JP2005502322A - 非天然アミノ酸のインビボ組込み - Google Patents
非天然アミノ酸のインビボ組込み Download PDFInfo
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- JP2005502322A JP2005502322A JP2002583449A JP2002583449A JP2005502322A JP 2005502322 A JP2005502322 A JP 2005502322A JP 2002583449 A JP2002583449 A JP 2002583449A JP 2002583449 A JP2002583449 A JP 2002583449A JP 2005502322 A JP2005502322 A JP 2005502322A
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Cited By (9)
| Publication number | Priority date | Publication date | Assignee | Title |
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| JP2009132704A (ja) * | 2001-04-19 | 2009-06-18 | Scripps Res Inst:The | 非天然アミノ酸のインビボ組込み |
| JP2010502218A (ja) * | 2006-09-08 | 2010-01-28 | アンブルックス,インコーポレイテッド | 修飾ヒト血漿ポリペプチドまたは修飾ヒトFc足場タンパク質ならびにこれらの利用 |
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| JP2010504096A (ja) * | 2006-09-21 | 2010-02-12 | ザ スクリップス リサーチ インスティテュート | 真正細菌における選択的に硫酸化された蛋白質の遺伝的にプログラムされた発現 |
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| AU2005322019B2 (en) * | 2004-12-22 | 2010-08-26 | Ambrx, Inc. | Formulations of human growth hormone comprising a non-naturally encoded amino acid |
| EP1828224B1 (en) | 2004-12-22 | 2016-04-06 | Ambrx, Inc. | Compositions 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 |
| BRPI0518661A2 (pt) * | 2004-12-22 | 2008-12-02 | Ambrx Inc | mÉtodos para expressço e purificaÇço do hormânio do crescimento humano recombinante |
| CN102732588B (zh) | 2004-12-22 | 2015-01-07 | Ambrx公司 | 氨酰基-tRNA合成酶的组合物及其用途 |
| NZ584597A (en) | 2004-12-22 | 2011-09-30 | Ambrx Inc | Modified human growth hormone |
| PA8660701A1 (es) | 2005-02-04 | 2006-09-22 | Pfizer Prod Inc | Agonistas de pyy y sus usos |
| US7723069B2 (en) * | 2005-04-05 | 2010-05-25 | Yale University | Site specific incorporation of phosphoserine into polypeptides using phosphoseryl-tRNA synthetase |
| EP1871795A4 (en) | 2005-04-08 | 2010-03-31 | Biogenerix Ag | COMPOSITIONS AND METHOD FOR PRODUCING GLYCOSYLATION MUTANTS OF A PROTEASE-RESISTANT HUMAN GROWTH HORMONE |
| WO2006122224A1 (en) | 2005-05-11 | 2006-11-16 | Wayne State University | Methods and compositions for the identification of antibiotics that are not susceptible to antibiotic resistance in pseudomonas aeruginosa |
| MX2007015058A (es) * | 2005-06-03 | 2008-01-28 | Ambrx Inc | Moleculas de interferon humano mejoradas y sus usos. |
| EP1891092A4 (en) * | 2005-06-03 | 2011-12-21 | Ambrx Inc | INSTALLATION OF NATURALLY CODED AMINO ACIDS IN PROTEINS |
| JP5068167B2 (ja) * | 2005-06-10 | 2012-11-07 | 中外製薬株式会社 | メグルミンを含有するタンパク質製剤の安定化剤、およびその利用 |
| WO2007005053A1 (en) * | 2005-06-30 | 2007-01-11 | Codon Devices, Inc. | Hierarchical assembly methods for genome engineering |
| DK2233156T3 (da) | 2005-07-15 | 2013-08-05 | Angiochem Inc | Anvendelse af aprotininpolypeptider som bærere i farmaceutiske konjugater |
| CA2782619A1 (en) * | 2005-07-15 | 2007-01-25 | Medical Research Council | Compositions and methods relating to orthogonal ribosome mrna pairs |
| US8008453B2 (en) | 2005-08-12 | 2011-08-30 | Amgen Inc. | Modified Fc molecules |
| CN103103238B (zh) * | 2005-08-18 | 2016-08-10 | Ambrx公司 | 一种在细胞中制造在特定位置处具有所选氨基酸的抗体或抗体片段多肽的方法 |
| CA2620886C (en) | 2005-08-31 | 2017-03-14 | The Regents Of The University Of California | Cellular libraries of peptide sequences (clips) and methods of using the same |
| BRPI0617191A2 (pt) * | 2005-10-12 | 2011-07-19 | Scripps Research Inst | modificação pós-traducional de polipeptìdeos expressos em fagos |
| CN106443006A (zh) | 2005-11-16 | 2017-02-22 | Ambrx公司 | 包括非天然氨基酸的方法和组合物 |
| SG170116A1 (en) * | 2005-12-14 | 2011-04-29 | 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 |
| CN102702105A (zh) * | 2005-12-30 | 2012-10-03 | Ambrx公司 | 含有非天然氨基酸和多肽的组合物、涉及非天然氨基酸和多肽的方法以及非天然氨基酸和多肽的用途 |
| US20090093405A1 (en) * | 2006-01-19 | 2009-04-09 | Ambrx, Inc. | Non-Natural Amino Acid Polypeptides Having Modified Immunogenicity |
| US20070178554A1 (en) * | 2006-02-01 | 2007-08-02 | Nima Shiva | Orthogonal Aminoacyl Synthetase-tRNA Pairs for Incorporating Unnatural Amino Acids Into Proteins |
| US20090081669A1 (en) * | 2006-02-01 | 2009-03-26 | Encode Bio, Inc. | Fluorescent Assays Using Orthogonal tRNA - Aminoacyl Synthetase Pairs |
| US7776535B2 (en) * | 2006-02-06 | 2010-08-17 | Franklin And Marshall College | Site-specific incorporation of fluorinated amino acids into proteins |
| EP1999259B1 (en) | 2006-03-03 | 2014-06-25 | California Institute of Technology | Site-specific incorporation of amino acids into molecules |
| EP1991680B1 (en) | 2006-03-09 | 2013-08-21 | The Scripps Research Institute | System for the expression of orthogonal translation components in eubacterial host cells |
| US7790847B2 (en) * | 2006-03-16 | 2010-09-07 | The Scripps Research Institute | Genetically programmed expression of proteins containing the unnatural amino acid phenylselenocysteine |
| US20080096819A1 (en) * | 2006-05-02 | 2008-04-24 | Allozyne, Inc. | Amino acid substituted molecules |
| CA2653748A1 (en) | 2006-05-02 | 2007-11-15 | Allozyne, Inc. | Non-natural amino acid substituted polypeptides |
| CA2652894A1 (en) | 2006-05-23 | 2007-12-06 | The Scripps Research Institute | Genetically encoded fluorescent coumarin amino acids |
| JP2009539805A (ja) * | 2006-06-09 | 2009-11-19 | ノバルティス アクチエンゲゼルシャフト | 安定化されたインスリン様増殖因子ポリペプチド |
| ATE533846T1 (de) * | 2006-06-28 | 2011-12-15 | Riken | Seprs-mutante und verfahren zur stellengerichteten einführung von phosphoserin in protein unter verwendung davon |
| ES2415635T3 (es) * | 2006-06-29 | 2013-07-26 | The Board Of Trustees Of The Leland Stanford Junior University | Síntesis acelular de proteínas que contienen aminoácidos no naturales |
| CN101517075A (zh) * | 2006-07-13 | 2009-08-26 | 中外制药株式会社 | 细胞死亡诱导剂 |
| AU2013202770B2 (en) * | 2006-09-08 | 2015-08-20 | Ambrx, Inc. | Modified human plasma polypeptide or Fc scaffolds and their uses |
| CA2662755C (en) | 2006-09-08 | 2017-04-04 | Ambrx, Inc. | Suppressor trna transcription in vertebrate cells |
| MX2009002524A (es) * | 2006-09-08 | 2009-06-22 | Ambrx Inc | Incorporacion especifica de sitio de aminoacidos no naturales por celulas de vertebrados. |
| AU2012203737B2 (en) * | 2006-09-08 | 2014-06-19 | Ambrx, Inc. | Modified human plasma polypeptide or Fc scaffolds and their uses |
| RU2009112104A (ru) | 2006-10-18 | 2010-11-27 | Зе Скрипс Ресеч Инститьют (Us) | Генетическое встраивание не встречающихся в природе аминокислот в белки клеток млекопитающих |
| CN101678079B (zh) | 2006-11-28 | 2013-12-25 | 韩诺生物制约株式会社 | 修饰的促红细胞生成素多肽及其治疗用途 |
