ES2734886T3 - Anticuerpos anti-clusterina y fragmentos de unión a antígeno y su uso para reducir el volumen tumoral - Google Patents
Anticuerpos anti-clusterina y fragmentos de unión a antígeno y su uso para reducir el volumen tumoral Download PDFInfo
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- ES2734886T3 ES2734886T3 ES10832474T ES10832474T ES2734886T3 ES 2734886 T3 ES2734886 T3 ES 2734886T3 ES 10832474 T ES10832474 T ES 10832474T ES 10832474 T ES10832474 T ES 10832474T ES 2734886 T3 ES2734886 T3 ES 2734886T3
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Landscapes
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| PCT/CA2010/001882 WO2011063523A1 (en) | 2009-11-24 | 2010-11-24 | Anti-clusterin antibodies and antigen binding fragments and their use to reduce tumor volume |
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| ES2543341T3 (es) | 2005-09-13 | 2015-08-18 | National Research Council Of Canada | Métodos y composiciones para modular la actividad de células tumorales |
| RU2627163C2 (ru) | 2009-11-24 | 2017-08-03 | Алетиа Байотерапьютикс Инк. | Антикластериновые антитела и антигенсвязывающие фрагменты и их использование для уменьшения объема новообразований |
| MX2014010164A (es) * | 2012-02-22 | 2014-11-25 | Alethia Biotherapeutics Inc | Co-uso de un inhibidor de clusterina con un inhibidor de egfr para tratar cancer. |
| WO2014159775A1 (en) * | 2013-03-14 | 2014-10-02 | Teva Pharmaceutical Industries Ltd. | Anti-clusterin monotherapy for cancer treatment |
| CN104267187A (zh) * | 2014-10-15 | 2015-01-07 | 吉林大学 | 检测尿液Clusterin含量试纸条的制备及应用 |
| CN105988004B (zh) * | 2015-01-30 | 2017-12-29 | 江苏众红生物工程创药研究院有限公司 | 人组织激肽释放酶1胶体金定量检测试纸卡 |
| AU2018246873B2 (en) | 2017-03-31 | 2021-05-06 | Merus N.V. | ErbB-2 and ErbB3 binding bispecific antibodies for use in the treatment f cells that have an NRG1 fusion gene |
| US11597764B2 (en) | 2017-06-15 | 2023-03-07 | Memorial Sloan Kettering Cancer Center | Anti-L1-CAM antibodies and uses thereof |
| CN107353341B (zh) * | 2017-08-17 | 2020-03-27 | 联合益康（北京）生物科技有限公司 | 一种抗clu抗体及应用、制备方法和试剂盒 |
| WO2020018364A1 (en) * | 2018-07-16 | 2020-01-23 | University Of Hawaii | Anti-galectin-9 antibody and methods of use thereof |
| CN111808194B (zh) * | 2020-07-13 | 2021-04-20 | 北京凯因科技股份有限公司 | 一种结合密蛋白的用于治疗癌症的人源化抗体 |
| KR20240014052A (ko) * | 2021-04-27 | 2024-01-31 | 알레시아 바이오쎄라퓨틱스 인코포레이티드 | 면역 세포의 종양내 침윤을 허용하는 방법 |
| KR20240013125A (ko) * | 2021-04-27 | 2024-01-30 | 알레시아 바이오쎄라퓨틱스 인코포레이티드 | 종양 침윤성 림프구 요법 |
| WO2025129072A1 (en) * | 2023-12-13 | 2025-06-19 | Corbus Pharmaceuticals, Inc. | Anti-alpha-v-beta-8 integrin antibodies and uses thereof |
| WO2025147775A1 (en) * | 2024-01-10 | 2025-07-17 | Alethia Biotherapeutics Inc. | Combination therapy for neoadjuvant treatment of cancer |
Family Cites Families (96)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| DE3933850A1 (de) | 1989-10-06 | 1991-04-18 | Schering Ag | Zytolyse-inhibitor (zli), eine diese blutplasmaprotein kodierende dna-sequenz, sowie ein plasmid, ein wirtsorganismus und ein verfahren zur gewinnung dieses proteins |
| EP0614984B2 (en) | 1993-03-05 | 2010-11-03 | Bayer HealthCare LLC | Anti-TNF alpha human monoclonal antibodies |
| US5595756A (en) | 1993-12-22 | 1997-01-21 | Inex Pharmaceuticals Corporation | Liposomal compositions for enhanced retention of bioactive agents |
| US6383808B1 (en) | 2000-09-11 | 2002-05-07 | Isis Pharmaceuticals, Inc. | Antisense inhibition of clusterin expression |
