ES2719548T3 - Anticuerpos humanizados para liv-1 y uso de los mismos para tratar el cáncer - Google Patents
Anticuerpos humanizados para liv-1 y uso de los mismos para tratar el cáncer Download PDFInfo
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- ES2719548T3 ES2719548T3 ES16200557T ES16200557T ES2719548T3 ES 2719548 T3 ES2719548 T3 ES 2719548T3 ES 16200557 T ES16200557 T ES 16200557T ES 16200557 T ES16200557 T ES 16200557T ES 2719548 T3 ES2719548 T3 ES 2719548T3
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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
- C07K16/30—Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies against material from animals or humans against receptors, cell surface antigens or cell surface determinants from tumour cells
- C07K16/3015—Breast
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- C—CHEMISTRY; METALLURGY
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- C07K16/18—Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies against material from animals or humans
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- C07K16/30—Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies against material from animals or humans against receptors, cell surface antigens or cell surface determinants from tumour cells
- C07K16/3053—Skin, nerves, brain
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- C—CHEMISTRY; METALLURGY
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- C07K16/18—Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies against material from animals or humans
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- C07K16/30—Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies against material from animals or humans against receptors, cell surface antigens or cell surface determinants from tumour cells
- C07K16/3069—Reproductive system, e.g. ovaria, uterus, testes, prostate
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- C—CHEMISTRY; METALLURGY
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- A61K2039/505—Medicinal preparations containing antigens or antibodies comprising antibodies
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- C07K2317/20—Immunoglobulins specific features characterized by taxonomic origin
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- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K2317/00—Immunoglobulins specific features
- C07K2317/50—Immunoglobulins specific features characterized by immunoglobulin fragments
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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)
- Preparation Of Compounds By Using Micro-Organisms (AREA)
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| SI3461847T1 (sl) * | 2010-12-06 | 2021-03-31 | Seagen Inc. | Humanizirana protitelesa proti LIV-1 in njihova uporaba pri zdravljenju raka |
| EP3722320A3 (en) | 2012-10-25 | 2020-12-30 | Bioverativ USA Inc. | Anti-complement c1s antibodies and uses thereof |
| PT2914291T (pt) | 2012-11-02 | 2022-05-05 | Bioverativ Usa Inc | Anticorpos anti-complemento c1s e suas utilizações |
| US9353150B2 (en) | 2012-12-04 | 2016-05-31 | Massachusetts Institute Of Technology | Substituted pyrazino[1′,2′:1 ,5]pyrrolo[2,3-b]-indole-1,4-diones for cancer treatment |
