CN109485729A - Bcma和cd3的结合分子 - Google Patents
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Cited By (1)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| CN114763383A (zh) * | 2021-01-13 | 2022-07-19 | 博生吉医药科技(苏州)有限公司 | 靶向人bcma的单克隆抗体及其应用 |
Families Citing this family (190)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| US20120034228A1 (en) * | 2008-10-01 | 2012-02-09 | Micromet Ag | CROSS-SPECIES-SPECIFIC PSCAxCD3, CD19xCD3, C-METxCD3, ENDOSIALINxCD3, EPCAMxCD3, IGF-1RxCD3 OR FAPALPHAxCD3 BISPECIFIC SINGLE CHAIN ANTIBODY |
| TWI679212B (zh) | 2011-11-15 | 2019-12-11 | 美商安進股份有限公司 | 針對ｂｃｍａ之e3以及ｃｄ３的結合分子 |
| ES2812849T3 (es) | 2012-02-24 | 2021-03-18 | Abbvie Stemcentrx Llc | Anticuerpos anti-DLL3 y procedimientos de utilización de los mismos |
| US9243058B2 (en) | 2012-12-07 | 2016-01-26 | Amgen, Inc. | BCMA antigen binding proteins |
| TW201425336A (zh) | 2012-12-07 | 2014-07-01 | Amgen Inc | Ｂｃｍａ抗原結合蛋白質 |
| JP2016507523A (ja) | 2013-02-05 | 2016-03-10 | エンクマフ アーゲー | ＣＤ３εおよびＢＣＭＡに対する二重特異的抗体 |
| EP2762496A1 (en) * | 2013-02-05 | 2014-08-06 | EngMab AG | Method for the selection of antibodies against BCMA |
| ES2731681T3 (es) | 2013-02-22 | 2019-11-18 | Abbvie Stemcentrx Llc | Conjugados de anticuerpo anti-DLL3 y PBD y usos de los mismos |
| AR095374A1 (es) * | 2013-03-15 | 2015-10-14 | Amgen Res Munich Gmbh | Moléculas de unión para bcma y cd3 |
| AU2014312215B2 (en) | 2013-08-28 | 2020-02-27 | Abbvie Stemcentrx Llc | Site-specific antibody conjugation methods and compositions |
| US10808026B2 (en) | 2013-10-09 | 2020-10-20 | Research Development Foundation | Monoclonal Olfml-3 antibodies and uses thereof |
| GB201317928D0 (en) | 2013-10-10 | 2013-11-27 | Ucl Business Plc | Molecule |
| GB201317929D0 (en) | 2013-10-10 | 2013-11-27 | Ucl Business Plc | Chimeric antigen receptor |
| MX379210B (es) | 2014-02-07 | 2025-03-10 | Univ Mcmaster | Acoplador trifuncional de antígeno de células t y métodos y usos del mismo. |
| EP3107576A4 (en) | 2014-02-21 | 2017-09-06 | Abbvie Stemcentrx LLC | Anti-dll3 antibodies and drug conjugates for use in melanoma |
| ES2737690T3 (es) | 2014-02-27 | 2020-01-15 | Ucl Business Ltd | Variantes de APRIL |
| CA2945620C (en) * | 2014-04-14 | 2022-12-06 | Cellectis | Bcma (cd269) specific chimeric antigen receptors for cancer immunotherapy |
| US9884921B2 (en) | 2014-07-01 | 2018-02-06 | Pfizer Inc. | Bispecific heterodimeric diabodies and uses thereof |
| EP2982692A1 (en) * | 2014-08-04 | 2016-02-10 | EngMab AG | Bispecific antibodies against CD3epsilon and BCMA |
| CA2963696A1 (en) * | 2014-10-09 | 2016-04-14 | Engmab Ag | Bispecific antibodies against cd3epsilon and ror1 for use in the treatment of ovarian cancer |
| RS60615B1 (sr) | 2014-11-20 | 2020-08-31 | Hoffmann La Roche | Zajednički laki lanci i postupci upotrebe |
| SG11201702976TA (en) | 2014-11-20 | 2017-05-30 | Hoffmann La Roche | T cell activating bispecific antigen binding molecules agiant folr1 and cd3 |
| EP3023437A1 (en) * | 2014-11-20 | 2016-05-25 | EngMab AG | Bispecific antibodies against CD3epsilon and BCMA |
| EP3029068A1 (en) * | 2014-12-03 | 2016-06-08 | EngMab AG | Bispecific antibodies against CD3epsilon and BCMA for use in the treatment of diseases |
| HUE053995T2 (hu) | 2014-12-05 | 2021-08-30 | Memorial Sloan Kettering Cancer Center | B-sejt-érési antigént célzó antitestek és alkalmazási eljárások |
| ES2966099T3 (es) * | 2014-12-05 | 2024-04-18 | Memorial Sloan Kettering Cancer Center | Receptores de antígeno quiméricos dirigidos al antígeno de maduración de células B y usos de los mismos |
| AU2016222746A1 (en) * | 2015-02-24 | 2017-09-07 | The University Of British Columbia | Continuous flow microfluidic system |
| RU2706582C2 (ru) | 2015-04-13 | 2019-11-19 | Пфайзер Инк. | Химерные антигенные рецепторы, нацеленные на антиген созревания B-клеток |
| MX2017013297A (es) | 2015-04-13 | 2018-06-19 | Pfizer | Anticuerpos terapeuticos y sus usos. |
| CN119219778A (zh) * | 2015-05-13 | 2024-12-31 | 埃博灵克斯股份有限公司 | 基于cd3反应性的t细胞募集多肽 |
| EP3466967A1 (en) * | 2015-05-18 | 2019-04-10 | TCR2 Therapeutics Inc. | Compositions and methods for tcr reprogramming using fusion proteins |
| KR20190080992A (ko) | 2015-05-21 | 2019-07-08 | 하푼 테라퓨틱스, 인크. | 삼중특이성 결합 단백질 및 사용 방법 |
| TWI796283B (zh) | 2015-07-31 | 2023-03-21 | 德商安美基研究（慕尼黑）公司 | Ｍｓｌｎ及ｃｄ３抗體構築體 |
| EA039859B1 (ru) | 2015-07-31 | 2022-03-21 | Эмджен Рисерч (Мюник) Гмбх | Биспецифические конструкты антител, связывающие egfrviii и cd3 |
| TWI829617B (zh) | 2015-07-31 | 2024-01-21 | 德商安美基研究（慕尼黑）公司 | Ｆｌｔ３及ｃｄ３抗體構築體 |
| TWI744242B (zh) * | 2015-07-31 | 2021-11-01 | 德商安美基研究（慕尼黑）公司 | Egfrviii及cd3抗體構築體 |
| CN108350073B (zh) * | 2015-08-03 | 2022-03-18 | 英格玛布有限责任公司 | 针对bcma的单克隆抗体 |
| NZ739721A (en) | 2015-08-07 | 2019-09-27 | Imaginab Inc | Antigen binding constructs to target molecules |
| CN105384825B (zh) | 2015-08-11 | 2018-06-01 | 南京传奇生物科技有限公司 | 一种基于单域抗体的双特异性嵌合抗原受体及其应用 |
| PT3337824T (pt) * | 2015-08-17 | 2020-09-10 | Janssen Pharmaceutica Nv | Anticorpos anti-bcma, moléculas de ligação a antigénio biespecíficas que ligam bcma e cd3, e suas utilizações |
| AU2016325858B2 (en) | 2015-09-24 | 2022-05-26 | Daiichi Sankyo Company, Limited | Anti-GARP antibody |
| CN109089419B (zh) | 2015-11-25 | 2024-03-01 | 威特拉公司 | April的抗体分子及其应用 |
| JOP20170017B1 (ar) * | 2016-01-25 | 2021-08-17 | Amgen Res Munich Gmbh | تركيب صيدلي يتضمن تركيبات جسم مضاد ثنائي الاختصاص |
| IL313507A (en) | 2016-02-03 | 2024-08-01 | Amgen Res Munich Gmbh | Constructs of bispecific antibodies to BCMA and CD3 that bind to T cells, preparations containing the same and uses thereof |
| IL260920B (en) | 2016-02-03 | 2022-09-01 | Amgen Res Munich Gmbh | Constructs of psma and cd3 bispecific antigens that bind to t-cells, preparations containing them and uses thereof |
| LT3433280T (lt) | 2016-03-22 | 2023-07-10 | F. Hoffmann-La Roche Ag | Proteazės aktyvuojamos t ląstelei bispecifinės molekulės |
| TWI761831B (zh) * | 2016-04-01 | 2022-04-21 | 美商凱特製藥公司 | 嵌合抗原受體（ｃａｒ）和ｔ細胞受體（ｔｃｒ）及彼等之用途 |
| US10550184B2 (en) | 2016-04-11 | 2020-02-04 | The Trustees Of Columbia University In The City Of New York | Humanized anti-rage antibody |
| US11623958B2 (en) | 2016-05-20 | 2023-04-11 | Harpoon Therapeutics, Inc. | Single chain variable fragment CD3 binding proteins |
| PL3461261T3 (pl) | 2016-05-20 | 2025-11-12 | Harpoon Therapeutics, Inc. | Białka wiążące jednołańcuchowy fragment zmienny CD3 |