| AU9312598A (en) | 1997-09-10 | 1999-03-29 | Allegheny University Of The Health Sciences | Inhibitors of collagen assembly |
| US6818749B1 (en) * | 1998-10-31 | 2004-11-16 | The United States Of America As Represented By The Department Of Health And Human Services | Variants of humanized anti carcinoma monoclonal antibody cc49 |
| WO2000034469A1 (en) | 1998-12-11 | 2000-06-15 | The Research Foundation Of State University Of New York At Albany | Compositions and methods for altering cell migration |
| DK1163254T3 (da) | 1999-02-26 | 2008-06-09 | Univ British Columbia | TRPM-2 antisense-behandling |
| US6900187B2 (en) | 1999-02-26 | 2005-05-31 | The University Of British Columbia | TRPM-2 antisense therapy using an oligonucleotide having 2′-O-(2-methoxy)ethyl modifications |
| CN1308347C (zh) | 1999-04-28 | 2007-04-04 | 德克萨斯大学董事会 | 用于通过选择性抑制vegf来治疗癌症的组合物和方法 |
| US6949245B1 (en) | 1999-06-25 | 2005-09-27 | Genentech, Inc. | Humanized anti-ErbB2 antibodies and treatment with anti-ErbB2 antibodies |
| US7291714B1 (en) | 1999-06-30 | 2007-11-06 | Millennium Pharmaceuticals, Inc. | Glycoprotein VI and uses thereof |
| US20050208558A1 (en) | 1999-10-19 | 2005-09-22 | Applera Corporation | Detection kits, such as nucleic acid arrays, for detecting the expression or 10,000 or more Drosophila genes and uses thereof |
| US7569551B2 (en) | 2000-02-25 | 2009-08-04 | The University Of British Columbia | Chemo- and radiation-sensitization of cancer by antisense TRPM-2 oligodeoxynucleotides |
| AU2001245280A1 (en) | 2000-03-07 | 2001-09-17 | Hyseq, Inc. | Novel nucleic acids and polypeptides |
| WO2001075177A2 (en) | 2000-04-03 | 2001-10-11 | The Government Of The United States Of America, As Represented By The Secretary, Department Of Health And Human Services | Tumor markers in ovarian cancer |
| US6812339B1 (en) | 2000-09-08 | 2004-11-02 | Applera Corporation | Polymorphisms in known genes associated with human disease, methods of detection and uses thereof |
| US7754208B2 (en) | 2001-01-17 | 2010-07-13 | Trubion Pharmaceuticals, Inc. | Binding domain-immunoglobulin fusion proteins |
| US20030133939A1 (en) | 2001-01-17 | 2003-07-17 | Genecraft, Inc. | Binding domain-immunoglobulin fusion proteins |
| EP1358326A2 (en) | 2001-02-09 | 2003-11-05 | Incyte Genomics, Inc. | Proteins associated with cell growth, differentiation, and death |
| CA2443644A1 (en) | 2001-04-04 | 2003-01-16 | Elan Corporation, Plc | Genetic analysis of peyers's patches and m cells and methods and compositions targeting peyer's patches and m cell receptors |
| MXPA03011365A (es) | 2001-06-13 | 2005-03-07 | Genmab As | Anticuerpos monoclonales humanos para el receptor de factor de crecimiento epidermico (egfr). |
| CN1671416B (zh) * | 2001-07-12 | 2013-01-02 | 杰斐逊·富特 | 超人源化抗体 |
| US20030134301A1 (en) | 2001-07-27 | 2003-07-17 | Brooksbank Robert Alan | Identification and use of molecules implicated in pain |
| US20070015145A1 (en) | 2001-08-14 | 2007-01-18 | Clifford Woolf | Nucleic acid and amino acid sequences involved in pain |
| US20040142325A1 (en) | 2001-09-14 | 2004-07-22 | Liat Mintz | Methods and systems for annotating biomolecular sequences |
| US20070082337A1 (en) | 2004-01-27 | 2007-04-12 | Compugen Ltd. | Methods of identifying putative gene products by interspecies sequence comparison and biomolecular sequences uncovered thereby |
| EP1504099A4 (en) | 2001-12-10 | 2006-05-10 | Nuvelo Inc | NEW NUCLEIC ACIDS AND POLYPEPTIDES |
