TW201302793A - 新穎之抗原結合蛋白 - Google Patents
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- C07K16/18—Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies against material from animals or humans
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- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K16/00—Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies
- C07K16/18—Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies against material from animals or humans
- C07K16/28—Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies against material from animals or humans against receptors, cell surface antigens or cell surface determinants
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- A61K39/00—Medicinal preparations containing antigens or antibodies
- A61K39/395—Antibodies; Immunoglobulins; Immune serum, e.g. antilymphocytic serum
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- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K16/00—Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies
- C07K16/18—Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies against material from animals or humans
- C07K16/32—Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies against material from animals or humans against translation products of oncogenes
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- C—CHEMISTRY; METALLURGY
- C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
- C12P—FERMENTATION OR ENZYME-USING PROCESSES TO SYNTHESISE A DESIRED CHEMICAL COMPOUND OR COMPOSITION OR TO SEPARATE OPTICAL ISOMERS FROM A RACEMIC MIXTURE
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- C07K—PEPTIDES
- C07K2317/00—Immunoglobulins specific features
- C07K2317/20—Immunoglobulins specific features characterized by taxonomic origin
- C07K2317/24—Immunoglobulins specific features characterized by taxonomic origin containing regions, domains or residues from different species, e.g. chimeric, humanized or veneered
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- C—CHEMISTRY; METALLURGY
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- C07K—PEPTIDES
- C07K2317/00—Immunoglobulins specific features
- C07K2317/30—Immunoglobulins specific features characterized by aspects of specificity or valency
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- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K2317/00—Immunoglobulins specific features
- C07K2317/50—Immunoglobulins specific features characterized by immunoglobulin fragments
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- C07K2317/565—Complementarity determining region [CDR]
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- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K2317/00—Immunoglobulins specific features
- C07K2317/70—Immunoglobulins specific features characterized by effect upon binding to a cell or to an antigen
- C07K2317/72—Increased effector function due to an Fc-modification
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- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K2317/00—Immunoglobulins specific features
- C07K2317/70—Immunoglobulins specific features characterized by effect upon binding to a cell or to an antigen
- C07K2317/73—Inducing cell death, e.g. apoptosis, necrosis or inhibition of cell proliferation
- C07K2317/732—Antibody-dependent cellular cytotoxicity [ADCC]
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- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K2317/00—Immunoglobulins specific features
- C07K2317/70—Immunoglobulins specific features characterized by effect upon binding to a cell or to an antigen
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- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K2317/00—Immunoglobulins specific features
- C07K2317/70—Immunoglobulins specific features characterized by effect upon binding to a cell or to an antigen
- C07K2317/77—Internalization into the cell
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- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K2317/00—Immunoglobulins specific features
- C07K2317/90—Immunoglobulins specific features characterized by (pharmaco)kinetic aspects or by stability of the immunoglobulin
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Landscapes
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- Epidemiology (AREA)
- Peptides Or Proteins (AREA)
- Micro-Organisms Or Cultivation Processes Thereof (AREA)
- Medicines That Contain Protein Lipid Enzymes And Other Medicines (AREA)
- Medicines Containing Antibodies Or Antigens For Use As Internal Diagnostic Agents (AREA)
- Preparation Of Compounds By Using Micro-Organisms (AREA)
- Pharmaceuticals Containing Other Organic And Inorganic Compounds (AREA)
- Medicines Containing Material From Animals Or Micro-Organisms (AREA)
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| US37984010P | 2010-09-03 | 2010-09-03 | |
| US201161440460P | 2011-02-08 | 2011-02-08 |
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| TW201302793A true TW201302793A (zh) | 2013-01-16 |
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| NZ600262A (en) | 2009-12-22 | 2013-06-28 | Roche Glycart Ag | Anti-her3 antibodies and uses thereof |
| PH12013500333A1 (en) | 2010-08-20 | 2013-04-22 | Novartis Ag | Antibodies for epidermal growth factor receptor 3 (her3) |
| WO2013078191A1 (en) | 2011-11-23 | 2013-05-30 | Medimmune, Llc | Binding molecules specific for her3 and uses thereof |
| ES2758433T3 (es) | 2011-12-05 | 2020-05-05 | Novartis Ag | Anticuerpos contra el receptor 3 del factor de crecimiento epidérmico (HER3) |
