JP2005506064A - キメラヘテロ多量体の生成のための組成物及び方法 - Google Patents
キメラヘテロ多量体の生成のための組成物及び方法 Download PDFInfo
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- C07K2317/50—Immunoglobulins specific features characterized by immunoglobulin fragments
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Cited By (4)
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| JP2013511268A (ja) * | 2009-11-18 | 2013-04-04 | ピエール、ファーブル、メディカマン | 新規なファージディスプレイベクター |
| JP2019501887A (ja) * | 2015-12-03 | 2019-01-24 | ユーシービー バイオファルマ エスピーアールエル | 多特異性抗体 |
Families Citing this family (287)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
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| US9250229B2 (en) | 2011-09-25 | 2016-02-02 | Theranos, Inc. | Systems and methods for multi-analysis |
| SG11201401422VA (en) * | 2011-10-27 | 2014-09-26 | Genmab As | Production of heterodimeric proteins |
| US11851476B2 (en) | 2011-10-31 | 2023-12-26 | Chugai Seiyaku Kabushiki Kaisha | Antigen-binding molecule having regulated conjugation between heavy-chain and light-chain |
| LT2782598T (lt) * | 2011-11-23 | 2020-07-27 | In3Bio Ltd. | Rekombinantiniai baltymai ir jų terapinis panaudojimas |
| WO2013119966A2 (en) | 2012-02-10 | 2013-08-15 | Genentech, Inc. | Single-chain antibodies and other heteromultimers |
| US9090694B2 (en) | 2012-04-30 | 2015-07-28 | Janssen Biotech, Inc. | ST2L antibody antagonists |
| RU2639287C2 (ru) | 2012-06-27 | 2017-12-20 | Ф. Хоффманн-Ля Рош Аг | Способ отбора и получения высокоселективных и мультиспецифичных нацеливающих групп с заданными свойствами, включающих по меньшей мере две различные связывающие группировки, и их применения |
| KR20150030744A (ko) | 2012-06-27 | 2015-03-20 | 에프. 호프만-라 로슈 아게 | 표적에 특이적으로 결합하는 하나 이상의 결합 단위를 포함하는 항체 Fc-영역 접합체의 제조 방법 및 그의 용도 |
| IN2015DN01115A (enExample) | 2012-07-13 | 2015-06-26 | Zymeworks Inc | |
| KR101963231B1 (ko) * | 2012-09-11 | 2019-03-28 | 삼성전자주식회사 | 이중특이 항체의 제작을 위한 단백질 복합체 및 이를 이용한 이중특이 항체 제조 방법 |
| US10329350B2 (en) * | 2012-12-26 | 2019-06-25 | Industrial Technology Research Institute | Method for producing a multivalent fab fragment with collagen-like peptide |
| 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 |
| US9168300B2 (en) | 2013-03-14 | 2015-10-27 | Oncomed Pharmaceuticals, Inc. | MET-binding agents and uses thereof |
| ES2882183T3 (es) | 2013-03-14 | 2021-12-01 | Univ Duke | Moléculas biespecíficas que son inmunorreactivas con células efectoras inmunitarias que expresan un receptor activador |
| CN105358575B (zh) | 2013-03-15 | 2020-09-22 | 詹森生物科技公司 | 干扰素α和ω抗体拮抗剂 |
| AU2014237362A1 (en) | 2013-03-15 | 2015-09-17 | Theranos Ip Company, Llc | Devices, systems and methods for sample preparation |
| KR20160006168A (ko) | 2013-03-18 | 2016-01-18 | 바이오서오엑스 프로덕스 비.브이. | 인간화 항-cd134(ox40) 항체 및 이의 용도 |
| SG11201601611WA (en) | 2013-09-06 | 2016-04-28 | Theranos Inc | Systems and methods for detecting infectious diseases |
| US10370776B2 (en) * | 2013-09-25 | 2019-08-06 | Idea Orchard, Llc | Antibody like protein |
| ES2881306T3 (es) | 2013-09-27 | 2021-11-29 | Chugai Pharmaceutical Co Ltd | Método para la producción de heteromultímeros de polipéptidos |
| LT3065774T (lt) | 2013-11-06 | 2021-09-10 | Janssen Biotech, Inc. | Anti-ccl17 antikūnai |
| JOP20200094A1 (ar) | 2014-01-24 | 2017-06-16 | Dana Farber Cancer Inst Inc | جزيئات جسم مضاد لـ pd-1 واستخداماتها |
| JOP20200096A1 (ar) | 2014-01-31 | 2017-06-16 | Children’S Medical Center Corp | جزيئات جسم مضاد لـ tim-3 واستخداماتها |
