CA2809443A1 - Novel antigen binding proteins - Google Patents
Novel antigen binding proteins Download PDFInfo
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- CA2809443A1 CA2809443A1 CA2809443A CA2809443A CA2809443A1 CA 2809443 A1 CA2809443 A1 CA 2809443A1 CA 2809443 A CA2809443 A CA 2809443A CA 2809443 A CA2809443 A CA 2809443A CA 2809443 A1 CA2809443 A1 CA 2809443A1
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- amino acid
- acid sequence
- antigen binding
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Classifications
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- 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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- 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
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- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
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- A61K—PREPARATIONS FOR MEDICAL, DENTAL OR TOILETRY PURPOSES
- 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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- C07K2317/00—Immunoglobulins specific features
- C07K2317/20—Immunoglobulins specific features characterized by taxonomic origin
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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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- 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
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- 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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- 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
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- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
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- C07K2317/70—Immunoglobulins specific features characterized by effect upon binding to a cell or to an antigen
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Landscapes
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- 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)
Applications Claiming Priority (5)
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| US37984010P | 2010-09-03 | 2010-09-03 | |
| US61/379,840 | 2010-09-03 | ||
| US201161440460P | 2011-02-08 | 2011-02-08 | |
| US61/440,460 | 2011-02-08 | ||
| PCT/US2011/050322 WO2012031198A2 (en) | 2010-09-03 | 2011-09-02 | Novel antigen binding proteins |
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| CA2809443A1 true CA2809443A1 (en) | 2012-03-08 |
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| Application Number | Title | Priority Date | Filing Date |
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| CA2809443A Abandoned CA2809443A1 (en) | 2010-09-03 | 2011-09-02 | Novel antigen binding proteins |
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| EP (1) | EP2611829A4 (enExample) |
| JP (1) | JP2013544492A (enExample) |
| KR (1) | KR20130101047A (enExample) |
| CN (1) | CN103189391A (enExample) |
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| BR (1) | BR112013005242A2 (enExample) |
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| CL (1) | CL2013000566A1 (enExample) |
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Cited By (1)
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| CN117903311A (zh) * | 2024-03-20 | 2024-04-19 | 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 |
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| HRP20160737T1 (hr) | 2009-12-22 | 2016-07-15 | Roche Glycart Ag | Anti-her3-protutijela i njihove uporabe |
| PH12013500333A1 (en) | 2010-08-20 | 2013-04-22 | Novartis Ag | Antibodies for epidermal growth factor receptor 3 (her3) |
| US9220775B2 (en) | 2011-11-23 | 2015-12-29 | Medimmune Llc | Binding molecules specific for HER3 and uses thereof |
| MX2014006731A (es) * | 2011-12-05 | 2015-06-04 | Novartis Ag | Anticuerpos para el receptor del factor de crecimiento epidermico 3 (her3) dirigidos al dominio iii y al dominio iv del her3. |