| EP1936340A1 (en) * | 2006-12-21 | 2008-06-25 | Koninklijke Philips Electronics N.V. | Sub wavelength aperture |
| EP2112928A4 (en) * | 2007-02-22 | 2014-01-08 | Univ Utah Res Found | SYNTHESIS OF NOVEL XYLOSIDES AND ITS POSSIBLE USES |
| CL2008000719A1 (es) * | 2007-03-12 | 2008-09-05 | Univ Tokushima Chugai Seiyaku | Agente terapeutico para cancer resistente a agentes quimioterapeuticos que comprende un anticuerpo que reconoce hla de clase i como ingrediente activo; composicion farmaceutica que comprende dicho anticuerpo; y metodo para tratar cancer resistente a |
| CN107501407B (zh) | 2007-03-30 | 2022-03-18 | Ambrx公司 | 经修饰fgf-21多肽和其用途 |
| EP2155890A4 (en) * | 2007-04-13 | 2010-04-21 | Salk Inst For Biological Studi | METHOD FOR THE GENETIC CODING OF NON-NATURAL AMINO ACIDS IN EUKARYONTIC CELLS USING ORTHOGONAL TRNA / SYNTHETASE PAIRS |
| US8114630B2 (en) * | 2007-05-02 | 2012-02-14 | 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 |
| DK2170930T3 (da) | 2007-06-04 | 2012-11-05 | Synergy Pharmaceuticals Inc | Agonister af guanylatcyclase, anvendelige til behandlingen af gastrointestinale sygdomme, inflammation, cancer og andre sygdomme |
| 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 |
| US8293685B2 (en) * | 2007-07-26 | 2012-10-23 | The Regents Of The University Of California | Methods for enhancing bacterial cell display of proteins and peptides |
| CA2707840A1 (en) | 2007-08-20 | 2009-02-26 | Allozyne, Inc. | Amino acid substituted molecules |
| WO2009036460A2 (en) * | 2007-09-14 | 2009-03-19 | Ambrx, Inc. | Modified human apolipoprotein a-i polypeptides and their uses |
| 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 |
| MX2010004464A (es) | 2007-10-25 | 2010-06-07 | Scripps Research Inst | Incorporacion genetica de 3-aminotirosina a reductasas. |
| US20090148887A1 (en) * | 2007-11-02 | 2009-06-11 | The Scripps Research Institute | Genetically encoded boronate amino acid |
| JP5764329B2 (ja) | 2007-11-02 | 2015-08-19 | ノバルティス アーゲー | 低比重リポタンパク質受容体関連タンパク質6(lrp6)を調節するための分子および方法 |
| 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 |
| MX338336B (es) | 2007-11-20 | 2016-04-07 | Ambrx Inc | Polipeptidos de insulina modificados y sus usos. |
| JP5563990B2 (ja) | 2008-01-03 | 2014-07-30 | ヴェレニウム コーポレイション | トランスフェラーゼおよびオキシドレダクターゼ、それらをコードする核酸並びにそれらを製造および使用する方法 |
| WO2009099763A1 (en) * | 2008-01-30 | 2009-08-13 | Indiana University Research And Technology Corporation | Ester-based peptide prodrugs |
| CA2712606A1 (en) | 2008-02-08 | 2009-08-13 | Ambrx, Inc. | Modified leptin polypeptides and their uses |
| US8318172B2 (en) * | 2008-02-08 | 2012-11-27 | The Scripps Research Institute | Breaking immunological tolerance with a genetically encoded unnatural amino acid |
| WO2009117622A2 (en) * | 2008-03-19 | 2009-09-24 | 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 |
| WO2009120922A2 (en) | 2008-03-27 | 2009-10-01 | Zymogenetics, Inc. | Compositions and methods for inhibiting pdgfrbeta and vegf-a |
| EP2271751B1 (en) | 2008-03-31 | 2015-07-22 | Pacific Biosciences of California, Inc. | Generation of modified polymerases for improved accuracy in single molecule sequencing |
| BRPI0913007A2 (pt) | 2008-05-02 | 2019-09-24 | Novartis Ag | moléculas de ligação aprimoradas à base de fibronectina e usos das mesmas |
| EP2328910B1 (en) | 2008-06-04 | 2014-08-06 | Synergy Pharmaceuticals Inc. | Agonists of guanylate cyclase useful for the treatment of gastrointestinal disorders, inflammation, cancer and other disorders |
| BRPI0915419A2 (pt) | 2008-06-20 | 2015-11-03 | Massachusetts Inst Technology | imunoglobulinas com agregação reduzida |
| WO2009158649A1 (en) | 2008-06-26 | 2009-12-30 | Atyr Pharma, Inc. | Compositions and methods comprising glycyl-trna synthetases having non-canonical biological activities |
| RU2016108598A (ru) | 2008-06-30 | 2018-11-23 | ИЭсБиЭйТЕК, ЭН АЛЬКОН БАЙОМЕДИКАЛ РИСЕРЧ ЮНИТ ЭлЭлСи | Функционализированные полипептиды |
| MX2011000009A (es) | 2008-07-10 | 2011-08-15 | Esbatech Alcon Biomed Res Unit | Metodos y composiciones para la administracion mejorada de macromoleculas. |
| ES2624828T3 (es) | 2008-07-16 | 2017-07-17 | Synergy Pharmaceuticals Inc. | Agonistas de la guanilato ciclasa útiles para el tratamiento de trastornos gastrointestinales, inflamación, cáncer y otros |
| UA118536C2 (uk) | 2008-07-23 | 2019-02-11 | Амбркс, Інк. | Модифікований поліпептид бичачого гранулоцитарного колонієстимулювального фактора та його застосування |
| US9182406B2 (en) * | 2008-08-04 | 2015-11-10 | Biodesy, Inc. | Nonlinear optical detection of molecules comprising an unnatural amino acid possessing a hyperpolarizability |
| WO2010022171A1 (en) * | 2008-08-19 | 2010-02-25 | Ferring International Center S.A. | Peptidic pth receptor agonists |
| NZ592249A (en) | 2008-09-26 | 2013-03-28 | Ambrx Inc | Non-natural amino acid replication-dependent microorganisms and vaccines |
| HUE035168T2 (en) | 2008-09-26 | 2018-05-02 | Ambrx Inc | Modified animal erythropoietin polypeptides and their applications |
| US8921314B2 (en) | 2008-10-15 | 2014-12-30 | Angiochem, Inc. | Conjugates of GLP-1 agonists and uses thereof |
| JP5542832B2 (ja) | 2008-10-24 | 2014-07-09 | アイアールエム・リミテッド・ライアビリティ・カンパニー | 生合成的に製造したピロリン−カルボキシ−リシンならびにピロリン−カルボキシ−リシンおよびピロリシン基の化学誘導体化を介する部位特異的タンパク質修飾 |
| JP5759379B2 (ja) | 2008-12-05 | 2015-08-05 | アンジオケム インコーポレーテッド | ニューロテンシンまたはニューロテンシンアナログおよびその使用 |
| US8609383B2 (en) | 2008-12-10 | 2013-12-17 | 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 |
| WO2010069074A1 (en) | 2008-12-17 | 2010-06-24 | Universite Du Quebec A Montreal | Membrane type-1 matrix metalloprotein inhibitors and uses thereof |
| JP5789515B2 (ja) | 2008-12-19 | 2015-10-07 | インディアナ ユニバーシティー リサーチ アンド テクノロジー コーポレーションIndiana University Research And Technology Corporation | インスリン類似体 |
| WO2010071807A1 (en) | 2008-12-19 | 2010-06-24 | Indiana University Research And Technology Corporation | Amide based glucagon superfamily peptide prodrugs |
| CN102300580A (zh) * | 2008-12-19 | 2011-12-28 | 印第安纳大学研究及科技有限公司 | 二肽连接的药剂 |
| CA2744558A1 (en) | 2008-12-19 | 2010-07-15 | Indiana University Research And Technology Corporation | Amide-based insulin prodrugs |
| WO2010096394A2 (en) | 2009-02-17 | 2010-08-26 | Redwood Biosciences, Inc. | Aldehyde-tagged protein-based drug carriers and methods of use |
| US20120004185A1 (en) | 2009-02-27 | 2012-01-05 | Atyr Pharma, Inc. | Polypeptide structural motifs associated with cell signaling activity |
| EP2414513B1 (en) * | 2009-03-31 | 2015-10-28 | Atyr Pharma, Inc. | 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 |