| EP3493844A4 (en) | 2016-05-20 | 2021-03-24 | Harpoon Therapeutics Inc. | SINGLE DOMAIN SERUM ALBUMIN BINDING PROTEIN |
| KR20190053835A (ko) | 2016-06-21 | 2019-05-20 | 테네오바이오, 인코포레이티드 | Cd3 결합 항체 |
| WO2018014260A1 (en) * | 2016-07-20 | 2018-01-25 | Nanjing Legend Biotech Co., Ltd. | Multispecific antigen binding proteins and methods of use thereof |
| AU2017306432A1 (en) | 2016-08-02 | 2019-03-21 | TCR2 Therapeutics Inc. | Compositions and methods for TCR reprogramming using fusion proteins |
| CN114395048B (zh) * | 2016-09-14 | 2025-01-28 | 特纳奥尼股份有限公司 | Cd3结合抗体 |
| BR112019007100A2 (pt) | 2016-10-07 | 2019-06-25 | Tcr2 Therapeutics Inc | composições e métodos para reprogramação de receptores de célula t com o uso de proteínas de fusão |
| WO2018068201A1 (en) | 2016-10-11 | 2018-04-19 | Nanjing Legend Biotech Co., Ltd. | Single-domain antibodies and variants thereof against ctla-4 |
| EP4295918A3 (en) * | 2016-11-02 | 2024-03-20 | Bristol-Myers Squibb Company | Bispecific antibody against bcma and cd3 and an immunological drug for combined use in treating multiple myeloma |
| US20190352409A1 (en) * | 2016-11-11 | 2019-11-21 | Autolus Limited | Chimeric antigen receptor |
| CA3044593A1 (en) | 2016-11-22 | 2018-05-31 | TCR2 Therapeutics Inc. | Compositions and methods for tcr reprogramming using fusion proteins |
| MX2019006045A (es) | 2016-11-23 | 2019-11-11 | Harpoon Therapeutics Inc | Proteinas triespecificas dirigidas a psma y metodos de uso. |
| KR20210087108A (ko) | 2016-11-23 | 2021-07-09 | 하푼 테라퓨틱스, 인크. | 전립선 특이 막 항원 결합 단백질 |
| AU2017366739B2 (en) | 2016-12-02 | 2023-11-23 | Angeles Therapeutics, Inc. | Synthetic immune receptors and methods of use thereof |
| CN116284402A (zh) | 2016-12-21 | 2023-06-23 | 特尼奥生物股份有限公司 | 仅有重链的抗bcma抗体 |
| JP2020506700A (ja) | 2017-01-31 | 2020-03-05 | ノバルティス アーゲー | 多重特異性を有するキメラｔ細胞受容体タンパク質を用いた癌の治療 |
| SG11201907253VA (en) * | 2017-02-10 | 2019-09-27 | Dragonfly Therapeutics Inc | Proteins binding bcma, nkg2d and cd16 |
| WO2018151836A1 (en) | 2017-02-17 | 2018-08-23 | Fred Hutchinson Cancer Research Center | Combination therapies for treatment of bcma-related cancers and autoimmune disorders |
| US11535668B2 (en) | 2017-02-28 | 2022-12-27 | Harpoon Therapeutics, Inc. | Inducible monovalent antigen binding protein |
| AU2018228719B2 (en) | 2017-02-28 | 2023-03-30 | Affimed Gmbh | Tandem diabody for CD16A-directed NK-cell engagement |
| EP3615068A1 (en) | 2017-04-28 | 2020-03-04 | Novartis AG | Bcma-targeting agent, and combination therapy with a gamma secretase inhibitor |
| WO2018201056A1 (en) | 2017-04-28 | 2018-11-01 | Novartis Ag | Cells expressing a bcma-targeting chimeric antigen receptor, and combination therapy with a gamma secretase inhibitor |
| SG10202107880XA (en) | 2017-05-12 | 2021-09-29 | Harpoon Therapeutics Inc | Mesothelin binding proteins |
| CA3063362A1 (en) | 2017-05-12 | 2018-11-15 | Harpoon Therapeutics, Inc. | Msln targeting trispecific proteins and methods of use |
| CA3065951A1 (en) | 2017-06-20 | 2018-12-27 | Teneoone, Inc. | Anti-bcma heavy chain-only antibodies |
| KR102742528B1 (ko) | 2017-06-20 | 2024-12-16 | 테네오바이오, 인코포레이티드 | 항-bcma 중쇄-단독 항체 |
| WO2019000223A1 (en) * | 2017-06-27 | 2019-01-03 | Nanjing Legend Biotech Co., Ltd. | ENABLERS OF IMMUNE EFFECTOR CELLS OF CHIMERIC ANTIBODIES AND METHODS OF USE THEREOF |
| TN2020000015A1 (en) | 2017-08-03 | 2021-10-04 | Amgen Inc | Interleukin-21 muteins and methods of treatment |
| WO2019035938A1 (en) | 2017-08-16 | 2019-02-21 | Elstar Therapeutics, Inc. | MULTISPECIFIC MOLECULES BINDING TO BCMA AND USES THEREOF |
| HRP20240485T1 (hr) | 2017-08-24 | 2024-07-05 | Novo Nordisk A/S | Pripravci glp-1 i njihova upotreba |
| EP4403175A3 (en) | 2017-09-08 | 2024-10-02 | Amgen Inc. | Inhibitors of kras g12c and methods of using the same |
| WO2019053613A2 (en) | 2017-09-14 | 2019-03-21 | Glaxosmithkline Intellectual Property Development Limited | POLY THERAPY FOR THE TREATMENT OF CANCER |
| CN118557697A (zh) | 2017-09-14 | 2024-08-30 | 葛兰素史密斯克莱知识产权发展有限公司 | 用于癌症的组合治疗 |
| EP3694878A1 (en) | 2017-09-14 | 2020-08-19 | GlaxoSmithKline Intellectual Property Development Limited | Combination treatment for cancer |
| WO2019071358A1 (en) | 2017-10-12 | 2019-04-18 | Mcmaster University | Y182T MUTATION T CELL ANTIGEN COUPLEUR AND METHODS AND USES THEREOF |
| PL3694529T3 (pl) | 2017-10-13 | 2024-12-16 | Harpoon Therapeutics, Inc. | Trójswoiste białka i sposoby zastosowania |
| IL315737A (en) | 2017-10-13 | 2024-11-01 | Harpoon Therapeutics Inc | B-cell maturation antigen-binding proteins |
| CA3079407A1 (en) | 2017-10-18 | 2019-04-25 | Novartis Ag | Compositions and methods for selective protein degradation |
| WO2019089969A2 (en) | 2017-11-01 | 2019-05-09 | Juno Therapeutics, Inc. | Antibodies and chimeric antigen receptors specific for b-cell maturation antigen |
| WO2019090003A1 (en) | 2017-11-01 | 2019-05-09 | Juno Therapeutics, Inc. | Chimeric antigen receptors specific for b-cell maturation antigen (bcma) |
| SG11202003427XA (en) | 2017-11-06 | 2020-05-28 | Juno Therapeutics Inc | Combination of a cell therapy and a gamma secretase inhibitor |
| AU2018369883A1 (en) | 2017-11-15 | 2020-05-28 | Novartis Ag | BCMA-targeting chimeric antigen receptor, CD19-targeting chimeric antigen receptor, and combination therapies |
| SG11202005005YA (en) | 2017-11-30 | 2020-06-29 | Novartis Ag | Bcma-targeting chimeric antigen receptor, and uses thereof |
| UA128757C2 (uk) | 2017-12-22 | 2024-10-16 | Тенеобіо, Інк. | Антитіла, які містять тільки важкі ланцюги, що зв'язуються з cd22 |
| MX2020006715A (es) * | 2017-12-27 | 2020-08-20 | Teneobio Inc | Anticuerpos especificos del heterodimero de cd3-delta/epsilon. |
| JP7369127B2 (ja) | 2017-12-28 | 2023-10-25 | ナンジン レジェンド バイオテック カンパニー，リミテッド | Ｔｉｇｉｔに対する単一ドメイン抗体及びその変異体 |
| EP3737408A1 (en) | 2018-01-08 | 2020-11-18 | Novartis AG | Immune-enhancing rnas for combination with chimeric antigen receptor therapy |
| WO2019139987A1 (en) | 2018-01-09 | 2019-07-18 | Elstar Therapeutics, Inc. | Calreticulin binding constructs and engineered t cells for the treatment of diseases |
| SG11202005605SA (en) | 2018-01-12 | 2020-07-29 | Amgen Inc | Anti-pd-1 antibodies and methods of treatment |
| KR102839330B1 (ko) | 2018-01-15 | 2025-07-30 | 난징 레전드 바이오테크 씨오., 엘티디. | Pd-1에 대한 단일-도메인 항체 및 이의 변이체 |