| US9732154B2 (en) | 2014-02-28 | 2017-08-15 | Janssen Biotech, Inc. | Anti-CD38 antibodies for treatment of acute lymphoblastic leukemia |
| ME03558B (me) | 2014-03-14 | 2020-07-20 | Novartis Ag | Molekuli anti-lag-3 antiтela i njihove upotrebe |
| WO2015142675A2 (en) | 2014-03-15 | 2015-09-24 | Novartis Ag | Treatment of cancer using chimeric antigen receptor |
| NZ726520A (en) | 2014-05-29 | 2018-12-21 | Macrogenics Inc | Tri-specific binding molecules that specifically bind to multiple cancer antigens and methods of use thereof |
| GB201409558D0 (en) | 2014-05-29 | 2014-07-16 | Ucb Biopharma Sprl | Method |
| TWI713453B (zh) | 2014-06-23 | 2020-12-21 | 美商健生生物科技公司 | 干擾素α及ω抗體拮抗劑 |
| GB201411320D0 (en) | 2014-06-25 | 2014-08-06 | Ucb Biopharma Sprl | Antibody construct |
| TWI693232B (zh) | 2014-06-26 | 2020-05-11 | 美商宏觀基因股份有限公司 | 與pd-1和lag-3具有免疫反應性的共價結合的雙抗體和其使用方法 |
| US9884921B2 (en) | 2014-07-01 | 2018-02-06 | Pfizer Inc. | Bispecific heterodimeric diabodies and uses thereof |
| GB201412659D0 (en) | 2014-07-16 | 2014-08-27 | Ucb Biopharma Sprl | Molecules |
| GB201412658D0 (en) | 2014-07-16 | 2014-08-27 | Ucb Biopharma Sprl | Molecules |
| WO2016014565A2 (en) | 2014-07-21 | 2016-01-28 | Novartis Ag | Treatment of cancer using humanized anti-bcma chimeric antigen receptor |
| BR112017001242A2 (pt) | 2014-07-21 | 2017-12-05 | Novartis Ag | tratamento de câncer usando um receptor antigênico quimérico a cd33 |
| JP2017528433A (ja) | 2014-07-21 | 2017-09-28 | ノバルティス アーゲー | 低い免疫増強用量のmTOR阻害剤とCARの組み合わせ |
| WO2016014553A1 (en) | 2014-07-21 | 2016-01-28 | Novartis Ag | Sortase synthesized chimeric antigen receptors |
| US20170209492A1 (en) | 2014-07-31 | 2017-07-27 | Novartis Ag | Subset-optimized chimeric antigen receptor-containing t-cells |
| JP6919118B2 (ja) | 2014-08-14 | 2021-08-18 | ノバルティス アーゲー | GFRα−4キメラ抗原受容体を用いる癌の治療 |
| MY189028A (en) | 2014-08-19 | 2022-01-20 | Novartis Ag | Anti-cd123 chimeric antigen receptor (car) for use in cancer treatment |
| MY192918A (en) | 2014-09-09 | 2022-09-15 | Janssen Biotech Inc | Combination therapies with anti-cd38 antibodies |
| CA2961636A1 (en) | 2014-09-17 | 2016-03-24 | Boris ENGELS | Targeting cytotoxic cells with chimeric receptors for adoptive immunotherapy |
| AU2015321546B2 (en) | 2014-09-26 | 2020-09-03 | Macrogenics, Inc. | Bi-specific monovalent diabodies that are capable of binding CD19 and CD3, and uses thereof |
| CN107108721B (zh) | 2014-09-29 | 2021-09-07 | 杜克大学 | 包含hiv-1包膜靶向臂的双特异性分子 |
| MX389663B (es) | 2014-10-14 | 2025-03-20 | Novartis Ag | Moleculas de anticuerpo que se unen a pd-l1 y usos de las mismas. |
| PL3227332T3 (pl) | 2014-12-03 | 2020-06-15 | F. Hoffmann-La Roche Ag | Wielospecyficzne przeciwciała |
| US20180334490A1 (en) | 2014-12-03 | 2018-11-22 | Qilong H. Wu | Methods for b cell preconditioning in car therapy |
| EP3227338A4 (en) | 2014-12-04 | 2018-05-16 | Janssen Biotech, Inc. | Anti-cd38 antibodies for treatment of acute myeloid leukemia |
| AU2015380455A1 (en) | 2015-01-26 | 2017-08-03 | Macrogenics, Inc. | Multivalent molecules comprising DR5-binding domains |
| WO2016159213A1 (ja) | 2015-04-01 | 2016-10-06 | 中外製薬株式会社 | ポリペプチド異種多量体の製造方法 |
| IL254817B2 (en) | 2015-04-08 | 2023-12-01 | Novartis Ag | Cd20 therapies, cd22 therapies, and combination therapies with a cd19 chimeric antigen receptor (car) - expressing cell |
| WO2016172583A1 (en) | 2015-04-23 | 2016-10-27 | Novartis Ag | Treatment of cancer using chimeric antigen receptor and protein kinase a blocker |