| UY34488A (es) * | 2011-12-05 | 2013-07-31 | Novartis Ag | Anticuerpos dirigidos al receptor de factor de crecimiento epidérmico 3 (her3) dirigidos contra el dominio iii y dominio iv del her3 |
| US20130196880A1 (en) * | 2012-01-27 | 2013-08-01 | Ventana Medical Systems, Inc. | Patterned devices and methods for detecting analytes |
| MA38165A1 (fr) * | 2012-11-08 | 2018-07-31 | Hoffmann La Roche | Protéines de liaison à l'antigène her3 se liant à l'épingle à cheveux beta de her3 |
| SG11201502534UA (en) | 2012-11-08 | 2015-05-28 | Hoffmann La Roche | Anti-her3/her4 antigen binding proteins binding to the beta-hairpin of her3 and the beta-hairpin of her4 |
| AR094403A1 (es) | 2013-01-11 | 2015-07-29 | Hoffmann La Roche | Terapia de combinación de anticuerpos anti-her3 |
| US11305012B2 (en) | 2013-09-24 | 2022-04-19 | Medimmune, Llc | Binding molecules specific for HER3 and uses thereof |
| EP3036259B1 (en) | 2013-10-04 | 2018-02-21 | Roche Diagnostics GmbH | Antibodies specifically binding to her3 |
| DK3805268T3 (da) | 2014-02-28 | 2025-01-20 | Merus Nv | Antistof, der binder erbb-2 og erbb-3 |
| US10844127B2 (en) | 2014-02-28 | 2020-11-24 | Merus N.V. | Antibodies that bind EGFR and ErbB3 |
| US10745490B2 (en) | 2014-04-11 | 2020-08-18 | Celldex Therapeutics, Inc. | Anti-ErbB antibodies and methods of use thereof |
| WO2015164723A1 (en) | 2014-04-25 | 2015-10-29 | The Trustees Of The University Of Pennsylvania | Methods and compositions for treating metastatic breast cancer and other cancers in the brain |
| CA2944895A1 (en) | 2014-05-14 | 2015-11-19 | F. Hoffmann-La Roche Ag | Anti-her3 antibodies binding to the beta-hairpin of her3 |
| RU2695220C2 (ru) | 2014-06-30 | 2019-07-22 | Тарведа Терапьютикс, Инк. | Нацеленные конъюгаты и частицы и их составы |
| US11254933B2 (en) * | 2014-07-14 | 2022-02-22 | The Regents Of The University Of California | CRISPR/Cas transcriptional modulation |
| US10526416B2 (en) | 2014-09-08 | 2020-01-07 | Yeda Research And Development Co. Ltd. | Anti-HER3 antibodies and uses of same |
| JP2017534574A (ja) | 2014-09-08 | 2017-11-24 | イェダ リサーチ アンド ディベロップメント カンパニー リミテッドYeda Research And Development Co.Ltd. | チロシンキナーゼ阻害薬(tki)に耐性のがんを処置するための組成物および方法 |
| WO2016059602A2 (en) * | 2014-10-16 | 2016-04-21 | Glaxo Group Limited | Methods of treating cancer and related compositions |
| CA3002957A1 (en) | 2015-10-23 | 2017-04-27 | Koninklijke Nederlandse Akademie Van Wetenschappen | Binding molecules that inhibit cancer growth |
| US11160871B2 (en) | 2015-10-28 | 2021-11-02 | Tarveda Therapeutics, Inc. | SSTR-targeted conjugates and particles and formulations thereof |
| US10689458B2 (en) | 2015-11-30 | 2020-06-23 | Pfizer Inc. | Site specific HER2 antibody drug conjugates |
| MA43416A (fr) | 2015-12-11 | 2018-10-17 | Regeneron Pharma | Méthodes pour ralentir ou empêcher la croissance de tumeurs résistantes au blocage de l'egfr et/ou d'erbb3 |
| CA3011949A1 (en) | 2016-03-15 | 2017-09-21 | Merrimack Pharmaceuticals, Inc. | Methods for treating er+, her2-, hrg+ breast cancer using combination therapies comprising an anti-erbb3 antibody |
| CN121086057A (zh) * | 2016-06-10 | 2025-12-09 | 德国癌症研究公共权益基金会 | 膜联蛋白的核心结构域及其在抗原递送和接种中的用途 |
| CN106543286A (zh) * | 2016-12-07 | 2017-03-29 | 上海邦耀生物科技有限公司 | 一种去岩藻糖抗her2抗体及其应用 |
| EP3600413A1 (en) | 2017-03-31 | 2020-02-05 | Merus N.V. | Erbb-2 and erbb3 binding bispecific antibodies for use in the treatment f cells that have an nrg1 fusion gene |
| KR102744809B1 (ko) | 2017-05-17 | 2024-12-23 | 메뤼스 엔.페. | 유방암 치료를 위한 ErbB-2/ErbB-3 이중특이적 항체와 내분비 치료의 조합 |
| WO2018215535A1 (en) * | 2017-05-23 | 2018-11-29 | Helmholtz Zentrum München - Deutsches Forschungszentrum für Gesundheit und Umwelt (GmbH) | Novel cd73 antibody, preparation and uses thereof |
| PL3665198T3 (pl) | 2017-08-09 | 2025-06-09 | Merus N.V. | Przeciwciała wiążące egfr i cmet |
| JP2021514662A (ja) * | 2018-03-08 | 2021-06-17 | フェインズ セラピューティクス,インコーポレーテッド | 抗tip−1抗体及びその使用 |
| WO2019185164A1 (en) * | 2018-03-29 | 2019-10-03 | Hummingbird Bioscience Holdings Pte. Ltd. | Her3 antigen-binding molecules |
| KR20220069935A (ko) * | 2019-09-27 | 2022-05-27 | 아게누스 인코포레이티드 | 이종이량체 단백질 |
| US20250243261A1 (en) * | 2022-04-08 | 2025-07-31 | Cz Biohub Sf, Llc | Antibody compositions and optimization methods |
| CN116286828B (zh) * | 2023-05-12 | 2023-08-18 | 中国人民解放军军事科学院军事医学研究院 | 一种寡聚核酸siRNA及其在制备用于预防和治疗肝癌的药物中的应用 |
| CN117903311B (zh) * | 2024-03-20 | 2024-10-25 | 湖南卓润生物科技有限公司 | sST2特异性结合蛋白及其制备方法和应用 |
| CN120352624B (zh) * | 2025-06-25 | 2025-08-26 | 北京溯本源和生物科技有限公司 | 一种用于hpv18型e7蛋白检测的单克隆抗体组合及应用 |
Family Cites Families (235)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| US5183884A (en) | 1989-12-01 | 1993-02-02 | United States Of America | Dna segment encoding a gene for a receptor related to the epidermal growth factor receptor |
| US6639061B1 (en) | 1999-07-07 | 2003-10-28 | Isis Pharmaceuticals, Inc. | C3′-methylene hydrogen phosphonate oligomers and related compounds |
| US5804396A (en) | 1994-10-12 | 1998-09-08 | Sugen, Inc. | Assay for agents active in proliferative disorders |
| WO1996014864A1 (en) | 1994-11-09 | 1996-05-23 | The Regents Of The University Of California | Immunoliposomes that optimize internalization into target cells |
| PT896586E (pt) | 1996-03-27 | 2007-01-31 | Genentech Inc | Anticorpos de erbb3 |
| US5968511A (en) | 1996-03-27 | 1999-10-19 | Genentech, Inc. | ErbB3 antibodies |
| CA2589421C (en) | 1996-03-27 | 2012-12-18 | Genentech, Inc. | Erbb3 antibodies |
| US5922845A (en) | 1996-07-11 | 1999-07-13 | Medarex, Inc. | Therapeutic multispecific compounds comprised of anti-Fcα receptor antibodies |