| BR112020014929A2 (pt) * | 2018-01-23 | 2020-12-08 | Nextcure, Inc. | Composição farmacêutica, métodos para aumentar, para reduzir, para intensificar ou induzir uma resposta imune em um indivíduo, molécula, anticorpo monoclonal ou fragmento de ligação ao antígeno do mesmo, ácido nucleico, anticorpo monoclonal anti-b7h4 ou fragmento de ligação ao antígeno do mesmo, anticorpo anti-b7h4 ou fragmento de ligação ao antígeno do mesmo, cadeias leve e pesada de anticorpo anti-b7h4, e, cadeias leve e pesada de anticorpo |
| AU2019215031B2 (en) | 2018-01-31 | 2025-10-09 | Novartis Ag | Combination therapy using a chimeric antigen receptor |
| US20200399383A1 (en) | 2018-02-13 | 2020-12-24 | Novartis Ag | Chimeric antigen receptor therapy in combination with il-15r and il15 |
| CA3089230A1 (en) | 2018-03-02 | 2019-09-06 | Cdr-Life Ag | Trispecific antigen binding proteins |
| WO2019178362A1 (en) | 2018-03-14 | 2019-09-19 | Elstar Therapeutics, Inc. | Multifunctional molecules that bind to calreticulin and uses thereof |
| CN116836297A (zh) * | 2018-04-12 | 2023-10-03 | 上海赛比曼生物科技有限公司 | 靶向bcma的嵌合抗原受体及其制法和应用 |
| KR20200143436A (ko) * | 2018-04-13 | 2020-12-23 | 아피메트 게엠베하 | Nk 세포 결합 항체 융합 구조체 |
| MX2020012217A (es) | 2018-05-14 | 2021-03-02 | Harpoon Therapeutics Inc | Porción de unión para activación condicional de moléculas de inmunoglobulina. |
| JOP20200292A1 (ar) | 2018-05-16 | 2020-11-15 | Stichting Vumc | Bcma / cd3 و gprdc5d / cd3 مضادات غير محددة للاستخدام في علاج السرطان |
| JP7398396B2 (ja) | 2018-06-01 | 2023-12-14 | ノバルティス アーゲー | Ｂｃｍａに対する結合分子及びその使用 |
| US12371497B2 (en) | 2018-06-08 | 2025-07-29 | Imaginab, Inc. | Antigen binding constructs to CD4 |
| AU2019297451A1 (en) | 2018-07-03 | 2021-01-28 | Marengo Therapeutics, Inc. | Anti-TCR antibody molecules and uses thereof |
| US11110123B2 (en) | 2018-07-17 | 2021-09-07 | Triumvira Immunologics Usa, Inc. | T cell-antigen coupler with various construct optimizations |
| WO2020018825A1 (en) | 2018-07-19 | 2020-01-23 | Regeneron Pharmaceuticals, Inc. | Chimeric antigen receptors with bcma specificity and uses thereof |
| TWI838389B (zh) | 2018-07-19 | 2024-04-11 | 美商再生元醫藥公司 | 雙特異性抗-BCMAｘ抗-CD3抗體及其用途 |
| CN116769032A (zh) | 2018-07-20 | 2023-09-19 | 坦尼奥第二公司 | 与cd19结合的重链抗体 |
| CA3105729A1 (en) * | 2018-07-31 | 2020-02-06 | Amgen Research (Munich) Gmbh | Dosing regimen for bcma-cd3 bispecific antibodies |
| EP3833392A4 (en) | 2018-08-08 | 2022-05-18 | Dragonfly Therapeutics, Inc. | Multi-specific binding proteins that bind bcma, nkg2d and cd16, and methods of use |
| MY204234A (en) | 2018-08-27 | 2024-08-16 | Regeneron Pharma | Use of raman spectroscopy in downstream purification |
| JP2021534779A (ja) * | 2018-08-27 | 2021-12-16 | アフィメッド ゲゼルシャフト ミット ベシュレンクテル ハフツンク | 抗体構築物がプレロードされた凍結保存ｎｋ細胞 |
| WO2020047452A2 (en) | 2018-08-31 | 2020-03-05 | Novartis Ag | Methods of making chimeric antigen receptor-expressing cells |
| US20210171909A1 (en) | 2018-08-31 | 2021-06-10 | Novartis Ag | Methods of making chimeric antigen receptor?expressing cells |
| DK3844189T3 (da) | 2018-08-31 | 2025-02-24 | Regeneron Pharma | Doseringsstrategi, der mindsker cytokinfrigivelsessyndrom for CD3/CD20-bispecifikke antistoffer |
| US12195544B2 (en) | 2018-09-21 | 2025-01-14 | Harpoon Therapeutics, Inc. | EGFR binding proteins and methods of use |
| CN113286817B (zh) | 2018-09-25 | 2025-01-28 | 哈普恩治疗公司 | Dll3结合蛋白及使用方法 |
| US11505614B2 (en) * | 2018-09-28 | 2022-11-22 | Amgen Inc. | Antibodies binding to soluble BCMA |
| CN109503716B (zh) * | 2018-10-08 | 2021-04-27 | 浙江生研生物科技有限公司 | 一种双特异性嵌合抗原受体分子及其在肿瘤治疗上的应用 |
| JP2022509454A (ja) | 2018-10-31 | 2022-01-20 | グラクソスミスクライン、インテレクチュアル、プロパティー、ディベロップメント、リミテッド | 癌の処置法 |
| KR20210113169A (ko) | 2018-11-01 | 2021-09-15 | 주노 쎄러퓨티크스 인코퍼레이티드 | Β세포 성숙 항원에 특이적인 키메라 항원 수용체를 이용한 치료 방법 |
| JP7410143B2 (ja) * | 2018-11-01 | 2024-01-09 | 山▲東▼新▲時▼代▲薬▼▲業▼有限公司 | 二重特異性抗体及びその用途 |
| AU2020224681A1 (en) | 2019-02-21 | 2021-09-16 | Marengo Therapeutics, Inc. | Antibody molecules that bind to NKp30 and uses thereof |
| GB2599228B (en) | 2019-02-21 | 2024-02-07 | Marengo Therapeutics Inc | Multifunctional molecules that bind to T cell related cancer cells and uses thereof |
| EP3930763A1 (en) | 2019-02-25 | 2022-01-05 | Novartis AG | Mesoporous silica particles compositions for viral delivery |
| PH12021552123A1 (en) | 2019-03-21 | 2022-08-22 | Regeneron Pharma | Combination of il-4/il-13 pathway inhibitors and plasma cell ablation for treating allergy |
| EP3942025A1 (en) | 2019-03-21 | 2022-01-26 | Novartis AG | Car-t cell therapies with enhanced efficacy |
| MX2021012205A (es) | 2019-04-05 | 2022-02-21 | Teneobio Inc | Anticuerpos de cadena pesada que se unen al psma. |
| EP3953455A1 (en) | 2019-04-12 | 2022-02-16 | Novartis AG | Methods of making chimeric antigen receptor-expressing cells |
| US20220251152A1 (en) | 2019-04-24 | 2022-08-11 | Novartis Ag | Compositions and methods for selective protein degradation |
| EP3972998A1 (en) | 2019-05-21 | 2022-03-30 | Novartis AG | Cd19 binding molecules and uses thereof |
| JP7665538B2 (ja) | 2019-06-14 | 2025-04-21 | テネオバイオ， インコーポレイテッド | Ｃｄ２２及びｃｄ３に結合する多重特異性重鎖抗体 |
| CN110229232B (zh) | 2019-06-19 | 2020-05-19 | 北京智仁美博生物科技有限公司 | 双特异性抗体及其用途 |
| AU2020307471A1 (en) * | 2019-06-24 | 2022-01-27 | Novartis Ag | Dosing regimen and combination therapies for multispecific antibodies targeting B-cell maturation antigen |
| CN112204135A (zh) * | 2019-07-06 | 2021-01-08 | 苏州克睿基因生物科技有限公司 | 一种表达cd3抗体受体复合物的免疫细胞及其用途 |
| WO2021004400A1 (zh) * | 2019-07-06 | 2021-01-14 | 苏州克睿基因生物科技有限公司 | 一种表达cd3抗体受体复合物的免疫细胞及其用途 |
| CN120204384A (zh) | 2019-08-06 | 2025-06-27 | 葛兰素史密斯克莱知识产权发展有限公司 | 生物药物组合物和相关方法 |
| EP4034638A4 (en) * | 2019-09-25 | 2024-07-17 | Fate Therapeutics, Inc. | MULTIPLE TARGETED EFFECTOR CELLS AND THEIR USE |
| US12479922B2 (en) * | 2019-10-10 | 2025-11-25 | Cytolynx Therapeutics Hong Kong Limited | Humanized monoclonal antibody targeting BCMA and having human monkey cross-reactivity |
| SMT202400373T1 (it) | 2019-11-11 | 2024-11-15 | Amgen Inc | Regime di dosaggio per agenti anti-bcma |
| EP4065158A2 (en) | 2019-11-26 | 2022-10-05 | Novartis AG | Chimeric antigen receptors binding bcma and cd19 and uses thereof |
| JP2023509708A (ja) | 2020-01-03 | 2023-03-09 | マレンゴ・セラピューティクス，インコーポレーテッド | 抗ｔｃｒ抗体分子およびその使用 |
| MX2022009844A (es) | 2020-02-18 | 2022-09-05 | Novo Nordisk As | Composiciones y usos del peptido similar al glucagon-1 (glp-1). |
| KR20220144841A (ko) | 2020-02-21 | 2022-10-27 | 하푼 테라퓨틱스, 인크. | Flt3 결합 단백질 및 사용 방법 |
| CN115175695A (zh) | 2020-02-27 | 2022-10-11 | 诺华股份有限公司 | 制备表达嵌合抗原受体的细胞的方法 |