| JP6441232B2 (ja) | 2012-12-27 | 2018-12-19 | サノフイＳａｎｏｆｉ | 抗ｌａｍｐ１抗体および抗体薬物コンジュゲート、ならびにその使用 |
| KR20160034404A (ko) * | 2013-07-31 | 2016-03-29 | 암젠 인크 | Ｆc-함유 폴리펩타이드의 안정화 |
| KR102356814B1 (ko) | 2013-10-15 | 2022-01-28 | 씨젠 인크. | 개선된 리간드-약물 컨쥬게이트 약물동력학을 위한 peg화된 약물-링커 |
| IL309933A (en) | 2014-02-17 | 2024-03-01 | Seagen Inc | Hydrophilic antibody-drug conjugates |
| HRP20230093T1 (hr) | 2015-04-06 | 2023-03-31 | Bioverativ Usa Inc. | Humanizirana anti-c1s protutijela i postupci njihove primjene |
| AU2016363013B2 (en) | 2015-12-04 | 2022-03-10 | Seagen Inc. | Conjugates of quaternized tubulysin compounds |
| US11793880B2 (en) | 2015-12-04 | 2023-10-24 | Seagen Inc. | Conjugates of quaternized tubulysin compounds |
| CA3011900A1 (en) | 2016-02-17 | 2017-08-24 | Seattle Genetics, Inc. | Bcma antibodies and use of same to treat cancer and immunological disorders |
| MA45324A (fr) * | 2016-03-15 | 2019-01-23 | Seattle Genetics Inc | Polythérapie utilisant un adc-liv1 et un agent chimiothérapeutique |
| WO2017165851A1 (en) | 2016-03-25 | 2017-09-28 | Seattle Genetics, Inc. | Process for the preparation of pegylated drug-linkers and intermediates thereof |
| US10918627B2 (en) | 2016-05-11 | 2021-02-16 | Massachusetts Institute Of Technology | Convergent and enantioselective total synthesis of Communesin analogs |
| KR20190038579A (ko) | 2016-08-09 | 2019-04-08 | 시애틀 지네틱스, 인크. | 개선된 물리화학적 특성을 갖는 자기 안정화 링커를 구비한 약물 접합체 |
| EA201891851A1 (ru) * | 2016-09-16 | 2019-04-30 | Сиэтл Дженетикс, Инк. | Антитела против bcma и их применение для лечения злокачественных новообразований и иммунологических нарушений |
| CN116554320A (zh) | 2016-10-12 | 2023-08-08 | 美国比奥维拉迪维股份有限公司 | 抗C1s抗体及其使用方法 |
| BR112019006778A2 (pt) | 2016-10-18 | 2019-10-15 | Seattle Genetics Inc | Composição de conjugado de aglutinante-fármaco, formulação, uso da mesma, método para preparar uma composição ou composto de conjugado de aglutinantefármaco,e, composto de ligante de fármaco |
| SG10202110182PA (en) | 2017-03-15 | 2021-10-28 | Silverback Therapeutics Inc | Benzazepine compounds, conjugates, and uses thereof |
| US11730822B2 (en) | 2017-03-24 | 2023-08-22 | Seagen Inc. | Process for the preparation of glucuronide drug-linkers and intermediates thereof |
| CA3060405C (en) | 2017-04-18 | 2020-06-16 | 3M Innovative Properties Company | Air filter media with post-pleat-deposited sorbent particles |
| MA51189A (fr) | 2017-04-27 | 2020-03-04 | Seattle Genetics Inc | Conjugués d'inhibiteur de la voie de récupération du nicotinamide adénine dinucléotide quaternarisé |
| WO2018209239A1 (en) | 2017-05-11 | 2018-11-15 | Massachusetts Institute Of Technology | Potent agelastatin derivatives as modulators for cancer invasion and metastasis |
| SG11202001762RA (en) * | 2017-09-02 | 2020-03-30 | Abbvie Inc | Anti-egfr antibody drug conjugates (adc) and uses thereof |
| EP3675908A4 (en) * | 2017-09-02 | 2021-05-12 | AbbVie Inc. | ANTI-EGFR-DRUG (ADC) ANTIBODY CONJUGATES AND ASSOCIATED USES |
| US10640508B2 (en) | 2017-10-13 | 2020-05-05 | Massachusetts Institute Of Technology | Diazene directed modular synthesis of compounds with quaternary carbon centers |