| CN1202247C (zh) | 1996-07-12 | 2005-05-18 | 基因技术股份有限公司 | 嵌合异源多亚基粘附素 |
| US20020002276A1 (en) | 1997-02-10 | 2002-01-03 | Genentech, Inc. | Chimeric heteromultimer adhesins |
| US6723694B1 (en) | 1997-05-21 | 2004-04-20 | The Children's Medical Center Corp. | Short peptides which selectively modulate intracellular signalling |
| US6416168B1 (en) | 1997-07-15 | 2002-07-09 | Silverbrook Research Pty Ltd | Pump action refill ink jet printing mechanism |
| ZA9811162B (en) | 1997-12-12 | 2000-06-07 | Genentech Inc | Treatment with anti-ERBB2 antibodies. |
| US20010023241A1 (en) | 1998-02-04 | 2001-09-20 | Sliwkowski Mark X. | Use of heregulin as a growth factor |
| AU2003203831B2 (en) | 1998-02-04 | 2006-08-10 | Genentech, Inc. | Use of heregulin as an epithelial cell growth factor |
| DE69920405T2 (de) | 1998-02-04 | 2006-01-05 | Genentech, Inc., South San Francisco | Verwendung des heregulins als epithelzellenwachstumsfaktor |
| US6417168B1 (en) | 1998-03-04 | 2002-07-09 | The Trustees Of The University Of Pennsylvania | Compositions and methods of treating tumors |
| ES2389387T3 (es) | 1998-03-17 | 2012-10-25 | Genentech, Inc. | Polipéptidos homólogos de VEGF y de BMP1 |
| ES2434961T5 (es) | 1998-04-20 | 2018-01-18 | Roche Glycart Ag | Ingeniería de glicosilación de anticuerpos para mejorar la citotoxicidad celular dependiente del anticuerpo |
| ZA200007412B (en) | 1998-05-15 | 2002-03-12 | Imclone Systems Inc | Treatment of human tumors with radiation and inhibitors of growth factor receptor tyrosine kinases. |
| AU2004200705A1 (en) | 1998-05-15 | 2004-03-18 | Imclone Systems Incorporated | Treatment of human tumors with radiation and inhibitors of growth factor receptor tyrosine kinases |
| AU4079999A (en) | 1998-05-15 | 1999-12-06 | Imclone Systems Incorporated | Treatment of human tumors with radiation and inhibitors of growth factor receptor tyrosine kinases |
| CA2345899A1 (en) | 1998-11-07 | 2000-05-18 | Genentech, Inc. | Method for enhancing proliferation of inner ear hair cells using ligands for her2 and/or her3 receptors |
| US6737056B1 (en) | 1999-01-15 | 2004-05-18 | Genentech, Inc. | Polypeptide variants with altered effector function |
| US7183387B1 (en) | 1999-01-15 | 2007-02-27 | Genentech, Inc. | Polypeptide variants with altered effector function |
| EP1169352A4 (en) * | 1999-04-14 | 2005-05-04 | Smithkline Beecham Corp | ANTIBODY AGAINST THE ERYTHROPOIETIN RECEPTOR |
| US7534866B2 (en) | 2005-10-19 | 2009-05-19 | Ibc Pharmaceuticals, Inc. | Methods and compositions for generating bioactive assemblies of increased complexity and uses |
| US6710186B2 (en) | 1999-06-14 | 2004-03-23 | Wisconsin Alumni Research Foundation | Oligomers and polymers of di-substituted cyclic imino carboxylic acids |
| AUPQ105799A0 (en) | 1999-06-18 | 1999-07-08 | Victor Chang Cardiac Research Institute, The | Cell growth inhibition |
| BRPI0012198B8 (pt) | 1999-06-25 | 2021-05-25 | Genentech Inc | anticorpos humanizados, composição e imunoconjugado |
| KR20020012292A (ko) | 1999-06-25 | 2002-02-15 | 제넨테크, 인크. | 항-ErbB 항체-메이탄시노이드 결합체를 사용한 치료방법 |
| US6949245B1 (en) | 1999-06-25 | 2005-09-27 | Genentech, Inc. | Humanized anti-ErbB2 antibodies and treatment with anti-ErbB2 antibodies |
| EP2110138A1 (en) | 1999-08-27 | 2009-10-21 | Genentech, Inc. | Dosages for treatment of anti-erbB2 antibodies |
| US7390632B2 (en) | 1999-09-30 | 2008-06-24 | Tumor Biology Investment Group, Inc. | Soluble ErbB3 receptor isoforms |
| US7732157B1 (en) | 1999-09-30 | 2010-06-08 | Tumor Biology Investment Group | Soluble epidermal growth factor receptor-like proteins and their uses in cancer detection methods |
| US7651703B2 (en) | 1999-10-15 | 2010-01-26 | Genentech, Inc. | Injection vehicle for polymer-based formulations |
| MXPA02006843A (es) | 2000-01-12 | 2004-04-05 | Ventana Med Syst Inc | Metodo para cuantificar una proteina por analisis de imagenes. |
| DK1666052T3 (da) | 2000-02-16 | 2011-09-12 | Genentech Inc | Anti-APRIL monoklonalt antistof og dets anvendelse til behandling af en immum-relateret sygdom eller cancer |
| US7097840B2 (en) | 2000-03-16 | 2006-08-29 | Genentech, Inc. | Methods of treatment using anti-ErbB antibody-maytansinoid conjugates |
| US6632979B2 (en) | 2000-03-16 | 2003-10-14 | Genentech, Inc. | Rodent HER2 tumor model |
| AU2007216733A1 (en) | 2000-04-11 | 2007-09-27 | Genentech, Inc. | Multivalent antibodies and uses therefor |
| MXPA02010011A (es) | 2000-04-11 | 2003-04-25 | Genentech Inc | Anticuerpos multivalentes y usos para los mismos. |
| FR2807767B1 (fr) | 2000-04-12 | 2005-01-14 | Lab Francais Du Fractionnement | Anticorps monoclonaux anti-d |
| US6277640B1 (en) | 2000-07-31 | 2001-08-21 | Isis Pharmaceuticals, Inc. | Antisense modulation of Her-3 expression |
| ATE356575T1 (de) | 2000-11-24 | 2007-04-15 | Freudenberg Carl Kg | Bodenwischer |
| US20030133939A1 (en) | 2001-01-17 | 2003-07-17 | Genecraft, Inc. | Binding domain-immunoglobulin fusion proteins |
| AU2008200400B2 (en) | 2001-01-17 | 2012-06-07 | Aptevo Research And Development Llc | Binding domain-immunoglobulin fusion proteins |
| EP1228766A1 (en) | 2001-01-31 | 2002-08-07 | Max-Planck-Gesellschaft zur Förderung der Wissenschaften e.V. | PYK2 phosphorylation by HER3 induces tumor invasion |
| AU2002240338C1 (en) | 2001-02-12 | 2007-05-17 | Medarex, Inc. | Human monoclonal antibodies to FC alpha receptor (CD89) |
| JP4398644B2 (ja) | 2001-04-06 | 2010-01-13 | ザ トラスティーズ オブ ザ ユニバーシティ オブ ペンシルベニア | ErbB界面ペプチド擬態およびその使用方法 |
| US20040116330A1 (en) | 2001-04-27 | 2004-06-17 | Kenichiro Naito | Preventive/therapeutic method for cancer |