| WO2010132341A2 (en) | 2009-05-11 | 2010-11-18 | Pfenex, Inc. | Production of recombinant proteins utilizing non-antibiotic selection methods and the incorporation of non-natural amino acids therein |
| WO2010141902A2 (en) | 2009-06-04 | 2010-12-09 | Novartis Ag | METHODS FOR IDENTIFICATION OF SITES FOR IgG CONJUGATION |
| CN102596993A (zh) | 2009-07-02 | 2012-07-18 | 安吉奥开米公司 | 多聚体肽结合物以及其应用 |
| US20110054019A1 (en) * | 2009-09-01 | 2011-03-03 | Pedro Anastacio Serrano-Ojeda | Cancer Starvation Therapy |
| US10292956B2 (en) | 2009-09-01 | 2019-05-21 | Serbig Pharmaceutics Corp. | Cancer starvation therapy |
| EP2311947A1 (en) * | 2009-10-14 | 2011-04-20 | Ludwig-Maximilians-Universität München | Protein synthesis via click chemistry |
| WO2011056494A1 (en) | 2009-10-26 | 2011-05-12 | Genentech, Inc. | Activin receptor-like kinase-1 antagonist and vegfr3 antagonist combinations |
| WO2011056502A1 (en) | 2009-10-26 | 2011-05-12 | Genentech, Inc. | Bone morphogenetic protein receptor type ii compositions and methods of use |
| 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 |
| EA201290541A1 (ru) | 2009-12-21 | 2013-05-30 | Амбркс, Инк. | Модифицированные бычьи соматотропиновые полипептиды и их применение |
| EP2516455A4 (en) | 2009-12-21 | 2013-05-22 | Ambrx Inc | MODIFIED SWINE SOMATOTROPIN POLYPEPTIDES AND THEIR USES |
| US9051593B2 (en) | 2009-12-21 | 2015-06-09 | Trustees Of Dartmouth College | Recombinant prokaryotes and use thereof for production of O-glycosylated proteins |
| US8637456B2 (en) | 2010-01-27 | 2014-01-28 | 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 |
| US20120296403A1 (en) | 2010-02-10 | 2012-11-22 | Novartis Ag | Methods and compounds for muscle growth |
| 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 |
| CN103118692A (zh) | 2010-04-26 | 2013-05-22 | Atyr医药公司 | 与半胱氨酰-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 |
| 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 |
| CA2797259C (en) | 2010-04-27 | 2020-09-29 | Atyr Pharma, Inc. | Innovative discovery of therapeutic, diagnostic, and antibody compositions related to protein fragments of threonyl trna synthetases |
| US8993723B2 (en) | 2010-04-28 | 2015-03-31 | Atyr Pharma, Inc. | Innovative discovery of therapeutic, diagnostic, and antibody compositions related to protein fragments of alanyl-tRNA synthetases |
| CN103118693B (zh) | 2010-04-29 | 2017-05-03 | Atyr 医药公司 | 与缬氨酰‑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 |
| 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 |
| ES2623805T3 (es) | 2010-05-03 | 2017-07-12 | Atyr Pharma, Inc. | Descubrimiento innovador de composiciones terapéuticas, de diagnóstico y de anticuerpos relacionadas con fragmentos de proteínas de fenilalanil-alfa-ARNt sintetasas |
| WO2011140135A2 (en) | 2010-05-03 | 2011-11-10 | Atyr Pharma, Inc. | Innovative discovery of therapeutic, diagnostic, and antibody compositions related to protein fragments of methionyl-trna synthetases |
| AU2011248355B2 (en) | 2010-05-03 | 2017-01-19 | Pangu Biopharma Limited | Innovative discovery of therapeutic, diagnostic, and antibody compositions related to protein fragments of Arginyl-tRNA synthetases |
| EP2566516B1 (en) | 2010-05-03 | 2019-07-03 | aTyr Pharma, Inc. | Innovative discovery of therapeutic, diagnostic, and antibody compositions related to protein fragments of seryl-trna synthetases |
| 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 |
| CA2798301C (en) | 2010-05-04 | 2020-09-15 | Atyr Pharma, Inc. | Innovative discovery of therapeutic, diagnostic, and antibody compositions related to protein fragments of glutamyl-prolyl-trna synthetases |
| WO2011143482A2 (en) | 2010-05-14 | 2011-11-17 | Atyr Pharma, Inc. | Innovative discovery of therapeutic, diagnostic, and antibody compositions related to protein fragments of phenylalanyl-beta-trna synthetases |
| WO2011146410A2 (en) | 2010-05-17 | 2011-11-24 | Atyr Pharma, Inc. | Innovative discovery of therapeutic, diagnostic, and antibody compositions related to protein fragments of leucyl-trna synthetases |
| CA2800375C (en) | 2010-05-27 | 2021-03-09 | Atyr Pharma, Inc. | Innovative discovery of therapeutic, diagnostic, and antibody compositions related to protein fragments of glutaminyl-trna synthetases |
| WO2011153277A2 (en) | 2010-06-01 | 2011-12-08 | Atyr Pharma, Inc. | Innovative discovery of therapeutic, diagnostic, and antibody compositions related to protein fragments of lysyl-trna synthetases |
| CN103068842B (zh) | 2010-06-16 | 2016-10-19 | 印第安纳大学研究及科技有限公司 | 对胰岛素受体具有高活性的单链胰岛素激动剂 |
| WO2011163462A2 (en) | 2010-06-24 | 2011-12-29 | Indiana University Research And Technology Corporation | Amide-based insulin prodrugs |
| US8778872B2 (en) | 2010-06-24 | 2014-07-15 | Indiana University Research And Technology Corporation | Amide based glucagon superfamily peptide 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 |
| CN103118695B (zh) | 2010-07-12 | 2016-08-03 | Atyr医药公司 | 与甘氨酰-tRNA合成酶的蛋白片段相关的治疗、诊断和抗体组合物的发现 |
| NZ603811A (en) * | 2010-07-12 | 2015-03-27 | Atyr Pharma Inc | Innovative discovery of therapeutic, diagnostic, and antibody compositions related to protein fragments of aspartyl-trna synthetases |
| EA030418B1 (ru) | 2010-07-12 | 2018-08-31 | ЭйТИР ФАРМА, ИНК. | ТЕРАПЕВТИЧЕСКАЯ КОМПОЗИЦИЯ И СПОСОБ ДЛЯ ЛЕЧЕНИЯ ВОСПАЛИТЕЛЬНОГО ЗАБОЛЕВАНИЯ, ПОЛИПЕПТИД АМИНОАЦИЛ-тРНК-СИНТЕТАЗЫ (AARS) |
| 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 |
| US9029506B2 (en) | 2010-08-25 | 2015-05-12 | Atyr Pharma, Inc. | Innovative discovery of therapeutic, diagnostic, and antibody compositions related to protein fragments of tyrosyl-tRNA synthetases |
| WO2012032181A2 (en) | 2010-09-10 | 2012-03-15 | Allozyne, Inc | Novel antibody derivatives |
| US9616097B2 (en) | 2010-09-15 | 2017-04-11 | Synergy Pharmaceuticals, Inc. | Formulations of guanylate cyclase C agonists and methods of use |
| TWI480288B (zh) | 2010-09-23 | 2015-04-11 | Lilly Co Eli | 牛顆粒細胞群落刺激因子及其變體之調配物 |
| CN103118696B (zh) * | 2010-10-06 | 2020-02-14 | Atyr 医药公司 | 与色氨酰-tRNA合成酶的蛋白片段相关的治疗、诊断和抗体组合物 |
| 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 |
| EP2670767B1 (en) | 2011-02-03 | 2017-12-20 | European Molecular Biology Laboratory | Unnatural amino acids comprising a cyclooctynyl or trans-cyclooctenyl analog group and uses thereof |
| AU2012230899A1 (en) | 2011-03-21 | 2013-10-10 | 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 |
| MX345538B (es) | 2011-05-27 | 2017-02-03 | Ambrx Inc | Composiciones que contienen, metodos que incluyen, y usos de derivados de dolastatina enlazados a aminoacidos no naturales. |