| KR101265180B1 (ko) | 2002-01-17 | 2013-05-29 | 더 유니버시티 오브 브리티쉬 콜롬비아 | 아이지에프비피-2 및 아이지에프비피-5를 억제하는 양특이성 안티센스 올리고뉴클레오티드, 이를 이용하여 약학적 조성물을 제조하는 방법 및 그 약학적 조성물 |
| EP1487857A4 (en) | 2002-03-07 | 2006-08-09 | Ludwig Inst Cancer Res | GENES OF ENDOTHELIAL CELLS OF LYMPHIA AND BLOOD |
| CA2492671C (en) | 2002-03-22 | 2012-04-17 | Aprogen, Inc. | Humanized antibody and process for preparing same |
| AU2003281287A1 (en) | 2002-07-04 | 2004-01-23 | Oxford Glycosciences (Uk) Ltd | Toxicity markers |
| US7285541B2 (en) | 2002-08-21 | 2007-10-23 | The University Of British Columbia | Treatment of melanoma by reduction in clusterin levels |
| KR101212512B1 (ko) | 2002-08-21 | 2012-12-26 | 더 유니버시티 오브 브리티쉬 콜롬비아 | 암-관련 단백질을 표적으로 하는 알엔에이아이 프로브 |
| EP1585482A4 (en) | 2002-09-25 | 2009-09-09 | Genentech Inc | NEW COMPOSITIONS AND METHODS FOR TREATING PSORIASIS |
| US20050048490A1 (en) | 2002-09-26 | 2005-03-03 | Incyte Corp. | Proteins associated with cell growth, differentiation, and death |
| WO2004030615A2 (en) | 2002-10-02 | 2004-04-15 | Genentech, Inc. | Compositions and methods for the diagnosis and treatment of tumor |
| US8722872B2 (en) | 2002-10-02 | 2014-05-13 | The University Of British Columbia | Compositions and methods for treatment of prostate and other cancers |
| DE10256900A1 (de) | 2002-11-29 | 2004-06-24 | Nemod Immuntherapie Ag | Tumorspezifische Erkennungsmoleküle |
| WO2004066941A2 (en) | 2003-01-24 | 2004-08-12 | Bayer Pharmaceuticals Corporation | Expression profiles for colon cancer and methods of use |
| WO2005049806A2 (en) | 2003-03-14 | 2005-06-02 | Nuvelo, Inc. | Novel nucleic acids and polypeptides |
| EP1610810A2 (en) | 2003-03-28 | 2006-01-04 | Applied Research Systems ARS Holding N.V. | Use of clusterin for the treatment and/or prevention of peripheral neurological diseases |
| US20050255114A1 (en) | 2003-04-07 | 2005-11-17 | Nuvelo, Inc. | Methods and diagnosis for the treatment of preeclampsia |
| JP2007523839A (ja) | 2003-04-18 | 2007-08-23 | ザ・ユニバーシティ・オブ・ブリティッシュ・コロンビア | 血管新生性障害の治療法 |
| US20040220131A1 (en) | 2003-04-18 | 2004-11-04 | The University Of British Columbia | Method for treatment of cancerous angiogenic disorders |
| WO2005014849A2 (en) | 2003-07-03 | 2005-02-17 | Euro-Celtique, S.A. | Genes associated with responses to neuropathic pain |
| AU2004262369A1 (en) | 2003-07-29 | 2005-02-10 | Bristol-Myers Squibb Company | Biomarkers of cyclin-dependent kinase modulation |
| WO2005019258A2 (en) | 2003-08-11 | 2005-03-03 | Genentech, Inc. | Compositions and methods for the treatment of immune related diseases |
| AU2004272607B2 (en) | 2003-09-11 | 2008-11-06 | Cornerstone Therapeutics Inc. | Monoclonal antibodies against HMGB1 |
| EP1708961B1 (en) | 2003-12-04 | 2011-03-09 | Abbott Biotherapeutics Corp. | Anti-ip-10 antibodies |
| AT412785B (de) | 2003-12-04 | 2005-07-25 | Kungl Andreas J Dr | Gag-bindungsproteine |
| GB0329254D0 (en) | 2003-12-17 | 2004-01-21 | Univ Manchester | Treatment of viral infections |
| GB0329958D0 (en) | 2003-12-24 | 2004-01-28 | Univ Manchester | Treatment of viral infections |
| US7309487B2 (en) | 2004-02-09 | 2007-12-18 | George Inana | Methods and compositions for detecting and treating retinal diseases |
| ITRM20040098A1 (it) | 2004-02-25 | 2004-05-25 | Univ Roma | Anticorpi oligoclonali anticlasterina per la diagnosi di neoplasie e la predizione del loro grado di malignita', metodo diagnostico e kit relativi. |