| WO2021173995A2 (en) | 2020-02-27 | 2021-09-02 | Novartis Ag | Methods of making chimeric antigen receptor-expressing cells |
| JP7750852B2 (ja) | 2020-03-19 | 2025-10-07 | アムジエン・インコーポレーテツド | ムチン１７に対する抗体及びその使用 |
| UY40003A (es) | 2020-04-29 | 2023-03-31 | Teneobio Inc | Anticuerpos de cadena pesada multiespecíficos con regiones constantes de cadena pesada modificadas |
| EP4186564A1 (en) | 2020-04-29 | 2023-05-31 | Teneoone, Inc. | Multispecific heavy chain antibodies with modified heavy chain constant regions |
| MX2022014166A (es) | 2020-05-11 | 2022-12-02 | Janssen Biotech Inc | Metodos para tratar el mieloma multiple. |
| WO2021234560A1 (en) | 2020-05-19 | 2021-11-25 | Janssen Biotech, Inc. | Compositions comprising a t cell redirection therapeutic and a vla-4 adhesion pathway inhibitor |
| KR20230024967A (ko) | 2020-06-11 | 2023-02-21 | 노파르티스 아게 | Zbtb32 억제제 및 이의 용도 |
| CA3189297A1 (en) | 2020-06-30 | 2022-01-06 | Nathan Trinklein | Multi-specific antibodies binding to bcma |
| MX2023002107A (es) | 2020-08-21 | 2023-03-15 | Novartis Ag | Composiciones y metodos para la generacion in vivo de celulas que expresan car. |
| MX2023003041A (es) | 2020-09-16 | 2023-05-09 | Amgen Inc | Métodos para administrar dosis terapéuticas de moléculas de acoplamiento a células t biespecíficas para el tratamiento de cáncer. |
| WO2022103781A1 (en) | 2020-11-10 | 2022-05-19 | Amgen Inc. | Methods for administering a bcma x cd3 binding molecule |
| CN114573703A (zh) * | 2020-12-02 | 2022-06-03 | 康诺亚生物医药科技（成都）有限公司 | 一种t细胞衔接器治疗剂的开发和应用 |
| WO2022135468A1 (zh) * | 2020-12-23 | 2022-06-30 | 信达生物制药(苏州)有限公司 | 抗bcma×cd3双特异性抗体及其用途 |
| HRP20250696T1 (hr) | 2021-01-28 | 2025-08-01 | Regeneron Pharmaceuticals, Inc. | Sastavi i postupci za liječenje sindroma oslobađanja citokina |
| WO2022216993A2 (en) | 2021-04-08 | 2022-10-13 | Marengo Therapeutics, Inc. | Multifuntional molecules binding to tcr and uses thereof |
| EP4330381A1 (en) | 2021-04-27 | 2024-03-06 | Novartis AG | Viral vector production system |
| JP2024521187A (ja) | 2021-05-28 | 2024-05-28 | グラクソスミスクライン、インテレクチュアル、プロパティー、ディベロップメント、リミテッド | ガンの治療のための組み合わせ療法 |
| US12016923B2 (en) | 2021-06-01 | 2024-06-25 | Triumvira Immunologics Usa, Inc. | Claudin 18.2 T cell-antigen couplers and uses thereof |
| CN119569887A (zh) * | 2021-06-24 | 2025-03-07 | 益科思特(北京)医药科技发展有限公司 | 结合bcma和cd3的双特异性抗体及其制备方法与应用 |
| US11453723B1 (en) | 2021-06-25 | 2022-09-27 | Mcmaster University | BCMA T cell-antigen couplers and uses thereof |
| WO2023012669A2 (en) | 2021-08-03 | 2023-02-09 | Glaxosmithkline Intellectual Property Development Limited | Biopharmaceutical compositions and stable isotope labeling peptide mapping method |
| TW202323521A (zh) | 2021-08-20 | 2023-06-16 | 瑞士商諾華公司 | 製備表現嵌合抗原受體的細胞之方法 |
| EP4412713A1 (en) | 2021-10-05 | 2024-08-14 | GlaxoSmithKline Intellectual Property Development Ltd | Combination therapies for treating cancer |
| IL312503A (en) | 2021-11-03 | 2024-07-01 | Janssen Biotech Inc | Methods of treating cancers and enhancing efficacy of bcmaxcd3 bispecific antibodies |
| CN118591560A (zh) | 2022-01-25 | 2024-09-03 | 葛兰素史密斯克莱知识产权发展有限公司 | 癌症的组合疗法 |
| AU2023254191A1 (en) | 2022-04-11 | 2024-10-17 | Regeneron Pharmaceuticals, Inc. | Compositions and methods for universal tumor cell killing |
| AU2023369684A1 (en) | 2022-10-26 | 2025-04-17 | Novartis Ag | Lentiviral formulations |
| WO2024121711A1 (en) | 2022-12-05 | 2024-06-13 | Glaxosmithkline Intellectual Property Development Limited | Methods of treatment using b-cell maturation antigen antagonists |
| WO2024173830A2 (en) | 2023-02-17 | 2024-08-22 | Regeneron Pharmaceuticals, Inc. | Induced nk cells responsive to cd3/taa bispecific antibodies |
| US12173081B2 (en) | 2023-03-21 | 2024-12-24 | Biograph 55, Inc. | CD19/CD38 multispecific antibodies |
| CN120641113A (zh) | 2023-03-31 | 2025-09-12 | 西比曼生物科技集团 | 靶向cd20和bcma的双特异性嵌合抗原受体 |
| CN121039153A (zh) * | 2023-04-11 | 2025-11-28 | 西比曼生物科技集团 | 靶向bcma和cd19的双特异性嵌合抗原受体 |
| WO2024246086A1 (en) | 2023-06-01 | 2024-12-05 | F. Hoffmann-La Roche Ag | Immunostimulatory antigen binding molecules that specifically bind to bcma |
| WO2024246083A1 (en) | 2023-06-01 | 2024-12-05 | F. Hoffmann-La Roche Ag | Bispecific antibodies targeting bcma and cd28 |
| WO2025160340A2 (en) | 2024-01-26 | 2025-07-31 | Regeneron Pharmaceuticals, Inc. | Combination immunosuppression for inhibiting an immune response and enabling immunogen administration and re-administration |
| US20250242056A1 (en) | 2024-01-26 | 2025-07-31 | Regeneron Pharmaceuticals, Inc. | Methods and compositions for using plasma cell depleting agents and/or b cell depleting agents to suppress host anti-aav antibody response and enable aav transduction and re-dosing |
| US20250262300A1 (en) | 2024-02-16 | 2025-08-21 | Kite Pharma, Inc. | Systems, methods, and kits for generating and administering engineered t cells and cd38 targeting compounds as a combination therapy |
| WO2025184567A1 (en) | 2024-03-01 | 2025-09-04 | Regeneron Pharmaceuticals, Inc. | Methods and compositions for re-dosing aav using anti-cd40 antagonistic antibody to suppress host anti-aav antibody response |
Citations (5)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| US20080213256A1 (en) * | 2004-02-16 | 2008-09-04 | Micromet Ag | Less Immunogenic Binding Molecules |
| CN101370830A (zh) * | 2005-09-26 | 2009-02-18 | 米德列斯公司 | 抗cd70的人单克隆抗体 |
| US20090325196A1 (en) * | 2008-04-25 | 2009-12-31 | Zymogenetics, Inc. | Levels of bcma protein expression on b cells and use in diagnostic methods |
| CN101675077A (zh) * | 2007-04-03 | 2010-03-17 | 米克罗麦特股份公司 | 跨种特异性的双特异性结合剂 |
| US20110275787A1 (en) * | 2008-10-01 | 2011-11-10 | Microment AG | Cross-species-specific single domain bispecific single chain antibody |
Family Cites Families (210)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| US556A (en) | 1838-01-09 | Machine foe | ||
| US2003A (en) | 1841-03-12 | Improvement in horizontal windivhlls | ||
| US70185A (en) | 1867-10-29 | fan oh be | ||
| US567A (en) | 1838-01-09 | Machine for r-uibbii | ||
| US1985A (en) | 1841-02-18 | Charles m | ||
| US4816A (en) | 1846-10-17 | Bell machinery for hotels | ||
| US5013A (en) | 1847-03-13 | Improvement in apparatus for the manufacture of malleable iron | ||
| US3773919A (en) | 1969-10-23 | 1973-11-20 | Du Pont | Polylactide-drug mixtures |
| US3691016A (en) | 1970-04-17 | 1972-09-12 | Monsanto Co | Process for the preparation of insoluble enzymes |
