CA2779559A1 - Variant fc regions - Google Patents
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- CA2779559A1 CA2779559A1 CA2779559A CA2779559A CA2779559A1 CA 2779559 A1 CA2779559 A1 CA 2779559A1 CA 2779559 A CA2779559 A CA 2779559A CA 2779559 A CA2779559 A CA 2779559A CA 2779559 A1 CA2779559 A1 CA 2779559A1
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- 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
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- 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
- C07K16/2803—Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies against material from animals or humans against receptors, cell surface antigens or cell surface determinants against the immunoglobulin superfamily
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- 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
- C07K16/2896—Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies against material from animals or humans against receptors, cell surface antigens or cell surface determinants against molecules with a "CD"-designation, not provided for elsewhere
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- C12N15/113—Non-coding nucleic acids modulating the expression of genes, e.g. antisense oligonucleotides; Antisense DNA or RNA; Triplex- forming oligonucleotides; Catalytic nucleic acids, e.g. ribozymes; Nucleic acids used in co-suppression or gene silencing
- C12N15/1135—Non-coding nucleic acids modulating the expression of genes, e.g. antisense oligonucleotides; Antisense DNA or RNA; Triplex- forming oligonucleotides; Catalytic nucleic acids, e.g. ribozymes; Nucleic acids used in co-suppression or gene silencing against oncogenes or tumor suppressor genes
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- C07K2317/73—Inducing cell death, e.g. apoptosis, necrosis or inhibition of cell proliferation
- C07K2317/734—Complement-dependent cytotoxicity [CDC]
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| PCT/US2005/025276 WO2006020114A2 (en) | 2004-08-04 | 2005-07-18 | Variant fc regions |
| CA2573192A CA2573192C (en) | 2004-08-04 | 2005-07-18 | Variant fc regions |
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| CA2573192A Division CA2573192C (en) | 2004-08-04 | 2005-07-18 | Variant fc regions |
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| CA2573192A Expired - Fee Related CA2573192C (en) | 2004-08-04 | 2005-07-18 | Variant fc regions |
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Families Citing this family (272)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| US7183387B1 (en) | 1999-01-15 | 2007-02-27 | Genentech, Inc. | Polypeptide variants with altered effector function |
| AU3672800A (en) | 1999-04-09 | 2000-11-14 | Kyowa Hakko Kogyo Co. Ltd. | Method for controlling the activity of immunologically functional molecule |
| US6946292B2 (en) | 2000-10-06 | 2005-09-20 | Kyowa Hakko Kogyo Co., Ltd. | Cells producing antibody compositions with increased antibody dependent cytotoxic activity |
| WO2002044394A2 (en) * | 2000-11-29 | 2002-06-06 | University Of Southern California | Targetet retoviral vectors for cancer immunotherapy |
| US20040132101A1 (en) | 2002-09-27 | 2004-07-08 | Xencor | Optimized Fc variants and methods for their generation |
| US8946387B2 (en) | 2002-08-14 | 2015-02-03 | Macrogenics, Inc. | FcγRIIB specific antibodies and methods of use thereof |
| US8968730B2 (en) | 2002-08-14 | 2015-03-03 | Macrogenics Inc. | FcγRIIB specific antibodies and methods of use thereof |
| US7960512B2 (en) | 2003-01-09 | 2011-06-14 | Macrogenics, Inc. | Identification and engineering of antibodies with variant Fc regions and methods of using same |
| CA2512729C (en) | 2003-01-09 | 2014-09-16 | Macrogenics, Inc. | Identification and engineering of antibodies with variant fc regions and methods of using same |
| US8388955B2 (en) | 2003-03-03 | 2013-03-05 | Xencor, Inc. | Fc variants |
| US20090010920A1 (en) | 2003-03-03 | 2009-01-08 | Xencor, Inc. | Fc Variants Having Decreased Affinity for FcyRIIb |
| JP2006524057A (ja) * | 2003-04-21 | 2006-10-26 | エペイウス バイオテクノロジーズ, インコーポレイテッド | 疾患を処置するための方法および組成物 |
| US20090123428A1 (en) * | 2003-04-21 | 2009-05-14 | Hall Frederick L | Pathotropic targeted gene delivery system for cancer and other disorders |
| US20070178066A1 (en) | 2003-04-21 | 2007-08-02 | Hall Frederick L | Pathotropic targeted gene delivery system for cancer and other disorders |
| US9051373B2 (en) | 2003-05-02 | 2015-06-09 | Xencor, Inc. | Optimized Fc variants |
| WO2005018572A2 (en) | 2003-08-22 | 2005-03-03 | Biogen Idec Ma Inc. | Improved antibodies having altered effector function and methods for making the same |
| JP2007536932A (ja) | 2004-05-10 | 2007-12-20 | マクロジェニクス,インコーポレーテッド | ヒト化FcγRIIB特異的抗体とその利用法 |
| WO2006085967A2 (en) * | 2004-07-09 | 2006-08-17 | Xencor, Inc. | OPTIMIZED ANTI-CD20 MONOCONAL ANTIBODIES HAVING Fc VARIANTS |
| JP5102028B2 (ja) | 2004-07-26 | 2012-12-19 | 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 | 抗cd154抗体 |
| CN101001873B (zh) | 2004-08-04 | 2013-03-13 | 曼璀克生物科技有限责任公司 | Fc区变体 |
| CA2587766A1 (en) | 2004-11-10 | 2007-03-01 | Macrogenics, Inc. | Engineering fc antibody regions to confer effector function |
| US8546543B2 (en) | 2004-11-12 | 2013-10-01 | Xencor, Inc. | Fc variants that extend antibody half-life |
| US8367805B2 (en) | 2004-11-12 | 2013-02-05 | Xencor, Inc. | Fc variants with altered binding to FcRn |
| US8802820B2 (en) | 2004-11-12 | 2014-08-12 | Xencor, Inc. | Fc variants with altered binding to FcRn |
| EP2325206B1 (en) | 2004-11-12 | 2014-03-19 | Xencor, Inc. | Fc variants with altered binding to fcrn |
| WO2006104989A2 (en) * | 2005-03-29 | 2006-10-05 | Verenium Corporation | Altered antibody fc regions and uses thereof |
| CA2605024C (en) | 2005-04-15 | 2018-05-22 | Macrogenics, Inc. | Covalent diabodies and uses thereof |
| US9963510B2 (en) | 2005-04-15 | 2018-05-08 | Macrogenics, Inc. | Covalent diabodies and uses thereof |
| US11254748B2 (en) | 2005-04-15 | 2022-02-22 | Macrogenics, Inc. | Covalent diabodies and uses thereof |
| US9284375B2 (en) | 2005-04-15 | 2016-03-15 | Macrogenics, Inc. | Covalent diabodies and uses thereof |
| US8309690B2 (en) * | 2005-07-01 | 2012-11-13 | Medimmune, Llc | Integrated approach for generating multidomain protein therapeutics |