| DK2714684T3 (en) | 2011-05-27 | 2018-11-26 | Ambrx Inc | COMPOSITIONS CONTAINING, PROCEDURE INVOLVING, AND APPLICATIONS OF NON-NATURAL AMINO ACID-BONDED DOLASTATIN DERIVATIVES |
| US11788111B2 (en) | 2011-07-11 | 2023-10-17 | 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 |
| US10876142B2 (en) | 2011-07-11 | 2020-12-29 | 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 |
| US10323236B2 (en) | 2011-07-22 | 2019-06-18 | 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 |
| UY34347A (es) | 2011-09-26 | 2013-04-30 | Novartis Ag | Proteínas de función dual para tratar trastornos metabólicos |
| WO2013068874A1 (en) | 2011-11-11 | 2013-05-16 | Pfizer Inc. | Antibody-drug conjugates |
| WO2013086216A1 (en) | 2011-12-06 | 2013-06-13 | Atyr Pharma, Inc. | Improved aspartyl-trna synthetases |
| US9822353B2 (en) | 2011-12-06 | 2017-11-21 | Atyr Pharma, Inc. | PEGylated aspartyl-tRNA synthetase polypeptides |
| CN104114183A (zh) | 2011-12-20 | 2014-10-22 | 印第安纳大学研究及科技有限公司 | 用于治疗糖尿病的基于ctp的胰岛素类似物 |
| EP2813512B1 (en) | 2011-12-28 | 2021-03-31 | Chugai Seiyaku Kabushiki Kaisha | Peptide-compound cyclization method |
| CN104220461A (zh) | 2011-12-29 | 2014-12-17 | Atyr医药公司 | 天冬氨酰-tRNA合成酶-FC缀合物 |
| US9395358B2 (en) | 2012-02-05 | 2016-07-19 | Biodesy, Inc. | Methods for detecting allosteric modulators of protein |
| DK2814514T3 (en) | 2012-02-16 | 2017-12-18 | Atyr Pharma Inc | Histidyl tRNA synthetases for the treatment of autoimmune and inflammatory diseases |
| SG11201406769RA (en) | 2012-05-10 | 2014-11-27 | Massachusetts Inst Technology | Agents for influenza neutralization |
| NZ703298A (en) | 2012-06-07 | 2016-04-29 | Ambrx Inc | Prostate-specific membrane antigen antibody drug conjugates |
| EP3505534A1 (en) | 2012-06-08 | 2019-07-03 | Sutro Biopharma, Inc. | Antibodies comprising sitespecific nonnatural amino acid residues, methods of their preparation and methods of their use |
| ES2712648T3 (es) | 2012-06-19 | 2019-05-14 | Ambrx Inc | Conjugados de fármaco de anticuerpo anti-CD70 |
| EP2863955B1 (en) | 2012-06-26 | 2016-11-23 | Sutro Biopharma, Inc. | Modified fc proteins comprising site-specific non-natural amino acid residues, conjugates of the same, methods of their preparation and methods of their use |
| CN103571804B (zh) * | 2012-08-10 | 2015-08-12 | 中国科学院生物物理研究所 | 3-吡唑基酪氨酸翻译系统及其应用 |
| EP2887966B1 (en) | 2012-08-22 | 2018-07-18 | The Government of the United States of America as represented by The Secretary of the Department of Health and Human Services | Engineered anthrax lethal toxin for targeted delivery |
| WO2014035364A2 (en) * | 2012-08-27 | 2014-03-06 | Empire Technology Development Llc | Gelatin alkyd peptides and uses thereof |
| ES2728864T3 (es) | 2012-08-31 | 2019-10-29 | Sutro Biopharma Inc | Aminoácidos modificados que comprenden un grupo azido |
| CA2885796C (en) | 2012-09-24 | 2022-05-03 | Allozyne, Inc. | Cell lines |
| WO2014052451A2 (en) | 2012-09-26 | 2014-04-03 | Indiana University Research And Technology Corporation | Insulin analog dimers |
| CN102875733B (zh) * | 2012-10-25 | 2014-06-11 | 西安科技大学 | 具有仿细胞外层膜结构的纳米颗粒及其制备方法 |
| US20140120116A1 (en) | 2012-10-26 | 2014-05-01 | The Chinese University Of Hong Kong | Treatment of cancer using smad3 inhibitor |
| UY35144A (es) | 2012-11-20 | 2014-06-30 | Novartis Ag | Miméticos lineales sintéticos de apelina para el tratamiento de insuficiencia cardiaca |
| LT2935320T (lt) | 2012-12-18 | 2019-11-11 | Novartis Ag | Stabilizuoti insulino tipo augimo faktoriaus polipeptidai |
| WO2014116730A2 (en) | 2013-01-23 | 2014-07-31 | The Board Of Trustees Of The Leland Stanford Junior University | Stabilized hepatitis b core polypeptide |
| US9545446B2 (en) | 2013-02-25 | 2017-01-17 | Synergy Pharmaceuticals, Inc. | Agonists of guanylate cyclase and their uses |
| US9255255B2 (en) | 2013-03-04 | 2016-02-09 | The Board Of Trustees Of The Leland Stanford Junior University | Synthesis of linear and branched polymers of polypeptides through direct conjugation |
| UY35368A (es) | 2013-03-08 | 2014-10-31 | Irm Llc | Péptidos y composiciones para el tratamiento de daño articular |
| BR112015023071A2 (pt) | 2013-03-14 | 2017-07-18 | Univ Indiana Res & Tech Corp | conjugados de insulina-incretina |
| US9486494B2 (en) | 2013-03-15 | 2016-11-08 | Synergy Pharmaceuticals, Inc. | Compositions useful for the treatment of gastrointestinal disorders |
| EP2968469A4 (en) | 2013-03-15 | 2016-08-31 | Longevity Biotech Inc | PEPTIDES COMPRISING NON-ENDOGENIC AMINO ACIDS AND METHODS OF MAKING AND USING SAME |
| US11156608B2 (en) | 2013-03-15 | 2021-10-26 | The Trustees Of The University Of Pennsylvania | Method for the site-specific covalent cross-linking of antibodies to surfaces |
| CA2905438A1 (en) | 2013-03-15 | 2014-09-25 | Synergy Pharmaceuticals Inc. | Agonists of guanylate cyclase and their uses |
| JP6397479B2 (ja) | 2013-03-15 | 2018-09-26 | エータイアー ファーマ, インコーポレイテッド | ヒスチジル−tRNAシンテターゼFcコンジュゲート |
| 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 |
| JP6606491B2 (ja) | 2013-06-05 | 2019-11-13 | 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 | グアニル酸シクラーゼcの超高純度アゴニスト、その作成および使用方法 |
| US9764039B2 (en) | 2013-07-10 | 2017-09-19 | Sutro Biopharma, Inc. | Antibodies comprising multiple site-specific non-natural amino acid residues, methods of their preparation and methods of their use |
| US10005838B2 (en) | 2013-07-19 | 2018-06-26 | The Regents Of The University Of California | Milk fat globule epidermal growth factor 8 regulates fatty acid uptake |
| CA2918074A1 (en) | 2013-07-25 | 2015-01-29 | Novartis Ag | Cyclic polypeptides for the treatment of heart failure |
| CA2918077A1 (en) | 2013-07-25 | 2015-01-29 | Novartis Ag | Bioconjugates of synthetic apelin polypeptides |
| US20150044192A1 (en) | 2013-08-09 | 2015-02-12 | President And Fellows Of Harvard College | Methods for identifying a target site of a cas9 nuclease |
| AU2014305843B2 (en) | 2013-08-09 | 2019-08-29 | Ardelyx, Inc. | Compounds and methods for inhibiting phosphate transport |
| US9359599B2 (en) | 2013-08-22 | 2016-06-07 | President And Fellows Of Harvard College | Engineered transcription activator-like effector (TALE) domains and uses thereof |
| US10011649B2 (en) | 2013-08-26 | 2018-07-03 | Arizona Board Of Regents On Behalf Of Arizona State University | High affinity synbodies for influenza |
| US9228207B2 (en) | 2013-09-06 | 2016-01-05 | President And Fellows Of Harvard College | Switchable gRNAs comprising aptamers |