| CA1023287A (en) | 1972-12-08 | 1977-12-27 | Boehringer Mannheim G.M.B.H. | Process for the preparation of carrier-bound proteins |
| US4179337A (en) | 1973-07-20 | 1979-12-18 | Davis Frank F | Non-immunogenic polypeptides |
| US4195128A (en) | 1976-05-03 | 1980-03-25 | Bayer Aktiengesellschaft | Polymeric carrier bound ligands |
| US4330440A (en) | 1977-02-08 | 1982-05-18 | Development Finance Corporation Of New Zealand | Activated matrix and method of activation |
| CA1093991A (en) | 1977-02-17 | 1981-01-20 | Hideo Hirohara | Enzyme immobilization with pullulan gel |
| US4229537A (en) | 1978-02-09 | 1980-10-21 | New York University | Preparation of trichloro-s-triazine activated supports for coupling ligands |
| US4263428A (en) | 1978-03-24 | 1981-04-21 | The Regents Of The University Of California | Bis-anthracycline nucleic acid function inhibitors and improved method for administering the same |
| JPS6023084B2 (ja) | 1979-07-11 | 1985-06-05 | 味の素株式会社 | 代用血液 |
| US4281061A (en) | 1979-07-27 | 1981-07-28 | Syva Company | Double antibody for enhanced sensitivity in immunoassay |
| IE52535B1 (en) | 1981-02-16 | 1987-12-09 | Ici Plc | Continuous release pharmaceutical compositions |
| US4447233A (en) | 1981-04-10 | 1984-05-08 | Parker-Hannifin Corporation | Medication infusion pump |
| US4485045A (en) | 1981-07-06 | 1984-11-27 | Research Corporation | Synthetic phosphatidyl cholines useful in forming liposomes |
| US4640835A (en) | 1981-10-30 | 1987-02-03 | Nippon Chemiphar Company, Ltd. | Plasminogen activator derivatives |
| EP0088046B1 (de) | 1982-02-17 | 1987-12-09 | Ciba-Geigy Ag | Lipide in wässriger Phase |
| US4475916A (en) | 1982-03-18 | 1984-10-09 | Merck & Co., Inc. | Osmotic drug delivery system |
| US4439196A (en) | 1982-03-18 | 1984-03-27 | Merck & Co., Inc. | Osmotic drug delivery system |
| US4447224A (en) | 1982-09-20 | 1984-05-08 | Infusaid Corporation | Variable flow implantable infusion apparatus |
| US4487603A (en) | 1982-11-26 | 1984-12-11 | Cordis Corporation | Implantable microinfusion pump system |
| GB8308235D0 (en) | 1983-03-25 | 1983-05-05 | Celltech Ltd | Polypeptides |
| US4816567A (en) | 1983-04-08 | 1989-03-28 | Genentech, Inc. | Recombinant immunoglobin preparations |
| US4486194A (en) | 1983-06-08 | 1984-12-04 | James Ferrara | Therapeutic device for administering medicaments through the skin |
| US4544545A (en) | 1983-06-20 | 1985-10-01 | Trustees University Of Massachusetts | Liposomes containing modified cholesterol for organ targeting |
| HUT35524A (en) | 1983-08-02 | 1985-07-29 | Hoechst Ag | Process for preparing pharmaceutical compositions containing regulatory /regulative/ peptides providing for the retarded release of the active substance |
| EP0143949B1 (en) | 1983-11-01 | 1988-10-12 | TERUMO KABUSHIKI KAISHA trading as TERUMO CORPORATION | Pharmaceutical composition containing urokinase |
| US4496689A (en) | 1983-12-27 | 1985-01-29 | Miles Laboratories, Inc. | Covalently attached complex of alpha-1-proteinase inhibitor with a water soluble polymer |
| US4694778A (en) | 1984-05-04 | 1987-09-22 | Anicon, Inc. | Chemical vapor deposition wafer boat |
| JPS6147500A (ja) | 1984-08-15 | 1986-03-07 | Res Dev Corp Of Japan | キメラモノクロ−ナル抗体及びその製造法 |
| EP0173494A3 (en) | 1984-08-27 | 1987-11-25 | The Board Of Trustees Of The Leland Stanford Junior University | Chimeric receptors by dna splicing and expression |
| GB8422238D0 (en) | 1984-09-03 | 1984-10-10 | Neuberger M S | Chimeric proteins |
| US4879231A (en) | 1984-10-30 | 1989-11-07 | Phillips Petroleum Company | Transformation of yeasts of the genus pichia |
| US4596556A (en) | 1985-03-25 | 1986-06-24 | Bioject, Inc. | Hypodermic injection apparatus |
| US4751180A (en) | 1985-03-28 | 1988-06-14 | Chiron Corporation | Expression using fused genes providing for protein product |
| EP0206448B1 (en) | 1985-06-19 | 1990-11-14 | Ajinomoto Co., Inc. | Hemoglobin combined with a poly(alkylene oxide) |
| US4935233A (en) | 1985-12-02 | 1990-06-19 | G. D. Searle And Company | Covalently linked polypeptide cell modulators |
| WO1987005330A1 (en) | 1986-03-07 | 1987-09-11 | Michel Louis Eugene Bergh | Method for enhancing glycoprotein stability |
| US5225539A (en) | 1986-03-27 | 1993-07-06 | Medical Research Council | Recombinant altered antibodies and methods of making altered antibodies |
| GB8607679D0 (en) | 1986-03-27 | 1986-04-30 | Winter G P | Recombinant dna product |
| GB8610600D0 (en) | 1986-04-30 | 1986-06-04 | Novo Industri As | Transformation of trichoderma |
| US4791192A (en) | 1986-06-26 | 1988-12-13 | Takeda Chemical Industries, Ltd. | Chemically modified protein with polyethyleneglycol |
| US4946778A (en) | 1987-09-21 | 1990-08-07 | Genex Corporation | Single polypeptide chain binding molecules |
| US5260203A (en) | 1986-09-02 | 1993-11-09 | Enzon, Inc. | Single polypeptide chain binding molecules |
| DE3883899T3 (de) | 1987-03-18 | 1999-04-22 | Sb2, Inc., Danville, Calif. | Geänderte antikörper. |
| JPH02500329A (ja) | 1987-05-21 | 1990-02-08 | クリエイテイブ・バイオマリキユールズ・インコーポレーテツド | ターゲット化多機能蛋白質 |
| US4941880A (en) | 1987-06-19 | 1990-07-17 | Bioject, Inc. | Pre-filled ampule and non-invasive hypodermic injection device assembly |
| US4790824A (en) | 1987-06-19 | 1988-12-13 | Bioject, Inc. | Non-invasive hypodermic injection device |
| US5476996A (en) | 1988-06-14 | 1995-12-19 | Lidak Pharmaceuticals | Human immune system in non-human animal |
| US5223409A (en) | 1988-09-02 | 1993-06-29 | Protein Engineering Corp. | Directed evolution of novel binding proteins |
| GB8823869D0 (en) | 1988-10-12 | 1988-11-16 | Medical Res Council | Production of antibodies |
| US5175384A (en) | 1988-12-05 | 1992-12-29 | Genpharm International | Transgenic mice depleted in mature t-cells and methods for making transgenic mice |
| US5530101A (en) | 1988-12-28 | 1996-06-25 | Protein Design Labs, Inc. | Humanized immunoglobulins |
| EP0402226A1 (en) | 1989-06-06 | 1990-12-12 | Institut National De La Recherche Agronomique | Transformation vectors for yeast yarrowia |
| US5683888A (en) | 1989-07-22 | 1997-11-04 | University Of Wales College Of Medicine | Modified bioluminescent proteins and their use |
| US5013556A (en) | 1989-10-20 | 1991-05-07 | Liposome Technology, Inc. | Liposomes with enhanced circulation time |
| WO1991006319A1 (en) | 1989-10-27 | 1991-05-16 | Arch Development Corporation | Methods and compositions for promoting immunopotentiation |