| CA2652434A1 (en) * | 2005-07-08 | 2007-01-18 | Xencor, Inc. | Optimized proteins that target ep-cam |
| US7923538B2 (en) | 2005-07-22 | 2011-04-12 | Kyowa Hakko Kirin Co., Ltd | Recombinant antibody composition |
| PT1919503E (pt) | 2005-08-10 | 2015-01-05 | Macrogenics Inc | Identificação e manipulação de anticorpos com a regiões de fc variantes e métodos de utilização dos mesmos |
| KR20080073293A (ko) | 2005-10-14 | 2008-08-08 | 메디뮨 엘엘씨 | 항체 라이브러리의 세포 디스플레이 |
| CA2647846C (en) | 2006-03-31 | 2016-06-21 | Chugai Seiyaku Kabushiki Kaisha | Methods for controlling blood pharmacokinetics of antibodies |
| CN105177091A (zh) | 2006-03-31 | 2015-12-23 | 中外制药株式会社 | 用于纯化双特异性抗体的抗体修饰方法 |
| CA2656224C (en) | 2006-06-26 | 2018-01-09 | Macrogenics, Inc. | Combination of fc.gamma.riib antibodies and cd20-specific antibodies and methods of use thereof |
| SI2029173T1 (sl) | 2006-06-26 | 2016-12-30 | Macrogenics, Inc. | Protitelesa, specifična za Fc RIIB, in postopki za njihovo uporabo |
| WO2008140603A2 (en) | 2006-12-08 | 2008-11-20 | Macrogenics, Inc. | METHODS FOR THE TREATMENT OF DISEASE USING IMMUNOGLOBULINS HAVING FC REGIONS WITH ALTERED AFFINITIES FOR FCγR ACTIVATING AND FCγR INHIBITING |
| AU2013202392B2 (en) * | 2006-12-20 | 2016-02-25 | Mmrglobal, Inc. | Antibodies and methods for making and using them |
| BRPI0720565A2 (pt) | 2006-12-20 | 2013-09-17 | Mmr Information Systems Inc | anticorpos e mÉtodos para a sua preparaÇço e seu uso |
| EP2125894B1 (en) | 2007-03-22 | 2018-12-19 | Biogen MA Inc. | Binding proteins, including antibodies, antibody derivatives and antibody fragments, that specifically bind cd154 and uses thereof |
| EP2068925A4 (en) | 2007-05-07 | 2011-08-31 | Medimmune Llc | ANTI-ICOS ANTIBODIES AND THEIR USE FOR THE TREATMENT OF CANCER, TRANSPLANTATIONS AND AUTOIMMUNE DISEASES |
| CN101952312A (zh) | 2007-07-31 | 2011-01-19 | 米迪缪尼有限公司 | 多特异性表位结合蛋白及其应用 |
| NZ583931A (en) | 2007-08-17 | 2012-06-29 | Purdue Research Foundation | Psma binding ligand-linker conjugates and methods for using |
| CN106519025B (zh) | 2007-09-26 | 2021-04-23 | 中外制药株式会社 | 利用cdr的氨基酸取代来改变抗体等电点的方法 |
| WO2009117030A2 (en) | 2007-12-19 | 2009-09-24 | Macrogenics, Inc. | Improved compositions for the prevention and treatment of smallpox |
| EP2604628A3 (en) | 2007-12-21 | 2013-08-21 | Medimmune Limited | Binding members for interleukin-4 receptor alpha (IL-4R) - 173 |
| US8092804B2 (en) | 2007-12-21 | 2012-01-10 | Medimmune Limited | Binding members for interleukin-4 receptor alpha (IL-4Rα)-173 |
| KR101616758B1 (ko) | 2007-12-26 | 2016-04-29 | 젠코어 인코포레이티드 | FcRn에 대한 변경된 결합성을 갖는 Fc 변이체 |
| CN102083460A (zh) | 2008-01-18 | 2011-06-01 | 米迪缪尼有限公司 | 用于位点特异性偶联的半胱氨酸工程化抗体 |
| US12492253B1 (en) | 2008-02-25 | 2025-12-09 | Xencor, Inc. | Anti-human C5 antibodies |
| DK2247304T3 (en) | 2008-04-02 | 2016-09-26 | Macrogenics Inc | Her2 / neu-specific antibodies and methods of use thereof |
| EP3045475B1 (en) | 2008-04-02 | 2017-10-04 | MacroGenics, Inc. | Bcr-complex-specific antibodies and methods of using same |
| CA2721052C (en) | 2008-04-11 | 2023-02-21 | Chugai Seiyaku Kabushiki Kaisha | Antigen-binding molecule capable of binding to two or more antigen molecules repeatedly |
| US8314213B2 (en) | 2008-04-18 | 2012-11-20 | Xencor, Inc. | Human equivalent monoclonal antibodies engineered from nonhuman variable regions |
| JP6049163B2 (ja) * | 2008-07-21 | 2016-12-21 | イミューノメディクス、インコーポレイテッドImmunomedics, Inc. | 改善された治療上の特徴のための抗体の構造変異体 |
| SG10201605250SA (en) * | 2008-10-14 | 2016-08-30 | Genentech Inc | Immunoglobulin variants and uses thereof |
| BRPI0921845A2 (pt) | 2008-11-12 | 2019-09-17 | Medimmune Llc | formulação aquosa estéril estável, forma de dosagem unitária farmacêutica, seringa pré-carregada, e, métodos para tratar uma doença ou distúrbio, para tratar ou prevenir rejeição, para esgotar células t que expressam icos em um paciente humano, e para interromper arquitetura central germinal em um órgão linfóide secundário de um primata |
| CN102802661B (zh) | 2009-06-22 | 2016-01-13 | 米迪缪尼有限公司 | 用于位点特异性偶联的工程改造的Fc区 |
| US9493578B2 (en) | 2009-09-02 | 2016-11-15 | Xencor, Inc. | Compositions and methods for simultaneous bivalent and monovalent co-engagement of antigens |
| JP5898082B2 (ja) | 2009-10-07 | 2016-04-06 | マクロジェニクス,インコーポレーテッド | フコシル化程度の変更により改良されたエフェクター機能を示すFc領域含有ポリペプチドおよびその使用法 |
| WO2011091078A2 (en) | 2010-01-19 | 2011-07-28 | Xencor, Inc. | Antibody fc variants with enhanced complement activity |
| US9951324B2 (en) | 2010-02-25 | 2018-04-24 | Purdue Research Foundation | PSMA binding ligand-linker conjugates and methods for using |
| PH12012501751A1 (en) | 2010-03-04 | 2012-11-12 | Macrogenics Inc | Antibodies reactive with b7-h3, immunologically active fragments thereof and uses thereof |
| NZ705128A (en) | 2010-03-04 | 2015-04-24 | Macrogenics Inc | Antibodies reactive with b7-h3, immunologically active fragments thereof and uses thereof |
| TWI667257B (zh) | 2010-03-30 | 2019-08-01 | 中外製藥股份有限公司 | 促進抗原消失之具有經修飾的FcRn親和力之抗體 |
| US20120100166A1 (en) | 2010-07-15 | 2012-04-26 | Zyngenia, Inc. | Ang-2 Binding Complexes and Uses Thereof |
| JP5964300B2 (ja) | 2010-08-02 | 2016-08-03 | マクロジェニクス,インコーポレーテッド | 共有結合型ダイアボディおよびその使用 |
| CA2808154A1 (en) | 2010-08-13 | 2012-02-16 | Medimmmune Limited | Monomeric polypeptides comprising variant fc regions and methods of use |
| WO2012022734A2 (en) | 2010-08-16 | 2012-02-23 | Medimmune Limited | Anti-icam-1 antibodies and methods of use |
| WO2012032080A1 (en) | 2010-09-07 | 2012-03-15 | F-Star Biotechnologische Forschungs- Und Entwicklungsges.M.B.H | Stabilised human fc |
| CN103328511B (zh) | 2010-09-10 | 2016-01-20 | 埃派斯进有限公司 | 抗-IL-1β抗体及其使用方法 |
| KR20140032944A (ko) * | 2010-10-20 | 2014-03-17 | 모르포테크, 인크. | 항폴레이트 수용체 알파 항체 당형태 |
| BR112013013354A2 (pt) | 2010-11-30 | 2020-10-06 | Chugai Seiyaku Kabushiki Kaisha | molécula de ligação ao antígeno capaz de se ligar a uma pluralidade de moléculas de antígeno repetidamente |
| 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 |
| CA3027071A1 (en) | 2011-01-14 | 2013-07-19 | The Regents Of The University Of California | Therapeutic antibodies against ror-1 protein and methods for use of same |