| JP2005505749A (ja) | 2001-05-21 | 2005-02-24 | アクララ バイオサイエンシーズ, インコーポレイテッド | タンパク質を分析するための方法および組成物 |
| US7745398B2 (en) | 2001-05-31 | 2010-06-29 | Tumor Biology Investment Group, Inc. | Soluble ErbB3 and treatment of cancer |
| US7744882B2 (en) | 2001-05-31 | 2010-06-29 | Tumor Biology Investment Group, Inc. | Soluble ErbB3 methods of detection and antibodies |
| IL159177A0 (en) | 2001-06-20 | 2004-06-01 | Prochon Biotech Ltd | Antibodies that block receptor protein tyrosine kinase activation, methods of screening for and uses thereof |
| EP1397837A2 (en) | 2001-06-21 | 2004-03-17 | Akzo Nobel N.V. | Manufacturing a solar cell foil connected in series via a temporary substrate |
| US7125680B2 (en) | 2001-07-27 | 2006-10-24 | The Regents Of The University Of California | Methods and materials for characterizing and modulating interaction between heregulin and HER3 |
| DE10137374A1 (de) | 2001-07-31 | 2003-02-27 | Ipk Inst Fuer Pflanzengenetik | Verfahren zur Herstellung von Arachidonsäure in transgenen Organismen |
| US7662374B2 (en) | 2001-08-03 | 2010-02-16 | The Trustees Of The University Of Pennsylvania | Monoclonal antibodies to activated erbB family members and methods of use thereof |
| AU2008200654B2 (en) | 2001-08-09 | 2010-04-29 | Max-Planck-Gesellschaft Zur Forderung Der Wissenschaften E.V. | Inhibitors of HER3 activity |
| EP1283053A1 (en) | 2001-08-09 | 2003-02-12 | Max-Planck-Gesellschaft zur Förderung der Wissenschaften e.V. | Inhibitors of HER3 activity |
| US8877901B2 (en) | 2002-12-13 | 2014-11-04 | Immunomedics, Inc. | Camptothecin-binding moiety conjugates |
| US7591994B2 (en) | 2002-12-13 | 2009-09-22 | Immunomedics, Inc. | Camptothecin-binding moiety conjugates |
| US20040132101A1 (en) | 2002-09-27 | 2004-07-08 | Xencor | Optimized Fc variants and methods for their generation |
| CA2480099C (en) | 2002-03-26 | 2019-01-08 | Zensun (Shanghai) Sci-Tech. Ltd. | Erbb3 based methods and compositions for treating neoplasms |
| JP4132912B2 (ja) | 2002-03-26 | 2008-08-13 | 日東電工株式会社 | ゲル電解質とその製造方法とその利用 |
| US7332580B2 (en) | 2002-04-05 | 2008-02-19 | The Regents Of The University Of California | Bispecific single chain Fv antibody molecules and methods of use thereof |
| US7332585B2 (en) | 2002-04-05 | 2008-02-19 | The Regents Of The California University | Bispecific single chain Fv antibody molecules and methods of use thereof |
| WO2003102132A2 (en) | 2002-04-26 | 2003-12-11 | Genetech, Inc. | Non-affinity purification of proteins |
| US20040229293A1 (en) | 2002-05-21 | 2004-11-18 | Po-Ying Chan-Hui | Surface receptor complexes as biomarkers |
| US20040229380A1 (en) | 2002-05-21 | 2004-11-18 | Po-Ying Chan-Hui | ErbB heterodimers as biomarkers |
| US20040229299A1 (en) | 2002-05-21 | 2004-11-18 | Badal M. Youssouf | Intracellular complexes as biomarkers |
| US20040229294A1 (en) | 2002-05-21 | 2004-11-18 | Po-Ying Chan-Hui | ErbB surface receptor complexes as biomarkers |
| US20040132097A1 (en) | 2002-06-19 | 2004-07-08 | Bacus Sarah S. | Method for predicting response to epidermal growth factor receptor-directed therapy |
| AU2003273218C1 (en) | 2002-07-15 | 2019-01-17 | F. Hoffmann - La Roche Ag | Methods for identifying tumors that are responsive to treatment with anti-ErbB2 antibodies |
| DE60329194D1 (de) | 2002-07-25 | 2009-10-22 | Aclara Biosciences Inc | Nachweis der rezeptoroligomerisierung |
| GB0225282D0 (en) | 2002-10-31 | 2002-12-11 | Astrazeneca Ab | assay |
| WO2004065417A2 (en) | 2003-01-23 | 2004-08-05 | Genentech, Inc. | Methods for producing humanized antibodies and improving yield of antibodies or antigen binding fragments in cell culture |
| EP1613661B1 (en) | 2003-04-04 | 2011-06-29 | Université de Lausanne | Peptabody for cancer treatment |
| US7189694B2 (en) | 2003-04-18 | 2007-03-13 | University Of Florida Research Foundation, Inc. | Inhibitors of autophosphorylation protein kinases |
| EP2348110B1 (en) | 2003-05-30 | 2013-03-27 | OncoTherapy Science, Inc. | Process for screening a drug response in cancer patients |
| DE602004019919D1 (de) | 2003-06-06 | 2009-04-23 | Genentech Inc | Modulation der wechselwirkung zwischen hgf-beta-kette und c-met |
| US20040254108A1 (en) | 2003-06-13 | 2004-12-16 | Jing Ma | Preparation and application of anti-tumor bifunctional fusion proteins |
| WO2005001048A2 (en) | 2003-06-13 | 2005-01-06 | Oncomax Acquisition Corp. | Preparation and application of anti-tumor bifunctional fusion proteins |
| US20050232931A1 (en) | 2003-06-13 | 2005-10-20 | Oncomax Acquisition Corp. | Preparation and application of anti-tumor bifunctional fusion proteins |
| US6836094B1 (en) | 2003-07-01 | 2004-12-28 | International Truck Intellectual Property Company, Llc | Motor vehicle battery disconnect switch circuits |
| US7531649B2 (en) | 2003-07-18 | 2009-05-12 | The Regents Of The University Of California | Aptamers to human epidermal growth factor receptor-3 |
| CA2531595C (en) | 2003-07-28 | 2015-12-08 | Genentech, Inc. | Reducing protein a leaching during protein a affinity chromatography |
| WO2005013804A2 (en) | 2003-08-05 | 2005-02-17 | Euro-Celtique S.A. | ErbB RECEPTOR METHODS AND KITS FOR MONITORING CHEMOTHERAPY RESISTANCE |
| WO2005014618A2 (en) | 2003-08-08 | 2005-02-17 | Immunomedics, Inc. | Bispecific antibodies for inducing apoptosis of tumor and diseased cells |
| CA2535510C (en) | 2003-08-11 | 2013-10-15 | Monogram Biosciences, Inc. | Detecting and profiling molecular complexes |
| US8399618B2 (en) | 2004-10-21 | 2013-03-19 | Xencor, Inc. | Immunoglobulin insertions, deletions, and substitutions |