| TW201328706A (zh) | 2011-12-05 | 2013-07-16 | Novartis Ag | 表皮生長因子受體３（ｈｅｒ３）之抗體 |
| EP2807272A1 (en) * | 2012-01-27 | 2014-12-03 | Ventana Medical Systems, Inc. | Devices and methods for detecting bio-analytes using optically decipherable patterns |
| MX2015005757A (es) | 2012-11-08 | 2015-11-18 | Hoffmann La Roche | Proteinas ligantes de antigeno her3 de union a la horquilla 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 |
| WO2015048008A2 (en) | 2013-09-24 | 2015-04-02 | Medimmune, Llc | Binding molecules specific for her3 and uses thereof |
| CN105593241B (zh) * | 2013-10-04 | 2020-07-10 | 豪夫迈·罗氏有限公司 | 特异性结合her3的抗体 |
| IL301147A (en) * | 2014-02-28 | 2023-05-01 | Merus Nv | An antibody that binds to ErbB-2 and ErbB-3 |
| EP3110846B1 (en) | 2014-02-28 | 2020-08-19 | 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 |
| JP6983511B2 (ja) | 2014-04-25 | 2021-12-17 | ザ・トラステイーズ・オブ・ザ・ユニバーシテイ・オブ・ペンシルベニア | 脳中の転移乳癌および他の癌を処置するための方法および組成物 |
| RU2016148682A (ru) | 2014-05-14 | 2018-06-19 | Ф. Хоффманн-Ля Рош Аг | Антитела против рецептора-3 к эпидермальному ростовому фактору человека (her3), связывающиеся с бета-шпилькой her3 |
| KR102062025B1 (ko) | 2014-06-30 | 2020-01-03 | 타베다 세라퓨틱스, 인코포레이티드 | 표적화된 콘주게이트 및 입자 및 그것의 제형 |
| EP3169776B1 (en) * | 2014-07-14 | 2025-09-03 | The Regents of The University of California | Crispr/cas transcriptional modulation |
| EP3191523B1 (en) | 2014-09-08 | 2019-08-07 | Yeda Research and Development Co., Ltd. | Compositions and methods for treating cancer resistant to a tyrosine kinase inhibitor (tki) |
| CA2959716A1 (en) | 2014-09-08 | 2016-03-17 | Yeda Research And Development Co. Ltd. | Anti-her3 antibodies and uses of same |
| WO2016059602A2 (en) * | 2014-10-16 | 2016-04-21 | Glaxo Group Limited | Methods of treating cancer and related compositions |
| HUE055222T2 (hu) | 2015-10-23 | 2021-11-29 | Merus Nv | Megkötõ molekulák, amelyek gátolják a rák növekedését |
| AU2016343817B2 (en) | 2015-10-28 | 2021-05-27 | Tva (Abc), Llc | SSTR-targeted conjugates and particles and formulations thereof |
| TWI726942B (zh) | 2015-11-30 | 2021-05-11 | 美商輝瑞股份有限公司 | 位點專一性ｈｅｒ２抗體藥物共軛體 |
| JP2018536682A (ja) | 2015-12-11 | 2018-12-13 | リジェネロン・ファーマシューティカルズ・インコーポレイテッドＲｅｇｅｎｅｒｏｎ Ｐｈａｒｍａｃｅｕｔｉｃａｌｓ， Ｉｎｃ． | Ｅｇｆｒ及び／またはｅｒｂｂ３遮断に耐性のある腫瘍の成長を低減または防止するための方法 |
| CN109310754A (zh) | 2016-03-15 | 2019-02-05 | 梅里麦克制药股份有限公司 | 使用包含抗erbb3抗体的联合疗法治疗er+、her2-、hrg+乳腺癌的方法 |
| 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 |
| CN110650752A (zh) | 2017-03-31 | 2020-01-03 | 美勒斯公司 | 用于治疗具有NRG1融合基因的细胞的ErbB-2和ErbB3结合双特异性抗体 |
| EA201992522A1 (ru) | 2017-05-17 | 2020-04-22 | Мерус Н.В. | КОМБИНАЦИЯ БИСПЕЦИФИЧЕСКОГО АНТИТЕЛА К ErbB-2/ErbB-3 С ЭНДОКРИННОЙ ТЕРАПИЕЙ РАКА МОЛОЧНОЙ ЖЕЛЕЗЫ |
| CN110753703B (zh) * | 2017-05-23 | 2024-04-09 | 德国亥姆霍兹慕尼黑中心健康与环境研究中心（有限公司） | 新的cd73抗体、其制备和用途 |
| EP3665198B9 (en) | 2017-08-09 | 2025-05-21 | Merus N.V. | Antibodies that bind egfr and cmet |
| CN111886024B (zh) * | 2018-03-08 | 2024-07-30 | 凡恩世制药(北京)有限公司 | 抗tip-1抗体及其用途 |
| WO2019185164A1 (en) * | 2018-03-29 | 2019-10-03 | Hummingbird Bioscience Holdings Pte. Ltd. | Her3 antigen-binding molecules |
| AU2020355253A1 (en) * | 2019-09-27 | 2022-03-24 | Agenus Inc. | Heterodimeric proteins |
| 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 |
| 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 |
| AU4155696A (en) | 1994-11-09 | 1996-06-06 | Regents Of The University Of California, The | Immunoliposomes that optimize internalization into target cells |
| US5968511A (en) | 1996-03-27 | 1999-10-19 | Genentech, Inc. | ErbB3 antibodies |
| ES2274537T5 (es) | 1996-03-27 | 2015-09-14 | Genentech, Inc. | Anticuerpos ErbB3 |
| 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 |
| EP0912734B1 (en) | 1996-07-12 | 2010-11-03 | Genentech, Inc. | Chimeric heteromultimer adhesins |
| 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. |
