EA029987B1 - Антитела к cd33 и их применение в лечении рака - Google Patents
Антитела к cd33 и их применение в лечении рака Download PDFInfo
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- EA029987B1 EA029987B1 EA201492137A EA201492137A EA029987B1 EA 029987 B1 EA029987 B1 EA 029987B1 EA 201492137 A EA201492137 A EA 201492137A EA 201492137 A EA201492137 A EA 201492137A EA 029987 B1 EA029987 B1 EA 029987B1
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- antibody
- heavy chain
- variable region
- seeg
- light chain
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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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| US201261649110P | 2012-05-18 | 2012-05-18 | |
| US13/804,227 US20130309223A1 (en) | 2012-05-18 | 2013-03-14 | CD33 Antibodies And Use Of Same To Treat Cancer |
| PCT/US2013/041209 WO2013173496A2 (en) | 2012-05-18 | 2013-05-15 | Cd33 antibodies and use of same to treat cancer |
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| EA201492137A1 EA201492137A1 (ru) | 2015-08-31 |
| EA029987B1 true EA029987B1 (ru) | 2018-06-29 |
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| CA2699837C (en) * | 2006-12-01 | 2017-06-13 | Seattle Genetics, Inc. | Variant target binding agents and uses thereof |
| US20130309223A1 (en) | 2012-05-18 | 2013-11-21 | Seattle Genetics, Inc. | CD33 Antibodies And Use Of Same To Treat Cancer |
| KR102538993B1 (ko) | 2013-10-15 | 2023-06-02 | 씨젠 인크. | 개선된 리간드-약물 컨쥬게이트 약물동력학을 위한 peg화된 약물-링커 |
| WO2015077605A1 (en) * | 2013-11-25 | 2015-05-28 | Seattle Genetics, Inc. | Preparing antibodies from cho cell cultures for conjugation |
| TW201533060A (zh) * | 2013-12-13 | 2015-09-01 | Genentech Inc | 抗cd33抗體及免疫結合物 |
| KR102532137B1 (ko) | 2014-02-11 | 2023-05-12 | 씨젠 인크. | 단백질의 선택적 환원 |
| EP3912641B1 (en) | 2014-02-17 | 2024-11-06 | Seagen Inc. | Hydrophilic drug-linker compounds |
| US9944702B2 (en) * | 2014-04-03 | 2018-04-17 | Cellectis | CD33 specific chimeric antigen receptors for cancer immunotherapy |
| JP6831777B2 (ja) * | 2014-07-21 | 2021-02-17 | ノバルティス アーゲー | Cd33キメラ抗原受容体を使用する癌の処置 |
| CA2973529A1 (en) | 2015-01-26 | 2016-08-04 | Cellectis | Cll1-specific multi-chain chimeric antigen receptor |
| HK1252675A1 (zh) | 2015-06-12 | 2019-05-31 | Alector Llc | 抗cd33抗体及其使用方法 |
| JP7376977B2 (ja) | 2015-06-12 | 2023-11-09 | アレクトル エルエルシー | 抗cd33抗体及びその使用方法 |
| TW201709932A (zh) * | 2015-06-12 | 2017-03-16 | 西雅圖遺傳學公司 | Cd123抗體及其共軛物 |
| IL256295B2 (en) * | 2015-06-30 | 2023-11-01 | Seagen Inc | Anti-NTB-A antibodies and related compositions and methods |
| CN108367043A (zh) | 2015-12-04 | 2018-08-03 | 西雅图基因公司 | 季铵化的微管溶素化合物的缀合物 |
| US11793880B2 (en) | 2015-12-04 | 2023-10-24 | Seagen Inc. | Conjugates of quaternized tubulysin compounds |
| WO2017160954A1 (en) | 2016-03-15 | 2017-09-21 | Seattle Genetics, Inc. | Combinations of pbd-based antibody drug conjugates with bcl-2 inhibitors |