| EP1681983A4 (en) | 2003-10-14 | 2008-12-10 | Monogram Biosciences Inc | RECEPTOR TYROSINE KINASE SIGNAL PATH ANALYSIS FOR DIAGNOSIS AND THERAPY |
| US20050130246A1 (en) | 2003-10-27 | 2005-06-16 | Hossein Salimi-Moosavi | Detecting human anti-therapeutic antibodies |
| JP2007510708A (ja) | 2003-11-06 | 2007-04-26 | ファイザー・プロダクツ・インク | 癌の治療における選択的erbB2阻害剤/抗erbB抗体の組合せ |
| US7754441B2 (en) | 2003-11-17 | 2010-07-13 | Genentech, Inc. | Compositions and methods for the treatment of tumor of hematopoietic origin |
| US7235641B2 (en) | 2003-12-22 | 2007-06-26 | Micromet Ag | Bispecific antibodies |
| JP4658967B2 (ja) | 2003-12-24 | 2011-03-23 | ジェネンテック, インコーポレイテッド | 造血系起源の腫瘍の治療のための組成物と方法 |
| US8323987B2 (en) | 2004-02-17 | 2012-12-04 | The University Of North Carolina At Chapel Hill | Modulation of epidermal growth factor heterodimer activity |
| JP2007528725A (ja) | 2004-02-20 | 2007-10-18 | ザ・トラスティーズ・オブ・ザ・ユニバーシティ・オブ・ペンシルバニア | 結合ペルオキシダーゼ模倣物及びその使用 |
| CA2564538A1 (en) | 2004-04-22 | 2005-12-01 | Oregon Health And Science University | Compositions and methods for modulating signaling mediated by igf-1 receptor and erbb receptors |
| CN1997382A (zh) | 2004-05-05 | 2007-07-11 | 梅里麦克制药股份有限公司 | 调节生物活性的双特异性结合剂 |
| JP2008500830A (ja) | 2004-06-01 | 2008-01-17 | ドマンティス リミテッド | 増加した血清半減期を有する二重特異性融合抗体 |
| AU2005249490B2 (en) | 2004-06-01 | 2010-07-29 | Genentech, Inc. | Antibody drug conjugates and methods |
| SV2006002143A (es) | 2004-06-16 | 2006-01-26 | Genentech Inc | Uso de un anticuerpo para el tratamiento del cancer resistente al platino |
| US20070197430A1 (en) | 2004-06-24 | 2007-08-23 | Jonathan Baell | Conjugates And Therapeutic Uses Thereof |
| ZA200701234B (en) | 2004-07-22 | 2008-12-31 | Genentech Inc | HER2 antibody composition |
| US20100111856A1 (en) | 2004-09-23 | 2010-05-06 | Herman Gill | Zirconium-radiolabeled, cysteine engineered antibody conjugates |
| CN101065151B (zh) | 2004-09-23 | 2014-12-10 | 健泰科生物技术公司 | 半胱氨酸改造的抗体和偶联物 |
| AU2005294347A1 (en) | 2004-10-05 | 2006-04-20 | Oregon Health And Science University | Compositions and methods for treating disease |
| CA2587617C (en) | 2004-11-12 | 2011-02-01 | Xencor, Inc. | Fc variants with altered binding to fcrn |
| CA2587926A1 (en) | 2004-11-22 | 2006-06-01 | Vertex Pharmaceuticals Incorporated | Bicyclic inhibitors or rho kinase |
| US7947839B2 (en) | 2004-12-01 | 2011-05-24 | Genentech, Inc. | Heterocyclic-substituted bis-1,8 naphthalimide compounds, antibody drug conjugates, and methods of use |
| EP2281841A3 (en) * | 2004-12-03 | 2013-10-23 | Merck Sharp & Dohme Corp. | Biomarkers for pre-selection of patients for anti-IGF1R therapy |
| JP2008523073A (ja) | 2004-12-07 | 2008-07-03 | ジェネンテック・インコーポレーテッド | Her阻害剤を用いた治療のための患者の選択 |
| CA2601700A1 (en) | 2004-12-21 | 2006-06-29 | Cell Signaling Technology, Inc. | Protein phosphorylation in egfr-signaling pathways |
| US7807789B2 (en) | 2004-12-21 | 2010-10-05 | Cell Signaling Technology, Inc. | Reagents for the detection of protein phosphorylation in EGFR-signaling pathways |
| CA2594356C (en) | 2005-01-05 | 2018-07-17 | F-Star Biotechnologische Forschungs- Und Entwicklungsges.M.B.H. | Synthetic immunoglobulin domains with binding properties engineered in regions of the molecule different from the complementarity determining regions |
| US7557181B2 (en) | 2005-01-11 | 2009-07-07 | Molecular Logix, Inc. | Pan-HER antagonists and methods of use |
| CA2592177A1 (en) | 2005-01-21 | 2006-07-27 | Genentech, Inc. | Fixed dosing of her antibodies |
| WO2006084018A2 (en) | 2005-02-02 | 2006-08-10 | Monogram Biosciences, Inc. | Methods for determining responsiveness to cancer therapy |
| KR101569300B1 (ko) | 2005-02-07 | 2015-11-13 | 로슈 글리카트 아게 | Egfr 에 결합하는 항원 결합 분자, 이를 코딩하는 벡터, 및 그의 용도 |
| US7718626B2 (en) | 2005-02-17 | 2010-05-18 | University Of Maryland, Baltimore | ErbB3 binding protein compositions and methods of use |
| CA2596133C (en) | 2005-02-23 | 2016-11-15 | Genentech, Inc. | Extending time to disease progression or survival in cancer patients |
| WO2006091209A2 (en) | 2005-02-23 | 2006-08-31 | Merrimack Pharmaceuticals, Inc. | Bispecific binding agents for modulating biological activity |
| JP2008535795A (ja) | 2005-03-07 | 2008-09-04 | ターゲッティド・モレキュラー・ダイアグナスティクス・エルエルシー | チロシンキナーゼインヒビター組成物、並びに疾患の治療におけるそれらの製造及び使用のための方法 |
| TW200642695A (en) | 2005-03-08 | 2006-12-16 | Genentech Inc | Methods for identifying tumors responsive to treatment with her dimerization inhibitors (HDIs) |
| AU2006232920B2 (en) | 2005-04-06 | 2011-09-29 | Ibc Pharmaceuticals, Inc. | Methods for generating stably linked complexes composed of homodimers, homotetramers or dimers of dimers and uses |
| DK1874821T3 (da) | 2005-04-26 | 2013-07-08 | Trion Pharma Gmbh | Kombination af antistoffer med glykokortikoider til behandling af kræft |
| EP1913160A2 (en) | 2005-07-29 | 2008-04-23 | Bayer Healthcare LLC | Diagnostic methods for the prediction of therapeutic success, recurrence free and overall survival in cancer therapy |
| CN103204935B (zh) | 2005-08-26 | 2014-12-10 | 罗氏格黎卡特股份公司 | 具有改变的细胞信号传导活性的修饰的抗原结合分子 |
| CA2624086A1 (en) | 2005-09-28 | 2007-04-05 | H. Lee Moffitt Cancer Center | Individualized cancer treatments |
| DK1931709T3 (en) | 2005-10-03 | 2017-03-13 | Xencor Inc | FC VARIETIES WITH OPTIMIZED FC RECEPTOR BINDING PROPERTIES |
| US20090252681A1 (en) | 2005-10-11 | 2009-10-08 | Ablynx N.V. | Nanobodies and Polypeptides Against EGFR and IGF-IR |
| US20110052570A1 (en) | 2005-10-26 | 2011-03-03 | Children's Medical Center Corporation | Method to prognose response to anti-egfr therapeutics |