| AU2003203831B2 (en) | 1998-02-04 | 2006-08-10 | Genentech, Inc. | Use of heregulin as an epithelial cell growth factor |
| US20010023241A1 (en) | 1998-02-04 | 2001-09-20 | Sliwkowski Mark X. | Use of heregulin as a growth factor |
| AU2581599A (en) | 1998-02-04 | 1999-08-23 | Genentech Inc. | Use of heregulin as an epithelial cell growth factor |
| US6417168B1 (en) | 1998-03-04 | 2002-07-09 | The Trustees Of The University Of Pennsylvania | Compositions and methods of treating tumors |
| IL138488A0 (en) | 1998-03-17 | 2001-10-31 | Genentech Inc | Polypeptides homologous to vegf and bmp1 |
| DK1071700T3 (da) | 1998-04-20 | 2010-06-07 | Glycart Biotechnology Ag | Glykosylerings-modifikation af antistoffer til forbedring af antistofafhængig cellulær cytotoksicitet |
| HK1040720A1 (zh) | 1998-05-15 | 2002-06-21 | 伊姆克罗尼系统公司 | 用辐射和生长因子受体酪氨酸激酶抑制剂治疗人肿瘤 |
| 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 |
| AU764037B2 (en) | 1998-11-07 | 2003-08-07 | Genentech Inc. | Method for enhancing proliferation of inner ear hair cells using ligands for HER2 and/or HER3 receptors |
| US7183387B1 (en) | 1999-01-15 | 2007-02-27 | Genentech, Inc. | Polypeptide variants with altered effector function |
| US6737056B1 (en) | 1999-01-15 | 2004-05-18 | Genentech, Inc. | Polypeptide variants with altered effector function |
| WO2000061637A1 (en) * | 1999-04-14 | 2000-10-19 | Smithkline Beecham Corporation | Erythropoietin receptor antibodies |
| 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 |
| BR0012196A (pt) | 1999-06-25 | 2002-03-19 | Genentech Inc | Método de tratamento de um tumor em mamìferos através do uso de conjugados de maitansinóide e anticorpo receptor anti-erbb e artigo industrializado |
| KR100850389B1 (ko) | 1999-06-25 | 2008-08-04 | 제넨테크, 인크. | 인간화 항-ＥｒｂＢ2 항체 및 항-ＥｒｂＢ2 항체를 사용한치료 방법 |
| US6949245B1 (en) | 1999-06-25 | 2005-09-27 | Genentech, Inc. | Humanized anti-ErbB2 antibodies and treatment with anti-ErbB2 antibodies |
| NZ517150A (en) | 1999-08-27 | 2005-01-28 | Genentech Inc | Dosages for treatment with 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 |
| AU2951801A (en) | 2000-01-12 | 2001-07-24 | Ventana Medical Systems, Inc. | Method for quantitating a protein by image analysis |
| IL150755A0 (en) | 2000-02-16 | 2003-02-12 | Genentech Inc | Uses of agonists and antagonists to modulate activity of tnf-related molecules |
| 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 |
| MXPA02010011A (es) | 2000-04-11 | 2003-04-25 | Genentech Inc | Anticuerpos multivalentes y usos para los mismos. |
| AU2007216733A1 (en) | 2000-04-11 | 2007-09-27 | Genentech, Inc. | Multivalent antibodies and uses therefor |
| 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 |
| AU2002221891A1 (en) | 2000-11-24 | 2002-06-03 | Carl Freudenberg Kg | Floor mop |
| AU2008200400B2 (en) | 2001-01-17 | 2012-06-07 | Aptevo Research And Development Llc | Binding domain-immunoglobulin fusion proteins |
| US20030133939A1 (en) | 2001-01-17 | 2003-07-17 | Genecraft, Inc. | 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 |
| EP1370588A2 (en) | 2001-02-12 | 2003-12-17 | 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 |
| PL373962A1 (en) | 2001-05-21 | 2005-09-19 | Aclara Biosciences, Inc. | Methods and compositions for analyzing proteins |
| US7744882B2 (en) | 2001-05-31 | 2010-06-29 | Tumor Biology Investment Group, Inc. | Soluble ErbB3 methods of detection and antibodies |
| US7745398B2 (en) | 2001-05-31 | 2010-06-29 | Tumor Biology Investment Group, Inc. | Soluble ErbB3 and treatment of cancer |
| AU2002314495A1 (en) | 2001-06-20 | 2003-01-02 | Prochon Biotech Ltd. | Antibodies that block receptor protein tyrosine kinase activation, methods of screening for and uses thereof |
| US7276658B2 (en) | 2001-06-21 | 2007-10-02 | 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 |
| WO2003012072A2 (en) | 2001-08-03 | 2003-02-13 | The Trustees Of The University Of Pennsylvania | Monoclonal antibodies to activated erbb family members and methods of use thereof |