| CA2827170A1 (en) | 2011-02-11 | 2012-08-16 | David M. Hilbert | Monovalent and multivalent multispecific complexes and uses thereof |
| EP2679681B2 (en) | 2011-02-25 | 2023-11-15 | Chugai Seiyaku Kabushiki Kaisha | FcgammaRIIB-specific FC antibody |
| RU2013144392A (ru) | 2011-03-03 | 2015-04-10 | Апексиджен, Инк. | Антитела к рецептору il-6 и способы применения |
| EP2683740B1 (en) | 2011-03-10 | 2018-07-04 | Omeros Corporation | Generation of anti-fn14 monoclonal antibodies by ex-vivo accelerated antibody evolution |
| HUE041335T2 (hu) | 2011-03-29 | 2019-05-28 | Roche Glycart Ag | Antitest FC-variánsok |
| SMT201700025T1 (it) | 2011-04-13 | 2017-03-08 | Bristol Myers Squibb Co | Proteine di fusione ad fc comprendenti nuovi raccordi o arrangiamenti |
| CN106928362B (zh) | 2011-04-29 | 2021-10-26 | 埃派斯进有限公司 | 抗-cd40抗体及其使用方法 |
| BR112013029892A2 (pt) | 2011-05-21 | 2016-12-20 | Macrogenics Inc | polipeptídeo, molécula de ligação a antígeno, diacorpo e uso de uma porção polipeptídica de uma proteína de ligação a soro desimunizada |
| DK2714738T3 (en) | 2011-05-24 | 2019-01-28 | Zyngenia Inc | MULTIVALENT AND MONOVALENT MULTISPECIFIC COMPLEXES AND THEIR APPLICATIONS |
| EP4011913A1 (en) | 2011-06-30 | 2022-06-15 | Chugai Seiyaku Kabushiki Kaisha | Heterodimerized polypeptide |
| UA117901C2 (uk) | 2011-07-06 | 2018-10-25 | Ґенмаб Б.В. | Спосіб посилення ефекторної функції вихідного поліпептиду, його варіанти та їх застосування |
| US9102724B2 (en) | 2011-08-12 | 2015-08-11 | Omeros Corporation | Anti-FZD10 monoclonal antibodies and methods for their use |
| JP6322411B2 (ja) | 2011-09-30 | 2018-05-09 | 中外製薬株式会社 | 複数の生理活性を有する抗原の消失を促進する抗原結合分子 |
| TWI681970B (zh) | 2011-09-30 | 2020-01-11 | 日商中外製藥股份有限公司 | 包含依離子濃度之條件對抗原之結合活性會改變之抗原結合分域、及於pH中性之條件下對FcRn有結合活性之FcRn結合分域、且誘導對標的抗原的免疫反應之抗原結合分子 |
| EP3210625B1 (en) | 2011-09-30 | 2019-08-28 | Dana-Farber Cancer Institute, Inc. | Therapeutic peptides comprising antibodies binding to mhc class 1 polypeptide related sequence a (mica) |
| KR20200096692A (ko) * | 2011-09-30 | 2020-08-12 | 추가이 세이야쿠 가부시키가이샤 | 항원의 소실을 촉진시키는 항원 결합 분자 |
| TW201326209A (zh) | 2011-09-30 | 2013-07-01 | Chugai Pharmaceutical Co Ltd | 具有促進抗原清除之FcRn結合域的治療性抗原結合分子 |
| WO2013065708A1 (ja) | 2011-10-31 | 2013-05-10 | 中外製薬株式会社 | 重鎖と軽鎖の会合が制御された抗原結合分子 |
| CA2854153A1 (en) | 2011-11-02 | 2013-05-10 | Apexigen, Inc. | Anti-kdr antibodies and methods of use |
| AU2012336069A1 (en) | 2011-11-07 | 2014-05-22 | Medimmune, Llc | Multispecific and multivalent binding proteins and uses thereof |
| CN104080909A (zh) | 2011-11-30 | 2014-10-01 | 中外制药株式会社 | 包含进入细胞内以形成免疫复合体的搬运体(载体)的药物 |
| CA2859755C (en) | 2011-12-23 | 2021-04-20 | Pfizer Inc. | Engineered antibody constant regions for site-specific conjugation and methods and uses therefor |
| TWI593705B (zh) | 2011-12-28 | 2017-08-01 | Chugai Pharmaceutical Co Ltd | Humanized anti-epiregulin antibody and cancer therapeutic agent containing the antibody as an active ingredient |
| KR102041412B1 (ko) * | 2011-12-30 | 2019-11-11 | 한미사이언스 주식회사 | 면역글로불린 Fc 단편 유도체 |
| CN113527469A (zh) | 2012-02-09 | 2021-10-22 | 中外制药株式会社 | 抗体的Fc区变异体 |
| CA2865158C (en) * | 2012-02-24 | 2022-11-01 | Chugai Seiyaku Kabushiki Kaisha | Antigen-binding molecule for promoting disappearance of antigen via fc.gamma.riib |
| EP2832856A4 (en) | 2012-03-29 | 2016-01-27 | Chugai Pharmaceutical Co Ltd | ANTI-LAMP5 ANTIBODIES AND USE THEREOF |
| EP2857419B1 (en) | 2012-05-30 | 2021-01-13 | Chugai Seiyaku Kabushiki Kaisha | Antigen-binding molecule for eliminating aggregated antigens |
| KR102677704B1 (ko) | 2012-05-30 | 2024-06-21 | 추가이 세이야쿠 가부시키가이샤 | 표적 조직 특이적 항원 결합 분자 |
| DK2869845T3 (da) * | 2012-07-06 | 2019-12-09 | Genmab Bv | Dimert protein med tredobbelte mutationer |
| JP6514103B2 (ja) * | 2012-07-06 | 2019-05-15 | ゲンマブ ビー.ブイ. | 三重変異を有する二量体タンパク質 |
| MX361337B (es) | 2012-07-13 | 2018-12-04 | Roche Glycart Ag | Anticuerpos biespecificos anti-factor de crecimiento endotelial vascular humano (vegf) / anti-angiopoyetina-2 humana (ang-2) y su uso en el tratamiento de enfermedades vasculares oculares. |
| JP6501521B2 (ja) | 2012-08-24 | 2019-04-17 | 中外製薬株式会社 | FcγRIIb特異的Fc領域改変体 |
| JP6774164B2 (ja) | 2012-08-24 | 2020-10-21 | 中外製薬株式会社 | マウスFcγRII特異的Fc抗体 |
| KR102270618B1 (ko) | 2012-10-30 | 2021-06-30 | 아펙시젠, 인코포레이티드 | 항-cd40 항체 및 사용 방법 |
| KR102149206B1 (ko) | 2012-11-08 | 2020-08-31 | 세센 바이오, 아이엔씨. | 인터루킨-6의 길항제 및 이의 용도 |
| KR102575825B1 (ko) | 2012-11-15 | 2023-09-06 | 엔도사이트, 인코포레이티드 | Psma 발현 세포에 의해 야기되는 질병을 치료하기 위한 컨쥬게이트 |
| MX363407B (es) | 2012-12-10 | 2019-03-22 | Biogen Ma Inc | Anticuerpos del antigeno 2 de celulas dendriticas anti-sangre y usos de los mismos. |
| TWI693073B (zh) | 2012-12-21 | 2020-05-11 | 日商中外製藥股份有限公司 | 對gpc3標的治療劑療法為有效之患者投與的gpc3標的治療劑 |
| EP4119947A1 (en) | 2012-12-21 | 2023-01-18 | Chugai Seiyaku Kabushiki Kaisha | Gpc3-targeting drug which is administered to patient responsive to gpc3-targeting drug therapy |
| KR102249779B1 (ko) | 2012-12-27 | 2021-05-07 | 추가이 세이야쿠 가부시키가이샤 | 헤테로이량화 폴리펩티드 |
| KR20220156667A (ko) * | 2013-01-10 | 2022-11-25 | 젠맵 비. 브이 | 인간 IgG1 Fc 영역 변이체 및 그의 용도 |
| EP3744728A1 (en) | 2013-02-12 | 2020-12-02 | Bristol-Myers Squibb Company | Tangential flow filtration based protein refolding methods |
| ES2870802T3 (es) | 2013-02-12 | 2021-10-27 | Bristol Myers Squibb Co | Métodos de replegado de proteínas a elevado pH |
| US9487587B2 (en) | 2013-03-05 | 2016-11-08 | Macrogenics, Inc. | Bispecific molecules that are immunoreactive with immune effector cells of a companion animal that express an activating receptor and cells that express B7-H3 and uses thereof |
| SG11201507424WA (en) | 2013-03-14 | 2015-10-29 | Macrogenics Inc | Bispecific molecules that are immunoreactive with immune effector cells that express an activating receptor |
| US10035860B2 (en) | 2013-03-15 | 2018-07-31 | Biogen Ma Inc. | Anti-alpha V beta 6 antibodies and uses thereof |
| CN105392801A (zh) | 2013-03-15 | 2016-03-09 | 比奥根Ma公司 | 使用抗αvβ5抗体治疗和预防急性肾损伤 |
| CA2907181C (en) | 2013-03-15 | 2023-10-17 | Viktor Roschke | Multivalent and monovalent multispecific complexes and their uses |
| US10035859B2 (en) | 2013-03-15 | 2018-07-31 | Biogen Ma Inc. | Anti-alpha V beta 6 antibodies and uses thereof |
| BR112015021576A2 (pt) | 2013-03-15 | 2017-10-10 | Dana Farber Cancer Inst Inc | peptídeos terapêuticos |
