing Co., Ltd. | Dual nitride stressor for semiconductor device and method of manufacturing |
| EP3309250A4 (en) * | 2015-06-09 | 2019-06-19 | National Institute of Advanced Industrial Science and Technology | AMINO ACID MODIFIED NUCLEIC ACID AND USE THEREOF |
| EP3307326B9 (en) | 2015-06-15 | 2021-02-24 | Angiochem Inc. | Methods for the treatment of leptomeningeal carcinomatosis |
| CN108289930A (zh) | 2015-07-10 | 2018-07-17 | 香港科技大学 | 用于治疗神经退行性和神经炎性病症的方法和组合物 |
| 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 |
| US12043852B2 (en) | 2015-10-23 | 2024-07-23 | President And Fellows Of Harvard College | Evolved Cas9 proteins for gene editing |
| WO2017109706A1 (en) | 2015-12-22 | 2017-06-29 | Novartis Ag | Methods of treating or ameliorating metabolic disorders using growth differentiation factor 15 (gdf-15) |
| US10294303B2 (en) | 2015-12-23 | 2019-05-21 | Amgen Inc. | Method of treating or ameliorating metabolic disorders using binding proteins for gastric inhibitory peptide receptor (GIPR) in combination with GLP-1 agonists |
| 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 |
| CA3009814A1 (en) | 2016-01-11 | 2017-07-20 | Synergy Pharmaceuticals, Inc. | Formulations and methods for treating ulcerative colitis |
| US11708413B2 (en) | 2016-01-27 | 2023-07-25 | Sutro Biopharma, Inc. | Anti-CD74 antibody conjugates, compositions comprising anti-CD74 antibody conjugates and methods of using anti-CD74 antibody conjugates |
| JP2019515677A (ja) | 2016-04-26 | 2019-06-13 | アール．ピー．シェーラー テクノロジーズ エルエルシー | 抗体複合体ならびにそれを作製および使用する方法 |
| EP3455628A4 (en) | 2016-05-09 | 2019-12-04 | Biodesy, Inc. | METHOD AND DEVICES FOR DETECTING INTERACTIONS OF PERIPHERAL MEMBRANE PROTEINS USING NONLINEAR OPTICAL TECHNIQUES |
| WO2017204729A1 (en) * | 2016-05-25 | 2017-11-30 | Fogelstrand Per | Method for preparing a biological sample for use in an immunolabeling process |
| CN110381988A (zh) | 2016-06-15 | 2019-10-25 | 诺华股份有限公司 | 使用骨形态发生蛋白6(bmp6)的抑制剂治疗疾病的方法 |
| KR20250103795A (ko) | 2016-08-03 | 2025-07-07 | 프레지던트 앤드 펠로우즈 오브 하바드 칼리지 | 아데노신 핵염기 편집제 및 그의 용도 |
| CN109804066A (zh) | 2016-08-09 | 2019-05-24 | 哈佛大学的校长及成员们 | 可编程cas9-重组酶融合蛋白及其用途 |
| US11542509B2 (en) | 2016-08-24 | 2023-01-03 | President And Fellows Of Harvard College | Incorporation of unnatural amino acids into proteins using base editing |
| AU2017342543B2 (en) | 2016-10-14 | 2024-06-27 | 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 |
| 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 |
| MX2019007248A (es) | 2016-12-19 | 2019-08-16 | Quantum Si Inc | Enzimas de polimerizacion para reacciones de secuenciacion. |
| WO2018119359A1 (en) | 2016-12-23 | 2018-06-28 | President And Fellows Of Harvard College | Editing of ccr5 receptor gene to protect against hiv infection |
| KR20190103256A (ko) | 2016-12-30 | 2019-09-04 | 수트로박스, 인코포레이티드 | 비자연 아미노산을 갖는 폴리펩타이드-항원 접합체 |
| US11951165B2 (en) | 2016-12-30 | 2024-04-09 | Vaxcyte, Inc. | Conjugated vaccine carrier proteins |
| JOP20190177A1 (ar) | 2017-01-17 | 2019-07-16 | Amgen Inc | طريقة لعلاج أو تحسين اضطرابات أيضية باستخدام مساعدات مستقبل glp-1 مقترنة بمناهضات لمستقبل ببتيد مثبط معوي (gipr) |
| US12391971B2 (en) | 2017-01-31 | 2025-08-19 | Chugai Seiyaku Kabushiki Kaisha | Method for synthesizing peptides in cell-free translation system |