| MA50943A (fr) | 2017-12-01 | 2020-10-07 | Seattle Genetics Inc | Anticorps anti-liv1 humanisés pour le traitement du cancer du sein |
| IL276546B2 (en) | 2018-02-20 | 2024-08-01 | Seagen Inc | Hydrophobic auristatin F compounds and their conjugates |
| US20220323596A1 (en) | 2018-09-12 | 2022-10-13 | Silverback Therapeutics, Inc. | Antibody conjugates of toll-like receptor agonists |
| WO2020056194A1 (en) | 2018-09-12 | 2020-03-19 | Silverback Therapeutics, Inc. | Benzazepine compounds, conjugates, and uses thereof |
| JP2022500404A (ja) | 2018-09-12 | 2022-01-04 | シルバーバック セラピューティックス インコーポレイテッド | 置換ベンゾアゼピン化合物、そのコンジュゲートおよび使用 |
| US20200113912A1 (en) | 2018-09-12 | 2020-04-16 | Silverback Therapeutics, Inc. | Methods and Compositions for the Treatment of Disease with Immune Stimulatory Conjugates |
| CN113015750A (zh) * | 2018-11-07 | 2021-06-22 | 克里斯珀医疗股份公司 | 抗liv1免疫细胞癌症疗法 |
| TW202112801A (zh) | 2019-06-05 | 2021-04-01 | 美商西雅圖遺傳學公司 | 純化遮蔽抗體之方法 |
| US11535634B2 (en) | 2019-06-05 | 2022-12-27 | Massachusetts Institute Of Technology | Compounds, conjugates, and compositions of epipolythiodiketopiperazines and polythiodiketopiperazines and uses thereof |
| US20220233709A1 (en) | 2019-06-05 | 2022-07-28 | Seagen Inc. | Masked Antibody Formulations |
| GB201908208D0 (en) * | 2019-06-10 | 2019-07-24 | Univ College Cardiff Consultants Ltd | An anti-mitotic agent |
| KR20220035486A (ko) | 2019-07-22 | 2022-03-22 | 씨젠 인크. | 암 치료를 위한 인간화 항-liv1 항체 |
| MX2022001719A (es) | 2019-08-15 | 2022-03-11 | Silverback Therapeutics Inc | Formulaciones de conjugados de benzazepina y usos de las mismas. |
| AU2020358726A1 (en) | 2019-10-01 | 2022-04-07 | Silverback Therapeutics, Inc. | Combination therapy with immune stimulatory conjugates |
| CN115066259A (zh) | 2019-12-09 | 2022-09-16 | 思进公司 | 使用liv1-adc和pd-1拮抗剂的组合疗法 |
| TWI877278B (zh) | 2019-12-30 | 2025-03-21 | 美商思進公司 | 以非海藻糖苷化抗－ｃｄ７０抗體治療癌症之方法 |
| JP7735291B2 (ja) | 2020-02-21 | 2025-09-08 | エーアールエス ファーマシューティカルズ、インコーポレイテッド | ネクチン－４抗体コンジュゲートおよびその使用 |
| AU2021300362A1 (en) | 2020-07-01 | 2023-02-23 | ARS Pharmaceuticals, Inc. | Anti-ASGR1 antibody conjugates and uses thereof |
| AU2021349385A1 (en) * | 2020-09-28 | 2023-05-25 | Seagen Inc. | Humanized anti-liv1 antibodies for the treatment of cancer |
| AR124681A1 (es) | 2021-01-20 | 2023-04-26 | Abbvie Inc | Conjugados anticuerpo-fármaco anti-egfr |
| WO2022182415A1 (en) | 2021-02-24 | 2022-09-01 | Massachusetts Institute Of Technology | Himastatin derivatives, and processes of preparation thereof, and uses thereof |
| WO2022198231A1 (en) | 2021-03-18 | 2022-09-22 | Seagen Inc. | Selective drug release from internalized conjugates of biologically active compounds |
| WO2023288236A1 (en) | 2021-07-14 | 2023-01-19 | Seagen Inc. | Antibody masking domains |
| EP4405387A1 (en) | 2021-09-24 | 2024-07-31 | Seagen Inc. | Improved antibody masking domains |
| WO2023111913A1 (en) | 2021-12-15 | 2023-06-22 | Crispr Therapeutics Ag | Engineered anti-liv1 cell with regnase-1 and/or tgfbrii disruption |
| WO2023217227A1 (zh) | 2022-05-12 | 2023-11-16 | 先声再明医药有限公司 | 喜树碱类衍生物及配体-药物偶联物 |