| AU2014233436B2 (en) | 2013-03-15 | 2019-12-05 | Atyr Pharma, Inc. | Histidyl-tRNA synthetase-Fc conjugates |
| CA2908350C (en) | 2013-04-02 | 2023-08-08 | Futa Mimoto | Fc region variant |
| WO2014208482A1 (ja) | 2013-06-24 | 2014-12-31 | 中外製薬株式会社 | ヒト化抗Epiregulin抗体を有効成分として含む腺癌以外の非小細胞肺癌の治療剤 |
| US11384149B2 (en) | 2013-08-09 | 2022-07-12 | Macrogenics, Inc. | Bi-specific monovalent Fc diabodies that are capable of binding CD32B and CD79b and uses thereof |
| UA116479C2 (uk) | 2013-08-09 | 2018-03-26 | Макродженікс, Інк. | БІСПЕЦИФІЧНЕ МОНОВАЛЕНТНЕ Fc-ДІАТІЛО, ЯКЕ ОДНОЧАСНО ЗВ'ЯЗУЄ CD32B I CD79b, ТА ЙОГО ЗАСТОСУВАННЯ |
| EP2839842A1 (en) | 2013-08-23 | 2015-02-25 | MacroGenics, Inc. | Bi-specific monovalent diabodies that are capable of binding CD123 and CD3 and uses thereof |
| EP2840091A1 (en) | 2013-08-23 | 2015-02-25 | MacroGenics, Inc. | Bi-specific diabodies that are capable of binding gpA33 and CD3 and uses thereof |
| EP3038657A2 (en) | 2013-08-28 | 2016-07-06 | Bioasis Technologies Inc. | Cns-targeted conjugates having modified fc regions and methods of use thereof |
| CN113667013B (zh) | 2013-10-02 | 2024-04-09 | 免疫医疗有限责任公司 | 中和抗甲型流感抗体及其用途 |
| WO2015057939A1 (en) | 2013-10-18 | 2015-04-23 | Biogen Idec Ma Inc. | Anti-s1p4 antibodies and uses thereof |
| SG11201602249RA (en) | 2013-10-18 | 2016-05-30 | Deutsches Krebsforsch | Labeled inhibitors of prostate specific membrane antigen (psma), their use as imaging agents and pharmaceutical agents for the treatment of prostate cancer |
| EA035171B1 (ru) | 2013-11-14 | 2020-05-08 | Эндосайт, Инк. | Конъюгаты на основе связывающихся с psma лигандов или ингибиторов psma для позитронно-эмиссионной томографии |
| KR102454360B1 (ko) | 2013-12-04 | 2022-10-12 | 추가이 세이야쿠 가부시키가이샤 | 화합물의 농도에 따라 항원 결합능이 변화되는 항원 결합 분자 및 그의 라이브러리 |
| CN106029694A (zh) | 2013-12-06 | 2016-10-12 | 达纳-法伯癌症研究院公司 | 治疗性肽 |
| US8980273B1 (en) | 2014-07-15 | 2015-03-17 | Kymab Limited | Method of treating atopic dermatitis or asthma using antibody to IL4RA |
| US8986691B1 (en) | 2014-07-15 | 2015-03-24 | Kymab Limited | Method of treating atopic dermatitis or asthma using antibody to IL4RA |
| GB201403875D0 (en) | 2014-03-05 | 2014-04-16 | Cantargia Ab | Novel antibodies and uses thereof |
| CA3124243A1 (en) | 2014-03-14 | 2015-09-17 | Dana-Farber Cancer Institute, Inc. | Vaccine compositions and methods for restoring nkg2d pathway function against cancers |
| MX380176B (es) | 2014-04-07 | 2025-03-12 | Chugai Pharmaceutical Co Ltd | Molecula ligada a antigeno inmunoactivada. |
| US11760807B2 (en) | 2014-05-08 | 2023-09-19 | Chugai Seiyaku Kabushiki Kaisha | GPC3-targeting drug which is administered to patient responsive to GPC3-targeting drug therapy |
| CN106459954A (zh) | 2014-05-13 | 2017-02-22 | 中外制药株式会社 | 用于具有免疫抑制功能的细胞的t细胞重定向的抗原结合分子 |
| ES2869459T3 (es) * | 2014-05-16 | 2021-10-25 | Medimmune Llc | Moléculas con unión a receptor de fc de neonato alterada que tiene propiedades terapéuticas y de diagnóstico potenciadas |
| AU2015271709B2 (en) | 2014-06-06 | 2020-11-26 | Bristol-Myers Squibb Company | Antibodies against glucocorticoid-induced tumor necrosis factor receptor (GITR) and uses thereof |
| GB201413913D0 (en) | 2014-08-06 | 2014-09-17 | Cantargia Ab | Novel antibodies and uses thereof |
| MA40764A (fr) | 2014-09-26 | 2017-08-01 | Chugai Pharmaceutical Co Ltd | Agent thérapeutique induisant une cytotoxicité |
| MX386297B (es) | 2014-09-29 | 2025-03-18 | Univ Duke | Moleculas biespecificas que comprenden un brazo orientado a la envoltura vih-1. |
| EP4268843B1 (en) | 2014-11-07 | 2025-09-03 | F. Hoffmann-La Roche Ltd | Improved il-6 antibodies |
| HRP20201756T8 (hr) | 2014-11-21 | 2021-08-20 | Bristol-Myers Squibb Company | Antitijela koja sadrže modificirane regije teškog lanca |
| TWI711630B (zh) | 2014-11-21 | 2020-12-01 | 美商必治妥美雅史谷比公司 | 抗cd73抗體及其用途 |
| MY181199A (en) | 2014-12-19 | 2020-12-21 | Chugai Pharmaceutical Co Ltd | Anti-myostatin antibodies, polypeptides containing variant fc regions, and methods of use |
| TWI617580B (zh) | 2014-12-19 | 2018-03-11 | 中外製藥股份有限公司 | 抗c5抗體及使用方法 |
| JP6180663B2 (ja) | 2014-12-23 | 2017-08-16 | ブリストル−マイヤーズ スクイブ カンパニーBristol−Myers Squibb Company | Tigitに対する抗体 |
| US10188759B2 (en) | 2015-01-07 | 2019-01-29 | Endocyte, Inc. | Conjugates for imaging |
| CN107108729A (zh) | 2015-02-05 | 2017-08-29 | 中外制药株式会社 | 包含离子浓度依赖性的抗原结合结构域的抗体,fc区变体,il‑8‑结合抗体,及其应用 |
| KR102788389B1 (ko) | 2015-04-06 | 2025-03-31 | 서브도메인, 엘엘씨 | 드 노보 결합 도메인 함유 폴리펩티드 및 그의 용도 |
| MX2017015041A (es) | 2015-05-29 | 2018-02-26 | Squibb Bristol Myers Co | Anticuerpos contra el miembro 4 de la superfamilia del receptor del factor de necrosis tumoral (ox40) y sus usos. |
| CA2991799A1 (en) | 2015-07-15 | 2017-01-19 | Zymeworks Inc. | Drug-conjugated bi-specific antigen-binding constructs |
| PH12018500386B1 (en) | 2015-09-18 | 2024-01-05 | Chugai Pharmaceutical Co Ltd | Il-8-binding antibodies and uses thereof |
| US11660340B2 (en) | 2015-11-18 | 2023-05-30 | Chugai Seiyaku Kabushiki Kaisha | Combination therapy using T cell redirection antigen binding molecule against cell having immunosuppressing function |
| EP3378488A4 (en) | 2015-11-18 | 2019-10-30 | Chugai Seiyaku Kabushiki Kaisha | METHOD FOR IMPROVING THE HUMORAL IMMUNE REACTION |
| JP6983776B2 (ja) | 2015-11-19 | 2021-12-17 | ブリストル−マイヤーズ スクイブ カンパニーBristol−Myers Squibb Company | グルココルチコイド誘発腫瘍壊死因子受容体(gitr)に対する抗体およびその使用 |
| CA3007031A1 (en) * | 2015-12-01 | 2017-06-08 | Genmab B.V. | Anti-death receptor antibodies and methods of use thereof |
| WO2017110981A1 (en) | 2015-12-25 | 2017-06-29 | Chugai Seiyaku Kabushiki Kaisha | Anti-myostatin antibodies and methods of use |
| CA3004288C (en) | 2015-12-28 | 2025-05-27 | Chugai Seiyaku Kabushiki Kaisha | METHOD FOR PROMOTING THE CLEARANCE EFFICIENCY OF A POLYPEPTIDE CONTAINING THE FC REGION |
| AR107708A1 (es) | 2016-02-23 | 2018-05-23 | Eleven Biotherapeutics Inc | Formulaciones de antagonista de il-6 y sus usos |
| CA3016187A1 (en) | 2016-03-04 | 2017-09-08 | Bristol-Myers Squibb Company | Combination therapy with anti-cd73 antibodies |
| BR112018068363A2 (pt) | 2016-03-14 | 2019-01-15 | Chugai Seiyaku Kabushiki Kaisha | fármaco terapêutico indutor de dano celular para uso em terapia de câncer |