| EP1283053A1 (en) | 2001-08-09 | 2003-02-12 | Max-Planck-Gesellschaft zur Förderung der Wissenschaften e.V. | Inhibitors of HER3 activity |
| AU2008200654B2 (en) | 2001-08-09 | 2010-04-29 | Max-Planck-Gesellschaft Zur Forderung Der Wissenschaften E.V. | Inhibitors of HER3 activity |
| WO2005063299A2 (en) | 2003-12-24 | 2005-07-14 | Genentech, Inc. | Compositions and methods for the treatment of tumor of hematopoietic origin |
| US7591994B2 (en) | 2002-12-13 | 2009-09-22 | Immunomedics, Inc. | Camptothecin-binding moiety conjugates |
| US8877901B2 (en) | 2002-12-13 | 2014-11-04 | Immunomedics, Inc. | Camptothecin-binding moiety conjugates |
| US20040132101A1 (en) | 2002-09-27 | 2004-07-08 | Xencor | Optimized Fc variants and methods for their generation |
| 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 |
| EP2400021B1 (en) | 2002-03-26 | 2016-11-30 | Zensun (Shanghai) Science & Technology, Co., Ltd. | ErbB3 based methods and compositions for treating neoplasms |
| 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 |
| HUE025101T2 (en) | 2002-04-26 | 2016-02-29 | Genentech Inc | Purification of proteins other than affinity purification |
| US20040229293A1 (en) | 2002-05-21 | 2004-11-18 | Po-Ying Chan-Hui | Surface receptor complexes 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 |
| US20040229380A1 (en) | 2002-05-21 | 2004-11-18 | Po-Ying Chan-Hui | ErbB heterodimers as biomarkers |
| WO2004000102A2 (en) | 2002-06-19 | 2003-12-31 | Abgenix, Inc. | Method for predicting response to epidermal growth factor receptor-directed therapy |
| WO2004008099A2 (en) | 2002-07-15 | 2004-01-22 | Genentech, Inc. | METHODS FOR IDENTIFYING TUMORS THAT ARE RESPONSIVE TO TREATMENT WITH ANTI-ErbB2 ANTIBODIES |
| JP4443407B2 (ja) | 2002-07-25 | 2010-03-31 | アクララ バイオサイエンシーズ， インコーポレイテッド | レセプターオリゴマー形成の検出 |
| GB0225282D0 (en) | 2002-10-31 | 2002-12-11 | Astrazeneca Ab | assay |
| AU2004205684A1 (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 |
| KR20060017585A (ko) | 2003-04-04 | 2006-02-24 | 유니베르시떼 드 로잔느 | 암 치료용 펩타바디 |
| US7189694B2 (en) | 2003-04-18 | 2007-03-13 | University Of Florida Research Foundation, Inc. | Inhibitors of autophosphorylation protein kinases |
| EP1633870B1 (en) | 2003-05-30 | 2013-03-27 | OncoTherapy Science, Inc. | Process for screening a drug response in cancer patients |
| ES2323425T3 (es) | 2003-06-06 | 2009-07-15 | Genentech, Inc. | Modulacion de la interaccion entre la cadena beta de hgf y c-met. |
| US20040254108A1 (en) | 2003-06-13 | 2004-12-16 | Jing Ma | 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 |
| EP1633398A4 (en) | 2003-06-13 | 2007-02-28 | Oncomax Acquisition Corp | PREPARATION AND APPLICATION OF BIFUNCTIONAL ANTI-TUMOR HYBRID 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 |
| JP4599355B2 (ja) | 2003-07-28 | 2010-12-15 | ジェネンテック， インコーポレイテッド | プロテインａアフィニティークロマトグラフィーの間のプロテインａの浸出の低減 |
| CA2534362A1 (en) | 2003-08-05 | 2005-02-17 | Euro-Celtique S.A. | Erbb receptor methods and kits for monitoring chemotherapy resistance |
| JP4818917B2 (ja) | 2003-08-08 | 2011-11-16 | イミューノメディクス、インコーポレイテッド | 腫瘍および罹患細胞のアポトーシスを誘発するための二重特異性抗体 |
| WO2005019470A2 (en) | 2003-08-11 | 2005-03-03 | 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 |
| WO2005045058A2 (en) | 2003-10-27 | 2005-05-19 | Monogram Biosciences, Inc. | Detecting human anti-therapeutic antibodies |
| WO2005044302A1 (en) | 2003-11-06 | 2005-05-19 | Pfizer Products Inc. | Selective erbb2 inhibitor/anti-erbb antibody combinations in the treatment of cancer |
| 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 |
| 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 |
| WO2005112969A2 (en) | 2004-04-22 | 2005-12-01 | Oregon Health And Science University | Herstatin or intron 8-encoded domain thereof for modulating signaling mediated by igf-1 receptor and erbb receptors |
| CA2565827A1 (en) | 2004-05-05 | 2005-12-15 | Merrimack Pharmaceuticals, Inc. | Bispecific binding agents for modulating biological activity |