| TW202421668A (zh) * | 2022-11-25 | 2024-06-01 | 大陸商江蘇恆瑞醫藥股份有限公司 | 抗liv-1抗體、其藥物偶聯物及其醫藥用途 |
| AU2024218701A1 (en) | 2023-02-07 | 2025-08-21 | LaNova Medicines Limited | Antibodies targeting liv-1 and uses thereof |
| CN120858117A (zh) * | 2023-03-15 | 2025-10-28 | 浙江博锐生物制药有限公司 | 抗liv-1抗体和抗liv-1抗体药物偶联物及其药物用途 |
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| WO2025146128A1 (zh) * | 2024-01-05 | 2025-07-10 | 海南先声再明医药股份有限公司 | 抗liv-1的抗体及其用途 |
| WO2025146137A1 (zh) * | 2024-01-05 | 2025-07-10 | 海南先声再明医药股份有限公司 | 抗liv-1抗体药物偶联物及其用途 |
| CN120040587B (zh) * | 2025-04-27 | 2025-08-08 | 上海宏成药业有限公司 | 抗liv-1抗体或其抗原结合片段及其用途 |
Family Cites Families (87)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| CH652145A5 (de) | 1982-01-22 | 1985-10-31 | Sandoz Ag | Verfahren zur in vitro-herstellung von hybridomen welche humane monoklonale antikoerper erzeugen. |
| US4634666A (en) | 1984-01-06 | 1987-01-06 | The Board Of Trustees Of The Leland Stanford Junior University | Human-murine hybridoma fusion partner |
| US5225539A (en) | 1986-03-27 | 1993-07-06 | Medical Research Council | Recombinant altered antibodies and methods of making altered antibodies |
| US4880935A (en) | 1986-07-11 | 1989-11-14 | Icrf (Patents) Limited | Heterobifunctional linking agents derived from N-succinimido-dithio-alpha methyl-methylene-benzoates |
| AU600575B2 (en) | 1987-03-18 | 1990-08-16 | Sb2, Inc. | Altered antibodies |
| IL89220A (en) | 1988-02-11 | 1994-02-27 | Bristol Myers Squibb Co | Anthracycline immunoconjugates, their production and pharmaceutical compositions containing them |
| ATE120454T1 (de) | 1988-06-14 | 1995-04-15 | Cetus Oncology Corp | Kupplungsmittel und sterisch gehinderte, mit disulfid gebundene konjugate daraus. |
| US5530101A (en) | 1988-12-28 | 1996-06-25 | Protein Design Labs, Inc. | Humanized immunoglobulins |
| US5859205A (en) | 1989-12-21 | 1999-01-12 | Celltech Limited | Humanised antibodies |
| DE69133566T2 (de) | 1990-01-12 | 2007-12-06 | Amgen Fremont Inc. | Bildung von xenogenen Antikörpern |
| US5427908A (en) | 1990-05-01 | 1995-06-27 | Affymax Technologies N.V. | Recombinant library screening methods |
| GB9015198D0 (en) | 1990-07-10 | 1990-08-29 | Brien Caroline J O | Binding substance |
| WO1993012227A1 (en) | 1991-12-17 | 1993-06-24 | Genpharm International, Inc. | Transgenic non-human animals capable of producing heterologous antibodies |
| US5789650A (en) | 1990-08-29 | 1998-08-04 | Genpharm International, Inc. | Transgenic non-human animals for producing heterologous antibodies |
| US5814318A (en) | 1990-08-29 | 1998-09-29 | Genpharm International Inc. | Transgenic non-human animals for producing heterologous antibodies |
| WO1992003918A1 (en) | 1990-08-29 | 1992-03-19 | Genpharm International, Inc. | Transgenic non-human animals capable of producing heterologous antibodies |
| US5625126A (en) | 1990-08-29 | 1997-04-29 | Genpharm International, Inc. | Transgenic non-human animals for producing heterologous antibodies |
| US5633425A (en) | 1990-08-29 | 1997-05-27 | Genpharm International, Inc. | Transgenic non-human animals capable of producing heterologous antibodies |