| US9737604B2 (en) | 2013-09-06 | 2017-08-22 | President And Fellows Of Harvard College | Use of cationic lipids to deliver CAS9 |
| US9322037B2 (en) | 2013-09-06 | 2016-04-26 | President And Fellows Of Harvard College | Cas9-FokI fusion proteins and uses thereof |
| MY176976A (en) | 2013-10-10 | 2020-08-28 | Bausch Health Ireland Ltd | Agonists of guanylate cyclase useful for the treatment of opioid induced dysfunctions |
| EP3055298B1 (en) | 2013-10-11 | 2020-04-29 | Sutro Biopharma, Inc. | Modified amino acids comprising tetrazine functional groups, methods of preparation, and methods of their use |
| EP3057605A1 (en) | 2013-10-18 | 2016-08-24 | Novartis AG | Methods of treating diabetes and related disorders |
| US20150166982A1 (en) | 2013-12-12 | 2015-06-18 | President And Fellows Of Harvard College | Methods for correcting pi3k point mutations |
| CA2936615C (en) | 2014-01-14 | 2023-06-13 | European Molecular Biology Laboratory | Multiple cycloaddition reactions for labeling of molecules |
| US10501734B2 (en) | 2014-02-06 | 2019-12-10 | Yale University | Compositions and methods of use thereof for making polypeptides with many instances of nonstandard amino acids |
| AU2015259465A1 (en) | 2014-05-13 | 2016-11-17 | 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 |
| CN106573955B (zh) | 2014-06-23 | 2021-02-26 | 诺华股份有限公司 | 位点特异性蛋白质修饰 |
| US10316322B2 (en) | 2014-07-02 | 2019-06-11 | 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 |
| US10077453B2 (en) | 2014-07-30 | 2018-09-18 | President And Fellows Of Harvard College | CAS9 proteins including ligand-dependent inteins |
| EP3189152A4 (en) | 2014-09-03 | 2018-04-04 | BioAtla LLC | Discovering and producing conditionally active biologic proteins in the same eukaryotic cell production hosts |
| CN108271356A (zh) | 2014-09-24 | 2018-07-10 | 印第安纳大学研究及科技有限公司 | 肠降血糖素-胰岛素缀合物 |
| 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 |
| HUE055311T2 (hu) | 2014-10-24 | 2021-11-29 | Bristol Myers Squibb Co | Módosított FGF-21 polipeptidek és azok felhasználása |
| EP4289483A3 (en) | 2014-12-04 | 2024-02-28 | Celgene Corporation | Biomolecule conjugates |
| WO2016106286A1 (en) | 2014-12-23 | 2016-06-30 | Biodesy, 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 |
| AU2016211161C1 (en) | 2015-01-30 | 2023-11-23 | The Regents Of The University Of California | Protein delivery in primary hematopoietic cells |
| DK3269809T3 (da) | 2015-03-13 | 2022-09-12 | Chugai Pharmaceutical Co Ltd | MODIFICERET AMINOACYL-tRNA-SYNTETASE OG ANVENDELSE DERAF |
| US10483262B2 (en) * | 2015-05-15 | 2019-11-19 | Taiwan Semiconductor Manufacturing Co., Ltd. | Dual nitride stressor for semiconductor device and method of manufacturing |
| EP3309250A4 (en) | 2015-06-09 | 2019-06-19 | National Institute of Advanced Industrial Science and Technology | AMINO ACID MODIFIED NUCLEIC ACID AND USE THEREOF |
| JP6823055B2 (ja) | 2015-06-15 | 2021-01-27 | アンジオケム インコーポレーテッド | 軟髄膜癌腫症の治療方法 |
| HK1258529A1 (zh) | 2015-07-10 | 2019-11-15 | 香港科技大学 | 用於治疗神经退行性和神经炎性病症的方法和组合物 |
| WO2017062334A1 (en) | 2015-10-05 | 2017-04-13 | Merck Sharp & Dohme Corp. | Antibody peptide conjugates that have agonist activity at both the glucagon and glucagon-like peptide 1 receptors |
| CA3002827A1 (en) | 2015-10-23 | 2017-04-27 | President And Fellows Of Harvard College | Nucleobase editors and uses thereof |
| JP6946304B2 (ja) | 2015-12-22 | 2021-10-06 | ノバルティス アーゲー | 増殖分化因子15(gdf−15)を使用して代謝障害を処置するまたは軽快させる方法 |
| MY197023A (en) | 2015-12-23 | 2023-05-22 | 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 |
| JP2019506383A (ja) | 2016-01-11 | 2019-03-07 | 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 | 潰瘍性大腸炎を治療するための製剤および方法 |
| CA3011455A1 (en) | 2016-01-27 | 2017-08-03 | Sutro Biopharma, Inc. | Anti-cd74 antibody conjugates, compositions comprising anti-cd74 antibody conjugates and methods of using anti-cd74 antibody conjugates |
| CA3019398A1 (en) | 2016-04-26 | 2017-11-02 | R.P. Scherer Technologies, Llc | Antibody conjugates and methods of making and using the same |
| WO2017196891A1 (en) | 2016-05-09 | 2017-11-16 | Biodesy, Inc. | Methods and devices for detection of peripheral membrane protein interactions using nonlinear optical techniques |
| WO2017204729A1 (en) * | 2016-05-25 | 2017-11-30 | Fogelstrand Per | Method for preparing a biological sample for use in an immunolabeling process |
| AU2017283787B2 (en) | 2016-06-15 | 2020-09-17 | Novartis Ag | Methods for treating disease using inhibitors of bone morphogenetic protein 6 (BMP6) |
| KR102827276B1 (ko) | 2016-08-03 | 2025-07-01 | 프레지던트 앤드 펠로우즈 오브 하바드 칼리지 | 아데노신 핵염기 편집제 및 그의 용도 |
| JP7201153B2 (ja) | 2016-08-09 | 2023-01-10 | プレジデント アンド フェローズ オブ ハーバード カレッジ | プログラム可能cas9-リコンビナーゼ融合タンパク質およびその使用 |
| US11542509B2 (en) | 2016-08-24 | 2023-01-03 | President And Fellows Of Harvard College | Incorporation of unnatural amino acids into proteins using base editing |
| EP3309260A1 (en) | 2016-10-14 | 2018-04-18 | European Molecular Biology Laboratory | Archaeal pyrrolysyl trna synthetases for orthogonal use |
| KR20240007715A (ko) | 2016-10-14 | 2024-01-16 | 프레지던트 앤드 펠로우즈 오브 하바드 칼리지 | 핵염기 에디터의 aav 전달 |
| CA3043667A1 (en) | 2016-11-14 | 2018-05-17 | Novartis Ag | Methods and compositions for treatment of cartilage damage and arthritis |
| CN109996809A (zh) | 2016-11-14 | 2019-07-09 | 诺华股份有限公司 | 与促融合蛋白minion相关的组合物、方法和治疗用途 |
| CN110268055A (zh) | 2016-12-19 | 2019-09-20 | 宽腾矽公司 | 用于测序反应的聚合酶 |
| US10745677B2 (en) | 2016-12-23 | 2020-08-18 | President And Fellows Of Harvard College | Editing of CCR5 receptor gene to protect against HIV infection |
| WO2018126229A2 (en) | 2016-12-30 | 2018-07-05 | Sutrovax, Inc. | Polypeptide-antigen conjugates with non-natural amino acids |
| 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 |
| AU2018219283B2 (en) | 2017-02-08 | 2022-05-19 | Bristol-Myers Squibb Company | Modified relaxin polypeptides comprising a pharmacokinetic enhancer and uses thereof |
| US12390514B2 (en) | 2017-03-09 | 2025-08-19 | President And Fellows Of Harvard College | Cancer vaccine |
| US11898179B2 (en) | 2017-03-09 | 2024-02-13 | President And Fellows Of Harvard College | Suppression of pain by gene editing |
| WO2018165629A1 (en) | 2017-03-10 | 2018-09-13 | President And Fellows Of Harvard College | Cytosine to guanine base editor |
| BR112019019655A2 (pt) | 2017-03-23 | 2020-04-22 | Harvard College | editores de nucleobase que compreendem proteínas de ligação a dna programáveis por ácido nucleico |
| 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 |