| EP1792622A1 (en) | 2005-11-11 | 2007-06-06 | GPC Biotech AG | Anti-proliferative combination therapy comprising a platinum-based chemotherapeutic agent and EGFR inhibitors or pyrimidine analogues |
| EP1963368B3 (en) | 2005-12-13 | 2020-06-10 | Eli Lilly And Company | Anti-il-17 antibodies |
| EP1800695A1 (en) | 2005-12-21 | 2007-06-27 | Fraunhofer-Gesellschaft zur Förderung der angewandten Forschung e.V. | Immuno-RNA-constructs |
| AR056857A1 (es) | 2005-12-30 | 2007-10-24 | U3 Pharma Ag | Anticuerpos dirigidos hacia her-3 (receptor del factor de crecimiento epidérmico humano-3) y sus usos |
| US7498142B2 (en) | 2006-01-31 | 2009-03-03 | Yeda Research And Development Co., Ltd. | Methods of identifying combinations of antibodies with an improved anti-tumor activity and compositions and methods using the antibodies |
| JP2009525048A (ja) | 2006-02-01 | 2009-07-09 | ザ ジョンズ ホプキンス ユニバーシティー | 腫瘍性障害または感染症に対する免疫学的予防法または免疫療法のためのポリペプチド−核酸複合体 |
| CA2646508A1 (en) | 2006-03-17 | 2007-09-27 | Biogen Idec Ma Inc. | Stabilized polypeptide compositions |
| WO2007115571A2 (en) | 2006-04-07 | 2007-10-18 | Enkam Pharmaceuticals A/S | Erbb receptor-derived peptide fragments |
| US20080038271A1 (en) | 2006-06-05 | 2008-02-14 | Amler Lukas C | Extending survival of cancer patients with elevated levels of EGF or TGF-alpha |
| CN101627053A (zh) * | 2006-06-12 | 2010-01-13 | 西福根有限公司 | 泛细胞表面受体特异的治疗剂 |
| CN105837690A (zh) | 2006-06-12 | 2016-08-10 | 新兴产品开发西雅图有限公司 | 具有效应功能的单链多价结合蛋白 |
| AR062223A1 (es) | 2006-08-09 | 2008-10-22 | Glycart Biotechnology Ag | Moleculas de adhesion al antigeno que se adhieren a egfr, vectores que los codifican, y sus usos de estas |
| WO2008019394A2 (en) | 2006-08-11 | 2008-02-14 | The Government Of The United States Of America As Represented By The Secretary, Dept Of Health And Human Services | Methods for treatment and diagnosis of psychiatric disorders |
| US8936780B2 (en) | 2006-08-30 | 2015-01-20 | Advanced Cardiovascular Systems, Inc. | Stimuli responsive polyester amide particles |
| WO2008027236A2 (en) | 2006-08-30 | 2008-03-06 | Genentech, Inc. | Multispecific antibodies |
| BRPI0715754A2 (pt) | 2006-08-31 | 2013-07-09 | Hoffmann La Roche | mÉtodo para a produÇço de fator do crescimento similar Á insulina i |
| MX2009003048A (es) | 2006-09-21 | 2009-09-07 | Prometheus Lab Inc | Disposiciones a base de anticuerpo para detectar transductores de multiple señal en celulas circulantes raras. |
| US20080076139A1 (en) | 2006-09-21 | 2008-03-27 | Sharat Singh | Methods and compositions for detecting the activation states of multiple signal transducers in rare circulating cells |
| BRPI0717416A2 (pt) | 2006-09-21 | 2013-11-12 | Prometheus Lab Inc | Método para realizar um imunoensaio complexo de alta produtividade, e, arranjo |
| US20080112961A1 (en) | 2006-10-09 | 2008-05-15 | Macrogenics, Inc. | Identification and Engineering of Antibodies with Variant Fc Regions and Methods of Using Same |
| EP2092075A2 (en) | 2006-11-06 | 2009-08-26 | Source Precision Medicine, Inc. | Gene expression profiling for identification, monitoring and treatment of melanoma |
| AU2007353412A1 (en) | 2006-11-21 | 2008-11-20 | Fox Chase Cancer Center | Anti-EGFR family antibodies, bispecific anti-EGFR family antibodies and methods of use thereof |
| EP2518508A1 (en) | 2006-11-28 | 2012-10-31 | U3 Pharma GmbH | Activated HER3 as a marker for predicting therapeutic efficacy |
| JP2010511382A (ja) | 2006-12-01 | 2010-04-15 | エージェンシー フォー サイエンス,テクノロジー アンド リサーチ | 癌関連タンパク質キナーゼ |
| US8652466B2 (en) | 2006-12-08 | 2014-02-18 | Macrogenics, Inc. | Methods for the treatment of disease using immunoglobulins having Fc regions with altered affinities for FcγRactivating and FcγRinhibiting |
| WO2008079280A1 (en) | 2006-12-21 | 2008-07-03 | Millipore Corporation | Purification of proteins |
| US8362217B2 (en) | 2006-12-21 | 2013-01-29 | Emd Millipore Corporation | Purification of proteins |
| US8569464B2 (en) | 2006-12-21 | 2013-10-29 | Emd Millipore Corporation | Purification of proteins |
| DE102007001370A1 (de) | 2007-01-09 | 2008-07-10 | Curevac Gmbh | RNA-kodierte Antikörper |
| CA2675014C (en) | 2007-01-17 | 2016-03-29 | Immunomedics, Inc. | Polymeric carriers of therapeutic agents and recognition moieties for antibody-based targeting of disease sites |
| KR101598229B1 (ko) | 2007-02-16 | 2016-02-26 | 메리맥 파마슈티컬즈, 인크. | Erbb3에 대한 항체 및 이의 용도 |
| CA2677108A1 (en) | 2007-03-02 | 2008-09-12 | Genentech, Inc. | Predicting response to a her inhibitor |
| AR065803A1 (es) | 2007-03-23 | 2009-07-01 | Smithkline Beecham Corp | Uso de un polipeptido de il- 18 humana y un anticuerpo anti- cd para preparar unmedicamento |
| CA2681790A1 (en) | 2007-03-30 | 2008-10-09 | F. Hoffmann-La Roche Ag | Composition of labeled and non-labeled monoclonal antibodies |
| AU2008239594B2 (en) | 2007-04-13 | 2013-10-24 | Beth Israel Deaconess Medical Center | Methods for treating cancer resistant to ErbB therapeutics |
| FR2915115B1 (fr) | 2007-04-23 | 2010-09-10 | Sames Technologies | Organe de pulverisation,dispositif de projection comportant un tel organe,installation de projection et methode de nettoyage d'un tel organe |
| AU2008259930B2 (en) | 2007-06-01 | 2014-05-29 | The Regents Of The University Of California | Multigene prognostic assay for lung cancer |
| BRPI0812777A2 (pt) | 2007-06-06 | 2014-12-02 | Hoffmann La Roche | Composição de um primeiro anticorpo monoclonal não-marcado que se liga a um antígeno de tumor e de um segundo anticorpo monoclonal que não sofre reação cruzada marcado com um marcador fluorescente nir |
| US20100183504A1 (en) | 2007-06-14 | 2010-07-22 | Fanqing Frank Chen | Multimodal imaging probes for in vivo targeted and non-targeted imaging and therapeutics |