| BRPI0510883B8 (pt) | 2004-06-01 | 2021-05-25 | Genentech Inc | composto conjugado de droga e anticorpo, composição farmacêutica, método de fabricação de composto conjugado de droga e anticorpo e usos de uma formulação, de um conjugado de droga e anticorpo e um agente quimioterapêutico e de uma combinação |
| AU2005250216B2 (en) | 2004-06-01 | 2009-12-10 | Domantis Limited | Bispecific fusion antibodies with enhanced serum half-life |
| GT200500155A (es) | 2004-06-16 | 2006-05-15 | Terapia del càncer resistente al platino | |
| NZ551934A (en) | 2004-06-24 | 2009-09-25 | Inst Medical W & E Hall | Conjugates comprising a targeting moiety and a peptide that mimics the apoptosis-inducing BH3-only proteins |
| KR20110050567A (ko) | 2004-07-22 | 2011-05-13 | 제넨테크, 인크. | Ｈｅｒ２ 항체 조성물 |
| 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 |
| CA2583230A1 (en) | 2004-10-05 | 2006-04-20 | Oregon Health And Science University | Compositions and methods for treating disease |
| EP2325206B1 (en) | 2004-11-12 | 2014-03-19 | Xencor, Inc. | Fc variants with altered binding to fcrn |
| EP1814882A1 (en) | 2004-11-22 | 2007-08-08 | Vertex Pharmaceuticals Incorporated | Pyrrolopyrazines and pyrazolopyrazines useful as inhibitors of protein kinases |
| US7947839B2 (en) | 2004-12-01 | 2011-05-24 | Genentech, Inc. | Heterocyclic-substituted bis-1,8 naphthalimide compounds, antibody drug conjugates, and methods of use |
| US7811562B2 (en) * | 2004-12-03 | 2010-10-12 | Schering Corporation | Biomarkers for pre-selection of patients for anti-IGF1R therapy |
| WO2006063042A2 (en) | 2004-12-07 | 2006-06-15 | Genentech, Inc. | Selecting patients for therapy with a her inhibitor |
| US7807789B2 (en) | 2004-12-21 | 2010-10-05 | Cell Signaling Technology, Inc. | Reagents for the detection of protein phosphorylation in EGFR-signaling pathways |
| WO2006068640A1 (en) | 2004-12-21 | 2006-06-29 | Cell Signaling Technology, Inc. | Protein phosphorylation in egfr-signaling pathways |
| PL1699826T3 (pl) | 2005-01-05 | 2009-08-31 | F Star Biotechnologische Forschungs Und Entw M B H | Syntetyczne domeny immunoglobulinowe o właściwościach wiążących modyfikowane w regionach cząsteczki różnych od regionów determinujących komplementarność |
| WO2006076041A2 (en) | 2005-01-11 | 2006-07-20 | Molecular Logix, Inc. | Pan-her antagonists and methods of use |
| TWI441646B (zh) | 2005-01-21 | 2014-06-21 | Genentech Inc | 帕妥珠單抗(pertuzumab)用於製備治療人類病患癌症之藥物的用途 |
| WO2006084018A2 (en) | 2005-02-02 | 2006-08-10 | Monogram Biosciences, Inc. | Methods for determining responsiveness to cancer therapy |
| PT1871805T (pt) | 2005-02-07 | 2019-12-02 | Roche Glycart Ag | Moléculas de ligação a antigénios que se ligam ao rfce, vetores que as codificam e as suas utilizações |
| US7718626B2 (en) | 2005-02-17 | 2010-05-18 | University Of Maryland, Baltimore | ErbB3 binding protein compositions and methods of use |
| WO2006091209A2 (en) | 2005-02-23 | 2006-08-31 | Merrimack Pharmaceuticals, Inc. | Bispecific binding agents for modulating biological activity |
| CA2596133C (en) | 2005-02-23 | 2016-11-15 | Genentech, Inc. | Extending time to disease progression or survival in cancer patients |
| AU2006220719A1 (en) | 2005-03-07 | 2006-09-14 | Ligacept, Llc | Tyrosine kinase inhibitor compositions and methods for manufacturing and using them in the treatment of disease |
| TW200642695A (en) | 2005-03-08 | 2006-12-16 | Genentech Inc | Methods for identifying tumors responsive to treatment with her dimerization inhibitors (HDIs) |
| CA2604032C (en) | 2005-04-06 | 2017-08-22 | Ibc Pharmaceuticals, Inc. | Methods for generating stably linked complexes composed of homodimers, homotetramers or dimers of dimers and uses |
| WO2006114115A1 (de) | 2005-04-26 | 2006-11-02 | Trion Pharma Gmbh | Kombination von antikörpern mit glukokortikoiden zur behandlung von krebs |