| WO2017159699A1 (en) | 2016-03-15 | 2017-09-21 | Chugai Seiyaku Kabushiki Kaisha | Methods of treating cancers using pd-1 axis binding antagonists and anti-gpc3 antibodies |
| EP3430034A1 (en) | 2016-03-16 | 2019-01-23 | Merrimack Pharmaceuticals, Inc. | Engineered trail for cancer therapy |
| CA3020864A1 (en) | 2016-04-15 | 2017-10-19 | Macrogenics, Inc. | Novel b7-h3-binding molecules, antibody drug conjugates thereof and methods of use thereof |
| US10968279B2 (en) | 2016-05-09 | 2021-04-06 | Bristol-Myers Squibb Company | TL1A antibodies and uses thereof |
| EP4512829A3 (en) | 2016-07-14 | 2025-06-11 | Bristol-Myers Squibb Company | Antibodies against tim3 and uses thereof |
| WO2018022479A1 (en) | 2016-07-25 | 2018-02-01 | Biogen Ma Inc. | Anti-hspa5 (grp78) antibodies and uses thereof |
| KR20250036943A (ko) | 2016-08-02 | 2025-03-14 | 비스테라, 인크. | 조작된 폴리펩티드 및 그의 용도 |
| JP6527643B2 (ja) | 2016-08-05 | 2019-06-05 | 中外製薬株式会社 | Il−8関連疾患の治療用又は予防用組成物 |
| SG11201900746RA (en) | 2016-08-12 | 2019-02-27 | Janssen Biotech Inc | Engineered antibodies and other fc-domain containing molecules with enhanced agonism and effector functions |
| WO2018044970A1 (en) | 2016-08-31 | 2018-03-08 | University Of Rochester | Human monoclonal antibodies to human endogenous retrovirus k envelope (herv-k) and uses thereof |
| SG10201607778XA (en) | 2016-09-16 | 2018-04-27 | Chugai Pharmaceutical Co Ltd | Anti-Dengue Virus Antibodies, Polypeptides Containing Variant Fc Regions, And Methods Of Use |
| GB201619652D0 (en) | 2016-11-21 | 2017-01-04 | Alligator Bioscience Ab | Novel polypeptides |
| CN110662770A (zh) | 2016-11-23 | 2020-01-07 | 比奥维拉迪维治疗股份有限公司 | 结合凝血因子ix和凝血因子x的双特异性抗体 |
| US11608374B2 (en) | 2017-01-30 | 2023-03-21 | Chugai Seiyaku Kabushiki Kaisha | Anti-sclerostin antibodies and methods of use |
| EP3583124A1 (en) | 2017-02-17 | 2019-12-25 | Bristol-Myers Squibb Company | Antibodies to alpha-synuclein and uses thereof |
| CN110352074B (zh) | 2017-02-28 | 2024-07-16 | 思进股份有限公司 | 用于偶联的半胱氨酸突变抗体 |
| US20190382490A1 (en) | 2017-02-28 | 2019-12-19 | Bristol-Myers Squibb Company | Use of anti-ctla-4 antibodies with enhanced adcc to enhance immune response to a vaccine |
| CN110709417B (zh) | 2017-04-07 | 2023-10-31 | 美天施生物科技有限责任两合公司 | 具有突变人IgG4的多肽 |
| JP7679175B2 (ja) | 2017-04-20 | 2025-05-19 | エータイアー ファーマ, インコーポレイテッド | 肺の炎症を治療するための組成物および方法 |
| WO2018213097A1 (en) | 2017-05-15 | 2018-11-22 | University Of Rochester | Broadly neutralizing anti-influenza monoclonal antibody and uses thereof |
| CA3064321A1 (en) | 2017-05-25 | 2018-11-29 | Bristol-Myers Squibb Company | Antibodies comprising modified heavy constant regions |
| AU2018281045A1 (en) * | 2017-06-05 | 2019-12-12 | Janssen Biotech, Inc. | Engineered multispecific antibodies and other multimeric proteins with asymmetrical CH2-CH3 region mutations |
| PT3456736T (pt) * | 2017-09-19 | 2021-05-28 | Tillotts Pharma Ag | Variantes de anticorpos |
| WO2019059411A1 (en) | 2017-09-20 | 2019-03-28 | Chugai Seiyaku Kabushiki Kaisha | DOSAGE FOR POLYTHERAPY USING PD-1 AXIS BINDING ANTAGONISTS AND GPC3 TARGETING AGENT |
| WO2019075090A1 (en) | 2017-10-10 | 2019-04-18 | Tilos Therapeutics, Inc. | ANTI-LAP ANTIBODIES AND USES THEREOF |
| JP7285267B2 (ja) | 2017-11-14 | 2023-06-01 | アーセルクス インコーポレイテッド | Dドメイン含有ポリペプチドおよびその使用 |
| EP3710589A4 (en) | 2017-11-14 | 2021-11-10 | Chugai Seiyaku Kabushiki Kaisha | ANTI-C1S ANTIBODIES AND METHOD OF USING |
| IL314701A (en) | 2017-11-14 | 2024-10-01 | Arcellx Inc | Multifunctional immune cell therapies |
| CN118271444A (zh) | 2017-12-19 | 2024-07-02 | 瑟罗泽恩奥普瑞汀公司 | Wnt替代分子和其用途 |
| JP7418332B2 (ja) | 2017-12-19 | 2024-01-19 | スロゼン オペレーティング, インコーポレイテッド | 抗フリズルド抗体及び使用方法 |
| US11746150B2 (en) | 2017-12-19 | 2023-09-05 | Surrozen Operating, Inc. | Anti-LRP5/6 antibodies and methods of use |
| WO2019126133A1 (en) | 2017-12-20 | 2019-06-27 | Alexion Pharmaceuticals, Inc. | Liquid formulations of anti-cd200 antibodies |
| US11802154B2 (en) | 2017-12-20 | 2023-10-31 | Alexion Pharmaceuticals, Inc. | Humanized anti-CD200 antibodies and uses thereof |
| CN120192415A (zh) | 2018-01-12 | 2025-06-24 | 百时美施贵宝公司 | 抗tim3抗体及其用途 |
| US20210107988A1 (en) * | 2018-01-24 | 2021-04-15 | Genmab B.V. | Polypeptide variants and uses thereof |
| JP2018138022A (ja) * | 2018-02-23 | 2018-09-06 | ゲンマブ ビー.ブイ. | ヒトIgG1 Fc領域変異体およびその使用 |
| IL277375B2 (en) | 2018-03-15 | 2025-08-01 | Chugai Pharmaceutical Co Ltd | Anti-dengue virus antibodies having cross-reactivity to zika virus and methods of use |
| KR20250154550A (ko) | 2018-03-21 | 2025-10-28 | 파이브 프라임 테라퓨틱스, 인크. | 산성 pH에서 VISTA에 결합하는 항체 |
| PE20210665A1 (es) | 2018-03-23 | 2021-03-31 | Bristol Myers Squibb Co | Anticuerpos contra mica y/o micb y sus usos |
| SG11202009625WA (en) | 2018-04-02 | 2020-10-29 | Bristol Myers Squibb Co | Anti-trem-1 antibodies and uses thereof |
| BR112020020961A2 (pt) | 2018-04-17 | 2021-01-19 | Endocyte, Inc. | Métodos de tratamento de câncer |
| US11958895B2 (en) | 2018-05-03 | 2024-04-16 | University Of Rochester | Anti-influenza neuraminidase monoclonal antibodies and uses thereof |
| EP3805400A4 (en) * | 2018-06-04 | 2022-06-29 | Chugai Seiyaku Kabushiki Kaisha | Antigen-binding molecule showing changed half-life in cytoplasm |
| DK3820906T3 (da) | 2018-07-05 | 2025-12-15 | Surrozen Operating Inc | Multispecifikke wnt-surrogatmolekyler og anvendelser deraf |
| MY201995A (en) | 2018-07-09 | 2024-03-28 | Five Prime Therapeutics Inc | Antibodies binding to ilt4 |
| JP7700036B2 (ja) | 2018-07-11 | 2025-06-30 | ファイヴ プライム セラピューティクス インク | 酸性pHでVISTAと結合する抗体 |
| SG10202106830VA (en) | 2018-08-10 | 2021-08-30 | Chugai Pharmaceutical Co Ltd | Anti-cd137 antigen-binding molecule and utilization thereof |
| JP2022504839A (ja) | 2018-10-10 | 2022-01-13 | ティロス・セラピューティクス・インコーポレイテッド | 抗lap抗体変異体及びその使用 |
| KR20210096167A (ko) | 2018-11-28 | 2021-08-04 | 브리스톨-마이어스 스큅 컴퍼니 | 변형된 중쇄 불변 영역을 포함하는 항체 |
| WO2020116560A1 (ja) | 2018-12-05 | 2020-06-11 | 株式会社バイカ・セラピュティクス | 抗体のFc領域改変体 |
| WO2020118011A1 (en) | 2018-12-06 | 2020-06-11 | Alexion Pharmaceuticals, Inc. | Anti-alk2 antibodies and uses thereof |
| WO2020154293A1 (en) | 2019-01-22 | 2020-07-30 | Bristol-Myers Squibb Company | Antibodies against il-7r alpha subunit and uses thereof |