| MX2019008449A (es) | 2017-02-08 | 2019-09-09 | Bristol Myers Squibb Co | Polipetidos de relaxina modificada que comprenden un mejorador farmacocinetico y sus usos. |
| EP3592853A1 (en) | 2017-03-09 | 2020-01-15 | President and Fellows of Harvard College | Suppression of pain by gene editing |
| EP3592381A1 (en) | 2017-03-09 | 2020-01-15 | President and Fellows of Harvard College | Cancer vaccine |
| KR20190127797A (ko) | 2017-03-10 | 2019-11-13 | 프레지던트 앤드 펠로우즈 오브 하바드 칼리지 | 시토신에서 구아닌으로의 염기 편집제 |
| 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 |
| EP3612215B1 (en) | 2017-04-20 | 2024-08-28 | aTyr Pharma, Inc. | Compositions for treating lung inflammation |
| 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 |
| CN117286182A (zh) | 2017-06-02 | 2023-12-26 | Ambrx公司 | 促进含非天然氨基酸的蛋白质产生的方法和组合物 |
| EP3636656A4 (en) | 2017-06-09 | 2021-04-14 | Chugai Seiyaku Kabushiki Kaisha | METHOD OF SYNTHESIS OF PEPTIDE WITH N-SUBSTITUTED AMINO ACID |
| BR112019024410A2 (pt) | 2017-06-20 | 2020-07-14 | Amgen Inc. | método de tratamento ou melhoria de disfunções metabólicas usando proteínas de ligação para receptor do peptídeo inibidor gástrico (gipr) em combinação com agonistas de glp 1 |
| 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). |
| CA3069321A1 (en) | 2017-07-11 | 2019-01-17 | 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 |
| EP3658588A1 (en) | 2017-07-26 | 2020-06-03 | Sutro Biopharma, Inc. | Methods of using anti-cd74 antibodies and antibody conjugates in treatment of t-cell lymphoma |
| CN111801345A (zh) | 2017-07-28 | 2020-10-20 | 哈佛大学的校长及成员们 | 使用噬菌体辅助连续进化(pace)的进化碱基编辑器的方法和组合物 |
| US20200181220A1 (en) | 2017-08-03 | 2020-06-11 | Synthorx, Inc. | Cytokine conjugates for the treatment of proliferative and infectious diseases |
| WO2019139645A2 (en) | 2017-08-30 | 2019-07-18 | President And Fellows Of Harvard College | High efficiency base editors comprising gam |
| WO2019051127A1 (en) | 2017-09-07 | 2019-03-14 | Cue Biopharma, Inc. | MULTIMER MODULATOR POLYPEPTIDE OF LYMPHOCYTE T HAVING CONJUGATION SITES AND METHODS OF USE THEREOF |
| SG11202002310UA (en) | 2017-09-18 | 2020-04-29 | Sutro Biopharma Inc | Anti- folate receptor alpha antibody conjugates and their uses |
| CA3082251A1 (en) | 2017-10-16 | 2019-04-25 | The Broad Institute, Inc. | Uses of adenosine base editors |
| JP7411414B2 (ja) | 2017-12-15 | 2024-01-11 | 中外製薬株式会社 | ペプチドの製造方法、及び塩基の処理方法 |
| EP3724214A4 (en) | 2017-12-15 | 2021-09-01 | The Broad Institute Inc. | SYSTEMS AND METHODS FOR PREDICTING REPAIR RESULTS IN GENETIC ENGINEERING |
| CN119410679A (zh) | 2018-05-01 | 2025-02-11 | Ambrx公司 | 一种用于优化抗体表达的方法 |
| WO2019226953A1 (en) | 2018-05-23 | 2019-11-28 | 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 |
| US20210356377A1 (en) * | 2018-09-07 | 2021-11-18 | Medimmune, Llc | Methods Of Cell Selection |
| CN111212661B (zh) | 2018-09-11 | 2023-09-12 | 北京泰德制药股份有限公司 | 白介素-2多肽偶联物及其用途 |
| US20220047716A1 (en) | 2018-09-17 | 2022-02-17 | Sutro Biopharma, Inc. | Combination therapies with anti-folate receptor antibody conjugates |
| US20220009986A1 (en) | 2018-10-19 | 2022-01-13 | Ambrx, Inc. | Interleukin-10 polypeptide conjugates, dimers thereof, and their uses |
| US12281338B2 (en) | 2018-10-29 | 2025-04-22 | 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 |
| WO2020095983A1 (ja) | 2018-11-07 | 2020-05-14 | 中外製薬株式会社 | Ｏ－置換セリン誘導体の製造方法 |