| US20090298061A1 (en) | 2005-07-29 | 2009-12-03 | Siemens Healthcare Diagnostics Inc. | Diagnostic Methods for the Prediction of Therapeutic Success, Recurrence Free and Overall Survival in Cancer Therapy |
| KR101460932B1 (ko) | 2005-08-26 | 2014-11-12 | 로슈 글리카트 아게 | 변형된 세포 신호 활성을 가진 개질된 항원 결합 분자 |
| 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 |
| ES2672221T3 (es) * | 2005-12-13 | 2018-06-13 | Eli Lilly And Company | Anticuerpos anti IL-17 |
| 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 |
| EP1986698A2 (en) | 2006-02-01 | 2008-11-05 | The Johns Hopkins University | Polypeptide-nucleic acid conjugate for immunoprophylaxis or immunotherapy for neoplastic or infectious disorders |
| AU2007227292B2 (en) | 2006-03-17 | 2012-04-12 | Biogen Ma Inc. | Stabilized polypeptide compositions |
| WO2007115571A2 (en) | 2006-04-07 | 2007-10-18 | Enkam Pharmaceuticals A/S | Erbb receptor-derived peptide fragments |
| JP2009539836A (ja) | 2006-06-05 | 2009-11-19 | ジェネンテック・インコーポレーテッド | ＥＧＦまたはＴＧＦ−αのレベルの上昇が生じている癌患者の生存の延長 |
| EP2418223A3 (en) | 2006-06-12 | 2013-01-16 | Emergent Product Development Seattle, LLC | Single-chain multivalent binding proteins with effector function |
| 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 |
| 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 |
| US20100316626A1 (en) | 2006-08-11 | 2010-12-16 | The Government Of The United States Of America As Represented By The Secretary | 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 |
| US10118970B2 (en) | 2006-08-30 | 2018-11-06 | Genentech, Inc. | Multispecific antibodies |
| CN101484469B (zh) | 2006-08-31 | 2012-12-12 | 弗·哈夫曼-拉罗切有限公司 | 生产胰岛素样生长因子-ⅰ的方法 |
| CA2664108C (en) | 2006-09-21 | 2016-01-26 | Prometheus Laboratories Inc. | Antibody-based arrays for detecting 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 |
| 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 |
| US20080112961A1 (en) | 2006-10-09 | 2008-05-15 | Macrogenics, Inc. | Identification and Engineering of Antibodies with Variant Fc Regions and Methods of Using Same |
| AU2007328427A1 (en) | 2006-11-06 | 2008-06-12 | 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 |
| WO2008064884A1 (en) | 2006-11-28 | 2008-06-05 | U3 Pharma Gmbh | Activated her3 as a marker for predicting therapeutic efficacy |
| WO2008066498A1 (en) | 2006-12-01 | 2008-06-05 | Agency For Science, Technology And Research | Cancer-related protein kinases |
| WO2008140603A2 (en) | 2006-12-08 | 2008-11-20 | Macrogenics, Inc. | METHODS FOR THE TREATMENT OF DISEASE USING IMMUNOGLOBULINS HAVING FC REGIONS WITH ALTERED AFFINITIES FOR FCγR ACTIVATING AND FCγR INHIBITING |
| US8569464B2 (en) | 2006-12-21 | 2013-10-29 | Emd Millipore Corporation | Purification of proteins |
| WO2008079302A2 (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 |
| DE102007001370A1 (de) | 2007-01-09 | 2008-07-10 | Curevac Gmbh | RNA-kodierte Antikörper |
| WO2008088658A2 (en) | 2007-01-17 | 2008-07-24 | Immunomedics, Inc. | Polymeric carriers of therapeutic agents and recognition moieties for antibody-based targeting of disease sites |
| HRP20131113T1 (hr) | 2007-02-16 | 2014-01-17 | Merrimack Pharmaceuticals, Inc. | Protutijela protiv erbb3 i njihova uporaba |
| PL2132573T3 (pl) | 2007-03-02 | 2014-09-30 | Genentech Inc | Prognozowanie odpowiedzi na inhibitor dimeryzacji HER oparte na niskiej ekspresji HER3 |
| 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 |
| US8715665B2 (en) | 2007-04-13 | 2014-05-06 | The General Hospital Corporation | 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 |
| EP2082065B1 (en) | 2007-06-01 | 2014-03-12 | The Regents of the University of California | Multigene prognostic assay for lung cancer |
| EP2155786B1 (en) | 2007-06-06 | 2015-11-18 | F. Hoffmann-La Roche AG | Composition of a first non-labeled monoclonal antibody binding to a tumor antigen and a non-cross reactive second monoclonal antibody labeled with a nir fluorescence label |