| CR20170526A (es) | 2015-05-20 | 2018-04-03 | Janssen Biotech Inc | ANTICUERPOS ANTI-CD38 PARA EL TRATAMIENTO DE AMILOIDOSIS DE CADENA LIGERA y OTRAS ENFERMEDADES MALIGNAS HEMATOLÓGICAS POSITIVAS PARA CD38 |
| TWI773646B (zh) | 2015-06-08 | 2022-08-11 | 美商宏觀基因股份有限公司 | 結合lag-3的分子和其使用方法 |
| MY192978A (en) | 2015-06-22 | 2022-09-20 | Janssen Biotech Inc | Combination therapies for heme malignancies with anti-cd38 antibodies and survivin inhibitors |
| HUE066300T2 (hu) | 2015-06-24 | 2024-07-28 | Janssen Biotech Inc | Immunmoduláció és szolid tumorok kezelése CD38-hoz specifikusan kötõdõ antitestekkel |
| GB201601075D0 (en) | 2016-01-20 | 2016-03-02 | Ucb Biopharma Sprl | Antibodies molecules |
| GB201601077D0 (en) | 2016-01-20 | 2016-03-02 | Ucb Biopharma Sprl | Antibody molecule |
| GB201601073D0 (en) | 2016-01-20 | 2016-03-02 | Ucb Biopharma Sprl | Antibodies |
| EP3878465A1 (en) | 2015-07-29 | 2021-09-15 | Novartis AG | Combination therapies comprising antibody molecules to tim-3 |
| DK3317301T3 (da) | 2015-07-29 | 2021-06-28 | Immutep Sas | Kombinationsterapier omfattende antistofmolekyler mod lag-3 |
| US20180222982A1 (en) | 2015-07-29 | 2018-08-09 | Novartis Ag | Combination therapies comprising antibody molecules to pd-1 |
| CN116333138A (zh) | 2015-07-30 | 2023-06-27 | 宏观基因有限公司 | Pd-1结合分子和其使用方法 |
| CA2994825A1 (en) | 2015-08-05 | 2017-02-09 | Janssen Biotech, Inc. | Anti-cd154 antibodies and methods of using them |
| PL3827845T3 (pl) | 2015-11-03 | 2022-07-11 | Janssen Biotech, Inc. | Formulacje podskórne przeciwciał anty-cd38 i ich zastosowania |
| GB201521389D0 (en) | 2015-12-03 | 2016-01-20 | Ucb Biopharma Sprl | Method |
| GB201521391D0 (en) * | 2015-12-03 | 2016-01-20 | Ucb Biopharma Sprl | Antibodies |
| GB201521382D0 (en) * | 2015-12-03 | 2016-01-20 | Ucb Biopharma Sprl | Antibodies |
| GB201521383D0 (en) | 2015-12-03 | 2016-01-20 | Ucb Biopharma Sprl And Ucb Celltech | Method |
| TW202208440A (zh) | 2015-12-14 | 2022-03-01 | 美商宏觀基因股份有限公司 | 對於pd-1和ctla-4具有免疫反應性的雙特異性分子及其使用方法 |
| EP3389712B1 (en) | 2015-12-17 | 2024-04-10 | Novartis AG | Antibody molecules to pd-1 and uses thereof |
| EP3390453A2 (en) | 2015-12-17 | 2018-10-24 | Janssen Biotech, Inc. | Antibodies specifically binding hla-dr and their uses |
| JP2019502695A (ja) | 2015-12-17 | 2019-01-31 | ノバルティス アーゲー | PD−1に対する抗体分子とC−Met阻害剤との組合せおよびその使用 |
| MA44140A (fr) | 2015-12-22 | 2021-05-19 | Dana Farber Cancer Inst Inc | Récepteur d'antigène chimérique (car) contre la mésothéline et anticorps contre l'inhibiteur de pd-l1 pour une utilisation combinée dans une thérapie anticancéreuse |
| JP7219005B2 (ja) | 2015-12-28 | 2023-02-07 | 中外製薬株式会社 | Fc領域含有ポリペプチドの精製を効率化するための方法 |
| WO2017125897A1 (en) | 2016-01-21 | 2017-07-27 | Novartis Ag | Multispecific molecules targeting cll-1 |
| WO2017142928A1 (en) | 2016-02-17 | 2017-08-24 | Macrogenics, Inc. | Ror1-binding molecules, and methods of use thereof |
| CA3016287A1 (en) | 2016-03-04 | 2017-09-08 | Novartis Ag | Cells expressing multiple chimeric antigen receptor (car) molecules and uses therefore |
| EP3431102A4 (en) | 2016-03-14 | 2019-09-25 | Chugai Seiyaku Kabushiki Kaisha | CELL DAMAGING THERAPEUTIC MEDICAMENT FOR USE IN CANCER THERAPY |
| GB201604458D0 (en) | 2016-03-16 | 2016-04-27 | Immatics Biotechnologies Gmbh | Peptides and combination of peptides for use in immunotherapy against cancers |
| EP3432924A1 (en) | 2016-03-23 | 2019-01-30 | Novartis AG | Cell secreted minibodies and uses thereof |
| MY198114A (en) | 2016-04-15 | 2023-08-04 | Macrogenics Inc | Novel b7-h3-binding molecules, antibody drug conjugates thereof and methods of use thereof |