| US20220153875A1 (en) | 2019-03-19 | 2022-05-19 | Chugai Seiyaku Kabushiki Kaisha | Antigen-binding molecule containing antigen-binding domain of which binding activity to antigen is changed depending on mta, and library for obtaining said antigen-binding domain |
| WO2020210358A1 (en) | 2019-04-08 | 2020-10-15 | Biogen Ma Inc. | Anti-integrin antibodies and uses thereof |
| CN113924118A (zh) | 2019-04-18 | 2022-01-11 | 百时美施贵宝公司 | 在低ph下具有增强的结合特异性的伊匹单抗变体 |
| CA3137649A1 (en) | 2019-05-15 | 2020-11-19 | Chugai Seiyaku Kabushiki Kaisha | An antigen-binding molecule, a pharmaceutical composition, and a method |
| CN120097929A (zh) | 2019-05-20 | 2025-06-06 | 因多塞特股份有限公司 | 制备psma缀合物的方法 |
| EP3999543A1 (en) | 2019-07-15 | 2022-05-25 | Bristol-Myers Squibb Company | Anti-trem-1 antibodies and uses thereof |
| CN114144435B (zh) | 2019-07-15 | 2024-06-25 | 百时美施贵宝公司 | 针对人trem-1的抗体及其用途 |
| MX2022003204A (es) | 2019-09-19 | 2022-04-18 | Bristol Myers Squibb Co | Anticuerpos de union al supresor de activacion de linfocitos t que contiene inmunoglobulina con dominio v (vista) a ph acido. |
| EP4126934A1 (en) | 2020-04-01 | 2023-02-08 | University of Rochester | Monoclonal antibodies against the hemagglutinin (ha) and neuraminidase (na) of influenza h3n2 viruses |
| KR20220161337A (ko) | 2020-04-01 | 2022-12-06 | 쿄와 기린 가부시키가이샤 | 항체 조성물 |
| EP4132971A1 (en) | 2020-04-09 | 2023-02-15 | Merck Sharp & Dohme LLC | Affinity matured anti-lap antibodies and uses thereof |
| JP2023523480A (ja) | 2020-04-28 | 2023-06-06 | ザ ロックフェラー ユニバーシティー | 中和抗sars-cov-2抗体およびその使用方法 |
| US20230192867A1 (en) | 2020-05-15 | 2023-06-22 | Bristol-Myers Squibb Company | Antibodies to garp |
| JP7048665B2 (ja) * | 2020-05-22 | 2022-04-05 | ゲンマブ ビー.ブイ. | ヒトIgG1 Fc領域変異体およびその使用 |
| EP4166574A4 (en) | 2020-06-10 | 2025-01-15 | Bica Therapeutics Inc. | FUSION PROTEIN WITH ERYTHROPOIETIN POLYPEPTIDE |
| AU2021306179A1 (en) | 2020-07-10 | 2023-03-02 | Invetx Inc. | Compositions for increasing half-life of a therapeutic agent in felines and methods of use |
| EP4240758A1 (en) | 2020-11-04 | 2023-09-13 | The Rockefeller University | Neutralizing anti-sars-cov-2 antibodies |
| EP4265637A4 (en) | 2020-12-18 | 2025-01-15 | Zhuhai Trinomab Pharmaceutical Co., Ltd. | RESPIRATORY SYNCYTIAL VIRUS SPECIFIC BINDING MOLECULE |
| WO2022136569A1 (en) | 2020-12-23 | 2022-06-30 | Cantargia Ab | Anti-il1rap antibody |
| EP4277926A1 (en) | 2021-01-15 | 2023-11-22 | The Rockefeller University | Neutralizing anti-sars-cov-2 antibodies |
| EP4313083A4 (en) | 2021-03-26 | 2025-06-18 | Arcellx, Inc. | MULTIFUNCTIONAL IMMUNE CELL THERAPIES |
| EP4314068A1 (en) | 2021-04-02 | 2024-02-07 | The Regents Of The University Of California | Antibodies against cleaved cdcp1 and uses thereof |
| WO2022235867A2 (en) | 2021-05-06 | 2022-11-10 | The Rockefeller University | Neutralizing anti-sars- cov-2 antibodies and methods of use thereof |
| WO2023147399A1 (en) | 2022-01-27 | 2023-08-03 | The Rockefeller University | Broadly neutralizing anti-sars-cov-2 antibodies targeting the n-terminal domain of the spike protein and methods of use thereof |
| WO2023191766A1 (en) * | 2022-03-28 | 2023-10-05 | Intervexion Therapeutics, Llc | ANTIBODIES WITH ALTERED FcRn AFFINITY |
| CN120865421A (zh) | 2022-07-22 | 2025-10-31 | 百时美施贵宝公司 | 结合至人类pad4的抗体及其用途 |
| WO2024107749A1 (en) | 2022-11-16 | 2024-05-23 | Attralus, Inc. | Fusion proteins that bind amyloid and the transferrin receptor and uses thereof |
| TW202500583A (zh) * | 2023-03-17 | 2025-01-01 | 美商美國禮來大藥廠 | Pd-1促效劑抗體及以pd-1促效劑抗體治療發炎或自體免疫皮膚疾病之方法 |
| WO2024200573A1 (en) | 2023-03-27 | 2024-10-03 | LAVA Therapeutics N.V. | Nectin-4 binding agents and methods of use |
| AU2024270136A1 (en) | 2023-05-05 | 2025-11-20 | Otsuka Pharmaceutical Co., Ltd. | Anti-il1rap antibodies |
| WO2025012118A2 (en) | 2023-07-07 | 2025-01-16 | LAVA Therapeutics N.V. | 5t4 binding agents and methods of use |
| WO2025024265A1 (en) | 2023-07-21 | 2025-01-30 | Bristol-Myers Squibb Company | Methods of assessing citrullination and activity of pad4 modulators |
| WO2025026282A1 (en) * | 2023-07-29 | 2025-02-06 | Shanghai Kaijin Biotechnology, Ltd | Modified type e multi-specific antibodies |
| WO2025072888A2 (en) | 2023-09-28 | 2025-04-03 | Novavax, Inc. | Anti-sars-cov-2 spike (s) antibodies and their use in treating covid-19 |
| WO2025085489A1 (en) | 2023-10-17 | 2025-04-24 | Bristol-Myers Squibb Company | Gspt1-degrading compounds, anti-cd33 antibodies and antibody-drug conjugates and uses thereof |
| US20250154262A1 (en) * | 2023-10-25 | 2025-05-15 | Ablynx N.V. | Fc DOMAIN VARIANTS WITH ENHANCED Fc RECEPTOR BINDING |
| WO2025155877A2 (en) | 2024-01-18 | 2025-07-24 | The Regents Of The University Of California | Antibodies binding to pad4 and uses thereof |
| WO2025174974A1 (en) | 2024-02-14 | 2025-08-21 | Bristol-Myers Squibb Company | Anti-cd33 antibodies and uses thereof |
| US20250269052A1 (en) | 2024-02-27 | 2025-08-28 | Bristol-Myers Squibb Company | Anti-ceacam5 antibody drug conjugates |
| WO2025184208A1 (en) | 2024-02-27 | 2025-09-04 | Bristol-Myers Squibb Company | Anti-ceacam5 antibodies and uses thereof |
| EP4653010A1 (en) | 2024-05-14 | 2025-11-26 | 35Pharma Inc. | Activin receptor type iib traps for use in improving body composition |
| WO2025245176A1 (en) | 2024-05-22 | 2025-11-27 | Bristol-Myers Squibb Company | Multispecific antibody constructs |
| WO2025255405A1 (en) | 2024-06-06 | 2025-12-11 | Bristol-Myers Squibb Company | Anti-fap antibodies and uses thereof |
| WO2025255349A1 (en) | 2024-06-06 | 2025-12-11 | Bristol-Myers Squibb Company | Multispecific anti-cd40 / anti-fap antibodies and uses thereof |
Family Cites Families (97)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| US5618920A (en) | 1985-11-01 | 1997-04-08 | Xoma Corporation | Modular assembly of antibody genes, antibodies prepared thereby and use |
| US5985599A (en) | 1986-05-29 | 1999-11-16 | The Austin Research Institute | FC receptor for immunoglobulin |
| US6893625B1 (en) | 1986-10-27 | 2005-05-17 | Royalty Pharma Finance Trust | Chimeric antibody with specificity to human B cell surface antigen |
| IL84285A (en) | 1986-10-27 | 1993-03-15 | Int Genetic Engineering | Chimeric antibody with specificity to human tumor antigen |