| US5661016A (en) | 1990-08-29 | 1997-08-26 | Genpharm International Inc. | Transgenic non-human animals capable of producing heterologous antibodies of various isotypes |
| US5874299A (en) | 1990-08-29 | 1999-02-23 | Genpharm International, Inc. | Transgenic non-human animals capable of producing heterologous antibodies |
| US5545806A (en) | 1990-08-29 | 1996-08-13 | Genpharm International, Inc. | Ransgenic non-human animals for producing heterologous antibodies |
| US5770429A (en) | 1990-08-29 | 1998-06-23 | Genpharm International, Inc. | Transgenic non-human animals capable of producing heterologous antibodies |
| US5877397A (en) | 1990-08-29 | 1999-03-02 | Genpharm International Inc. | Transgenic non-human animals capable of producing heterologous antibodies of various isotypes |
| DE69230142T2 (de) | 1991-05-15 | 2000-03-09 | Cambridge Antibody Technology Ltd. | Verfahren zur herstellung von spezifischen bindungspaargliedern |
| US5858657A (en) | 1992-05-15 | 1999-01-12 | Medical Research Council | Methods for producing members of specific binding pairs |
| CA2103059C (en) | 1991-06-14 | 2005-03-22 | Paul J. Carter | Method for making humanized antibodies |
| EP0656367A1 (en) | 1991-08-22 | 1995-06-07 | Becton, Dickinson and Company | Method and composition for cancer therapy and for prognosticating responses to cancer theraphy |
| US5565332A (en) | 1991-09-23 | 1996-10-15 | Medical Research Council | Production of chimeric antibodies - a combinatorial approach |
| US5622929A (en) | 1992-01-23 | 1997-04-22 | Bristol-Myers Squibb Company | Thioether conjugates |
| US5733743A (en) | 1992-03-24 | 1998-03-31 | Cambridge Antibody Technology Limited | Methods for producing members of specific binding pairs |
| ATE199392T1 (de) | 1992-12-04 | 2001-03-15 | Medical Res Council | Multivalente und multispezifische bindungsproteine, deren herstellung und verwendung |
| US6214345B1 (en) | 1993-05-14 | 2001-04-10 | Bristol-Myers Squibb Co. | Lysosomal enzyme-cleavable antitumor drug conjugates |
| US5877218A (en) | 1994-01-10 | 1999-03-02 | Teva Pharmaceutical Industries, Ltd. | Compositions containing and methods of using 1-aminoindan and derivatives thereof and process for preparing optically active 1-aminoindan derivatives |
| CA2132500A1 (en) | 1994-09-20 | 1996-03-21 | David Lockwood Manning | Methods for predicting the behaviour of breast tumours |
| DE69626849T2 (de) | 1995-12-22 | 2003-12-24 | Bristol-Myers Squibb Co., Princeton | Verzweigte hydrazongruppen enthaltende kuppler |
| US5834597A (en) | 1996-05-20 | 1998-11-10 | Protein Design Labs, Inc. | Mutated nonactivating IgG2 domains and anti CD3 antibodies incorporating the same |
| US6130237A (en) | 1996-09-12 | 2000-10-10 | Cancer Research Campaign Technology Limited | Condensed N-aclyindoles as antitumor agents |
| EP0939824B1 (en) | 1996-10-31 | 2007-06-06 | Abbott Laboratories | Reagents and methods useful for detecting diseases of the breast |
| US6066778A (en) | 1996-11-06 | 2000-05-23 | The Regents Of The University Of Michigan | Transgenic mice expressing APC resistant factor V |
| WO1998034118A1 (en) | 1997-01-30 | 1998-08-06 | Yale University | Diagnostic methods and compositions based on the distribution of rad51 |