| SI3443096T1 (sl) | 2016-04-15 | 2023-07-31 | Novartis Ag | Sestavki in postopki za selektivno izražanje himerni antigenskih receptorjev |
| JP7320943B2 (ja) | 2016-04-28 | 2023-08-04 | 中外製薬株式会社 | 抗体含有製剤 |
| EP3464375A2 (en) | 2016-06-02 | 2019-04-10 | Novartis AG | Therapeutic regimens for chimeric antigen receptor (car)- expressing cells |
| JP2019527678A (ja) | 2016-06-28 | 2019-10-03 | ユーエムセー・ユトレヒト・ホールディング・ベー・フェー | CD38に特異的に結合する抗体によるIgE媒介疾患の治療 |
| CN120285179A (zh) | 2016-07-15 | 2025-07-11 | 诺华股份有限公司 | 使用与激酶抑制剂组合的嵌合抗原受体治疗和预防细胞因子释放综合征 |
| IL264486B2 (en) | 2016-07-28 | 2025-04-01 | Novartis Ag | Combination therapies of chimeric antigen receptors and PD-1 inhibitors |
| SG11201900885VA (en) | 2016-08-01 | 2019-02-27 | Novartis Ag | Treatment of cancer using a chimeric antigen receptor in combination with an inhibitor of a pro-m2 macrophage molecule |
| EP3523331A1 (en) | 2016-10-07 | 2019-08-14 | Novartis AG | Chimeric antigen receptors for the treatment of cancer |
| EP4653464A2 (en) | 2016-12-23 | 2025-11-26 | MacroGenics, Inc. | Adam9-binding molecules, and methods of use thereof |
| JP7117311B2 (ja) | 2017-01-26 | 2022-08-12 | ゼットリップ ホールディング リミテッド | Cd47抗原結合単位およびその使用 |
| EP4043485A1 (en) | 2017-01-26 | 2022-08-17 | Novartis AG | Cd28 compositions and methods for chimeric antigen receptor therapy |
| EP3585431A4 (en) | 2017-02-24 | 2020-12-16 | MacroGenics, Inc. | BISPECIFIC BINDING MOLECULES CAPABLE OF BINDING TO CD137 AND TUMOR ANTIGENS, AND THEIR USES |
| US20200048359A1 (en) | 2017-02-28 | 2020-02-13 | Novartis Ag | Shp inhibitor compositions and uses for chimeric antigen receptor therapy |
| CN106905435B (zh) * | 2017-03-13 | 2020-04-10 | 武汉海沙百得生物技术有限公司 | 一种制备基于蛋白a突变体的结合蛋白的方法 |
| EP3615055A1 (en) | 2017-04-28 | 2020-03-04 | Novartis AG | Cells expressing a bcma-targeting chimeric antigen receptor, and combination therapy with a gamma secretase inhibitor |
| WO2018201051A1 (en) | 2017-04-28 | 2018-11-01 | Novartis Ag | Bcma-targeting agent, and combination therapy with a gamma secretase inhibitor |
| CN108866635B (zh) * | 2017-05-09 | 2021-11-26 | 安升(上海)医药科技有限公司 | 多特异性蛋白药物及其文库、以及制备方法和应用 |
| UY37758A (es) | 2017-06-12 | 2019-01-31 | Novartis Ag | Método de fabricación de anticuerpos biespecíficos, anticuerpos biespecíficos y uso terapéutico de dichos anticuerpos |
| EP3641812A1 (en) | 2017-06-22 | 2020-04-29 | Novartis AG | Antibody molecules to cd73 and uses thereof |
| AU2018292618A1 (en) | 2017-06-27 | 2019-12-19 | Novartis Ag | Dosage regimens for anti-TIM-3 antibodies and uses thereof |
| EP3652209A2 (en) | 2017-07-11 | 2020-05-20 | Compass Therapeutics LLC | Agonist antibodies that bind human cd137 and uses thereof |
| KR20250025039A (ko) | 2017-07-20 | 2025-02-20 | 노파르티스 아게 | 항-lag-3 항체의 투여 요법 및 그의 용도 |
| WO2019089753A2 (en) | 2017-10-31 | 2019-05-09 | Compass Therapeutics Llc | Cd137 antibodies and pd-1 antagonists and uses thereof |
| AU2018361430B2 (en) | 2017-11-01 | 2025-08-14 | Chugai Seiyaku Kabushiki Kaisha | Antibody variant and isoform with lowered biological activity |
| AU2018368731A1 (en) | 2017-11-16 | 2020-05-14 | Novartis Ag | Combination therapies |
| US11851497B2 (en) | 2017-11-20 | 2023-12-26 | Compass Therapeutics Llc | CD137 antibodies and tumor antigen-targeting antibodies and uses thereof |
| JP2021505637A (ja) | 2017-12-12 | 2021-02-18 | マクロジェニクス,インコーポレーテッド | 二重特異性cd16結合分子、及び疾患の治療におけるその使用 |
| EP3737692A4 (en) | 2018-01-09 | 2021-09-29 | Elstar Therapeutics, Inc. | CALRETICULIN AND MODIFIED T-LYMPHOCYTES BINDING CONSTRUCTIONS FOR THE TREATMENT OF DISEASES |