| IL85035A0 (en) | 1987-01-08 | 1988-06-30 | Int Genetic Eng | Polynucleotide molecule,a chimeric antibody with specificity for human b cell surface antigen,a process for the preparation and methods utilizing the same |
| DE3883899T3 (de) * | 1987-03-18 | 1999-04-22 | Sb2, Inc., Danville, Calif. | Geänderte antikörper. |
| US4861579A (en) | 1988-03-17 | 1989-08-29 | American Cyanamid Company | Suppression of B-lymphocytes in mammals by administration of anti-B-lymphocyte antibodies |
| GB8916400D0 (en) | 1989-07-18 | 1989-09-06 | Dynal As | Modified igg3 |
| GB9022543D0 (en) | 1990-10-17 | 1990-11-28 | Wellcome Found | Antibody production |
| JPH06501705A (ja) | 1990-11-05 | 1994-02-24 | ブリストル−マイアーズ スクイブ カンパニー | 抗−腫瘍抗体及び生物学的活性剤の組合せによる相乗治療 |
| GB9105245D0 (en) | 1991-03-12 | 1991-04-24 | Lynxvale Ltd | Binding molecules |
| EP0640094A1 (en) | 1992-04-24 | 1995-03-01 | The Board Of Regents, The University Of Texas System | Recombinant production of immunoglobulin-like domains in prokaryotic cells |
| US5736137A (en) | 1992-11-13 | 1998-04-07 | Idec Pharmaceuticals Corporation | Therapeutic application of chimeric and radiolabeled antibodies to human B lymphocyte restricted differentiation antigen for treatment of B cell lymphoma |
| DE69303494T2 (de) | 1992-11-13 | 1997-01-16 | Idec Pharma Corp | Therapeutische verwendung von chimerischen und markierten antikörper gegen menschlichen b lymphozyt beschränkter differenzierung antigen für die behandlung von b-zell-lymphoma |
| US5550362A (en) | 1992-11-20 | 1996-08-27 | Intermec Corporation | Method and apparatus for calibrating a bar code scanner |
| WO1994029351A2 (en) | 1993-06-16 | 1994-12-22 | Celltech Limited | Antibodies |
| US5417972A (en) | 1993-08-02 | 1995-05-23 | The Board Of Trustees Of The Leland Stanford Junior University | Method of killing B-cells in a complement independent and an ADCC independent manner using antibodies which specifically bind CDIM |
| GB9316989D0 (en) | 1993-08-16 | 1993-09-29 | Lynxvale Ltd | Binding molecules |
| US5595721A (en) | 1993-09-16 | 1997-01-21 | Coulter Pharmaceutical, Inc. | Radioimmunotherapy of lymphoma using anti-CD20 |
| WO1996004925A1 (en) | 1994-08-12 | 1996-02-22 | Immunomedics, Inc. | Immunoconjugates and humanized antibodies specific for b-cell lymphoma and leukemia cells |
| US6121022A (en) | 1995-04-14 | 2000-09-19 | Genentech, Inc. | Altered polypeptides with increased half-life |
| US6750334B1 (en) | 1996-02-02 | 2004-06-15 | Repligen Corporation | CTLA4-immunoglobulin fusion proteins having modified effector functions and uses therefor |
| JP4046354B2 (ja) | 1996-03-18 | 2008-02-13 | ボード オブ リージェンツ,ザ ユニバーシティ オブ テキサス システム | 増大した半減期を有する免疫グロブリン様ドメイン |
| US5834597A (en) | 1996-05-20 | 1998-11-10 | Protein Design Labs, Inc. | Mutated nonactivating IgG2 domains and anti CD3 antibodies incorporating the same |
| ATE386809T1 (de) | 1996-08-02 | 2008-03-15 | Bristol Myers Squibb Co | Ein verfahren zur inhibierung immunglobulininduzierter toxizität aufgrund von der verwendung von immunoglobinen in therapie und in vivo diagnostik |
| WO1998023289A1 (en) | 1996-11-27 | 1998-06-04 | The General Hospital Corporation | MODULATION OF IgG BINDING TO FcRn |
| US6277375B1 (en) | 1997-03-03 | 2001-08-21 | Board Of Regents, The University Of Texas System | Immunoglobulin-like domains with increased half-lives |
| US6183744B1 (en) | 1997-03-24 | 2001-02-06 | Immunomedics, Inc. | Immunotherapy of B-cell malignancies using anti-CD22 antibodies |
| US6306393B1 (en) | 1997-03-24 | 2001-10-23 | Immunomedics, Inc. | Immunotherapy of B-cell malignancies using anti-CD22 antibodies |
| DE19721700C1 (de) | 1997-05-23 | 1998-11-19 | Deutsches Krebsforsch | Mutierter OKT3-Antikörper |
| JP3919235B2 (ja) | 1997-06-13 | 2007-05-23 | ジェネンテク,インコーポレイテッド | 抗体製剤 |
| US6171586B1 (en) | 1997-06-13 | 2001-01-09 | Genentech, Inc. | Antibody formulation |
| JP2002506353A (ja) | 1997-06-24 | 2002-02-26 | ジェネンテック・インコーポレーテッド | ガラクトシル化糖タンパク質の方法及び組成物 |
| WO1999022764A1 (en) | 1997-10-31 | 1999-05-14 | Genentech, Inc. | Methods and compositions comprising glycoprotein glycoforms |
| US6194551B1 (en) | 1998-04-02 | 2001-02-27 | Genentech, Inc. | Polypeptide variants |
| US6528624B1 (en) | 1998-04-02 | 2003-03-04 | Genentech, Inc. | Polypeptide variants |
| US6242195B1 (en) | 1998-04-02 | 2001-06-05 | Genentech, Inc. | Methods for determining binding of an analyte to a receptor |
| PT1068241E (pt) | 1998-04-02 | 2007-11-19 | Genentech Inc | Variantes de anticorpos e respectivos fragmentos |
| GB9809951D0 (en) | 1998-05-08 | 1998-07-08 | Univ Cambridge Tech | Binding molecules |
| KR101063278B1 (ko) | 1998-08-11 | 2011-09-07 | 바이오겐 아이덱 인크. | B-세포 림프종을 치료하기 위한 항-cd20 항체를 포함하는 약제 |
| US20020142374A1 (en) | 1998-08-17 | 2002-10-03 | Michael Gallo | Generation of modified molecules with increased serum half-lives |
| US6224866B1 (en) | 1998-10-07 | 2001-05-01 | Biocrystal Ltd. | Immunotherapy of B cell involvement in progression of solid, nonlymphoid tumors |
| EP1131093A4 (en) | 1998-11-09 | 2002-05-02 | Idec Pharma Corp | TREATMENT OF HEMATOLOGICAL VILTIES ASSOCIATED WITH CIRCULATING TUMOR CELLS USING CHIMERIC ANTI-CD20 ANTIBODIES |
| AU761516B2 (en) | 1998-11-09 | 2003-06-05 | Biogen Inc. | Chimeric anti-CD20 antibody treatment of patients receiving BMT or PBSC transplants |
| AU1728800A (en) | 1998-11-18 | 2000-06-05 | Genentech Inc. | Antibody variants with higher binding affinity compared to parent antibodies |
| GB9900009D0 (en) * | 1999-01-04 | 1999-02-24 | Ml Lab Plc | Gene therapy |
| US6737056B1 (en) | 1999-01-15 | 2004-05-18 | Genentech, Inc. | Polypeptide variants with altered effector function |
| KR101077001B1 (ko) | 1999-01-15 | 2011-10-26 | 제넨테크, 인크. | 효과기 기능이 변화된 폴리펩티드 변이체 |
| US6897044B1 (en) | 1999-01-28 | 2005-05-24 | Biogen Idec, Inc. | Production of tetravalent antibodies |
| KR20020027311A (ko) | 1999-05-07 | 2002-04-13 | 제넨테크, 인크. | B 세포 표면 마커에 결합하는 길항물질을 이용한자가면역 질환의 치료 |
| EP1194167B1 (en) | 1999-06-09 | 2009-08-19 | Immunomedics, Inc. | Immunotherapy of autoimmune disorders using antibodies which target b-cells |
| ITMI991299A1 (it) | 1999-06-11 | 2000-12-11 | Consiglio Nazionale Ricerche | Uso di anticorpi contro antigeni di superficie per il trattamento della malattia trapianto contro ospite |
| CN1373672A (zh) | 1999-07-12 | 2002-10-09 | 杰南技术公司 | 应用结合cd20的拮抗剂阻断对外来抗原的免疫应答 |