| US11560566B2 (en) | 2017-05-12 | 2023-01-24 | President And Fellows Of Harvard College | Aptazyme-embedded guide RNAs for use with CRISPR-Cas9 in genome editing and transcriptional activation |
| LT3630977T (lt) | 2017-06-02 | 2024-04-25 | Ambrx, Inc. | Baltymų, kurių sudėtyje yra negamtinių aminorūgščių, gamybos skatinimo būdai ir kompozicijos |
| KR102744693B1 (ko) | 2017-06-09 | 2024-12-18 | 추가이 세이야쿠 가부시키가이샤 | N-치환 아미노산을 포함하는 펩타이드의 합성 방법 |
| PE20200013A1 (es) | 2017-06-20 | 2020-01-06 | Amgen Inc | Metodo para tratar o mejorar trastornos metabolicos con proteinas de union para el receptor peptidico inhibidor gastrico (gipr) en combinacion con agonistas de glp-1 |
| MA49459A (fr) | 2017-06-21 | 2020-04-29 | Amgen Inc | Méthode de traitement ou d'amélioration des troubles métaboliques à l'aide de protéines de liaison antagonistes pour protéines de fusion agonistes du récepteur du peptide inhibiteur gastrique (gipr)/récepteur glp-1 |
| 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 |
| US20200207859A1 (en) | 2017-07-26 | 2020-07-02 | Sutro Biopharma, Inc. | Methods of using anti-cd74 antibodies and antibody conjugates in treatment of t-cell lymphoma |
| JP2020534795A (ja) | 2017-07-28 | 2020-12-03 | プレジデント アンド フェローズ オブ ハーバード カレッジ | ファージによって支援される連続的進化(pace)を用いて塩基編集因子を進化させるための方法および組成物 |
| AR112969A1 (es) | 2017-08-03 | 2020-01-15 | Synthorx Inc | Conjugados de citoquina para el tratamiento de enfermedades proliferativas e infecciosas |
| WO2019139645A2 (en) | 2017-08-30 | 2019-07-18 | President And Fellows Of Harvard College | High efficiency base editors comprising gam |
| TW201920249A (zh) | 2017-09-07 | 2019-06-01 | 美商信號生物製藥公司 | 具有結合位點之t細胞調節多聚體多肽及其使用方法 |
| KR20200051802A (ko) | 2017-09-18 | 2020-05-13 | 서트로 바이오파마, 인크. | 항-엽산 수용체 알파 항체 접합체 및 이의 용도 |
| CN111757937A (zh) | 2017-10-16 | 2020-10-09 | 布罗德研究所股份有限公司 | 腺苷碱基编辑器的用途 |
| CN111479819B (zh) | 2017-12-15 | 2024-06-14 | 中外制药株式会社 | 制备肽的方法和处理碱的方法 |
| EP3724214A4 (en) | 2017-12-15 | 2021-09-01 | The Broad Institute Inc. | SYSTEMS AND METHODS FOR PREDICTING REPAIR RESULTS IN GENETIC ENGINEERING |
| WO2019213331A1 (en) | 2018-05-01 | 2019-11-07 | Ambrx, Inc. | A method for optimizing antibody expression |
| 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 |
| EP3847271A4 (en) * | 2018-09-07 | 2022-10-12 | MedImmune, LLC | Methods of cell selection |
| EP4389145A3 (en) | 2018-09-11 | 2024-08-21 | Ambrx, Inc. | Interleukin-2 polypeptide conjugates and their uses |
| WO2020060944A1 (en) | 2018-09-17 | 2020-03-26 | Sutro Biopharma, Inc. | Combination therapies with anti-folate receptor antibody conjugates |
| EP3867265A1 (en) | 2018-10-19 | 2021-08-25 | 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 |
| WO2020097261A1 (en) | 2018-11-06 | 2020-05-14 | The United States Of America As Represented By The Secretary Of The Department Of Health And Human Services | New compositions and methods for treating beta-globinopathies |
| EP3878836B1 (en) | 2018-11-07 | 2025-07-23 | Chugai Seiyaku Kabushiki Kaisha | O-substituted serine derivative production method |
| CN113056475B (zh) | 2018-11-30 | 2024-09-24 | 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 |
| JP7695885B2 (ja) | 2019-02-12 | 2025-06-19 | アンブルックス,インコーポレイテッド | 抗体-tlrアゴニストコンジュゲートを含有する組成物、その方法、及び使用 |
| EP3696189A1 (en) | 2019-02-14 | 2020-08-19 | European Molecular Biology Laboratory | Means and methods for preparing engineered target proteins by genetic code expansion in a target protein selective manner |
| CN113785058B (zh) * | 2019-03-04 | 2024-12-24 | 得克萨斯A&M大学系统 | 制作和利用琥珀专性的噬菌体展示文库的方法 |
| US12071396B2 (en) | 2019-03-15 | 2024-08-27 | Chugai Seiyaku Kabushiki Kaisha | Method for preparing aromatic amino acid derivative |
| GB2601617B (en) | 2019-03-19 | 2024-02-21 | Broad Inst Inc | Methods and compositions for editing nucleotide sequences |
| EP3956349A1 (en) | 2019-04-17 | 2022-02-23 | 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 |
| US12258304B2 (en) | 2019-05-20 | 2025-03-25 | 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 |
| WO2020247803A2 (en) | 2019-06-07 | 2020-12-10 | Massachusetts Institute Of Technology | Frameshift suppressor trna compositions and methods of use |
| EP3980423A1 (en) | 2019-06-10 | 2022-04-13 | Sutro Biopharma, Inc. | 5h-pyrrolo[3,2-d]pyrimidine-2,4-diamino compounds and antibody conjugates thereof |
| 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 |
| WO2020264429A1 (en) | 2019-06-28 | 2020-12-30 | Quantum-Si Incorporated | Polymerizing enzymes for sequencing reactions |
| EP4041873A4 (en) | 2019-10-08 | 2023-10-25 | Trustees of Boston College | PROTEINS CONTAINING SEVERAL DIFFERENT UNNATURAL AMINO ACIDS AND METHODS FOR PRODUCING AND USING SUCH PROTEINS |
| WO2021072328A1 (en) | 2019-10-10 | 2021-04-15 | The Broad Institute, Inc. | Methods and compositions for prime editing rna |
| 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 |
| WO2021076795A1 (en) * | 2019-10-15 | 2021-04-22 | Trustees Of Boston College | Chimeric thermostable aminoacyl-trna synthetase for enhanced unnatural amino acid incorporation |
| US11149280B2 (en) | 2019-10-29 | 2021-10-19 | Yale University | Engineering organisms resistant to viruses and horizontally transferred genetic elements |
| SG10202111127YA (en) | 2019-11-07 | 2021-11-29 | Chugai Pharmaceutical Co Ltd | Cyclic Peptide Compound Having Kras Inhibitory Action |
| CN113597434B (zh) | 2019-12-31 | 2022-07-01 | 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 |
| WO2021138581A1 (en) | 2020-01-03 | 2021-07-08 | The United States Of America, As Represented By The Secretary, Department Of Health And Human Services | Tnap locally administered for promoting periodontal health |
| CN115322794B (zh) | 2020-01-11 | 2025-09-19 | 北京质肽生物医药科技有限公司 | Glp-1和fgf21的融合蛋白的缀合物 |
| EP4107258A4 (en) * | 2020-02-20 | 2024-04-17 | B.G. Negev Technologies and Applications Ltd., at Ben-Gurion University | MUTANT AMINOACYL-ARNT 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 |
| EP4139340A1 (en) | 2020-04-22 | 2023-03-01 | Merck Sharp & Dohme LLC | Human interleukin-2 conjugates biased for the interleukin-2 receptor beta gammac dimer and conjugated to a nonpeptidic, water-soluble polymer |
| US12351850B2 (en) | 2020-04-30 | 2025-07-08 | Sutro Biopharma, Inc. | Methods of producing full-length antibodies using E. coli |
| JP2023524288A (ja) | 2020-05-05 | 2023-06-09 | ジェネンテック, インコーポレイテッド | チロシナーゼ媒介部位特異的タンパク質コンジュゲーションのためのシステム及び方法 |
| EP4146804A1 (en) | 2020-05-08 | 2023-03-15 | The Broad Institute Inc. | Methods and compositions for simultaneous editing of both strands of a target double-stranded nucleotide sequence |
