CA2749846C - Methods of determining patient response by measurement of her-3 - Google Patents
Methods of determining patient response by measurement of her-3 Download PDFInfo
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| JP6402173B2 (ja) | 2013-04-05 | 2018-10-10 | 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 | Her3の検出に基づく癌の診断、予後予測、および処置を容易にするためのシステムおよび方法 |
| 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 |
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| EP0484027B1 (en) | 1990-11-02 | 1996-12-18 | Zeneca Limited | Polysubstituted phthalocyanines |
| US5578498A (en) | 1991-05-22 | 1996-11-26 | Behringwerke Ag | Metal chelate containing compositions for use in chemiluminescent assays |
| US6251581B1 (en) | 1991-05-22 | 2001-06-26 | Dade Behring Marburg Gmbh | Assay method utilizing induced luminescence |
| US5340716A (en) | 1991-06-20 | 1994-08-23 | Snytex (U.S.A.) Inc. | Assay method utilizing photoactivated chemiluminescent label |
| US5565552A (en) | 1992-01-21 | 1996-10-15 | Pharmacyclics, Inc. | Method of expanded porphyrin-oligonucleotide conjugate synthesis |
| US5622929A (en) | 1992-01-23 | 1997-04-22 | Bristol-Myers Squibb Company | Thioether conjugates |
| EP1997894B1 (en) | 1992-02-06 | 2011-03-30 | Novartis Vaccines and Diagnostics, Inc. | Biosynthetic binding protein for cancer marker |
| ATE162892T1 (de) | 1992-07-31 | 1998-02-15 | Behringwerke Ag | Photoaktivierbare chemiluminizierende matrices |
| US5565324A (en) | 1992-10-01 | 1996-10-15 | The Trustees Of Columbia University In The City Of New York | Complex combinatorial chemical libraries encoded with tags |
| GB2301366B (en) | 1994-03-29 | 1998-07-29 | Celltech Therapeutics Ltd | Antibodies against E-selectin |
| US5986076A (en) | 1994-05-11 | 1999-11-16 | Trustees Of Boston University | Photocleavable agents and conjugates for the detection and isolation of biomolecules |
| US5968511A (en) | 1996-03-27 | 1999-10-19 | Genentech, Inc. | ErbB3 antibodies |
| SE9601676D0 (sv) | 1996-04-30 | 1996-04-30 | Ulf Landegren | Improved probing of specific mucleic acids |
| US5945526A (en) | 1996-05-03 | 1999-08-31 | Perkin-Elmer Corporation | Energy transfer dyes with enhanced fluorescence |
| US5763602A (en) | 1996-10-01 | 1998-06-09 | Li; Ying-Syi | Methods of syntheses of phthalocyanine compounds |
| US7371376B1 (en) | 1996-10-18 | 2008-05-13 | Genentech, Inc. | Anti-ErbB2 antibodies |
| ZA9811162B (en) | 1997-12-12 | 2000-06-07 | Genentech Inc | Treatment with anti-ERBB2 antibodies. |
| US6175752B1 (en) | 1998-04-30 | 2001-01-16 | Therasense, Inc. | Analyte monitoring device and methods of use |
| US6541214B1 (en) | 1998-11-13 | 2003-04-01 | Oregon Heath Science University | N-terminally truncated HER-2/neu protein as a cancer prognostic indicator |
| US6001673A (en) | 1999-02-11 | 1999-12-14 | Ericsson Inc. | Methods for packaging integrated circuit devices including cavities adjacent active regions |
| US6322980B1 (en) | 1999-04-30 | 2001-11-27 | Aclara Biosciences, Inc. | Single nucleotide detection using degradation of a fluorescent sequence |
| US6514700B1 (en) * | 1999-04-30 | 2003-02-04 | Aclara Biosciences, Inc. | Nucleic acid detection using degradation of a tagged sequence |
| US20040248150A1 (en) | 1999-04-02 | 2004-12-09 | Sharat Singh | Methods employing oligonucleotide-binding e-tag probes |