| US8557244B1 (en) | 1999-08-11 | 2013-10-15 | Biogen Idec Inc. | Treatment of aggressive non-Hodgkins lymphoma with anti-CD20 antibody |
| CN100389825C (zh) | 1999-08-11 | 2008-05-28 | 拜奥根Idec公司 | 用抗cd20抗体治疗累及骨髓的非霍奇金淋巴瘤患者 |
| AU6929100A (en) | 1999-08-23 | 2001-03-19 | Biocrystal Limited | Methods and compositions for immunotherapy of b cell involvement in promotion ofa disease condition comprising multiple sclerosis |
| DK1265928T3 (da) | 2000-01-27 | 2010-11-15 | Medimmune Llc | RSV-neutraliserende antistoffer med ultra høj affinitet |
| AU4314801A (en) | 2000-02-11 | 2001-08-20 | Lexigen Pharm Corp | Enhancing the circulating half-life of antibody-based fusion proteins |
| KR20020091170A (ko) | 2000-03-31 | 2002-12-05 | 아이덱 파마슈티칼즈 코포레이션 | B 세포 림프종의 치료를 위한 항-사이토카인 항체 또는길항제 및 항-cd20의 조합된 사용 |
| CA2399940A1 (en) | 2000-04-13 | 2001-10-25 | The Rockefeller University | Enhancement of antibody-mediated immune responses |
| BR0110364A (pt) | 2000-04-25 | 2003-12-30 | Idec Pharma Corp | Administração intratecal de rituximab para tratamento de linfomas do sistema nervoso central |
| JP2004512262A (ja) | 2000-06-20 | 2004-04-22 | アイデック ファーマスーティカルズ コーポレイション | 非放射性抗cd20抗体/放射標識抗cd22抗体の組合せ |
| US20020128448A1 (en) | 2000-10-20 | 2002-09-12 | Idec Pharmaceuticals Corporation | Variant IgG3 Rituxan and therapeutic use thereof |
| DK1355919T3 (da) | 2000-12-12 | 2011-03-14 | Medimmune Llc | Molekyler med længere halveringstider, sammensætninger og anvendelser deraf |
| US20030133939A1 (en) | 2001-01-17 | 2003-07-17 | Genecraft, Inc. | Binding domain-immunoglobulin fusion proteins |
| PL372140A1 (en) | 2001-01-29 | 2005-07-11 | Idec Pharmaceuticals Corporation | Modified antibodies and methods of use |
| JP2005500018A (ja) | 2001-04-02 | 2005-01-06 | アイデック ファーマスーティカルズ コーポレイション | GnTIIIと同時発現する組換え抗体 |
| ES2364816T3 (es) | 2001-04-02 | 2011-09-14 | Genentech, Inc. | Terapia de combinación. |
| WO2003061694A1 (en) | 2001-05-10 | 2003-07-31 | Seattle Genetics, Inc. | Immunosuppression of the humoral immune response by anti-cd20 antibodies |
| US7321026B2 (en) | 2001-06-27 | 2008-01-22 | Skytech Technology Limited | Framework-patched immunoglobulins |
| EP2295468B1 (en) | 2002-02-14 | 2015-07-08 | Immunomedics, Inc. | Anti-CD20 antibodies and fusion proteins thereof and methods of use |
| US20040002587A1 (en) | 2002-02-20 | 2004-01-01 | Watkins Jeffry D. | Fc region variants |
| US20040110226A1 (en) | 2002-03-01 | 2004-06-10 | Xencor | Antibody optimization |
| US20040132101A1 (en) * | 2002-09-27 | 2004-07-08 | Xencor | Optimized Fc variants and methods for their generation |
| US7317091B2 (en) | 2002-03-01 | 2008-01-08 | Xencor, Inc. | Optimized Fc variants |
| WO2005056606A2 (en) * | 2003-12-03 | 2005-06-23 | Xencor, Inc | Optimized antibodies that target the epidermal growth factor receptor |
| DK1534335T4 (en) | 2002-08-14 | 2015-10-05 | Macrogenics Inc | FCGAMMARIIB-SPECIFIC ANTIBODIES AND PROCEDURES FOR USE THEREOF |
| EP2298805A3 (en) | 2002-09-27 | 2011-04-13 | Xencor, Inc. | Optimized Fc variants and methods for their generation |
| KR100932340B1 (ko) | 2002-10-17 | 2009-12-16 | 젠맵 에이/에스 | Cd20에 대한 인간 모노클로날 항체 |
| CN103833854B (zh) | 2002-12-16 | 2017-12-12 | 健泰科生物技术公司 | 免疫球蛋白变体及其用途 |
| CA2512729C (en) * | 2003-01-09 | 2014-09-16 | Macrogenics, Inc. | Identification and engineering of antibodies with variant fc regions and methods of using same |
| EP1613350B1 (en) | 2003-04-09 | 2009-03-18 | Genentech, Inc. | Therapy of autoimmune disease in a patient with an inadequate response to a tnf-alpha inhibitor |
| KR101412271B1 (ko) | 2003-05-09 | 2014-06-25 | 듀크 유니버시티 | Cd20-특이적 항체 및 이를 이용한 방법 |
| AR044388A1 (es) | 2003-05-20 | 2005-09-07 | Applied Molecular Evolution | Moleculas de union a cd20 |
| US8147832B2 (en) | 2003-08-14 | 2012-04-03 | Merck Patent Gmbh | CD20-binding polypeptide compositions and methods |
| BRPI0416262B1 (pt) | 2003-11-05 | 2022-04-12 | Roche Glycart Ag | Anticorpo anti-cd20 humano tipo ii humanizado, seu método de produção, seus usos, bem como polinucleotídeo isolado, vetor de expressão e composição farmacêutica |
| DE602005015542D1 (de) | 2004-01-12 | 2009-09-03 | Applied Molecular Evolution | Varianten der fc-region |
| EP1740946B1 (en) | 2004-04-20 | 2013-11-06 | Genmab A/S | Human monoclonal antibodies against cd20 |
| WO2006085967A2 (en) | 2004-07-09 | 2006-08-17 | Xencor, Inc. | OPTIMIZED ANTI-CD20 MONOCONAL ANTIBODIES HAVING Fc VARIANTS |
| JP2008505174A (ja) | 2004-07-15 | 2008-02-21 | ゼンコー・インコーポレイテッド | 最適化Fc変異体 |
| CN101001873B (zh) | 2004-08-04 | 2013-03-13 | 曼璀克生物科技有限责任公司 | Fc区变体 |
| AR052774A1 (es) | 2004-10-08 | 2007-04-04 | Wyeth Corp | Inmunoterapia para trastornos autoinmunes |
| EP2325206B1 (en) | 2004-11-12 | 2014-03-19 | Xencor, Inc. | Fc variants with altered binding to fcrn |
| FR2879204B1 (fr) | 2004-12-15 | 2007-02-16 | Lab Francais Du Fractionnement | Anticorps cytotoxique dirige contre les proliferations hematopoietiques lymphoides de type b. |
| JP2008526998A (ja) | 2005-01-13 | 2008-07-24 | ジェネンテック・インコーポレーテッド | 治療方法 |
| DOP2006000029A (es) | 2005-02-07 | 2006-08-15 | Genentech Inc | Antibody variants and uses thereof. (variantes de un anticuerpo y usos de las mismas) |
| AU2006230413B8 (en) | 2005-03-31 | 2011-01-20 | Xencor, Inc | Fc variants with optimized properties |
-
2005
- 2005-07-18 CN CN2005800261833A patent/CN101001873B/zh not_active Expired - Fee Related
- 2005-07-18 ES ES05773014T patent/ES2426816T3/es not_active Expired - Lifetime
- 2005-07-18 PL PL05773014T patent/PL1776384T3/pl unknown
- 2005-07-18 CA CA2779559A patent/CA2779559A1/en not_active Abandoned
- 2005-07-18 EP EP08163100.4A patent/EP2213683B1/en not_active Expired - Lifetime
- 2005-07-18 CA CA2573192A patent/CA2573192C/en not_active Expired - Fee Related
- 2005-07-18 US US11/572,634 patent/US7740847B2/en active Active
- 2005-07-18 PL PL08163100T patent/PL2213683T3/pl unknown
- 2005-07-18 DK DK05773014.5T patent/DK1776384T3/da active
- 2005-07-18 MX MX2007001345A patent/MX2007001345A/es active IP Right Grant
- 2005-07-18 KR KR1020077002748A patent/KR100864549B1/ko not_active Expired - Fee Related
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| Date | Code | Title | Description |
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Effective date: 20140425 |