| EP1027444A1 (en) | 1997-10-31 | 2000-08-16 | Abbott Laboratories | Reagents and methods useful for detecting diseases of the breast |
| EP1032706A1 (en) | 1997-11-18 | 2000-09-06 | Abbott Laboratories | Reagents and methods useful for detecting diseases of the breast |
| AU2010699A (en) | 1997-12-24 | 1999-07-19 | Corixa Corporation | Compounds for immunotherapy and diagnosis of breast cancer and methods for theiruse |
| CA2347906A1 (en) | 1998-08-04 | 2000-02-17 | Diadexus, Inc. | A novel method of diagnosing, monitoring, staging, imaging and treating breast cancer |
| EP1953229A3 (en) | 1998-10-15 | 2008-12-24 | Novartis Vaccines and Diagnostics, Inc. | Metastatic breast and colon cancer regulated genes |
| CA2625839A1 (en) | 1999-02-05 | 2000-08-10 | Samsung Electronics Co., Ltd. | Image texture retrieving method and apparatus thereof |
| AU3395900A (en) | 1999-03-12 | 2000-10-04 | Human Genome Sciences, Inc. | Human lung cancer associated gene sequences and polypeptides |
| US6762020B1 (en) | 1999-03-15 | 2004-07-13 | Protein Design Labs, Inc. | Methods of diagnosing breast cancer |
| US20040141983A1 (en) | 1999-03-15 | 2004-07-22 | Protein Design Labs, Inc. | Compositions against cancer antigen LIV-1 and uses thereof |
| IL150592A0 (en) | 2000-01-25 | 2003-02-12 | Genentech Inc | Liv-1 related protein, polynucleotides encoding the same and use thereof for treatment of cancer |
| WO2001096372A2 (en) | 2000-06-13 | 2001-12-20 | University College Cardiff Consultants Ltd | Zinc transporters proteins and their use in medicinal preparations |
| US6964849B2 (en) | 2001-01-11 | 2005-11-15 | Curagen Corporation | Proteins and nucleic acids encoding same |
| US6884869B2 (en) | 2001-04-30 | 2005-04-26 | Seattle Genetics, Inc. | Pentapeptide compounds and uses related thereto |
| AU2002322280A1 (en) | 2001-06-21 | 2003-01-21 | Millennium Pharmaceuticals, Inc. | Compositions, kits, and methods for identification, assessment, prevention, and therapy of breast cancer |
| US20030068636A1 (en) | 2001-06-21 | 2003-04-10 | Millennium Pharmaceuticals, Inc. | Compositions, kits and methods for identification, assessment, prevention, and therapy of breast and ovarian cancer |
| IL166244A0 (en) | 2001-07-12 | 2006-01-15 | Jefferson Foote | Super humanized antibodies |
| US7091186B2 (en) | 2001-09-24 | 2006-08-15 | Seattle Genetics, Inc. | p-Amidobenzylethers in drug delivery agents |
| ES2305481T3 (es) | 2002-03-08 | 2008-11-01 | Pdl Biopharma, Inc. | Anticuerpos contra el antigeno cancerigeno tmeff2 y usos de los mismos. |
| EP2353611B1 (en) | 2002-07-31 | 2015-05-13 | Seattle Genetics, Inc. | Drug conjugates and their use for treating cancer, an autoimmune disease or an infectious disease |
| MXPA05007940A (es) * | 2003-01-27 | 2007-06-14 | Biogen Idec Inc | Composiciones y metodos para el tratamiento del cancer usando igsf9 y liv-1. |
| WO2004067564A2 (en) | 2003-01-29 | 2004-08-12 | Protein Design Labs, Inc. | Compositions against cancer antigen liv-1 and uses thereof |
| KR20050010267A (ko) | 2003-07-18 | 2005-01-27 | 삼성전자주식회사 | 식각장치 |
| KR101520209B1 (ko) | 2003-11-06 | 2015-05-13 | 시애틀 지네틱스, 인크. | 리간드에 접합될 수 있는 모노메틸발린 화합물 |