| US20230201319A1 (en) | 2020-05-22 | 2023-06-29 | Takeda Pharmaceutical Company Limited | Adamts13 compositions and methods for treating and diagnosing complications of coronavirus disease |
| WO2022040596A1 (en) | 2020-08-20 | 2022-02-24 | Ambrx, Inc. | Antibody-tlr agonist conjugates, methods and uses thereof |
| KR20230069187A (ko) * | 2020-09-14 | 2023-05-18 | 서트로 바이오파마, 인크. | 무세포 단백질 합성 시스템을 이용한 항체의 대량 생산 방법 |
| WO2022068920A1 (en) | 2020-09-30 | 2022-04-07 | Beijing Ql Biopharmaceutical Co., Ltd. | Polypeptide conjugates and methods of uses |
| JP2024512775A (ja) | 2021-04-03 | 2024-03-19 | アンブルックス,インコーポレイテッド | 抗her2抗体薬物コンジュゲート及びその使用 |
| US20230016731A1 (en) * | 2021-05-21 | 2023-01-19 | The Regents Of The University Of California | Affinity purification sequencing |
| EP4366782A1 (en) | 2021-07-09 | 2024-05-15 | Bright Peak Therapeutics AG | Conjugates of checkpoint inhibitors with il-2, and uses thereof |
| US20230201365A1 (en) | 2021-07-09 | 2023-06-29 | Bright Peak Therapeutics Ag | Modified cd20 antibodies and uses thereof |
| KR20240040134A (ko) | 2021-07-09 | 2024-03-27 | 브라이트 피크 테라퓨틱스 아게 | 항체 접합체 및 이의 제조 |
| EP4366781A1 (en) | 2021-07-09 | 2024-05-15 | Bright Peak Therapeutics AG | Checkpoint inhibitors conjugated to il-2, and uses thereof |
| EP4366779A1 (en) | 2021-07-09 | 2024-05-15 | Bright Peak Therapeutics AG | Modified tnf-antibodies and uses thereof |
| EP4399283A2 (en) | 2021-09-06 | 2024-07-17 | Veraxa Biotech GmbH | Novel aminoacyl-trna synthetase variants for genetic code expansion in eukaryotes |
| IL311389A (en) * | 2021-09-17 | 2024-05-01 | Absci Corp | Transfer RNA composition and use in the production of proteins containing non-standard amino acids |
| US20240384267A1 (en) | 2021-09-20 | 2024-11-21 | The Broad Institute, Inc. | Compositions and methods for multiplex decoding of quadruplet codons |
| IL312221A (en) | 2021-10-20 | 2024-06-01 | 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 |
| 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 |
| KR20240105469A (ko) | 2021-11-25 | 2024-07-05 | 베락사 바이오테크 게엠베하 | 유전자 코드 확장을 이용하는 부위-특이적 접합에 의해 제조되는 개선된 항체-페이로드 접합체 (apc) |
| AU2022404647A1 (en) | 2021-12-08 | 2024-06-13 | European Molecular Biology Laboratory | Hydrophilic tetrazine-functionalized payloads for preparation of targeting conjugates |
| US20250092106A1 (en) | 2022-01-25 | 2025-03-20 | The Regents Of The University Of California | Vegf mutants and modulation of integrin-mediated signaling |
| WO2023161857A1 (en) | 2022-02-23 | 2023-08-31 | Bright Peak Therapeutics Ag | Bifunctional cytokine compositions |
| IL314889A (en) | 2022-02-23 | 2024-10-01 | Bright Peak Therapeutics Ag | IL-18 immunocytokines specific for immune antigens and uses thereof |
| JP2025512832A (ja) | 2022-03-30 | 2025-04-22 | 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の液体医薬組成物およびその使用の方法 |
| CA3259758A1 (en) | 2022-06-30 | 2024-01-04 | Sutro Biopharma Inc | Anti-ROR1 antibodies and antibody conjugates, compositions comprising anti-ROR1 antibodies or antibody conjugates, and methods of manufacturing and using anti-ROR1 antibodies and antibody conjugates |
| NL2033185B1 (en) | 2022-09-29 | 2024-04-08 | Stichting Vu | Compounds for rna stabilisation and delivery |
| CN120344270A (zh) | 2022-10-07 | 2025-07-18 | Ambrx 公司 | 药物接头及其抗体缀合物 |
| WO2024091824A1 (en) | 2022-10-26 | 2024-05-02 | Ada Forsyth Institute, Inc. | Differentiation and reprogramming of chondrocyte |
| EP4656732A1 (en) * | 2022-12-31 | 2025-12-03 | Kangma-Healthcode (Shanghai) Biotech Co., Ltd | In-vitro cell-free protein synthesis system for inserting non-natural amino acid, and method and use |
| US20240376170A1 (en) | 2023-01-11 | 2024-11-14 | Bright Peak Therapeutics Ag | Conditionally activated proteins and methods of use |
| IL322121A (en) | 2023-01-16 | 2025-09-01 | Ambrx Inc | Anti-CD70 antibody-drug conjugates |
| WO2024178310A1 (en) | 2023-02-23 | 2024-08-29 | Ambrx, Inc. | Trop2-directed antibody-drug conjugates and uses thereof |
| WO2024211306A1 (en) | 2023-04-03 | 2024-10-10 | Sutro Biopharma, Inc. | Rf1 ko e. coli strains |
| WO2024241086A1 (en) | 2023-05-24 | 2024-11-28 | Ambrx, Inc. | Pegylated bovine interferon lambda and methods of use thereof |
| 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 |
| WO2025041102A1 (en) | 2023-08-23 | 2025-02-27 | Bright Peak Therapeutics Ag | Targeted immune activation with il-18 immunocytokines |
| US20250197467A1 (en) | 2023-08-23 | 2025-06-19 | Bright Peak Therapeutics Ag | Activatable il-18 immunocytokines and uses thereof |
| WO2025080711A1 (en) | 2023-10-13 | 2025-04-17 | Sutro Biopharma, Inc. | Dual payload antibody drug conjugates |
| 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 |
| WO2025184315A1 (en) | 2024-02-29 | 2025-09-04 | Amgen Inc. | Glucagon receptor agonists, conjugated to glucose-dependent insulinotropic polypeptide antibodies |
| 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 |
Citations (1)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| JP2004537984A (ja) * | 2001-04-19 | 2004-12-24 | ザ スクリップス リサーチ インスティテュート | 直交tRNA−アミノアシルtRNAシンテターゼ対を生産するための方法及び組成物 |
Family Cites Families (48)
| 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 |
| EP0822990A4 (en) | 1995-04-24 | 2002-07-03 | Chromaxome Corp | METHODS OF GENERATING AND SCREENING NEW METABOLIC PATHWAYS |
| 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 |
| 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. |
| ATE526414T1 (de) | 2002-10-16 | 2011-10-15 | Scripps Research Inst | Ortsspezifische einbindung von ketoaminosäuren in proteine |
| KR20050073559A (ko) | 2002-10-16 | 2005-07-14 | 더 스크립스 리서치 인스티튜트 | 당단백질 합성 |
| US7642085B2 (en) | 2002-12-22 | 2010-01-05 | The Scripps Research Institute | Protein arrays |
| KR101171397B1 (ko) | 2003-04-17 | 2012-08-07 | 더 스크립스 리서치 인스티튜트 | 진핵 유전자 코드의 확장 |
| CA2527877A1 (en) | 2003-06-18 | 2005-01-13 | The Scripps Research Institute | Unnatural reactive amino acid genetic code additions |
| ATE386133T1 (de) | 2003-07-07 | 2008-03-15 | Scripps Research Inst | Zusammensetzungen der orthogonalen lysyl-trna und aminoacyl-trna synthetase paaren und ihre verwendungen |
| US7527943B2 (en) | 2003-07-07 | 2009-05-05 | The Scripps Research Institute | Compositions of orthogonal glutamyl-tRNA and aminoacyl-tRNA synthetase pairs and uses thereof |
| 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 |
| BRPI0415308A (pt) | 2003-10-14 | 2006-12-05 | Scripps Research Inst | incorporação especìfica de local de aminoácidos redox ativos em proteìnas |