| EP3433278A4 (en) | 2016-03-25 | 2019-11-06 | Seattle Genetics, Inc. | METHOD FOR THE PRODUCTION OF PEGYLATED ACTIVE LINKERS AND INTERMEDIATE PRODUCTS THEREOF |
| US20190117787A1 (en) * | 2016-04-15 | 2019-04-25 | Seattle Genetics, Inc. | Combinations of cd33 antibody drug conjugates with hypomethylating agents |
| EP3463463A4 (en) * | 2016-06-03 | 2020-01-15 | Seattle Genetics, Inc. | Combination of cd33 antibody drug conjugates with chemotherapeutic agents |
| EP3469001A4 (en) | 2016-06-09 | 2020-05-06 | Seattle Genetics, Inc. | COMBINATIONS OF PBD-BASED ANTIBODY CONJUGATES WITH FLT3 INHIBITORS |
| BR112019001945A2 (pt) | 2016-08-09 | 2019-05-07 | Seattle Genetics, Inc. | composição de conjugado de fármaco aglutinante, formulação farmaceuticamente aceitável, métodos para tratar uma doença ou afecção hiperproliferativa, para inibir a multiplicação de uma célula tumoral ou célula cancerígena e para preparar uma composição de conjugado de fármaco aglutinado, e, composto |
| TWI835714B (zh) | 2016-10-18 | 2024-03-21 | 美商思進公司 | 菸鹼醯胺腺嘌呤二核苷酸補救合成(salvage pathway)抑制劑之靶向投遞 |
| MA46952A (fr) | 2016-12-01 | 2019-10-09 | Regeneron Pharma | Anticorps anti-pd-l1 radiomarqués pour imagerie immuno-pet |
| BR112019011277A2 (pt) | 2016-12-02 | 2019-10-22 | University Of Southern California | polinucleotídeo, sistema de expressão recombinante, vetor, polipeptídeo, célula recombinante, polipeptídeo de receptor imune sintético isolado ou heterodímero de polipeptídeo, célula efetora imune ou célula-tronco, população de células imunes ou efetoras, métodos de fabricação de uma célula efetora imune que expressa sir, de geração de uma população de células modificadas por rna, de fornecimento de imunidade antidoença e de tratamento ou prevenção de uma doença, composição, uso ou método, kit, e, sequência de aminoácidos. |
| JP7337698B2 (ja) | 2017-02-28 | 2023-09-04 | シージェン インコーポレイテッド | コンジュゲート化のためのシステイン突然変異抗体 |
| BR112019017751A2 (pt) | 2017-02-28 | 2020-04-07 | Vor Biopharma, Inc. | composições e métodos de inibição de proteínas de linhagem específica |
| JP7527787B2 (ja) | 2017-03-24 | 2024-08-05 | シージェン インコーポレイテッド | グルクロニド薬物-リンカーの調製のためのプロセスおよびその中間体 |
| TW201904613A (zh) | 2017-04-27 | 2019-02-01 | 美商西雅圖遺傳學公司 | 季鹼化菸鹼醯胺腺二核苷酸補救合成抑制劑結合物 |
| JP2020519640A (ja) * | 2017-05-17 | 2020-07-02 | イミュノジェン, インコーポレイテッド | 抗cd33イムノコンジュゲート投与計画 |
| WO2018218207A1 (en) * | 2017-05-26 | 2018-11-29 | Fred Hutchinson Cancer Research Center | Anti-cd33 antibodies and uses thereof |
| CA3061755A1 (en) | 2017-08-03 | 2019-02-07 | Alector Llc | Anti-trem2 antibodies and methods of use thereof |
| PE20200486A1 (es) | 2017-08-03 | 2020-03-03 | Alector Llc | Anticuerpos anti-cd33 y metodos para utilizarlos |
| CN117003875A (zh) | 2017-09-29 | 2023-11-07 | 第一三共株式会社 | 抗体或其功能性片段、多核苷酸、表达载体、宿主细胞、糖链重构抗体、药物组合物、应用 |
| TWI838358B (zh) | 2018-02-20 | 2024-04-11 | 美商思進公司 | 疏水性奧瑞他汀(auristatin)f化合物及其結合物 |
| SG11202007943RA (en) * | 2018-02-20 | 2020-09-29 | Dragonfly Therapeutics Inc | Antibody variable domains targeting cd33, and use thereof |