| WO2009003082A2 (en) | 2007-06-26 | 2008-12-31 | Vanderbilt University | Immunological compositions as cancer biomarkers and/or therapeutics |
| WO2009003145A1 (en) | 2007-06-26 | 2008-12-31 | University Of Miami | Antibody-endostatin fusion protein and its variants |
| CA3113365A1 (en) | 2007-07-09 | 2009-01-15 | Genentech, Inc. | Prevention of disulfide bond reduction during recombinant production of polypeptides |
| BRPI0813583A2 (pt) | 2007-07-13 | 2014-12-30 | Prometheus Lab Inc | Métodos para selecionar um medicamento anticâncer, para identificar a resposta de um tumor pulmonar, e para prognosticar a resposta de um paciente, e, arranjo |
| WO2009023266A1 (en) | 2007-08-14 | 2009-02-19 | Ludwig Institute For Cancer Research | Generation of antibodies to cell-surface receptors and cancer-associated proteins including egfr family members |
| ES2536772T3 (es) | 2007-09-21 | 2015-05-28 | The Regents Of The University Of California | El interferón dirigido demuestra potentes actividades apoptóticas y antitumorales |
| US20110091473A1 (en) | 2007-10-22 | 2011-04-21 | Genmab A/S | Novel antibody therapies |
| US20120047586A9 (en) | 2007-10-24 | 2012-02-23 | Otsuka Chemical Co., Ltd | Polypeptide having enhanced effector function |
| EP2602623B1 (en) | 2008-02-25 | 2015-09-16 | Nestec S.A. | Mehtod for the detection of intracellular truncated receptors |
| AU2009221729A1 (en) | 2008-03-06 | 2009-09-11 | Genentech, Inc. | Combination therapy with c-met and HER antagonists |
| EP2106806A1 (en) | 2008-03-31 | 2009-10-07 | Fraunhofer-Gesellschaft zur Förderung der Angewandten Forschung e.V. | Nanoparticles for targeted delivery of active agents to the lung |
| EP2860260A1 (en) | 2008-04-11 | 2015-04-15 | Merrimack Pharmaceuticals, Inc. | Human serum albumin linkers and conjugates thereof |
| SG190572A1 (en) | 2008-04-29 | 2013-06-28 | Abbott Lab | Dual variable domain immunoglobulins and uses thereof |
| RU2487877C2 (ru) | 2008-04-30 | 2013-07-20 | Иммьюноджен, Инк. | Высокоэффективные конъюгаты и гидрофильные сшивающие агенты (линкеры) |
| WO2009134870A1 (en) | 2008-04-30 | 2009-11-05 | Immunogen, Inc. | Potent cell-binding agent drug conjugates |
| UY31800A (es) | 2008-05-05 | 2009-11-10 | Smithkline Beckman Corp | Metodo de tratamiento de cancer usando un inhibidor de cmet y axl y un inhibidor de erbb |
| CA2727278A1 (en) | 2008-06-16 | 2010-01-21 | Immunogen, Inc. | Novel synergistic effects |
| EP2138511A1 (en) | 2008-06-27 | 2009-12-30 | Max-Planck-Gesellschaft zur Förderung der Wissenschaften e.V. | HER3 as a determinant for the prognosis of melanoma |
| MX2010014574A (es) | 2008-07-08 | 2011-04-27 | Abbott Lab | Inmunoglobulinas de dominio variable dual para prostaglandina e2 y usos de las mismas. |
| US8445219B2 (en) | 2008-07-25 | 2013-05-21 | Merck Patent Gmbh | Method of determination of receptor binding saturation effected by monoclonal antibodies |
| US8056451B2 (en) | 2008-07-28 | 2011-11-15 | Irwin Industrial Tool Company | Locking pliers |
| US20100033482A1 (en) | 2008-08-11 | 2010-02-11 | Interactive Relighting of Dynamic Refractive Objects | Interactive Relighting of Dynamic Refractive Objects |
| AU2009281721A1 (en) | 2008-08-15 | 2010-02-18 | Merrimack Pharmaceuticals, Inc. | Methods and systems for predicting response of cells to a therapeutic agent |
| US8084222B2 (en) | 2008-09-26 | 2011-12-27 | Eureka Therapeutics, Inc. | Methods for generating host cells |
| CN102753193A (zh) | 2008-10-31 | 2012-10-24 | 比奥根艾迪克Ma公司 | Light靶向分子及其用途 |
| EP3622968A1 (en) | 2008-10-31 | 2020-03-18 | The General Hospital Corporation | Compositions and methods for delivering a substance to a biological target |
| KR20110112301A (ko) | 2008-11-18 | 2011-10-12 | 메리맥 파마슈티컬즈, 인크. | 인간 혈청 알부민 링커 및 그 콘쥬게이트 |
| US20100169729A1 (en) | 2008-12-30 | 2010-07-01 | Datta Shamanna M | Enabling an integrated memory controller to transparently work with defective memory devices |
| EP2380025B1 (en) | 2009-01-14 | 2013-09-11 | The United States of America, as represented by The Secretary, Department of Health and Human Services | Ratio based biomarkers and methods of use thereof |
| BRPI1007321A2 (pt) | 2009-01-15 | 2018-07-10 | Laboratory Corp America Holdings | métodos para medir e/ou quantificar a presença e/ou quantidade de her-3 ou her-3 em um complexo em uma amostra de um paciente, e para determinar se um indivíduo com um câncer é provável de responder ao tratamento com uma terapia alvejada, e, anticorpo. |
| SG172984A1 (en) | 2009-01-15 | 2011-08-29 | Lab Corp America Holdings | Methods of determining patient response by measurement of her-2 expression |
| PT3903829T (pt) | 2009-02-13 | 2023-06-02 | Immunomedics Inc | Imunoconjugados com uma ligação intracelular clivável |
| EP2401621B1 (en) | 2009-02-24 | 2013-08-14 | Roche Diagnostics GmbH | Use of s-erbb-3 as a marker for cancer |
| WO2010099186A1 (en) | 2009-02-25 | 2010-09-02 | Merck Sharp & Dohme Corp. | Her2 antibody compositions |
| NZ594665A (en) | 2009-03-20 | 2013-08-30 | Genentech Inc | Bispecific anti-her antibodies |
| US8362215B2 (en) | 2009-04-29 | 2013-01-29 | Trellis Bioscience, Llc | Antibodies immunoreactive with heregulin-coupled HER3 |
| US20120121586A1 (en) | 2009-05-29 | 2012-05-17 | Astrid Kiermaier | Modulators for her2 signaling in her2 expressing patients with gastric cancer |
| WO2011005481A1 (en) | 2009-06-22 | 2011-01-13 | Medimmune, Llc | ENGINEERED Fc REGIONS FOR SITE-SPECIFIC CONJUGATION |