| US6627400B1 (en) * | 1999-04-30 | 2003-09-30 | Aclara Biosciences, Inc. | Multiplexed measurement of membrane protein populations |
| US6682887B1 (en) * | 1999-04-30 | 2004-01-27 | Aclara Biosciences, Inc. | Detection using degradation of a tagged sequence |
| US7037654B2 (en) * | 1999-04-30 | 2006-05-02 | Aclara Biosciences, Inc. | Methods and compositions for enhancing detection in determinations employing cleavable electrophoretic tag reagents |
| US6673550B2 (en) * | 1999-04-30 | 2004-01-06 | Aclara Biosciences, Inc. | Electrophoretic tag reagents comprising fluorescent compounds |
| US7001725B2 (en) * | 1999-04-30 | 2006-02-21 | Aclara Biosciences, Inc. | Kits employing generalized target-binding e-tag probes |
| US6649351B2 (en) * | 1999-04-30 | 2003-11-18 | Aclara Biosciences, Inc. | Methods for detecting a plurality of analytes by mass spectrometry |
| US20030235832A1 (en) | 2000-06-21 | 2003-12-25 | Ahmed Chenna | Multiplexed analysis by chromatographic separation of molecular tags |
| US20030092012A1 (en) | 2001-11-09 | 2003-05-15 | Ahmed Chenna | Methods for detecting a plurality of analytes by chromatography |
| SI1187632T1 (sl) | 1999-05-14 | 2009-04-30 | Genentech Inc | Zdravljenje z anti-ErbB2 protitelesi |
| DE60042693D1 (de) | 1999-08-27 | 2009-09-17 | Genentech Inc | Dosierung für die behandlung mit anti erbb2-antikörpern |
| MXPA02006778A (es) * | 2000-01-12 | 2004-04-05 | Ventana Inc | Metodo para determinar la respuesta a una terapia de cancer. |
| US7306904B2 (en) | 2000-02-18 | 2007-12-11 | Olink Ab | Methods and kits for proximity probing |
| US6743911B2 (en) | 2000-03-14 | 2004-06-01 | Shell Oil Company | Process for the carbonylation of pentenenitrile |
| GB0007911D0 (en) * | 2000-03-30 | 2000-05-17 | Novartis Ag | Organic compounds |
| US20030207300A1 (en) | 2000-04-28 | 2003-11-06 | Matray Tracy J. | Multiplex analytical platform using molecular tags |
| US7160735B2 (en) | 2000-04-28 | 2007-01-09 | Monogram Biosciences, Inc. | Tagged microparticle compositions and methods |
| US7537938B2 (en) | 2000-04-28 | 2009-05-26 | Monogram Biosciences, Inc. | Biomarker detection in circulating cells |
| US20040067498A1 (en) | 2000-04-28 | 2004-04-08 | Ahmed Chenna | Detection of nucleic acid sequences by cleavage and separation of tag-containing structures |
| US20030170734A1 (en) | 2000-04-28 | 2003-09-11 | Stephen Williams | Multiplexed assays using electrophoretically separated molecular tags |
| US7771929B2 (en) | 2000-04-28 | 2010-08-10 | Monogram Biosciences, Inc. | Tag library compounds, compositions, kits and methods of use |
| JP4796259B2 (ja) | 2000-05-04 | 2011-10-19 | シーメンス・ヘルスケア・ダイアグノスティックス・プロダクツ・ゲーエムベーハー | 複数のアナライトの検出において使用するための組成物 |
| US6547654B2 (en) | 2000-07-22 | 2003-04-15 | Americo Del Raso | Automatic abrasive sleeve tightening means and quick release system for an oscillating spindle sander |
| AU7922201A (en) * | 2000-08-08 | 2002-02-18 | Aclara Biosciences Inc | Multiplexed enzymatic assays |
| AU2001280222A1 (en) | 2000-08-19 | 2002-03-04 | Sung-Cheol Kim | Communication line separator |
| ES2394293T3 (es) | 2001-02-28 | 2013-01-30 | Bio Life Science Forschungs- Und Entwicklungsges.M.B.H. | Vacuna contra cánceres que están asociados con el oncogén HER-2/neu |