| MX2020008684A (es) | 2018-02-20 | 2020-12-07 | Dragonfly Therapeutics Inc | Proteinas de union multiespecificas que se unen a cd33, nkg2d y cd16 y metodos de uso. |
| CN113423725A (zh) | 2018-08-28 | 2021-09-21 | Vor生物制药股份有限公司 | 遗传工程化造血干细胞及其用途 |
| CN112912144A (zh) * | 2018-08-31 | 2021-06-04 | 艾利妥 | 抗cd33抗体及其使用方法 |
| EP3849565A4 (en) | 2018-09-12 | 2022-12-28 | Fred Hutchinson Cancer Research Center | REDUCTION OF CD33 EXPRESSION TO SELECTIVELY PROTECT THERAPEUTIC CELLS |
| CN112672757A (zh) * | 2018-09-25 | 2021-04-16 | 中央研究院 | 抗-唾液酸结合性免疫球蛋白样凝集素的抗体、包括该抗体的药学组合物及其用途 |
| EP3877414A1 (en) | 2018-11-07 | 2021-09-15 | CRISPR Therapeutics AG | Anti-cd33 immune cell cancer therapy |
| JP7401456B2 (ja) | 2018-11-14 | 2023-12-19 | 第一三共株式会社 | 抗cdh6抗体-ピロロベンゾジアゼピン誘導体コンジュゲート |
| WO2020172621A1 (en) | 2019-02-22 | 2020-08-27 | Memorial Sloan Kettering Cancer Center | Cd33 antibodies and methods of using the same to treat cancer |
| KR20210141630A (ko) | 2019-03-25 | 2021-11-23 | 다이이찌 산쿄 가부시키가이샤 | 항 her2 항체-피롤로벤조디아제핀 유도체 콘주게이트 |
| TWI856078B (zh) | 2019-03-25 | 2024-09-21 | 日商第一三共股份有限公司 | 抗體–吡咯并苯二氮呯衍生物結合物、其製造方法及其用途 |
| CA3139180A1 (en) | 2019-03-27 | 2020-10-01 | Daiichi Sankyo Company, Limited | Combination of antibody-pyrrolobenzodiazepine derivative conjugate and parp inhibitor |
| KR20220016083A (ko) | 2019-04-30 | 2022-02-08 | 센티 바이오사이언시스, 인코포레이티드 | 키메라 수용체 및 이의 사용 방법 |
| AU2020287378A1 (en) * | 2019-06-06 | 2022-02-03 | Mythic Therapeutics, Inc. | Antigen-binding protein constructs and uses thereof |
| WO2021138407A2 (en) | 2020-01-03 | 2021-07-08 | Marengo Therapeutics, Inc. | Multifunctional molecules that bind to cd33 and uses thereof |
| US20230144405A1 (en) * | 2020-03-31 | 2023-05-11 | Fred Hutchinson Cancer Center | Human anti-cd33 antibodies and uses thereof |
| JP2023519932A (ja) * | 2020-03-31 | 2023-05-15 | フレッド ハッチンソン キャンサー センター | 抗cd33抗体及びその使用 |
| MX2022012621A (es) | 2020-04-10 | 2023-01-18 | Seagen Inc | Enlazadores de variantes de carga. |
| US20210402001A1 (en) * | 2020-06-30 | 2021-12-30 | David I. Cohen | Zinc Porters, and their Monoclonal Antibody Conjugates, for the Prevention and Treatment of COVID-19 (SARS-CoV-2), Other Infections, and Cancers |
| TW202227479A (zh) | 2020-09-02 | 2022-07-16 | 日商第一三共股份有限公司 | 新穎內-β-N-乙醯葡萄糖胺苷酶 |
| AU2021380681A1 (en) * | 2020-11-11 | 2023-06-15 | Versapeutics Inc. | Antibody variants against wnt receptor ryk |
| AU2022207708A1 (en) | 2021-01-13 | 2023-07-27 | Daiichi Sankyo Company, Limited | Antibody-pyrrolobenzodiazepine derivative conjugate |
| JP2024504728A (ja) | 2021-01-26 | 2024-02-01 | サイトケアズ (シャンハイ) インコーポレイテッド | キメラ抗原受容体(car)構築物およびcar構築物を発現するnk細胞 |
| US12036286B2 (en) | 2021-03-18 | 2024-07-16 | Seagen Inc. | Selective drug release from internalized conjugates of biologically active compounds |
| KR20230171980A (ko) | 2021-04-20 | 2023-12-21 | 씨젠 인크. | 항체 의존성 세포 독성의 조절 |