| CN119143631A (zh) | 2018-11-30 | 2024-12-17 | 中外制药株式会社 | 用于肽化合物或酰胺化合物的脱保护方法和在固相反应中的树脂脱除方法以及用于生产肽化合物的方法 |
| US12351837B2 (en) | 2019-01-23 | 2025-07-08 | The Broad Institute, Inc. | Supernegatively charged proteins and uses thereof |
| US20200246467A1 (en) | 2019-02-06 | 2020-08-06 | Synthorx, Inc. | Il-2 conjugates and methods of use thereof |
| US20220226488A1 (en) | 2019-02-12 | 2022-07-21 | Ambrx, Inc. | Compositions containing, methods and uses of antibody-tlr agonist conjugates |
| 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 |
| US12371817B2 (en) | 2019-03-04 | 2025-07-29 | The Texas A&M University System | Methods of making and utilizing amber-obligated phage display libraries |
| US12071396B2 (en) | 2019-03-15 | 2024-08-27 | Chugai Seiyaku Kabushiki Kaisha | Method for preparing aromatic amino acid derivative |
| DE112020001306T5 (de) | 2019-03-19 | 2022-01-27 | Massachusetts Institute Of Technology | Verfahren und zusammensetzungen zur editierung von nukleotidsequenzen |
| US12473543B2 (en) | 2019-04-17 | 2025-11-18 | The Broad Institute, Inc. | Adenine base editors with reduced off-target effects |
| US20220362394A1 (en) | 2019-05-03 | 2022-11-17 | Sutro Biopharma, Inc. | Anti-bcma antibody conjugates |
| WO2020236907A1 (en) * | 2019-05-20 | 2020-11-26 | Albert Einstein College Of Medicine | Compounds and methods for treatment of bacterial infections |
| US20220233673A1 (en) | 2019-06-04 | 2022-07-28 | Institut Curie | METHODS OF PRODUCING SHIGA TOXIN B-SUBUNIT (STxB) MONOMERS AND OLIGOMERS, AND USES THEREOF |
| US12139708B2 (en) | 2019-06-07 | 2024-11-12 | 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 |
| US20220259202A1 (en) | 2019-06-17 | 2022-08-18 | 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 |
| MX2022000055A (es) | 2019-06-28 | 2022-05-30 | Quantum Si Inc | Enzimas de polimerización para reacciones de secuenciación. |
| US20220403438A1 (en) | 2019-10-08 | 2022-12-22 | 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 |
| JP2022552137A (ja) * | 2019-10-15 | 2022-12-15 | トラスティーズ オブ ボストン カレッジ | 非天然アミノ酸組み込み増強のためのキメラ耐熱性アミノアシルｔＲＮＡシンテターゼ |
| US11149280B2 (en) | 2019-10-29 | 2021-10-19 | Yale University | Engineering organisms resistant to viruses and horizontally transferred genetic elements |
| WO2021092162A1 (en) * | 2019-11-05 | 2021-05-14 | Aditya Kunjapur | Biosynthesis of para-nitro-l-phenylalanine |
| BR112022007535A2 (pt) | 2019-11-07 | 2022-07-12 | Chugai Pharmaceutical Co Ltd | Composto peptídico cíclico tendo ação inibitória de kras |
| CN116925237A (zh) | 2019-12-31 | 2023-10-24 | 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 |
| US12478662B2 (en) | 2020-01-03 | 2025-11-25 | The United States of America as represented by the Secretary Department of Heath and Human Services | TNAP locally administered for promoting periodontal health |
| WO2021139744A1 (en) | 2020-01-11 | 2021-07-15 | Beijing Ql Biopharmaceutical Co., Ltd. | Conjugates of fusion proteins of glp-1 and fgf21 |
| 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 |
| EP4114852A1 (en) | 2020-03-03 | 2023-01-11 | Sutro Biopharma, Inc. | Antibodies comprising site-specific glutamine tags, methods of their preparation and methods of their use |
| JP2023517595A (ja) | 2020-03-11 | 2023-04-26 | アンブルックス，インコーポレイテッド | インターロイキン－２ポリペプチド結合物およびその使用方法 |
| 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 |