| WO2005058961A2 (en) * | 2003-12-12 | 2005-06-30 | Amgen Inc. | Antibodies specific for human galanin, and uses thereof |
| US7501121B2 (en) | 2004-06-17 | 2009-03-10 | Wyeth | IL-13 binding agents |
| TWI355389B (en) | 2004-07-30 | 2012-01-01 | Rinat Neuroscience Corp | Antibodies directed against amyloid-beta peptide a |
| US20060222653A1 (en) * | 2004-11-12 | 2006-10-05 | Xencor, Inc. | Antibodies operably linked to selected chemoattractants |
| WO2006124269A2 (en) | 2005-05-16 | 2006-11-23 | Amgen Fremont Inc. | Human monoclonal antibodies that bind to very late antigen-1 for the treatment of inflammation and other disorders |
| WO2007030642A2 (en) | 2005-09-07 | 2007-03-15 | Medimmune, Inc. | Toxin conjugated eph receptor antibodies |
| JP2009541208A (ja) | 2006-04-13 | 2009-11-26 | ノバルティス・バクシーンズ・アンド・ダイアグノスティクス・インコーポレイテッド | がんを処置し、診断しもしくは検出する方法 |
| EP2609932B1 (en) | 2006-12-01 | 2022-02-02 | Seagen Inc. | Variant target binding agents and uses thereof |
| AR066240A1 (es) * | 2007-04-23 | 2009-08-05 | Wyeth Corp | Metodos y composiciones para tratar y monitorear el tratamiento de trastornos asociados con il-13 |
| EA023031B1 (ru) * | 2007-11-30 | 2016-04-29 | Глаксо Груп Лимитед | Антиген-связывающая конструкция и ее применение |
| EP2282773B2 (en) | 2008-05-02 | 2025-03-05 | Seagen Inc. | Methods and compositions for making antibodies and antibody derivatives with reduced core fucosylation |
| RU2011101378A (ru) | 2008-06-16 | 2012-07-27 | Сайвидон Дайагностикс Гмбх (De) | Алгоритмы предсказания исхода у пациентов с узловой формой рака молочной железы после химиотерапии |
| US20110195995A1 (en) | 2008-10-14 | 2011-08-11 | Wittliff James L | Methods of Optimizing Treatment of Estrogen-Receptor Positive Breast Cancers |
| WO2010069858A1 (en) | 2008-12-19 | 2010-06-24 | F. Hoffmann-La Roche Ag | Pharmaceutical composition |
| US8642270B2 (en) | 2009-02-09 | 2014-02-04 | Vm Institute Of Research | Prognostic biomarkers to predict overall survival and metastatic disease in patients with triple negative breast cancer |
| US20110165566A1 (en) | 2009-07-09 | 2011-07-07 | Wittliff James L | Methods of optimizing treatment of breast cancer |
| MX353186B (es) | 2009-09-03 | 2018-01-05 | Genentech Inc | Metodos para el tratamiento, diagnosis y monitoreo de artritis reumatoide. |
| SI3461847T1 (sl) | 2010-12-06 | 2021-03-31 | Seagen Inc. | Humanizirana protitelesa proti LIV-1 in njihova uporaba pri zdravljenju raka |
| WO2012125712A2 (en) | 2011-03-14 | 2012-09-20 | Respira Health, Llc | Lung tumor classifier for current and former smokers |
| EP2839860B1 (en) | 2012-10-12 | 2019-05-01 | MedImmune Limited | Pyrrolobenzodiazepines and conjugates thereof |
| MA45324A (fr) | 2016-03-15 | 2019-01-23 | Seattle Genetics Inc | Polythérapie utilisant un adc-liv1 et un agent chimiothérapeutique |
| MA50943A (fr) | 2017-12-01 | 2020-10-07 | Seattle Genetics Inc | Anticorps anti-liv1 humanisés pour le traitement du cancer du sein |
| CN113015750A (zh) | 2018-11-07 | 2021-06-22 | 克里斯珀医疗股份公司 | 抗liv1免疫细胞癌症疗法 |
| GB201908208D0 (en) | 2019-06-10 | 2019-07-24 | Univ College Cardiff Consultants Ltd | An anti-mitotic agent |
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