| AU2022283467A1 (en) | 2021-05-28 | 2023-12-07 | Seagen Inc. | Anthracycline antibody conjugates |
| KR20240113514A (ko) | 2021-11-30 | 2024-07-22 | 다이이찌 산쿄 가부시키가이샤 | 프로테아제 분해성 마스크 항체 |
| JPWO2023153442A1 (enExample) | 2022-02-09 | 2023-08-17 | ||
| EP4488378A1 (en) | 2022-03-02 | 2025-01-08 | Daiichi Sankyo Company, Limited | Method for producing fc-containing molecule |
| KR20250004952A (ko) | 2022-03-17 | 2025-01-08 | 씨젠 인크. | 캄프토테신 접합체 |
| WO2024129756A1 (en) | 2022-12-13 | 2024-06-20 | Seagen Inc. | Site-specific engineered cysteine antibody drug conjugates |
| CN116375874B (zh) * | 2023-04-14 | 2023-12-26 | 上海精翰生物科技有限公司 | 一种cd33抗体及其应用 |
| TW202535940A (zh) | 2023-10-24 | 2025-09-16 | 美商思進公司 | 化學治療化合物及使用方法 |
| WO2025149947A1 (en) | 2024-01-12 | 2025-07-17 | Seagen Inc. | Antibody-drug conjugates |
| WO2025174974A1 (en) * | 2024-02-14 | 2025-08-21 | Bristol-Myers Squibb Company | Anti-cd33 antibodies and uses thereof |
| CN119080935A (zh) * | 2024-10-11 | 2024-12-06 | 上海市同仁医院 | 一种抗人SMIM45-107aa单克隆抗体及其用途 |
Citations (5)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| US20020022031A1 (en) * | 2000-08-08 | 2002-02-21 | Goldenberg David M. | Immunotherapy for chronic myelocytic leukemia |
| US20070190060A1 (en) * | 2004-03-15 | 2007-08-16 | Wyeth | Passive targeting of cytotoxic agents |
| US20100158909A1 (en) * | 2006-12-01 | 2010-06-24 | Seattle Genetics, Inc. | Variant Target Binding Agents and Uses Thereof |
| US20110206700A1 (en) * | 2002-11-07 | 2011-08-25 | Immunogen Inc. | Anti-cd33 antibodies and methods for treatment of acute myeloid leukemia using the same |
| US20120082670A1 (en) * | 2010-10-04 | 2012-04-05 | Boehringer Ingelheim International Gmbh | Cd33 binding agents |
Family Cites Families (48)
| 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. |
| US4816567A (en) | 1983-04-08 | 1989-03-28 | Genentech, Inc. | Recombinant immunoglobin preparations |
| 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 |
| EP0307434B2 (en) | 1987-03-18 | 1998-07-29 | Scotgen Biopharmaceuticals, Inc. | Altered antibodies |
| 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 |
| ATE356869T1 (de) | 1990-01-12 | 2007-04-15 | 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 |
| US5877397A (en) | 1990-08-29 | 1999-03-02 | Genpharm International Inc. | Transgenic non-human animals capable of producing heterologous antibodies of various isotypes |
| US5625126A (en) | 1990-08-29 | 1997-04-29 | Genpharm International, Inc. | Transgenic 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 |
| US5661016A (en) | 1990-08-29 | 1997-08-26 | Genpharm International Inc. | Transgenic non-human animals capable of producing heterologous antibodies of various isotypes |
| US5814318A (en) | 1990-08-29 | 1998-09-29 | Genpharm International Inc. | Transgenic non-human animals for producing heterologous antibodies |
| US5545806A (en) | 1990-08-29 | 1996-08-13 | Genpharm International, Inc. | Ransgenic non-human animals for producing heterologous antibodies |