| KR20230004682A (ko) | 2020-04-22 | 2023-01-06 | 머크 샤프 앤드 돔 엘엘씨 | 인터류킨-2 수용체 베타 감마c 이량체에 대해 편향되고 비펩티드성 수용성 중합체에 접합된 인간 인터류킨-2 접합체 |
| 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 |
| JP2023525304A (ja) | 2020-05-08 | 2023-06-15 | ザ ブロード インスティテュート，インコーポレーテッド | 標的二本鎖ヌクレオチド配列の両鎖同時編集のための方法および組成物 |
| WO2021234458A1 (en) | 2020-05-22 | 2021-11-25 | Takeda Pharmaceutical Company Limited | Adamts13 compositions and methods for treating and diagnosing complications of coronavirus disease |
| JP2023538071A (ja) | 2020-08-20 | 2023-09-06 | 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、その方法及び使用 |
| EP4211156A1 (en) * | 2020-09-14 | 2023-07-19 | Sutro Biopharma, Inc. | Method for large scale production of antibodies using a cell-free protein synthesis system |
| JP2023545684A (ja) | 2020-09-30 | 2023-10-31 | ベイジン キューエル バイオファーマシューティカル カンパニー，リミテッド | ポリペプチドコンジュゲートおよび使用の方法 |
| IL307282A (en) | 2021-04-03 | 2023-11-01 | Ambrx Inc | Antidote conjugates against HER2 and their applications |
| US20230016731A1 (en) * | 2021-05-21 | 2023-01-19 | The Regents Of The University Of California | Affinity purification sequencing |
| KR20240041379A (ko) | 2021-07-09 | 2024-03-29 | 브라이트 피크 테라퓨틱스 아게 | Il-2에 접합된 체크포인트 억제제 및 이의 용도 |
| CA3222357A1 (en) | 2021-07-09 | 2023-01-12 | Bertolt Kreft | Modified il-2 polypeptides for treatment of inflammatory and autoimmune diseases |
| US20230201364A1 (en) | 2021-07-09 | 2023-06-29 | Bright Peak Therapeutics Ag | Antibody conjugates and manufacture thereof |
| US20230201365A1 (en) | 2021-07-09 | 2023-06-29 | Bright Peak Therapeutics Ag | Modified cd20 antibodies and uses thereof |
| CA3222359A1 (en) | 2021-07-09 | 2023-01-12 | Bright Peak Therapeutics Ag | Conjugates of checkpoint inhibitors with il-2, and uses thereof |
| 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 |
| JP2024533596A (ja) * | 2021-09-17 | 2024-09-12 | アブサイ コーポレイション | トランスファーｒｎａの組成、及び非標準アミノ酸を含むタンパク質の生産における使用 |
| WO2023069816A2 (en) | 2021-09-20 | 2023-04-27 | The Broad Institute, Inc. | Compositions and methods for multiplex decoding of quadruplet codons |
| AU2022369312A1 (en) | 2021-10-20 | 2024-05-02 | Synthekine, Inc. | Heterodimeric fc cytokines and uses thereof |
| 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 |
| EP4186529B1 (en) | 2021-11-25 | 2025-07-09 | Veraxa Biotech GmbH | Improved antibody-payload conjugates (apcs) prepared by site-specific conjugation utilizing genetic code expansion |
| AU2022404647A1 (en) | 2021-12-08 | 2024-06-13 | European Molecular Biology Laboratory | Hydrophilic tetrazine-functionalized payloads for preparation of targeting conjugates |
| WO2023146807A1 (en) | 2022-01-25 | 2023-08-03 | The Regents Of The University Of California | Vegf mutants and modulation of integrin-mediated signaling |
| CN119053347A (zh) | 2022-02-23 | 2024-11-29 | 明峰治疗股份公司 | 免疫抗原特异性il-18免疫细胞因子及其用途 |
| WO2023161857A1 (en) | 2022-02-23 | 2023-08-31 | Bright Peak Therapeutics Ag | Bifunctional cytokine compositions |
| CA3252113A1 (en) | 2022-03-30 | 2023-10-05 | Beijing Ql Biopharmaceutical Co Ltd | Liquid pharmaceutical compositions of polypeptide conjugates and their methods of use |
| CN120076831A (zh) | 2022-06-30 | 2025-05-30 | 苏特罗生物制药公司 | 抗ror1抗体和抗体缀合物、包含抗ror1抗体或抗体缀合物的组合物、以及制备和使用抗ror1抗体和抗体缀合物的方法 |