| WO2009045579A2 (en) | 2007-06-14 | 2009-04-09 | The Regents Of The University Of California | Multimodal imaging probes for in vivo targeted and non-targeted imaging and therapeutics |
| US8501417B2 (en) | 2007-06-26 | 2013-08-06 | Vanderbilt University | Immunological compositions as cancer biomarkers and/or therapeutics |
| US20110038865A1 (en) | 2007-06-26 | 2011-02-17 | University Of Miami | Antibody- endostatin fusion protein and its variants |
| PL4365189T3 (pl) | 2007-07-09 | 2025-05-26 | F. Hoffmann-La Roche Ag | Zapobieganie redukcji wiązania disiarczkowego podczas rekombinacyjnego wytwarzania polipeptydów |
| ES2526211T3 (es) | 2007-07-13 | 2015-01-08 | Nestec S.A. | Selección de fármacos para la terapia del cáncer de pulmón utilizando matrices basadas en anticuerpos |
| 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 |
| CN103880965B (zh) | 2007-09-21 | 2018-02-16 | 加利福尼亚大学董事会 | 被导靶的干扰素显示强的细胞凋亡和抗肿瘤活性 |
| WO2009052830A1 (en) | 2007-10-22 | 2009-04-30 | Genmab A/S | Novel antibody therapies |
| JP5620106B2 (ja) | 2007-10-24 | 2014-11-05 | 株式会社糖鎖工学研究所 | 増強されたエフェクター機能を有するポリペプチド |
| EP2618146B1 (en) | 2008-02-25 | 2015-06-17 | Nestec S.A. | Drug selection for breast cancer therapy using antibody-based arrays |
| 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 |
| CN102057054B (zh) | 2008-04-11 | 2015-06-10 | 梅里麦克制药股份有限公司 | 人血清白蛋白接头以及其结合物 |
| JP5646457B2 (ja) | 2008-04-29 | 2014-12-24 | アッヴィ・インコーポレイテッド | 二重可変ドメイン免疫グロブリン及びその使用 |
| WO2009134870A1 (en) | 2008-04-30 | 2009-11-05 | Immunogen, Inc. | Potent cell-binding agent drug conjugates |
| MX2010011808A (es) | 2008-04-30 | 2011-03-04 | Immunogen Inc | Conjugados potentes y enlazadores hidrofilicos. |
| 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 |
| SG191679A1 (en) | 2008-06-16 | 2013-07-31 | 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. |
| JP2011529172A (ja) | 2008-07-25 | 2011-12-01 | メルク パテント ゲゼルシャフト ミット ベシュレンクテル ハフツング | モノクローナル抗体によるレセプター結合飽和を測定する方法 |
| 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 |
| CN102224255A (zh) | 2008-08-15 | 2011-10-19 | 梅里麦克制药股份有限公司 | 用于预测细胞对治疗剂的应答的方法和系统 |
| JP2012503656A (ja) | 2008-09-26 | 2012-02-09 | エウレカ セラピューティクス，インコーポレイテッド | 変異体グリコシル化パターンを有する細胞株およびタンパク質 |
| CN102271712B (zh) | 2008-10-31 | 2015-11-25 | 通用医疗公司 | 用于将物质递送至生物靶标的组合物和方法 |
| AU2009308707A1 (en) | 2008-10-31 | 2010-05-06 | Biogen Idec Ma Inc. | LIGHT targeting molecules and uses thereof |
| US8927694B2 (en) | 2008-11-18 | 2015-01-06 | Merrimack Pharmaceuticals, Inc. | Human serum albumin linkers and conjugates thereof |
| US20100169729A1 (en) | 2008-12-30 | 2010-07-01 | Datta Shamanna M | Enabling an integrated memory controller to transparently work with defective memory devices |
| EP2667194A3 (en) | 2009-01-14 | 2014-06-04 | The United States of America, as represented by The Secretary, Department of Health and Human Services | Ratio based biomarkers and methods of use thereof |
| EP2387717B1 (en) | 2009-01-15 | 2014-12-10 | Laboratory Corporation of America Holdings | Methods of determining patient response by measurement of her-2 expression |
| JP5746051B2 (ja) | 2009-01-15 | 2015-07-08 | ラボラトリー コーポレイション オブ アメリカ ホールディングス | Ｈｅｒ−３の測定による患者の反応を判定する方法 |
| PL3939617T3 (pl) | 2009-02-13 | 2025-03-17 | Immunomedics, Inc. | Związki pośrednie do wytwarzania koniugatów z wiązaniem rozszczepialnym wewnątrzkomórkowo |
| CN102326081B (zh) | 2009-02-24 | 2014-11-19 | 霍夫曼-拉罗奇有限公司 | s-ErbB-3作为癌症标志物的应用 |
| EP2400984A4 (en) | 2009-02-25 | 2013-01-23 | Merck Sharp & Dohme | HER2 ANTIBODY COMPOSITIONS |
| MA33198B1 (fr) | 2009-03-20 | 2012-04-02 | Genentech Inc | Anticorps anti-her di-spécifiques |
| AU2010242914B2 (en) | 2009-04-29 | 2014-11-13 | Trellis Bioscience, Llc | Improved antibodies immunoreactive with heregulin-coupled HER3 |
| EP2435071A1 (en) | 2009-05-29 | 2012-04-04 | F. Hoffmann-La Roche AG | Modulators for her2 signaling in her2 expressing patients with gastric cancer |
| CN102802661B (zh) | 2009-06-22 | 2016-01-13 | 米迪缪尼有限公司 | 用于位点特异性偶联的工程改造的Fc区 |