| US5312335A (en) | 1989-11-09 | 1994-05-17 | Bioject Inc. | Needleless hypodermic injection device |
| US5064413A (en) | 1989-11-09 | 1991-11-12 | Bioject, Inc. | Needleless hypodermic injection device |
| US5859205A (en) | 1989-12-21 | 1999-01-12 | Celltech Limited | Humanised antibodies |
| US5292658A (en) | 1989-12-29 | 1994-03-08 | University Of Georgia Research Foundation, Inc. Boyd Graduate Studies Research Center | Cloning and expressions of Renilla luciferase |
| US6673986B1 (en) | 1990-01-12 | 2004-01-06 | Abgenix, Inc. | Generation of xenogeneic antibodies |
| US6075181A (en) | 1990-01-12 | 2000-06-13 | Abgenix, Inc. | Human antibodies derived from immunized xenomice |
| US6150584A (en) | 1990-01-12 | 2000-11-21 | Abgenix, Inc. | Human antibodies derived from immunized xenomice |
| ATE139258T1 (de) | 1990-01-12 | 1996-06-15 | Cell Genesys Inc | Erzeugung xenogener antikörper |
| US5789650A (en) | 1990-08-29 | 1998-08-04 | Genpharm International, Inc. | Transgenic non-human animals for 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 |
| US5874299A (en) | 1990-08-29 | 1999-02-23 | 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 |
| AU664976B2 (en) | 1990-08-29 | 1995-12-14 | Gene Pharming Europe Bv | Homologous recombination in mammalian cells |
| US5770429A (en) | 1990-08-29 | 1998-06-23 | Genpharm International, Inc. | Transgenic non-human animals capable of producing heterologous antibodies |
| 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 |
| US6255458B1 (en) | 1990-08-29 | 2001-07-03 | Genpharm International | High affinity human antibodies and human antibodies against digoxin |
| US5661016A (en) | 1990-08-29 | 1997-08-26 | Genpharm International Inc. | Transgenic non-human animals capable of producing heterologous antibodies of various isotypes |
| US5633425A (en) | 1990-08-29 | 1997-05-27 | Genpharm International, Inc. | Transgenic non-human animals capable of producing heterologous antibodies |
| AU8507191A (en) | 1990-08-29 | 1992-03-30 | Genpharm International, Inc. | Transgenic non-human animals capable of producing heterologous antibodies |
| ES2142801T3 (es) | 1991-03-11 | 2000-05-01 | Univ Georgia Res Found | Clonacion y expresion de luciferasa de renilla. |
| WO1992022670A1 (en) | 1991-06-12 | 1992-12-23 | Genpharm International, Inc. | Early detection of transgenic embryos |
| EP0940468A1 (en) | 1991-06-14 | 1999-09-08 | Genentech, Inc. | Humanized antibody variable domain |
| WO1992022645A1 (en) | 1991-06-14 | 1992-12-23 | Genpharm International, Inc. | Transgenic immunodeficient non-human animals |
| AU2515992A (en) | 1991-08-20 | 1993-03-16 | Genpharm International, Inc. | Gene targeting in animal cells using isogenic dna constructs |
| US5565332A (en) | 1991-09-23 | 1996-10-15 | Medical Research Council | Production of chimeric antibodies - a combinatorial approach |
| WO1993015722A1 (en) | 1992-02-07 | 1993-08-19 | Syntex (Usa) Inc. | Controlled delivery of pharmaceuticals from preformed porous microparticles |
| US7381803B1 (en) | 1992-03-27 | 2008-06-03 | Pdl Biopharma, Inc. | Humanized antibodies against CD3 |
| US5383851A (en) | 1992-07-24 | 1995-01-24 | Bioject Inc. | Needleless hypodermic injection device |
| US5981175A (en) | 1993-01-07 | 1999-11-09 | Genpharm Internation, Inc. | Methods for producing recombinant mammalian cells harboring a yeast artificial chromosome |
| DE69435112D1 (de) | 1993-09-10 | 2008-08-21 | Univ Columbia | Verwendung von grünem fluoreszenzprotein |
| WO1995021191A1 (en) | 1994-02-04 | 1995-08-10 | William Ward | Bioluminescent indicator based upon the expression of a gene for a modified green-fluorescent protein |
| US5643763A (en) | 1994-11-04 | 1997-07-01 | Genpharm International, Inc. | Method for making recombinant yeast artificial chromosomes by minimizing diploid doubling during mating |
| US6214388B1 (en) | 1994-11-09 | 2001-04-10 | The Regents Of The University Of California | Immunoliposomes that optimize internalization into target cells |
| US5777079A (en) | 1994-11-10 | 1998-07-07 | The Regents Of The University Of California | Modified green fluorescent proteins |
| US5731168A (en) | 1995-03-01 | 1998-03-24 | Genentech, Inc. | Method for making heteromultimeric polypeptides |
| US6037453A (en) | 1995-03-15 | 2000-03-14 | Genentech, Inc. | Immunoglobulin variants |
| EP0822830B1 (en) | 1995-04-27 | 2008-04-02 | Amgen Fremont Inc. | Human anti-IL-8 antibodies, derived from immunized xenomice |
| EP0823941A4 (en) | 1995-04-28 | 2001-09-19 | Abgenix Inc | HUMAN ANTIBODIES DERIVED FROM IMMUNIZED XENO MOUSES |
| US5811524A (en) | 1995-06-07 | 1998-09-22 | Idec Pharmaceuticals Corporation | Neutralizing high affinity human monoclonal antibodies specific to RSV F-protein and methods for their manufacture and therapeutic use thereof |
| AU6113396A (en) | 1995-06-14 | 1997-01-15 | Regents Of The University Of California, The | Novel high affinity human antibodies to tumor antigens |
| ES2176484T3 (es) | 1995-08-18 | 2002-12-01 | Morphosys Ag | Bancos de proteinas/(poli)peptidos. |
| ATE352613T1 (de) | 1995-08-29 | 2007-02-15 | Kirin Brewery | Chimäres tier und methode zu dessen herstellung |
| US5874304A (en) | 1996-01-18 | 1999-02-23 | University Of Florida Research Foundation, Inc. | Humanized green fluorescent protein genes and methods |
| US5804387A (en) | 1996-02-01 | 1998-09-08 | The Board Of Trustees Of The Leland Stanford Junior University | FACS-optimized mutants of the green fluorescent protein (GFP) |
| US5876995A (en) | 1996-02-06 | 1999-03-02 | Bryan; Bruce | Bioluminescent novelty items |
| US5925558A (en) | 1996-07-16 | 1999-07-20 | The Regents Of The University Of California | Assays for protein kinases using fluorescent protein substrates |
| US5976796A (en) | 1996-10-04 | 1999-11-02 | Loma Linda University | Construction and expression of renilla luciferase and green fluorescent protein fusion genes |
| EP1500329B1 (en) | 1996-12-03 | 2012-03-21 | Amgen Fremont Inc. | Human antibodies that specifically bind human TNF alpha |
| JP3795533B2 (ja) | 1996-12-12 | 2006-07-12 | プロルーム・リミテツド | 感染性物質を検出及び同定するための方法及び装置 |
| US20020062010A1 (en) | 1997-05-02 | 2002-05-23 | Genentech, Inc. | Method for making multispecific antibodies having heteromultimeric and common components |
| US20020173629A1 (en) | 1997-05-05 | 2002-11-21 | Aya Jakobovits | Human monoclonal antibodies to epidermal growth factor receptor |