| CA3090249A1 (en) | 2018-01-31 | 2019-08-08 | Novartis Ag | Combination therapy using a chimeric antigen receptor |
| AU2019222666B2 (en) | 2018-02-15 | 2025-12-04 | Macrogenics, Inc. | Variant CD3-binding domains and their use in combination therapies for the treatment of disease |
| US12152073B2 (en) | 2018-03-14 | 2024-11-26 | Marengo Therapeutics, Inc. | Multifunctional molecules that bind to calreticulin and uses thereof |
| US20210147547A1 (en) | 2018-04-13 | 2021-05-20 | Novartis Ag | Dosage Regimens For Anti-Pd-L1 Antibodies And Uses Thereof |
| US20210047405A1 (en) | 2018-04-27 | 2021-02-18 | Novartis Ag | Car t cell therapies with enhanced efficacy |
| CA3099450A1 (en) | 2018-05-08 | 2019-11-14 | Amgen Inc. | Bispecific antibodies with cleavable c-terminal charge-paired tags |
| AU2019270624B2 (en) | 2018-05-16 | 2024-05-02 | Janssen Biotech, Inc. | Methods of treating cancers and enhancing efficacy of T cell redirecting therapeutics |
| AU2019272575A1 (en) | 2018-05-21 | 2020-12-10 | Compass Therapeutics Llc | Compositions and methods for enhancing the killing of target cells by NK cells |
| WO2019226658A1 (en) | 2018-05-21 | 2019-11-28 | Compass Therapeutics Llc | Multispecific antigen-binding compositions and methods of use |
| US20210213063A1 (en) | 2018-05-25 | 2021-07-15 | Novartis Ag | Combination therapy with chimeric antigen receptor (car) therapies |
| US20210214459A1 (en) | 2018-05-31 | 2021-07-15 | Novartis Ag | Antibody molecules to cd73 and uses thereof |
| TWI848951B (zh) | 2018-06-01 | 2024-07-21 | 瑞士商諾華公司 | 針對bcma之結合分子及其用途 |
| AU2019284911A1 (en) | 2018-06-13 | 2020-12-17 | Novartis Ag | BCMA chimeric antigen receptors and uses thereof |
| US20210238268A1 (en) | 2018-06-19 | 2021-08-05 | Atarga, Llc | Antibody molecules to complement component 5 and uses thereof |
| AU2019297451A1 (en) | 2018-07-03 | 2021-01-28 | Marengo Therapeutics, Inc. | Anti-TCR antibody molecules and uses thereof |
| AR116109A1 (es) | 2018-07-10 | 2021-03-31 | Novartis Ag | Derivados de 3-(5-amino-1-oxoisoindolin-2-il)piperidina-2,6-diona y usos de los mismos |
| WO2020021465A1 (en) | 2018-07-25 | 2020-01-30 | Advanced Accelerator Applications (Italy) S.R.L. | Method of treatment of neuroendocrine tumors |
| MX2021005594A (es) | 2018-11-13 | 2021-10-22 | Compass Therapeutics Llc | Constructos multiespecificos de union contra moleculas de puntos de control y usos de los mismos. |
| JP2022513255A (ja) | 2018-12-20 | 2022-02-07 | ノバルティス アーゲー | HDM2-p53相互作用阻害剤とBCL2阻害剤との組み合わせ及び癌を処置するためのその使用 |
| WO2020128972A1 (en) | 2018-12-20 | 2020-06-25 | Novartis Ag | Dosing regimen and pharmaceutical combination comprising 3-(1-oxoisoindolin-2-yl)piperidine-2,6-dione derivatives |
| MX2021007672A (es) | 2018-12-24 | 2021-09-30 | Sanofi Sa | Proteinas de union multiespecificas con dominios fab mutantes. |
| SG11202106393SA (en) | 2018-12-24 | 2021-07-29 | Sanofi Sa | Pseudofab-based multispecific binding proteins |
| TWI852977B (zh) | 2019-01-10 | 2024-08-21 | 美商健生生物科技公司 | 前列腺新抗原及其用途 |
| ES2982474T3 (es) | 2019-02-15 | 2024-10-16 | Novartis Ag | Derivados de 3-(1-oxoisoindolin-2-il)piperidin-1,6-diona sustituidos y usos de estos |
| ES3032659T3 (en) | 2019-02-15 | 2025-07-23 | Novartis Ag | 3-(1-oxo-5-(piperidin-4-yl)isoindolin-2-yl)piperidine-2,6-dione derivatives and uses thereof |
| US10871640B2 (en) | 2019-02-15 | 2020-12-22 | Perkinelmer Cellular Technologies Germany Gmbh | Methods and systems for automated imaging of three-dimensional objects |