| US7741071B2 (en) | 2003-12-18 | 2010-06-22 | The Scripps Research Institute | Selective incorporation of 5-hydroxytryptophan into proteins in mammalian cells |
| US7399619B2 (en) | 2004-05-25 | 2008-07-15 | The Scripps Research Institute | Site specific incorporation of heavy atom-containing unnatural amino acids into proteins for structure determination |
| BRPI0515547A (pt) | 2004-09-21 | 2008-07-29 | Scripps Research Inst | incorporação in vivo de aminoácidos alquinil em proteìnas em eubacterias |
| WO2006034410A2 (en) | 2004-09-21 | 2006-03-30 | The Scripps Resarch Institute | Adding photoregulated amino acids to the genetic code |
| US20060110784A1 (en) | 2004-09-22 | 2006-05-25 | The Scripps Research Institute | Site-specific labeling of proteins for NMR studies |
| WO2006045116A2 (en) | 2004-10-20 | 2006-04-27 | The Scripps Research Institute | In vivo site-specific incorporation of n-acetyl-galactosamine amino acids in eubacteria |
| WO2006110182A2 (en) | 2004-10-27 | 2006-10-19 | 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 |
| BRPI0617191A2 (pt) | 2005-10-12 | 2011-07-19 | Scripps Research Inst | modificação pós-traducional de polipeptìdeos expressos em fagos |
| EP1991680B1 (en) | 2006-03-09 | 2013-08-21 | The Scripps Research Institute | System for the expression of orthogonal translation components in eubacterial host cells |
| US7790847B2 (en) | 2006-03-16 | 2010-09-07 | The Scripps Research Institute | Genetically programmed expression of proteins containing the unnatural amino acid phenylselenocysteine |
| CA2652894A1 (en) | 2006-05-23 | 2007-12-06 | The Scripps Research Institute | Genetically encoded fluorescent coumarin amino acids |
| US7421795B2 (en) * | 2006-08-04 | 2008-09-09 | Seagate Technology Llc | Sapphire alignment fixture |
| WO2008036392A2 (en) | 2006-09-21 | 2008-03-27 | The Scripps Research Institute | Genetically programmed expression of selectively sulfated proteins in eubacteria |
| RU2009112104A (ru) | 2006-10-18 | 2010-11-27 | Зе Скрипс Ресеч Инститьют (Us) | Генетическое встраивание не встречающихся в природе аминокислот в белки клеток млекопитающих |
| TWI334126B (en) * | 2007-07-17 | 2010-12-01 | Au Optronics Corp | Voltage adjusting circuit, method, and display apparatus having the same |
| JP4978419B2 (ja) * | 2007-10-23 | 2012-07-18 | 富士ゼロックス株式会社 | 光送受信モジュール |
| MX2010004464A (es) | 2007-10-25 | 2010-06-07 | Scripps Research Inst | Incorporacion genetica de 3-aminotirosina a reductasas. |
| US9249408B2 (en) | 2007-11-02 | 2016-02-02 | The Scripps Research Institute | Directed evolution using proteins comprising unnatural amino acids |
| 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 |
| US8218509B2 (en) * | 2008-01-15 | 2012-07-10 | Apple Inc. | Dynamic allocation of communication resources in a wireless system |
| US8318172B2 (en) | 2008-02-08 | 2012-11-27 | The Scripps Research Institute | Breaking immunological tolerance with a genetically encoded unnatural amino acid |
| WO2009151491A2 (en) | 2008-02-27 | 2009-12-17 | The Scripps Research Institute | In vivo incorporation of an unnatural amino acid comprising a 1,2-aminothiol group |
| US8609383B2 (en) | 2008-12-10 | 2013-12-17 | 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 |
| WO2010114615A2 (en) | 2009-04-03 | 2010-10-07 | The Scripps Research Institute | A facile system for encoding unnatural amino acids in mammalian cells |
-
2002
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- 2002-04-19 EP EP02731454.1A patent/EP1456360B1/en not_active Expired - Lifetime
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- 2002-04-19 MX MXPA03009563A patent/MXPA03009563A/es active IP Right Grant
- 2002-04-19 WO PCT/US2002/012635 patent/WO2002086075A2/en not_active Ceased
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- 2002-04-19 US US10/126,931 patent/US7083970B2/en not_active Expired - Lifetime
- 2002-04-19 EP EP09006800.8A patent/EP2128246B1/en not_active Expired - Lifetime
- 2002-04-19 DK DK02731454.1T patent/DK1456360T3/en active
- 2002-04-19 AU AU2002256292A patent/AU2002256292C1/en not_active Expired
- 2002-04-19 AU AU2002303431A patent/AU2002303431C1/en not_active Expired
- 2002-04-19 CA CA2443757A patent/CA2443757C/en not_active Expired - Lifetime
- 2002-04-19 CA CA2444098A patent/CA2444098C/en not_active Expired - Lifetime
- 2002-04-19 WO PCT/US2002/012465 patent/WO2002085923A2/en not_active Ceased
- 2002-04-19 DK DK10182672.5T patent/DK2322631T3/en active
- 2002-04-19 ES ES09006800.8T patent/ES2464532T3/es not_active Expired - Lifetime
- 2002-04-19 DK DK09006800.8T patent/DK2128246T3/da active
- 2002-04-19 EP EP10182672.5A patent/EP2322631B1/en not_active Expired - Lifetime
- 2002-04-19 EP EP14167479.6A patent/EP2796546B1/en not_active Expired - Lifetime
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Patent Citations (2)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| JP2004537984A (ja) * | 2001-04-19 | 2004-12-24 | ザ スクリップス リサーチ インスティテュート | 直交tRNA−アミノアシルtRNAシンテターゼ対を生産するための方法及び組成物 |
| JP2009132704A (ja) * | 2001-04-19 | 2009-06-18 | Scripps Res Inst:The | 非天然アミノ酸のインビボ組込み |
Cited By (12)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| JP2009132704A (ja) * | 2001-04-19 | 2009-06-18 | Scripps Res Inst:The | 非天然アミノ酸のインビボ組込み |
| JP2010502218A (ja) * | 2006-09-08 | 2010-01-28 | アンブルックス,インコーポレイテッド | 修飾ヒト血漿ポリペプチドまたは修飾ヒトFc足場タンパク質ならびにこれらの利用 |
| JP2010502222A (ja) * | 2006-09-08 | 2010-01-28 | アンブルックス,インコーポレイテッド | 脊椎動物細胞用のハイブリッドサプレッサーtrna |
| US8618257B2 (en) | 2006-09-08 | 2013-12-31 | Ambrx, Inc. | Modified human plasma polypeptide or Fc scaffolds and their uses |
| JP2010504096A (ja) * | 2006-09-21 | 2010-02-12 | ザ スクリップス リサーチ インスティテュート | 真正細菌における選択的に硫酸化された蛋白質の遺伝的にプログラムされた発現 |
| JP2011502507A (ja) * | 2007-11-02 | 2011-01-27 | ザ スクリプス リサーチ インスティチュート | 非天然アミノ酸を含有する蛋白質を使用する指向的進化 |
| JP2011527886A (ja) * | 2007-12-11 | 2011-11-10 | ザ スクリプス リサーチ インスティチュート | メタノール資化性酵母ピキア・パストリスにおけるインビボ非天然アミノ酸発現 |
| WO2011158895A1 (ja) * | 2010-06-16 | 2011-12-22 | 独立行政法人理化学研究所 | 非天然タンパク質製造用の組換え細菌の作製方法、及びその利用 |
| JP5858543B2 (ja) * | 2010-06-16 | 2016-02-10 | 国立研究開発法人理化学研究所 | 非天然タンパク質製造用の組換え細菌の作製方法、及びその利用 |
| US9340790B2 (en) | 2010-06-16 | 2016-05-17 | Riken | Method for constructing recombinant bacterium for producing non-native protein, and utilization of 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 |
| JP2022554396A (ja) * | 2019-11-05 | 2022-12-28 | ニトロ バイオサイエンシーズ, インコーポレイテッド | パラ-ニトロ-l-フェニルアラニンの生合成 |
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