| US7183388B2 (en) | 2001-03-30 | 2007-02-27 | The Regents Of The University Of California | Anti-MUC-1 single chain antibodies for tumor targeting |
| WO2002094998A2 (en) | 2001-05-21 | 2002-11-28 | Aclara Biosciences, Inc. | Analyzing phosphorylated proteins |
| KR20040082273A (ko) | 2001-05-21 | 2004-09-24 | 아클라라 바이오사이언시스 인코퍼레이티드 | 단백질 분석을 위한 방법 및 조성물 |
| AU2002344221A1 (en) | 2001-05-26 | 2002-12-09 | Aclara Biosciences, Inc. | Catalytic amplification of multiplexed assay signals |
| AU2002316577A1 (en) | 2001-07-09 | 2003-01-29 | Aclara Biosciences, Inc. | Cell-screening assay and composition |
| WO2003055439A2 (en) | 2001-07-18 | 2003-07-10 | The Regents Of The University Of California | Her2/neu target antigen and use of same to stimulate an immune response |
| US20040241688A1 (en) | 2001-07-19 | 2004-12-02 | Cuneyt Bukusoglu | Human tissue specific drug screening procedure |
| GB2378245A (en) | 2001-08-03 | 2003-02-05 | Mats Nilsson | Nucleic acid amplification method |
| EP1414496B1 (en) | 2001-08-07 | 2010-10-20 | Galephar M/F | Pharmaceutical composition containing a combinaition of ppar-alpha, pravastatin and polyglycolized glyceride |
| EP1283053A1 (en) | 2001-08-09 | 2003-02-12 | Max-Planck-Gesellschaft zur Förderung der Wissenschaften e.V. | Inhibitors of HER3 activity |
| EP1434535A1 (en) | 2001-10-12 | 2004-07-07 | Gyne Ideas Limited | Biomaterial comprising microfeatures |
| WO2003033741A1 (en) | 2001-10-16 | 2003-04-24 | Aclara Biosciences, Inc. | Universal e-tag primer and probe compositions and methods |
| US7045311B2 (en) * | 2001-10-25 | 2006-05-16 | Monogram Biosciences, Inc. | Whole cell assay systems for cell surface proteases |
| WO2003042658A2 (en) | 2001-11-09 | 2003-05-22 | Aclara Biosciences, Inc. | Methods and compositions for enhancing detection in determinations employing cleavable electrophoretic tag reagents |
| WO2003042699A1 (en) | 2001-11-09 | 2003-05-22 | Aclara Biosciences Inc. | Tagged microparticle compositions and methods |
| CA2465588A1 (en) | 2001-11-09 | 2003-05-22 | Aclara Biosciences, Inc. | Detection of nucleic acid sequences by cleavage and separation of tag-containing structures |
| AU2002357309A1 (en) | 2001-12-18 | 2003-06-30 | Aclara Biosciences, Inc. | Photoactivation device and method |
| US7135174B2 (en) | 2002-01-07 | 2006-11-14 | Amgen Fremont, Inc. | Antibodies directed to PDGFD and uses thereof |
| EP1478667B1 (en) * | 2002-02-26 | 2010-09-08 | SIGMA-TAU Industrie Farmaceutiche Riunite S.p.A. | Anti-human tenascin monoclonal antibody |
| JP2006509183A (ja) * | 2002-03-05 | 2006-03-16 | アクララ バイオサイエンシーズ, インコーポレイテッド | 膜結合増感剤を用いる多重分析 |
| DK2261369T3 (da) | 2002-03-13 | 2014-07-28 | Genomic Health Inc | Genekspressionsprofilering i biopsier af tumorvæv |
| EP1490533A4 (en) | 2002-04-02 | 2007-07-04 | Aclara Biosciences Inc | MULTIPLEXASSAYS USING ELECTROPHORETICALLY SEPARATED MOLECULAR MARKERS |
| US20040248151A1 (en) | 2002-04-05 | 2004-12-09 | Ventana Medical Systems, Inc. | Method for predicting the response to HER2-directed therapy |
| 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 |
| US20040229293A1 (en) | 2002-05-21 | 2004-11-18 | Po-Ying Chan-Hui | Surface receptor complexes as biomarkers |
| US7402397B2 (en) | 2002-05-21 | 2008-07-22 | Monogram Biosciences, Inc. | Detecting and profiling molecular complexes |