| EP3927747A1 (en) | 2019-02-21 | 2021-12-29 | Marengo Therapeutics, Inc. | Antibody molecules that bind to nkp30 and uses thereof |
| CN119661722A (zh) | 2019-02-21 | 2025-03-21 | 马伦戈治疗公司 | 结合t细胞相关癌细胞的多功能分子及其用途 |
| US20220088075A1 (en) | 2019-02-22 | 2022-03-24 | The Trustees Of The University Of Pennsylvania | Combination therapies of egfrviii chimeric antigen receptors and pd-1 inhibitors |
| PH12021552414A1 (en) | 2019-03-29 | 2022-07-25 | Atarga Llc | Anti fgf23 antibody |
| US12037378B2 (en) | 2019-05-21 | 2024-07-16 | Novartis Ag | Variant CD58 domains and uses thereof |
| CA3140142A1 (en) | 2019-05-21 | 2020-11-26 | Novartis Ag | Trispecific binding molecules against bcma and uses thereof |
| BR112021023048A2 (pt) | 2019-05-21 | 2022-04-19 | Novartis Ag | Moléculas de ligação a cd19 e usos das mesmas |
| US12077585B2 (en) | 2019-07-26 | 2024-09-03 | Janssen Biotech, Inc. | Proteins comprising kallikrein related peptidase 2 antigen binding domains and their uses |
| DE102019121007A1 (de) | 2019-08-02 | 2021-02-04 | Immatics Biotechnologies Gmbh | Antigenbindende Proteine, die spezifisch an MAGE-A binden |
| CN114585651A (zh) | 2019-08-08 | 2022-06-03 | 再生元制药公司 | 新型抗原结合分子形式 |
| PH12022550348A1 (en) | 2019-08-15 | 2022-12-12 | Janssen Biotech Inc | Materials and methods for improved single chain variable fragments |
| CN114786679A (zh) | 2019-10-21 | 2022-07-22 | 诺华股份有限公司 | 具有维奈托克和tim-3抑制剂的组合疗法 |
| CN114786680A (zh) | 2019-10-21 | 2022-07-22 | 诺华股份有限公司 | Tim-3抑制剂及其用途 |
| AU2020379735A1 (en) | 2019-11-05 | 2022-05-26 | Regeneron Pharmaceuticals, Inc. | N-terminal SCFV multispecific binding molecules |
| CA3163104A1 (en) | 2019-11-26 | 2021-06-03 | Novartis Ag | Chimeric antigen receptors and uses thereof |
| US20210188934A1 (en) | 2019-12-20 | 2021-06-24 | Regeneron Pharmaceuticals, Inc. | Novel il2 agonists and methods of use thereof |
| MX2022007759A (es) | 2019-12-20 | 2022-07-19 | Novartis Ag | Combinacion del anticuerpo anti tim-3 mbg453 y anticuerpo anti tgf-beta nis793, con o sin decitabina o el anticuerpo anti pd-1 spartalizumab, para el tratamiento de mielofibrosis y sindrome mielodisplasico. |
| GB2609554B (en) | 2020-01-03 | 2025-08-20 | Marengo Therapeutics Inc | Anti-TCR antibody molecules and uses thereof |
| US20210222244A1 (en) | 2020-01-17 | 2021-07-22 | Becton, Dickinson And Company | Methods and compositions for single cell secretomics |
| EP4090335A1 (en) | 2020-01-17 | 2022-11-23 | Novartis AG | Combination comprising a tim-3 inhibitor and a hypomethylating agent for use in treating myelodysplastic syndrome or chronic myelomonocytic leukemia |
| IL295129A (en) | 2020-01-30 | 2022-09-01 | Umoja Biopharma Inc | Bispecific transduction enhancer |
| TW202144388A (zh) | 2020-02-14 | 2021-12-01 | 美商健生生物科技公司 | 在卵巢癌中表現之新抗原及其用途 |
| TW202144389A (zh) | 2020-02-14 | 2021-12-01 | 美商健生生物科技公司 | 在多發性骨髓瘤中表現之新抗原及其用途 |
| EP4106813A4 (en) | 2020-02-21 | 2024-03-27 | MacroGenics, Inc. | CD137 BINDING MOLECULES AND THEIR USES |
| BR112022016633A2 (pt) | 2020-02-27 | 2022-12-13 | Novartis Ag | Métodos para produzir células que expressam receptor de antígeno quimérico |
| UY40280A (es) | 2020-03-13 | 2023-07-31 | Janssen Biotech Inc | Dominios de unión a antígeno que se unen a la proteina cd33 de la superficie de células mieloides |
| CN116249549A (zh) | 2020-03-27 | 2023-06-09 | 诺华股份有限公司 | 用于治疗增殖性疾病和自身免疫病症的双特异性组合疗法 |
| JP2023523794A (ja) | 2020-05-01 | 2023-06-07 | ノバルティス アーゲー | 人工操作免疫グロブリン |