| NL2033185B1 (en) | 2022-09-29 | 2024-04-08 | Stichting Vu | Compounds for rna stabilisation and delivery |
| 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 |
| KR20250131790A (ko) * | 2022-12-31 | 2025-09-03 | 강마-헬스코드 (상하이) 바이오테크 컴퍼니 리미티드 | 비천연 아미노산 삽입용 시험관 내 무세포 단백질 합성 시스템, 방법 및 응용 |
| WO2024150175A1 (en) | 2023-01-11 | 2024-07-18 | Bright Peak Therapeutics Ag | Conditionally activated proteins and methods of use |
| 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 |
| 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 |
| WO2025021929A1 (en) | 2023-07-27 | 2025-01-30 | Veraxa Biotech Gmbh | Hydrophilic trans-cyclooctene (hytco) compounds, constructs and conjugates containing the same |
| WO2025041055A1 (en) | 2023-08-22 | 2025-02-27 | Ambrx, Inc. | Anti-psma adc conjugate compositions and methods of use thereof |
| WO2025041101A1 (en) | 2023-08-23 | 2025-02-27 | Bright Peak Therapeutics Ag | Activatable il-18 immunocytokines and uses thereof |
| WO2025041102A1 (en) | 2023-08-23 | 2025-02-27 | Bright Peak Therapeutics Ag | Targeted immune activation with il-18 immunocytokines |
| WO2025080711A1 (en) | 2023-10-13 | 2025-04-17 | Sutro Biopharma, Inc. | Dual payload antibody drug conjugates |
| WO2025081117A2 (en) | 2023-10-13 | 2025-04-17 | 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 |
| US20250276080A1 (en) | 2024-02-29 | 2025-09-04 | Amgen Inc. | Glucagon receptor agonists and conjugates to glucose-dependent insulinotropic polypeptide antagonists |
| 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 |
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 |
| 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 |
| US6706504B1 (en) | 1996-11-12 | 2004-03-16 | The Scripps Research Institute | Tissue type plasminogen activator (t-PA) variants: compositions and methods of use |
| EP1490483B1 (en) * | 2001-04-19 | 2015-06-03 | The Scripps Research Institute | In vivo incorporation of unnatural amino acids |
| 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. |
| DK1578949T3 (da) | 2002-10-16 | 2009-07-27 | Scripps Research Inst | Stedspecifik optagelse af keto-aminnosyrer hos proteiner |
| KR20050073559A (ko) | 2002-10-16 | 2005-07-14 | 더 스크립스 리서치 인스티튜트 | 당단백질 합성 |
| EP1583816A4 (en) | 2002-12-22 | 2007-06-13 | Scripps Research Inst | PROTEIN ARRAYS |
| 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 |
| 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 |
| 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 |
| WO2005007870A2 (en) | 2003-07-07 | 2005-01-27 | The Scripps Research Institute | COMPOSITIONS OF ORTHOGONAL LEUCYL-tRNA AND AMINOACYL-tRNA SYNTHETASE PAIRS AND USES THEREOF |
| WO2005038002A2 (en) | 2003-10-14 | 2005-04-28 | The Scripps Research Institute | Site-specific incorporation of redox active amino acids into proteins |
| BRPI0417801A (pt) | 2003-12-18 | 2007-04-10 | Scripps Research Inst | incorporação seletiva de 5-hidroxitriptofano em proteìnas de células mamìferas |
| 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 |
| EP1797177A4 (en) | 2004-09-21 | 2008-07-09 | Scripps Research Inst | ADDITION OF PHOTOREGULATED AMINO ACIDS TO THE GENETIC CODE |
| 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 |
| FR2888097B1 (fr) * | 2005-07-06 | 2007-10-05 | Oreal | Dispositif de conditionnement et d'application comportant un organe d'essorage |