| WO2005094899A1 (en) | 2004-04-02 | 2005-10-13 | The University Of British Columbia | Clusterin antisense therapy for treatment of cancer |
| MX2007000383A (es) | 2004-07-09 | 2007-03-12 | Tripath Imaging Inc | Metodos y composiciones para la deteccion de enfermedad ovarica. |
| GB0421639D0 (en) | 2004-09-29 | 2004-10-27 | Proteome Sciences Plc | Methods and compositions relating to alzheimer's disease |
| AU2005291486A1 (en) * | 2004-10-01 | 2006-04-13 | Max-Planck-Gesellschaft Zur Forderung Der Wissenschaften E.V. | Novel antibodies directed to the mammalian EAG1 ion channel protein |
| CA2584646C (en) | 2004-11-23 | 2015-11-03 | The University Of British Columbia | Treatment of cancer with a combination of an agent that perturbs the egf signaling pathway and an oligonucleotide that reduces clusterin levels |
| DE602006011574D1 (de) | 2005-01-27 | 2010-02-25 | Five Prime Therapeutics Inc | Leitsequenzen zur anleitung von polypeptidsekretion und verfahren zur herstellung |
| US7883858B2 (en) | 2005-01-27 | 2011-02-08 | Institute For Systems Biology | Methods for identifying and monitoring drug side effects |
| WO2006089586A1 (en) | 2005-02-23 | 2006-08-31 | Medizinische Universität Graz | Use of a compound with clusterin activity for the treatment of diseases associated with the deposition of abnormal proteins |
| CN101171263A (zh) | 2005-03-04 | 2008-04-30 | 比奥根艾迪克Ma公司 | 通过合理修饰互补决定区残基使免疫球蛋白可变区人源化的方法 |
| US20080307537A1 (en) | 2005-03-31 | 2008-12-11 | Dana-Farber Cancer Institute, Inc. | Compositions and Methods for the Identification, Assessment, Prevention, and Therapy of Neurological Diseases, Disorders and Conditions |
| WO2006113678A2 (en) | 2005-04-15 | 2006-10-26 | Oncomethylome Sciences, Inc. | Methylation markers for diagnosis and treatment of cancers |
| WO2007022248A2 (en) | 2005-08-16 | 2007-02-22 | Sloan Kettering Institute For Cancer Research | Methods of detection of cancer using peptide profiles |
| US7612181B2 (en) | 2005-08-19 | 2009-11-03 | Abbott Laboratories | Dual variable domain immunoglobulin and uses thereof |
| ES2543341T3 (es) | 2005-09-13 | 2015-08-18 | National Research Council Of Canada | Métodos y composiciones para modular la actividad de células tumorales |
| MX2008004693A (es) | 2005-10-21 | 2008-09-03 | Catalyst Biosciences Inc | Proteasas modificadas que inhiben la activacion del complemento. |
| US7972802B2 (en) | 2005-10-31 | 2011-07-05 | University Of Washington | Lipoprotein-associated markers for cardiovascular disease |
| EP1790664A1 (en) * | 2005-11-24 | 2007-05-30 | Ganymed Pharmaceuticals AG | Monoclonal antibodies against claudin-18 for treatment of cancer |
| WO2007073478A2 (en) | 2005-12-19 | 2007-06-28 | Genizon Biosciences Inc. | Genemap of the human genes associated with crohn's disease |
| US20080293070A1 (en) | 2005-12-21 | 2008-11-27 | Rafick-Pierre Sekaly | Markers for Memory T Cells and Uses Thereof |
| KR100679173B1 (ko) | 2006-02-28 | 2007-02-06 | 주식회사 바이오인프라 | 위암 진단용 단백질 마커 및 이를 이용한 진단키트 |
| US8025878B2 (en) * | 2006-03-23 | 2011-09-27 | Bioarctic Neuroscience Ab | Protofibril selective antibodies and the use thereof |
| US20080026485A1 (en) | 2006-04-18 | 2008-01-31 | Wolfgang Hueber | Antibody profiling for determination of patient responsiveness |
| WO2008021290A2 (en) | 2006-08-09 | 2008-02-21 | Homestead Clinical Corporation | Organ-specific proteins and methods of their use |