| US20040229380A1 (en) | 2002-05-21 | 2004-11-18 | Po-Ying Chan-Hui | ErbB heterodimers as biomarkers |
| US20090111127A1 (en) | 2002-05-21 | 2009-04-30 | Monogram Biosciences Inc. | Surface Receptor Complexes as Biomarkers |
| US20040229294A1 (en) | 2002-05-21 | 2004-11-18 | Po-Ying Chan-Hui | ErbB surface receptor complexes as biomarkers |
| US20040229299A1 (en) | 2002-05-21 | 2004-11-18 | Badal M. Youssouf | Intracellular complexes as biomarkers |
| US20040175765A1 (en) | 2002-07-05 | 2004-09-09 | Sharat Singh | Cell-screening assay and composition |
| ATE535254T1 (de) * | 2002-07-15 | 2011-12-15 | Genentech Inc | Behandlung von krebs mit dem anti-erbb2- antikörper rhumab 2c4 |
| ES2332310T3 (es) | 2002-07-25 | 2010-02-02 | Aclara Biosciences, Inc. | Deteccion de oligomerizacion de receptor. |
| CA2493671A1 (en) | 2002-07-26 | 2004-02-05 | Aclara Biosciences, Inc. | Lipophilic electrophoretic probes |
| US20040091850A1 (en) | 2002-11-08 | 2004-05-13 | Travis Boone | Single cell analysis of membrane molecules |
| WO2004061446A1 (en) | 2002-12-18 | 2004-07-22 | Aclara Biosciences, Inc. | Single cell analysis of membrane molecules |
| EP1599492A4 (en) | 2003-01-17 | 2008-09-24 | Virologic Inc | RECIPIENTS DORPHANIZATION BY USING MARKED MOLECULAR LIBRARIES |
| BRPI0408950A (pt) | 2003-04-01 | 2006-03-28 | Monogram Biosciences Inc | método para determinar a situação de doença de um paciente, e, método para selecionar um paciente para tratamento de um cáncer com um ou mais medicamentos de ação dimérica |
| US20100291594A1 (en) | 2003-07-17 | 2010-11-18 | Laboratory Corporation Of America Holdings | ErbB Surface Receptor Complexes as Biomarkers |
| US7402398B2 (en) | 2003-07-17 | 2008-07-22 | Monogram Biosciences, Inc. | Measuring receptor homodimerization |
| EP1653986A4 (en) | 2003-08-01 | 2007-03-14 | Smithkline Beecham Corp | TREATMENT OF CANCERS EXPRESSING P95 SP ERBB2 / SP |
| EP1673399B1 (en) | 2003-08-11 | 2017-04-05 | Monogram BioSciences, Inc. | Detecting and profiling molecular complexes |
| WO2005017493A2 (en) | 2003-08-15 | 2005-02-24 | Smithkline Beecham Corporation | Biomarkers in cancer |
| US20050106571A1 (en) | 2003-10-02 | 2005-05-19 | The Regents Of The University Of California | Mammalian T1R3 sweet taste receptors |
| EP1681983A4 (en) | 2003-10-14 | 2008-12-10 | Monogram Biosciences Inc | RECEPTOR TYROSINE KINASE SIGNAL PATH ANALYSIS FOR DIAGNOSIS AND THERAPY |
| CA2543830A1 (en) | 2003-10-27 | 2005-05-19 | Monogram Biosciences, Inc. | Detecting human anti-therapeutic antibodies |
| PT1674111E (pt) * | 2004-07-09 | 2010-12-15 | Chugai Pharmaceutical Co Ltd | Anticorpo anti-glipicano 3 |
| US20080254497A1 (en) | 2004-10-15 | 2008-10-16 | Monogram Biosciences, Inc. | Response Predictors for Erbb Pathway-Specific Drugs |
| KR20070105967A (ko) | 2004-11-03 | 2007-10-31 | 아이리스 몰레큘라 다이아그노스틱스, 인코오포레이티드 | 균질 분석물 탐지 |
| US7939267B2 (en) | 2004-11-04 | 2011-05-10 | Laboratory Corporation Of America Holdings | Detection of activation of endothelial cells as surrogate marker for angiogenesis |
| US7862995B2 (en) * | 2004-12-10 | 2011-01-04 | Targeted Molecular Diagnostics | Methods and materials for predicting responsiveness to treatment with dual tyrosine kinase inhibitor |