| AU2010273319B2 (en) | 2009-07-15 | 2015-01-22 | Nestec S.A. | Drug selection for gastric cancer therapy using antibody-based arrays |
| SI2462158T1 (en) | 2009-08-06 | 2018-04-30 | F. Hoffmann-La Roche Ag | Method to improve virus removal in protein purification |
| WO2011019620A1 (en) | 2009-08-10 | 2011-02-17 | Genentech, Inc. | Antibodies with enhanced adcc function |
| CA2771744A1 (en) | 2009-08-21 | 2011-02-24 | Merrimack Pharmaceuticals, Inc. | Antibodies against the ectodomain of erbb3 and uses thereof |
| EP2475390A4 (en) | 2009-09-09 | 2014-01-01 | Quintiles Transnat Corp | METHODS AND COMPOSITIONS FOR THE TREATMENT OF TYROSINE KINASE RECEPTOR MEDIATION DISEASES OR DISORDERS |
| BR112012007760A2 (pt) | 2009-10-07 | 2015-08-25 | Macrogenics Inc | Método de atenuar fucosilação pós translacional de uma região fc de igc humana, anticorpo que se liga especificamente a um antigeno de câncer caracteristico de um cancêr polipeptideo |
| EP2486052A4 (en) | 2009-10-09 | 2013-05-01 | Merck Sharp & Dohme | GENERATION, LABELING AND USE OF ANTI-HER3 ANTIBODIES |
| WO2011047180A1 (en) | 2009-10-14 | 2011-04-21 | Merrimack Pharmaceuticals, Inc. | Bispecific binding agents targeting igf-1r and erbb3 signalling and uses thereof |
| PL2719708T3 (pl) | 2009-11-13 | 2018-04-30 | Daiichi Sankyo Europe Gmbh | Materiał i sposoby leczenia lub zapobiegania chorobom związanym z HER-3 |
| WO2011103242A1 (en) | 2010-02-18 | 2011-08-25 | Genentech, Inc. | Neuregulin antagonists and use thereof in treating cancer |
| US20130225424A1 (en) | 2010-03-03 | 2013-08-29 | Targeted Molecular Diagnostics, Llc | Methods for determining responsiveness to a drug based upon determination of ras mutation and/or ras amplification |
| SG183532A1 (en) | 2010-03-11 | 2012-09-27 | Merrimack Pharmaceuticals Inc | Use of erbb3 inhibitors in the treatment of triple negative and basal-like breast cancers |
| US8481687B2 (en) | 2010-04-09 | 2013-07-09 | Aveo Pharmaceuticals, Inc. | Anti-ErbB3 antibodies |
| WO2011139629A2 (en) | 2010-04-26 | 2011-11-10 | Biogen Idec Ma Inc. | Light targeting molecules and uses thereof |
| WO2011143414A1 (en) | 2010-05-13 | 2011-11-17 | Fox Chase Cancer Center | RECOMBINANTLY PRODUCED ANTIBODIES TARGETING ErbB SIGNALING MOLECULES AND METHODS OF USE THEREOF FOR THE DIAGNOSIS AND TREATMENT OF DISEASE |
| WO2011146568A1 (en) | 2010-05-19 | 2011-11-24 | Genentech, Inc. | Predicting response to a her inhibitor |
| SG185354A1 (en) | 2010-05-20 | 2012-12-28 | Ablynx Nv | Biological materials related to her3 |
| WO2012103341A1 (en) | 2011-01-27 | 2012-08-02 | Merrimack Pharmaceuticals, Inc. | Treatment of advanced solid stage tumors using anti-erbb3 antibodies |
| CN103649117B (zh) | 2011-02-04 | 2016-09-14 | 霍夫曼-拉罗奇有限公司 | Fc变体及其生成方法 |
| WO2012106578A1 (en) | 2011-02-04 | 2012-08-09 | The United States Of America, As Represented By The Secretary, Department Of Health And Human Services | HIV NEUTRALIZING ANTIBODIES HAVING MUTATIONS IN CONSTANT DOMAIN (Fc) |
| JP6228014B2 (ja) | 2011-02-07 | 2017-11-08 | リサーチ ディベロップメント ファウンデーション | 操作された免疫グロブリンFcポリペプチド |
| JP2014509850A (ja) | 2011-03-06 | 2014-04-24 | メルク セロノ ソシエテ アノニム | 低フコース細胞株およびその使用 |
| AU2012229102B2 (en) | 2011-03-17 | 2016-02-04 | Cernostics, Inc. | Systems and compositions for diagnosing Barrett's esophagus and methods of using the same |
-
2011
- 2011-09-01 TW TW100131536A patent/TW201302793A/zh unknown
- 2011-09-02 JP JP2013527341A patent/JP2013544492A/ja active Pending
- 2011-09-02 EA EA201390328A patent/EA201390328A1/ru unknown
- 2011-09-02 MX MX2013002535A patent/MX2013002535A/es unknown
- 2011-09-02 NZ NZ607680A patent/NZ607680A/en not_active IP Right Cessation
- 2011-09-02 PH PH1/2013/500353A patent/PH12013500353A1/en unknown
- 2011-09-02 SG SG2013013057A patent/SG187930A1/en unknown
- 2011-09-02 KR KR1020137008415A patent/KR20130101047A/ko not_active Withdrawn
- 2011-09-02 CN CN2011800533015A patent/CN103189391A/zh active Pending
- 2011-09-02 MA MA35784A patent/MA34555B1/fr unknown
- 2011-09-02 WO PCT/US2011/050322 patent/WO2012031198A2/en not_active Ceased
- 2011-09-02 SG SG10201401681PA patent/SG10201401681PA/en unknown
- 2011-09-02 BR BR112013005242A patent/BR112013005242A2/pt not_active IP Right Cessation
- 2011-09-02 US US13/639,918 patent/US9085622B2/en active Active
- 2011-09-02 PE PE2013000314A patent/PE20140133A1/es not_active Application Discontinuation
- 2011-09-02 AU AU2011295726A patent/AU2011295726B2/en not_active Ceased
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- 2011-09-05 UY UY0001033591A patent/UY33591A/es unknown
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- 2013-03-20 CR CR20130128A patent/CR20130128A/es unknown
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| CL2013000566A1 (es) | 2014-01-24 |
| EP2611829A2 (en) | 2013-07-10 |
| AU2011295726B2 (en) | 2014-11-06 |
| AU2011295726A1 (en) | 2013-03-21 |
| EP2611829A4 (en) | 2014-05-07 |
| WO2012031198A3 (en) | 2012-05-18 |
| EA201390328A1 (ru) | 2013-08-30 |
| NZ607680A (en) | 2015-02-27 |
| MA34555B1 (fr) | 2013-09-02 |
| MX2013002535A (es) | 2013-06-03 |
| PE20140133A1 (es) | 2014-02-09 |
| US20130156779A1 (en) | 2013-06-20 |
| SG10201401681PA (en) | 2014-07-30 |
| CR20130128A (es) | 2013-06-28 |
| KR20130101047A (ko) | 2013-09-12 |
| UY33591A (es) | 2012-03-30 |
| CO6690769A2 (es) | 2013-06-17 |
| WO2012031198A2 (en) | 2012-03-08 |
| CN103189391A (zh) | 2013-07-03 |
| SG187930A1 (en) | 2013-03-28 |
| CA2809443A1 (en) | 2012-03-08 |
| BR112013005242A2 (pt) | 2016-06-28 |
| US9085622B2 (en) | 2015-07-21 |
| PH12013500353A1 (en) | 2013-03-25 |
| JP2013544492A (ja) | 2013-12-19 |
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