| WO2008049239A1 (en) | 2006-10-27 | 2008-05-02 | Mount Sinai Hospital | Endometrial biomarkers |
| WO2008085024A1 (en) | 2007-01-12 | 2008-07-17 | Erasmus University Medical Center Rotterdam | Identification and detection of peptides relating to specific disorders |
| GB0703652D0 (en) | 2007-02-26 | 2007-04-04 | Univ Bradford | Method for the allosteric modulation of beta1 integrin |
| WO2009006382A1 (en) | 2007-07-02 | 2009-01-08 | Purdue Research Foundation | Detection of glycopeptides and glycoproteins for medical diagnostics |
| WO2009034562A2 (en) | 2007-09-11 | 2009-03-19 | Dublin City University | A method of assessing lung squamous cell carcinoma status in an individual |
| WO2009061382A2 (en) | 2007-11-02 | 2009-05-14 | Marban Eduardo T | Cardiac stem cell and myocyte secreted paracrine factors and uses thereof |
| US7923253B2 (en) | 2007-11-05 | 2011-04-12 | Battelle Memorial Institute | Method for identifying type I diabetes mellitus in humans |
| EP2071336A1 (en) | 2007-12-13 | 2009-06-17 | Fraunhofer-Gesellschaft zur Förderung der angewandten Forschung e.V. | Serum proteomic for finding diagnostic markers and for monitoring therapeutical intervention in treatment of hepatocellular carcinoma |
| WO2009117030A2 (en) * | 2007-12-19 | 2009-09-24 | Macrogenics, Inc. | Improved compositions for the prevention and treatment of smallpox |
| EP2080812A1 (en) | 2008-01-18 | 2009-07-22 | Transmedi SA | Compositions and methods of detecting post-stop peptides |
| EP2240196A2 (en) * | 2008-01-22 | 2010-10-20 | Compugen Ltd. | Clusterin derived peptide |
| WO2009116860A1 (en) | 2008-03-17 | 2009-09-24 | Vereniging Het Nederlands Kanker Instituut | Markers providing prognosis of metastasis among cancer patients |
| KR101110758B1 (ko) | 2008-06-02 | 2012-02-15 | 경북대학교 산학협력단 | 뇌졸중 표적용 펩티드 및 이의 용도 |
| US8148088B2 (en) | 2008-07-18 | 2012-04-03 | Abgent | Regulation of autophagy pathway phosphorylation and uses thereof |
| WO2010030980A2 (en) | 2008-09-12 | 2010-03-18 | University Of South Florida | Akt and clusterin as biomarkers of chemotherapeutic responsiveness |
| EP2419440B1 (en) | 2009-04-17 | 2015-11-11 | National Research Council of Canada | Peptide ligands for clusterin and uses thereof |
| RU2627163C2 (ru) | 2009-11-24 | 2017-08-03 | Алетиа Байотерапьютикс Инк. | Антикластериновые антитела и антигенсвязывающие фрагменты и их использование для уменьшения объема новообразований |
| MX2014010164A (es) | 2012-02-22 | 2014-11-25 | Alethia Biotherapeutics Inc | Co-uso de un inhibidor de clusterina con un inhibidor de egfr para tratar cancer. |
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| CN102666585A (zh) | 2012-09-12 |
| HRP20191129T1 (hr) | 2019-09-20 |
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| EA034462B1 (ru) | 2020-02-11 |
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| CN102666585B (zh) | 2015-02-18 |
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| EA201390744A1 (ru) | 2013-11-29 |
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| EP2504363A4 (en) | 2013-10-09 |
| EP2504363A1 (en) | 2012-10-03 |
| CA2928846A1 (en) | 2011-06-03 |
| EP2504363B1 (en) | 2019-05-08 |
| RU2012126098A (ru) | 2013-12-27 |
| US8802826B2 (en) | 2014-08-12 |
| JP2013511288A (ja) | 2013-04-04 |
| US20120282251A1 (en) | 2012-11-08 |
| WO2011063523A1 (en) | 2011-06-03 |
| US20140302020A1 (en) | 2014-10-09 |
| PT2504363T (pt) | 2019-08-02 |
| CA2776513A1 (en) | 2011-06-03 |
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