| US5789650A (en) | 1990-08-29 | 1998-08-04 | Genpharm International, Inc. | Transgenic non-human animals for producing heterologous antibodies |
| WO1993012227A1 (en) | 1991-12-17 | 1993-06-24 | Genpharm International, Inc. | Transgenic non-human animals capable of producing heterologous antibodies |
| US5633425A (en) | 1990-08-29 | 1997-05-27 | Genpharm International, Inc. | Transgenic non-human animals capable of producing heterologous antibodies |
| CA2089661C (en) | 1990-08-29 | 2007-04-03 | Nils Lonberg | Transgenic non-human animals capable of producing heterologous antibodies |
| US5874299A (en) | 1990-08-29 | 1999-02-23 | Genpharm International, Inc. | Transgenic non-human animals capable of producing heterologous antibodies |
| US5858657A (en) | 1992-05-15 | 1999-01-12 | Medical Research Council | Methods for producing members of specific binding pairs |
| DE69230142T2 (de) | 1991-05-15 | 2000-03-09 | Cambridge Antibody Technology Ltd. | Verfahren zur herstellung von spezifischen bindungspaargliedern |
| DE122004000008I1 (de) | 1991-06-14 | 2005-06-09 | Genentech Inc | Humanisierter Heregulin Antikörper. |
| US5565332A (en) | 1991-09-23 | 1996-10-15 | Medical Research Council | Production of chimeric antibodies - a combinatorial approach |
| 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 |
| 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 |
| US5834597A (en) | 1996-05-20 | 1998-11-10 | Protein Design Labs, Inc. | Mutated nonactivating IgG2 domains and anti CD3 antibodies incorporating the same |
| ATE490518T1 (de) | 1999-02-05 | 2010-12-15 | Samsung Electronics Co Ltd | Verfahren und vorrichtung zum wiederauffinden von texturbildern |
| MXPA05000511A (es) | 2001-07-12 | 2005-09-30 | Jefferson Foote | Anticuepros super humanizados. |
| PT2357006E (pt) | 2002-07-31 | 2016-01-22 | Seattle Genetics Inc | Conjugados de fármacos e sua utilização para tratamento do cancro, de uma doença autoimune ou de uma doença infeciosa |
| US7419811B2 (en) | 2003-02-28 | 2008-09-02 | The Board Of Trustees Of The University Of Illinois | Use of specifically engineered enzymes to enhance the efficacy of prodrugs |
| SG149815A1 (en) | 2003-11-06 | 2009-02-27 | Seattle Genetics Inc | Monomethylvaline compounds capable of conjugation to ligands |
| MX2007000998A (es) | 2004-07-30 | 2007-07-11 | Rinat Neuroscience Corp | Anticuerpos dirigidos peptido beta-amiloide y procedimientos que usan los mismos. |
| TR201808537T4 (tr) | 2004-09-23 | 2018-07-23 | Genentech Inc | Sistein değiştirilmiş antikorlar ve konjugatlar. |
| ES2708763T3 (es) | 2005-07-07 | 2019-04-11 | Seattle Genetics Inc | Compuestos de monometilvalina que tienen modificaciones de la cadena lateral de fenilalanina en el extremo C |
| US8871720B2 (en) | 2005-07-07 | 2014-10-28 | Seattle Genetics, Inc. | Monomethylvaline compounds having phenylalanine carboxy modifications at the C-terminus |