| WO2006068640A1 (en) * | 2004-12-21 | 2006-06-29 | Cell Signaling Technology, Inc. | Protein phosphorylation in egfr-signaling pathways |
| WO2006084018A2 (en) | 2005-02-02 | 2006-08-10 | Monogram Biosciences, Inc. | Methods for determining responsiveness to cancer therapy |
| EP1846558A2 (en) * | 2005-02-09 | 2007-10-24 | Genentech, Inc. | Inhibiting her2 shedding with matrix metalloprotease antagonists |
| US20060212956A1 (en) | 2005-03-14 | 2006-09-21 | Genentech, Inc. | Animal model of ligand activated HER2 expressing tumors |
| JP2006316040A (ja) | 2005-05-13 | 2006-11-24 | Genentech Inc | Herceptin(登録商標)補助療法 |
| WO2006133460A2 (en) * | 2005-06-09 | 2006-12-14 | Yale University | Methods for diagnosing and treating breast cancer based on a her/er ratio |
| US7700299B2 (en) | 2005-08-12 | 2010-04-20 | Hoffmann-La Roche Inc. | Method for predicting the response to a treatment |
| CN1928563B (zh) | 2005-09-09 | 2010-04-28 | 上海张江生物技术有限公司 | 乳腺癌的免疫组化诊断试剂盒和测试片 |
| WO2007041502A2 (en) * | 2005-09-30 | 2007-04-12 | Monogram Biosciences | Methods for determining responsiveness to cancer therapy |
| EP2049568A2 (en) | 2006-04-07 | 2009-04-22 | Københavns Universitet | Erbb receptor-derived peptide fragments |
| EP1997832A1 (en) * | 2007-05-29 | 2008-12-03 | Ganymed Pharmaceuticals AG | Monoclonal antibodies against Claudin-18 for treatment of cancer |
| JP5117165B2 (ja) | 2007-11-09 | 2013-01-09 | 花王株式会社 | 水中油型乳化組成物の製造方法 |
| CA2706763C (en) | 2007-11-27 | 2013-07-30 | Laboratory Corporation Of America Holdings | Enhanced method for detecting and/or quantifying an analyte in a sample |
| CN101230390A (zh) | 2007-12-07 | 2008-07-30 | 湖北大学 | 一种用于妇科恶性肿瘤早期筛选的基因芯片及其检测方法 |
| EP2235536A4 (en) | 2007-12-20 | 2011-05-04 | Lab Corp America Holdings | HER-2-DIAGNOSTIC PROCEDURE |
| ES2342646B1 (es) | 2008-06-02 | 2011-04-26 | Institut De Recerca Hospital Universitari Vall Hebron | Metodo de diagnostico de canceres que expresan el receptor her-2 o sus variantes truncadas. |
| EP2337795A2 (en) | 2008-10-01 | 2011-06-29 | Dako Denmark A/S | Mhc multimers in cancer vaccines and immune monitoring |
| ES2637411T3 (es) | 2008-12-01 | 2017-10-13 | Laboratory Corporation Of America Holdings | Métodos y ensayos para medir p95 Y/O p95 en una muestra y anticuerpos específicos para p95 |
| JP2012515353A (ja) | 2009-01-15 | 2012-07-05 | 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−2発現の測定による患者の反応を判定する方法 |
| 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 |
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| IL214072A (en) | 2016-08-31 |
| US20100210034A1 (en) | 2010-08-19 |
| AU2010204583A2 (en) | 2011-09-01 |
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| ES2535723T3 (es) | 2015-05-14 |
| SG172983A1 (en) | 2011-08-29 |
| US9766242B2 (en) | 2017-09-19 |
| KR20110120891A (ko) | 2011-11-04 |
| US20160061839A1 (en) | 2016-03-03 |
| BRPI1007321A2 (pt) | 2018-07-10 |
| EP2387711A4 (en) | 2012-07-18 |
| EP2387711A1 (en) | 2011-11-23 |
| JP5746051B2 (ja) | 2015-07-08 |
| CN102460152A (zh) | 2012-05-16 |
| CA2749846A1 (en) | 2010-07-22 |
| US20130071859A1 (en) | 2013-03-21 |
| US10775382B2 (en) | 2020-09-15 |
| US20180164319A1 (en) | 2018-06-14 |
| SG10201408392PA (en) | 2015-01-29 |
| JP2012515226A (ja) | 2012-07-05 |
| WO2010083470A1 (en) | 2010-07-22 |
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