| EP2454598B1 (en) | 2009-07-15 | 2017-03-22 | DiaTech Holdings, Inc. | 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 |
| WO2011022727A2 (en) | 2009-08-21 | 2011-02-24 | Merrimack Pharmaceuticals, Inc. | Antibodies against the ectodomain of erbb3 and uses thereof |
| WO2011031840A1 (en) | 2009-09-09 | 2011-03-17 | Quintiles Transnational Corp. | Methods and compositions for the treatment of receptor tyrosine kinase mediated diseases or disorders |
| JP5898082B2 (ja) | 2009-10-07 | 2016-04-06 | マクロジェニクス，インコーポレーテッド | フコシル化程度の変更により改良されたエフェクター機能を示すＦｃ領域含有ポリペプチドおよびその使用法 |
| JP2013507378A (ja) | 2009-10-09 | 2013-03-04 | メルク・シャープ・エンド・ドーム・コーポレイション | 抗ｈｅｒ３抗体の製造、特徴づけ及びその用途 |
| CA2777242A1 (en) | 2009-10-14 | 2011-04-21 | Merrimack Pharmaceuticals, Inc. | Bispecific binding agents targeting igf-1r and erbb3 signalling and uses thereof |
| NO2719708T3 (enExample) | 2009-11-13 | 2018-03-24 | ||
| JP5981853B2 (ja) | 2010-02-18 | 2016-08-31 | ジェネンテック， インコーポレイテッド | ニューレグリンアンタゴニスト及び癌の治療におけるそれらの使用 |
| WO2011109625A1 (en) | 2010-03-03 | 2011-09-09 | Targeted Molecular Diagnostics, Llc | Methods for determining responsiveness to a drug based upon determination of ras mutation and/or ras amplification |
| NZ602084A (en) | 2010-03-11 | 2014-07-25 | Merrimack Pharmaceuticals Inc | Use of erbb3 inhibitors in the treatment of triple negative and basal-like breast cancers |
| ES2566602T3 (es) | 2010-04-09 | 2016-04-14 | Aveo Pharmaceuticals, Inc. | Anticuerpos anti-ErbB3 |
| WO2011139629A2 (en) | 2010-04-26 | 2011-11-10 | Biogen Idec Ma Inc. | Light targeting molecules and uses thereof |
| EP2569334A4 (en) | 2010-05-13 | 2014-01-22 | Fox Chase Cancer Ct | RECOMBINANT-PRODUCED ANTIBODIES FOR THE TARGETING OF ERBB SIGNALING MOLECULES AND METHOD FOR THEIR USE FOR DISEASE DIAGNOSIS AND TREATMENT |
| WO2011146568A1 (en) | 2010-05-19 | 2011-11-24 | Genentech, Inc. | Predicting response to a her inhibitor |
| AU2011254557B2 (en) | 2010-05-20 | 2015-09-03 | 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) |
| US8952132B2 (en) | 2011-02-07 | 2015-02-10 | Research Development Foundation | Engineered immunoglobulin FC polypeptides |
| AU2012226398B9 (en) | 2011-03-06 | 2017-04-13 | Merck Serono S.A. | Low fucose cell lines and uses thereof |
| WO2012125807A2 (en) | 2011-03-17 | 2012-09-20 | Cernostics, Inc. | Systems and compositions for diagnosing barrett's esophagus and methods of using the same |
-
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- 2011-09-02 CA CA2809443A patent/CA2809443A1/en not_active Abandoned
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- 2011-09-02 EP EP11822713.1A patent/EP2611829A4/en not_active Withdrawn
- 2011-09-02 SG SG2013013057A patent/SG187930A1/en unknown
- 2011-09-02 US US13/639,918 patent/US9085622B2/en active Active
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Cited By (1)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| CN117903311A (zh) * | 2024-03-20 | 2024-04-19 | 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 |
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| SG10201401681PA (en) | 2014-07-30 |
| SG187930A1 (en) | 2013-03-28 |
| MA34555B1 (fr) | 2013-09-02 |
| US9085622B2 (en) | 2015-07-21 |
| CN103189391A (zh) | 2013-07-03 |
| EP2611829A4 (en) | 2014-05-07 |
| PE20140133A1 (es) | 2014-02-09 |
| CR20130128A (es) | 2013-06-28 |
| CO6690769A2 (es) | 2013-06-17 |
| AU2011295726B2 (en) | 2014-11-06 |
| PH12013500353A1 (en) | 2013-03-25 |
| JP2013544492A (ja) | 2013-12-19 |
| TW201302793A (zh) | 2013-01-16 |
| NZ607680A (en) | 2015-02-27 |
| KR20130101047A (ko) | 2013-09-12 |
| US20130156779A1 (en) | 2013-06-20 |
| CL2013000566A1 (es) | 2014-01-24 |
| EP2611829A2 (en) | 2013-07-10 |
| EA201390328A1 (ru) | 2013-08-30 |
| UY33591A (es) | 2012-03-30 |
| BR112013005242A2 (pt) | 2016-06-28 |
| AU2011295726A1 (en) | 2013-03-21 |
| MX2013002535A (es) | 2013-06-03 |
| WO2012031198A2 (en) | 2012-03-08 |
| WO2012031198A3 (en) | 2012-05-18 |
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