| MX2022014239A (es) | 2020-05-12 | 2023-02-09 | Regeneron Pharma | Nuevos agonistas de il10 y metodos para su uso. |
| KR20230017841A (ko) | 2020-05-27 | 2023-02-06 | 얀센 바이오테크 인코포레이티드 | Cd3 항원 결합 도메인을 포함하는 단백질 및 이의 용도 |
| MX2022015852A (es) | 2020-06-23 | 2023-01-24 | Novartis Ag | Regimen de dosificacion que comprende derivados de 3-(1-oxoisoindolin-2-il)piperidina-2,6-diona. |
| US20240279353A1 (en) | 2020-07-06 | 2024-08-22 | Kiromic BioPharma, Inc. | Mesothelin isoform binding molecules and chimeric pd1 receptor molecules, cells containing the same and uses thereof |
| EP4175664A2 (en) | 2020-07-06 | 2023-05-10 | Janssen Biotech, Inc. | Prostate neoantigens and their uses |
| PH12023550015A1 (en) | 2020-07-16 | 2024-03-11 | Novartis Ag | Anti-betacellulin antibodies, fragments thereof, and multi-specific binding molecules |
| WO2022026592A2 (en) | 2020-07-28 | 2022-02-03 | Celltas Bio, Inc. | Antibody molecules to coronavirus and uses thereof |
| TW202221028A (zh) | 2020-07-29 | 2022-06-01 | 美商健生生物科技公司 | 包括hla-g抗原結合域之蛋白及其用途 |
| EP4188549A1 (en) | 2020-08-03 | 2023-06-07 | Novartis AG | Heteroaryl substituted 3-(1-oxoisoindolin-2-yl)piperidine-2,6-dione derivatives and uses thereof |
| US20230321285A1 (en) | 2020-08-31 | 2023-10-12 | Advanced Accelerator Applications International Sa | Method of treating psma-expressing cancers |
| EP4204020A1 (en) | 2020-08-31 | 2023-07-05 | Advanced Accelerator Applications International S.A. | Method of treating psma-expressing cancers |
| TW202233672A (zh) | 2020-10-22 | 2022-09-01 | 美商健生生物科技公司 | 包括類δ配體3(DLL3)抗原結合區之蛋白質及其用途 |
| AU2021373366A1 (en) | 2020-11-06 | 2023-06-01 | Novartis Ag | Cd19 binding molecules and uses thereof |
| US20240002509A1 (en) | 2020-11-06 | 2024-01-04 | Novartis Ag | ANTIBODY Fc VARIANTS |
| CN116390933A (zh) | 2020-11-06 | 2023-07-04 | 诺华股份有限公司 | 治疗b细胞恶性肿瘤的抗cd19剂和b细胞靶向剂组合疗法 |
| CA3198447A1 (en) | 2020-11-13 | 2022-05-19 | Novartis Ag | Combination therapies with chimeric antigen receptor (car)-expressing cells |
| WO2022108627A1 (en) | 2020-11-18 | 2022-05-27 | Kiromic Biopharma, Inc.Kiromic Biopharma, Inc. | Gamma-delta t cell manufacturing processes and chimeric pd1 receptor molecules |
| JP2024505049A (ja) | 2021-01-29 | 2024-02-02 | ノバルティス アーゲー | 抗cd73及び抗entpd2抗体のための投与方式並びにその使用 |
| WO2022186063A1 (ja) * | 2021-03-01 | 2022-09-09 | C4U株式会社 | Cas3タンパク質を製造する方法 |
| CN117098781A (zh) | 2021-03-24 | 2023-11-21 | 詹森生物科技公司 | 靶向cd22和cd79b的抗体 |
| CA3214307A1 (en) | 2021-03-24 | 2022-09-29 | Janssen Biotech, Inc. | Proteins comprising cd3 antigen binding domains and uses thereof |
| TW202304979A (zh) | 2021-04-07 | 2023-02-01 | 瑞士商諾華公司 | 抗TGFβ抗體及其他治療劑用於治療增殖性疾病之用途 |
| TW202307007A (zh) | 2021-05-04 | 2023-02-16 | 美商再生元醫藥公司 | 多特異性fgf21受體促效劑及其等用途 |
| CN117597365A (zh) | 2021-05-04 | 2024-02-23 | 再生元制药公司 | 多特异性fgf21受体激动剂及其应用 |
| AR125874A1 (es) | 2021-05-18 | 2023-08-23 | Novartis Ag | Terapias de combinación |
| IL308134A (en) | 2021-06-22 | 2023-12-01 | Novartis Ag | BISPECIFIC ANTIBODIES FOR USE IN THE TREATMENT OF HIDRADENITIS SUPPURATIVA |
| US20250066441A1 (en) | 2021-07-19 | 2025-02-27 | Regeneron Pharmaceuticals, Inc. | Il12 receptor agonists and methods of use thereof |
| WO2023022965A2 (en) | 2021-08-16 | 2023-02-23 | Regeneron Pharmaceuticals, Inc. | Novel il27 receptor agonists and methods of use thereof |
| AU2022344595A1 (en) | 2021-09-13 | 2024-05-02 | Janssen Biotech, Inc | CD33 X Vδ2 MULTISPECIFIC ANTIBODIES FOR THE TREATMENT OF CANCER |
| EP4405396A2 (en) | 2021-09-20 | 2024-07-31 | Voyager Therapeutics, Inc. | Compositions and methods for the treatment of her2 positive cancer |