| US7910702B2 (en) | 2006-07-28 | 2011-03-22 | The Governors Of The University Of Alberta | Recombinant antibodies to sclerotinia antigens |
| SI2211904T1 (sl) | 2007-10-19 | 2016-12-30 | Seattle Genetics, Inc. | CD19 vezavna sredstva in njihove uporabe |
| KR101667319B1 (ko) | 2008-08-05 | 2016-10-18 | 도레이 카부시키가이샤 | 암의 치료 및 예방용 의약 조성물 |
| GB0819095D0 (en) * | 2008-10-17 | 2008-11-26 | Spirogen Ltd | Pyrrolobenzodiazepines |
| US8735552B2 (en) * | 2009-03-10 | 2014-05-27 | Gene Techno Science Co., Ltd. | Generation, expression and characterization of the humanized K33N monoclonal antibody |
| DE102009045006A1 (de) | 2009-09-25 | 2011-04-14 | Technische Universität Dresden | Anti-CD33 Antikörper und ihre Anwendung zum Immunotargeting bei der Behandlung von CD33-assoziierten Erkrankungen |
| KR101671360B1 (ko) | 2010-04-15 | 2016-11-01 | 시애틀 지네틱스, 인크. | 표적화된 피롤로벤조디아제핀 접합체 |
| US20130309223A1 (en) | 2012-05-18 | 2013-11-21 | Seattle Genetics, Inc. | CD33 Antibodies And Use Of Same To Treat Cancer |
| BR112015013444B1 (pt) * | 2012-12-13 | 2022-11-01 | Immunomedics, Inc | Uso de um imunoconjugado |
| US9610361B2 (en) | 2013-03-13 | 2017-04-04 | Seattle Genetics, Inc. | Cyclodextrin and antibody-drug conjugate formulations |
-
2013
- 2013-03-14 US US13/804,227 patent/US20130309223A1/en not_active Abandoned
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-
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- 2014-11-17 IL IL235733A patent/IL235733B/en unknown
- 2014-12-15 ZA ZA2014/09224A patent/ZA201409224B/en unknown
-
2017
- 2017-01-20 US US15/411,947 patent/US10787514B2/en active Active
-
2018
- 2018-05-17 AU AU2018203508A patent/AU2018203508C1/en not_active Ceased
-
2020
- 2020-05-22 AU AU2020203365A patent/AU2020203365B2/en not_active Ceased
- 2020-07-29 US US16/942,647 patent/US20210047404A1/en not_active Abandoned
Patent Citations (5)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| US20020022031A1 (en) * | 2000-08-08 | 2002-02-21 | Goldenberg David M. | Immunotherapy for chronic myelocytic leukemia |
| US20110206700A1 (en) * | 2002-11-07 | 2011-08-25 | Immunogen Inc. | Anti-cd33 antibodies and methods for treatment of acute myeloid leukemia using the same |
| US20070190060A1 (en) * | 2004-03-15 | 2007-08-16 | Wyeth | Passive targeting of cytotoxic agents |
| US20100158909A1 (en) * | 2006-12-01 | 2010-06-24 | Seattle Genetics, Inc. | Variant Target Binding Agents and Uses Thereof |
| US20120082670A1 (en) * | 2010-10-04 | 2012-04-05 | Boehringer Ingelheim International Gmbh | Cd33 binding agents |
Non-Patent Citations (1)
| Title |
|---|
| FELDMAN et al. "Phase III Randomized Multicenter Study of a Humanized Anti-CD33 Monoclonal Antibody, Lintuzumab, in Combination With Chemotherapy, Versus Chemotherapy Alone in Patients With Refractory or First-Relapsed Acute Myeloid Leukemia," Journal of Clinical Oncology, 20 June 2005 (20.06.2005), vol, 23, No. 18, Pgs. 4110-4116. entire document * |
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