| CA2624290A1 (en) | 2005-10-12 | 2007-04-26 | Scripps Research Institute | Selective posttranslational modification of phage-displayed polypeptides |
| 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 |
| US7421795B2 (en) * | 2006-08-04 | 2008-09-09 | Seagate Technology Llc | Sapphire alignment fixture |
| CA2663052A1 (en) | 2006-09-21 | 2008-03-27 | The Scripps Research Institute | Genetically programmed expression of selectively sulfated proteins in eubacteria |
| US20080166766A1 (en) | 2006-10-18 | 2008-07-10 | The Scripps Research Institute | Genetic incorporation of unnatural amino acids into proteins in mammalian cells |
| 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 |
| KR20100088618A (ko) | 2007-10-25 | 2010-08-09 | 더 스크립스 리서치 인스티튜트 | 리덕타제 내로의 3-아미노티로신의 유전적 도입 |
| US20090148887A1 (en) | 2007-11-02 | 2009-06-11 | The Scripps Research Institute | Genetically encoded boronate amino acid |
| BRPI0819092A2 (pt) | 2007-11-02 | 2014-10-14 | Scripps Research Inst | Evolução direcionada usando proteínas que compreendem aminoácidos não naturais. |
| 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 |
| KR20100125290A (ko) | 2008-02-08 | 2010-11-30 | 더 스크립스 리서치 인스티튜트 | 유전적으로 코딩된 비천연 아미노산에 의한 면역 내성의 파괴 |
| US20110076718A1 (en) | 2008-02-27 | 2011-03-31 | 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 |
| US8637306B2 (en) | 2008-12-10 | 2014-01-28 | The Scripps Research Institute | Production of carrier-peptide conjugates using chemically reactive unnatural amino acids |
| 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 EP EP02725743.5A patent/EP1490483B1/en not_active Expired - Lifetime
- 2002-04-19 ES ES09006800.8T patent/ES2464532T3/es not_active Expired - Lifetime
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- 2002-04-19 MX MXPA03009566A patent/MXPA03009566A/es active IP Right Grant
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- 2004-12-17 US US11/017,550 patent/US20050250183A1/en not_active Abandoned
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- 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
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- 2006-10-18 US US11/583,551 patent/US7638300B2/en not_active Expired - Lifetime
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- 2007-05-04 US US11/800,455 patent/US7915025B2/en not_active Expired - Fee Related
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- 2007-10-26 US US11/978,217 patent/US20110027867A1/en not_active Abandoned
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- 2007-10-26 US US11/978,156 patent/US8173392B2/en not_active Expired - Fee Related
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- 2008-11-06 JP JP2008285996A patent/JP2009132704A/ja active Pending
- 2008-11-06 JP JP2008285997A patent/JP2009077731A/ja active Pending
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- 2009-01-26 IL IL196714A patent/IL196714A/en active IP Right Grant
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- 2011-08-02 US US13/196,829 patent/US20120202243A1/en not_active Abandoned
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- 2012-05-18 US US13/475,792 patent/US9163271B2/en not_active Expired - Fee Related
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- 2015-04-29 HK HK15104166.3A patent/HK1203558A1/en unknown
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