| ATE319745T1 (de) | 1997-05-21 | 2006-03-15 | Biovation Ltd | Verfahren zur herstellung von nicht-immunogenen proteinen |
| US5994511A (en) | 1997-07-02 | 1999-11-30 | Genentech, Inc. | Anti-IgE antibodies and methods of improving polypeptides |
| AU739331B2 (en) | 1997-10-01 | 2001-10-11 | Boston Scientific Limited | Dilation systems and related methods |
| JP4169478B2 (ja) | 1998-04-21 | 2008-10-22 | マイクロメット アーゲー | Ｃｄ１９×ｃｄ３特異的ポリペプチドおよびその使用 |
| WO1999066951A2 (en) | 1998-06-22 | 1999-12-29 | Immunomedics, Inc. | Use of bi-specific antibodies for pre-targeting diagnosis and therapy |
| DK1100830T3 (da) | 1998-07-28 | 2004-01-19 | Micromet Ag | Heterominiantistoffer |
| AU776910B2 (en) | 1998-12-08 | 2004-09-23 | Merck Patent Gesellschaft Mit Beschrankter Haftung | Modifying protein immunogenicity |
| CN1342202A (zh) | 1999-01-07 | 2002-03-27 | 津莫吉尼蒂克斯公司 | 可溶性受体br43×2和应用方法 |
| US20020142000A1 (en) | 1999-01-15 | 2002-10-03 | Digan Mary Ellen | Anti-CD3 immunotoxins and therapeutic uses therefor |
| US6833268B1 (en) | 1999-06-10 | 2004-12-21 | Abgenix, Inc. | Transgenic animals for producing specific isotypes of human antibodies via non-cognate switch regions |
| JP4787439B2 (ja) | 1999-08-17 | 2011-10-05 | バイオジェン・アイデック・エムエイ・インコーポレイテッド | 免疫調節因子であるｂａｆｆレセプター（ｂｃｍａ） |
| UA74798C2 (uk) | 1999-10-06 | 2006-02-15 | Байоджен Айдек Ма Інк. | Спосіб лікування раку у ссавця за допомогою поліпептиду, що протидіє взаємодії april з його рецепторами |
| AU2001263114A1 (en) | 2000-05-12 | 2001-11-26 | Amgen Inc | Methods and compositions of matter concerning april/g70, bcma, blys/agp-3, and taci |
| UY27087A1 (es) | 2001-01-05 | 2002-06-20 | Pfizer | Anticuerpos contra el receptor del factor de crecimiento similar a insulina |
| US20030012783A1 (en) | 2001-02-20 | 2003-01-16 | Wayne Kindsvogel | Antibodies that bind both BCMA and TACI |
| BRPI0210405B8 (pt) | 2001-06-13 | 2021-05-25 | Genmab As | anticorpo monoclonal humano, molécula biespecífica, método in vitro para inibir o crescimento de uma célula expressando egfr, para induzir a citólise de uma célula expressando egfr, e para detectar a presença de antígeno egfr ou uma célula expressando egfr em uma amostra, e, vetor de expressão |
| AR039067A1 (es) | 2001-11-09 | 2005-02-09 | Pfizer Prod Inc | Anticuerpos para cd40 |
| EP1461442B1 (en) | 2001-11-30 | 2017-09-06 | Amgen Fremont Inc. | Transgenic animals bearing human ig lambda light chain genes |
| US7435797B2 (en) | 2002-04-10 | 2008-10-14 | Genentech, Inc. | Anti-HER2 antibody variants |
| WO2003089930A1 (en) | 2002-04-22 | 2003-10-30 | Georgetown University | Peripheral-type benzodiazepine receptor expression level as an index of organ damage and regeneration |
| WO2005056606A2 (en) | 2003-12-03 | 2005-06-23 | Xencor, Inc | Optimized antibodies that target the epidermal growth factor receptor |
| US8784821B1 (en) | 2003-05-31 | 2014-07-22 | Amgen Research (Munich) Gmbh | Human-anti-human cd3 binding molecules |
| EP1629012B1 (en) | 2003-05-31 | 2018-11-28 | Amgen Research (Munich) GmbH | Pharmaceutical compositions comprising bispecific anti-cd3, anti-cd19 antibody constructs for the treatment of b-cell related disorders |
| KR20060015602A (ko) | 2003-05-31 | 2006-02-17 | 마이크로메트 에이지 | ＥｐＣＡＭ 에 대한 이중 특이성 항체를 포함하는약학조성물 |
| KR20120125634A (ko) | 2003-10-16 | 2012-11-16 | 마이크로메트 에이지 | 다중특이적 탈면역화된 ｃｄ3-바인더 |
| US7235641B2 (en) | 2003-12-22 | 2007-06-26 | Micromet Ag | Bispecific antibodies |
| WO2005077981A2 (en) | 2003-12-22 | 2005-08-25 | Xencor, Inc. | Fc POLYPEPTIDES WITH NOVEL Fc LIGAND BINDING SITES |
| JP4541014B2 (ja) | 2004-01-13 | 2010-09-08 | キヤノンアネルバ株式会社 | プラズマ支援スパッタ成膜装置 |
| JP2008505607A (ja) | 2004-01-29 | 2008-02-28 | ジェネンテック・インコーポレーテッド | Ｂｃｍａの細胞外ドメインの変異体とその使用法 |
| JP4812748B2 (ja) | 2004-04-06 | 2011-11-09 | ノビミューン エスアー | 自己免疫性疾患および炎症性疾患を処置する方法 |
| EA010350B1 (ru) | 2004-06-03 | 2008-08-29 | Новиммун С.А. | Антитела против cd3 и способы их применения |
| US20060067930A1 (en) | 2004-08-19 | 2006-03-30 | Genentech, Inc. | Polypeptide variants with altered effector function |
| WO2006138181A2 (en) | 2005-06-14 | 2006-12-28 | Amgen Inc. | Self-buffering protein formulations |
| US8663634B2 (en) | 2005-07-11 | 2014-03-04 | Macrogenics, Inc. | Methods for the treatment of autoimmune disorders using immunosuppressive monoclonal antibodies with reduced toxicity |
| AU2006291005A1 (en) | 2005-09-12 | 2007-03-22 | Novimmune S.A. | Anti-CD3 antibody formulations |
| DK1940881T3 (en) | 2005-10-11 | 2017-02-20 | Amgen Res Munich Gmbh | COMPOSITIONS WITH ARTICLE CROSS-SPECIFIC ANTIBODIES AND APPLICATIONS THEREOF |
| US20090226466A1 (en) | 2005-11-03 | 2009-09-10 | Sherman Fong | Therapeutic anti-her2 antibody fusion polypeptides |
| AU2006318539B2 (en) | 2005-11-23 | 2012-09-13 | Genentech, Inc. | Methods and compositions related to B cell assays |
| US20070264687A1 (en) | 2005-12-15 | 2007-11-15 | Min-Yuan Chou | Recombinant triplex scaffold-based polypeptides |
| US7910703B2 (en) | 2006-03-10 | 2011-03-22 | Zymogenetics, Inc. | Antagonists to IL-17A, IL-17F, and IL-23P19 and methods of use |
| EP2418223A3 (en) | 2006-06-12 | 2013-01-16 | Emergent Product Development Seattle, LLC | Single-chain multivalent binding proteins with effector function |
| GB0614780D0 (en) | 2006-07-25 | 2006-09-06 | Ucb Sa | Biological products |
| US20230357444A1 (en) | 2007-04-03 | 2023-11-09 | Amgen Research (Munich) Gmbh | Cross-species-specific binding domain |
| HUE040467T2 (hu) | 2007-04-03 | 2019-03-28 | Amgen Res Munich Gmbh | Keresztfaj-specifikus kötõdomén |
| FI2155783T4 (fi) * | 2007-04-03 | 2022-12-15 | Lajien välisesti spesifinen cd3-epsilon-sitoutumisdomeeni | |
| CA2682605A1 (en) | 2007-04-18 | 2008-10-30 | Zymogenetics, Inc. | Single chain fc, methods of making and methods of treatment |
| US7998018B2 (en) | 2007-04-30 | 2011-08-16 | GM Global Technology Operations LLC | Multi-speed transmission |
| CN101802197A (zh) | 2007-05-14 | 2010-08-11 | 比奥根艾迪克Ma公司 | 单链FC（ScFc）区、包含其的结合多肽及与其相关的方法 |
| US20120034228A1 (en) | 2008-10-01 | 2012-02-09 | Micromet Ag | CROSS-SPECIES-SPECIFIC PSCAxCD3, CD19xCD3, C-METxCD3, ENDOSIALINxCD3, EPCAMxCD3, IGF-1RxCD3 OR FAPALPHAxCD3 BISPECIFIC SINGLE CHAIN ANTIBODY |
| ES2582603T5 (es) | 2008-10-01 | 2022-12-02 | Amgen Res Munich Gmbh | Anticuerpos biespecíficos de cadena sencilla con especificidad por antígenos diana de alto peso molecular |
| WO2010037836A2 (en) | 2008-10-01 | 2010-04-08 | Micromet Ag | Cross-species-specific psmaxcd3 bispecific single chain antibody |
| BRPI0823231A2 (pt) | 2008-11-26 | 2015-06-16 | Glaxo Group Ltd | Domínio variável único da imunoglobulina anti-interleucina-13 (il-13), antagonista da interleucina-13 (il-13), uso da antagonista, método para tratar e/ou prevenir uma condição mediada pela il-13 em um paciente, dispositivo de dispensação pulmonar contendo o antagonista, ligando específico duplo, ácido nucléico isolado ou recombinante, vetor, célula hospedeira, método para produzir polipeptídeo, e, proteína de fusão. |
| SI2406284T1 (sl) | 2009-03-10 | 2017-01-31 | Biogen Ma Inc. | Anti-bcma protitelesa |
| EP2424567B1 (en) | 2009-04-27 | 2018-11-21 | OncoMed Pharmaceuticals, Inc. | Method for making heteromultimeric molecules |
| UY32979A (es) | 2009-10-28 | 2011-02-28 | Abbott Lab | Inmunoglobulinas con dominio variable dual y usos de las mismas |
| US20130129723A1 (en) | 2009-12-29 | 2013-05-23 | Emergent Product Development Seattle, Llc | Heterodimer Binding Proteins and Uses Thereof |
| BR112012026227A2 (pt) | 2010-04-13 | 2020-08-04 | Celldex Therapeutics, Inc. | anticorpo monoclonal humano ou humanizado, molécula biespecífica, vetor de expressão, célula transformada, composição, e, usos de um anticorpo |
| CN103124788B (zh) | 2010-05-21 | 2016-01-13 | 梅里麦克制药股份有限公司 | 双特异性融合蛋白 |
| US9410994B2 (en) | 2010-11-15 | 2016-08-09 | Lg Electronics Inc. | Refrigerator and operation method thereof |
| US20130273055A1 (en) | 2010-11-16 | 2013-10-17 | Eric Borges | Agents and methods for treating diseases that correlate with bcma expression |
| TWI807362B (zh) | 2010-11-30 | 2023-07-01 | 日商中外製藥股份有限公司 | 細胞傷害誘導治療劑 |
| EP2655624B1 (en) | 2010-12-23 | 2017-11-29 | Biogen MA Inc. | Linker peptides and polypeptides comprising same |
| US20140105915A1 (en) | 2011-05-27 | 2014-04-17 | Glaxo Group Limited | Bcma (cd269/tnfrsf17) - binding proteins |
| ES2857734T3 (es) | 2011-08-23 | 2021-09-29 | Roche Glycart Ag | Moléculas de unión a antígeno activadoras de linfocitos T biespecíficas |
| WO2013026837A1 (en) | 2011-08-23 | 2013-02-28 | Roche Glycart Ag | Bispecific t cell activating antigen binding molecules |
| TWI679212B (zh) | 2011-11-15 | 2019-12-11 | 美商安進股份有限公司 | 針對ｂｃｍａ之e3以及ｃｄ３的結合分子 |
| EP2872170A4 (en) | 2012-07-13 | 2016-06-22 | Zymeworks Inc | ASYMMETRIC BISPECIFIC HETERODIMERS WITH ANTI-CD3 CONSTRUCTS |
| JOP20200236A1 (ar) | 2012-09-21 | 2017-06-16 | Regeneron Pharma | الأجسام المضادة لمضاد cd3 وجزيئات ربط الأنتيجين ثنائية التحديد التي تربط cd3 وcd20 واستخداماتها |
| EP2731280B8 (en) | 2012-11-07 | 2019-03-20 | Telefonaktiebolaget LM Ericsson (publ) | Loopback-based built-in-self-test |
| TW201425336A (zh) | 2012-12-07 | 2014-07-01 | Amgen Inc | Ｂｃｍａ抗原結合蛋白質 |
| US9243058B2 (en) | 2012-12-07 | 2016-01-26 | Amgen, Inc. | BCMA antigen binding proteins |
| CA2898100C (en) | 2013-01-14 | 2023-10-10 | Xencor, Inc. | Novel heterodimeric proteins |
| JO3519B1 (ar) | 2013-01-25 | 2020-07-05 | Amgen Inc | تركيبات أجسام مضادة لأجل cdh19 و cd3 |
| EP2762497A1 (en) | 2013-02-05 | 2014-08-06 | EngMab AG | Bispecific antibodies against CD3epsilon and BCMA |
| JP2016507523A (ja) | 2013-02-05 | 2016-03-10 | エンクマフ アーゲー | ＣＤ３εおよびＢＣＭＡに対する二重特異的抗体 |
| US9458245B2 (en) | 2013-03-06 | 2016-10-04 | Merrimack Pharmaceuticals, Inc. | ANTI-C-MET tandem Fc bispecific antibodies |
| US20140308285A1 (en) | 2013-03-15 | 2014-10-16 | Amgen Inc. | Heterodimeric bispecific antibodies |
| AR095374A1 (es) * | 2013-03-15 | 2015-10-14 | Amgen Res Munich Gmbh | Moléculas de unión para bcma y cd3 |
| SI2970449T1 (sl) | 2013-03-15 | 2019-11-29 | Amgen Res Munich Gmbh | Enoverižne vezavne molekule, ki vsebujejo N-terminalni ABP |
| US20140302037A1 (en) | 2013-03-15 | 2014-10-09 | Amgen Inc. | BISPECIFIC-Fc MOLECULES |
| US20160257748A1 (en) | 2013-09-25 | 2016-09-08 | Amgen Inc. | V-c-fc-v-c antibody |
| AU2015294834B2 (en) | 2014-07-31 | 2021-04-29 | Amgen Research (Munich) Gmbh | Optimized cross-species specific bispecific single chain antibody constructs |
| US10259887B2 (en) | 2014-11-26 | 2019-04-16 | Xencor, Inc. | Heterodimeric antibodies that bind CD3 and tumor antigens |
| HRP20211273T1 (hr) | 2014-11-26 | 2021-11-12 | Xencor, Inc. | Heterodimerna protutijela koja vežu cd3 i cd20 |
| AR104309A1 (es) | 2015-04-17 | 2017-07-12 | Bayer Pharma AG | Construcciones de anticuerpos biespecíficos para cdh3 y cd3 |
| TWI796283B (zh) | 2015-07-31 | 2023-03-21 | 德商安美基研究（慕尼黑）公司 | Ｍｓｌｎ及ｃｄ３抗體構築體 |
| TWI793062B (zh) | 2015-07-31 | 2023-02-21 | 德商安美基研究（慕尼黑）公司 | Ｄｌｌ３及ｃｄ３抗體構築體 |
| TWI717375B (zh) | 2015-07-31 | 2021-02-01 | 德商安美基研究（慕尼黑）公司 | Ｃｄ７０及ｃｄ３抗體構築體 |
| EA039859B1 (ru) | 2015-07-31 | 2022-03-21 | Эмджен Рисерч (Мюник) Гмбх | Биспецифические конструкты антител, связывающие egfrviii и cd3 |
| TWI829617B (zh) | 2015-07-31 | 2024-01-21 | 德商安美基研究（慕尼黑）公司 | Ｆｌｔ３及ｃｄ３抗體構築體 |
| TWI744242B (zh) | 2015-07-31 | 2021-11-01 | 德商安美基研究（慕尼黑）公司 | Egfrviii及cd3抗體構築體 |
| IL260920B (en) | 2016-02-03 | 2022-09-01 | Amgen Res Munich Gmbh | Constructs of psma and cd3 bispecific antigens that bind to t-cells, preparations containing them and uses thereof |
| IL313507A (en) | 2016-02-03 | 2024-08-01 | Amgen Res Munich Gmbh | Constructs of bispecific antibodies to BCMA and CD3 that bind to T cells, preparations containing the same and uses thereof |
| EP4295918A3 (en) | 2016-11-02 | 2024-03-20 | Bristol-Myers Squibb Company | Bispecific antibody against bcma and cd3 and an immunological drug for combined use in treating multiple myeloma |
| TWI868050B (zh) | 2017-05-05 | 2025-01-01 | 美商安進公司 | 用於改良儲存及投與之包含雙特異性抗體構築體之醫藥組成物 |
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Patent Citations (5)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| US20080213256A1 (en) * | 2004-02-16 | 2008-09-04 | Micromet Ag | Less Immunogenic Binding Molecules |
| CN101370830A (zh) * | 2005-09-26 | 2009-02-18 | 米德列斯公司 | 抗cd70的人单克隆抗体 |
| CN101675077A (zh) * | 2007-04-03 | 2010-03-17 | 米克罗麦特股份公司 | 跨种特异性的双特异性结合剂 |
| US20090325196A1 (en) * | 2008-04-25 | 2009-12-31 | Zymogenetics, Inc. | Levels of bcma protein expression on b cells and use in diagnostic methods |
| US20110275787A1 (en) * | 2008-10-01 | 2011-11-10 | Microment AG | Cross-species-specific single domain bispecific single chain antibody |
Cited By (1)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| CN114763383A (zh) * | 2021-01-13 | 2022-07-19 | 博生吉医药科技(苏州)有限公司 | 靶向人bcma的单克隆抗体及其应用 |
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