| US20250019455A1 (en) | 2021-09-24 | 2025-01-16 | Pharmaceutica Nv | Proteins comprising cd20 binding domains, and uses thereof |
| CN118119642A (zh) | 2021-10-28 | 2024-05-31 | 诺华股份有限公司 | 工程化Fc变体 |
| AU2022380722A1 (en) | 2021-11-03 | 2024-06-20 | Janssen Biotech, Inc. | Methods of treating cancers and enhancing efficacy of bcmaxcd3 bispecific antibodies |
| TW202334223A (zh) | 2021-11-11 | 2023-09-01 | 美商再生元醫藥公司 | Cd20-pd1結合分子及其使用方法 |
| US20250034559A1 (en) | 2021-11-17 | 2025-01-30 | Voyager Therapeutics, Inc. | Compositions and methods for the treatment of tau-related disorders |
| CA3239224A1 (en) | 2021-11-22 | 2023-05-25 | Janssen Biotech, Inc. | Compositions comprising enhanced multispecific binding agents for an immune response |
| TW202342548A (zh) | 2022-02-07 | 2023-11-01 | 美商威特拉公司 | 抗獨特型(anti-idiotype)抗體分子及其用途 |
| AR129136A1 (es) | 2022-04-26 | 2024-07-17 | Novartis Ag | Anticuerpos multiespecíficos que se dirigen a il-13 e il-18 |
| CN119546628A (zh) | 2022-05-11 | 2025-02-28 | 再生元制药公司 | 多特异性结合分子前蛋白及其用途 |
| EP4522757A2 (en) | 2022-05-13 | 2025-03-19 | Voyager Therapeutics, Inc. | Compositions and methods for the treatment of her2 positive cancer |
| WO2023230594A1 (en) | 2022-05-27 | 2023-11-30 | Regeneron Pharmaceuticals, Inc. | Interleukin-2 proproteins and uses thereof |
| WO2023235848A1 (en) | 2022-06-04 | 2023-12-07 | Regeneron Pharmaceuticals, Inc. | Interleukin-2 proproteins and uses thereof |
| TW202435912A (zh) | 2022-08-03 | 2024-09-16 | 美商航海家醫療公司 | 用於穿過血腦屏障之組合物及方法 |
| EP4573110A1 (en) | 2022-08-18 | 2025-06-25 | Regeneron Pharmaceuticals, Inc. | Interferon proproteins and uses thereof |
| US20240067691A1 (en) | 2022-08-18 | 2024-02-29 | Regeneron Pharmaceuticals, Inc. | Interferon receptor agonists and uses thereof |
| AU2023375177A1 (en) | 2022-11-02 | 2025-06-19 | Janssen Biotech, Inc. | Methods of treating cancers |
| CN120344558A (zh) * | 2022-12-08 | 2025-07-18 | 上海星赛生物科技有限公司 | 双特异性/多特异性抗体及其用途 |
| AU2023395983A1 (en) | 2022-12-16 | 2025-06-05 | Regeneron Pharmaceuticals, Inc. | Antigen-binding molecules that bind to aav particles and uses |
| EP4638729A1 (en) | 2022-12-23 | 2025-10-29 | Regeneron Pharmaceuticals, Inc. | Ace2 fusion proteins and uses thereof |
| WO2024151978A1 (en) | 2023-01-13 | 2024-07-18 | Regeneron Pharmaceuticals, Inc. | Il12 receptor agonists and methods of use thereof |
| EP4649092A1 (en) | 2023-01-13 | 2025-11-19 | Regeneron Pharmaceuticals, Inc. | Fgfr3 binding molecules and methods of use thereof |
| WO2024168061A2 (en) | 2023-02-07 | 2024-08-15 | Ayan Therapeutics Inc. | Antibody molecules binding to sars-cov-2 |
| IL322940A (en) | 2023-02-28 | 2025-10-01 | Regeneron Pharma | Multivalent anti-spike protein binding molecules and their uses |
| IL322890A (en) | 2023-02-28 | 2025-10-01 | Regeneron Pharma | Multispecific molecules containing an MHC-peptide complex containing an MHC domain and an antigenic peptide and a partially targeted immune cell antigen |
| AU2024269008A1 (en) | 2023-05-10 | 2025-11-27 | Regeneron Pharmaceuticals, Inc. | Cd20-pd1 binding molecules and methods of use thereof |
| WO2024238415A1 (en) | 2023-05-12 | 2024-11-21 | Regeneron Pharmaceuticals, Inc. | Interferon receptor antagonists and uses thereof |
| US20250011449A1 (en) | 2023-06-11 | 2025-01-09 | Regeneron Pharmaceuticals, Inc. | Circularized antibody molecules |
| WO2025034715A1 (en) | 2023-08-07 | 2025-02-13 | Janssen Biotech, Inc. | Gucy2c antibodies and uses thereof |
| EP4630457A1 (en) | 2023-08-18 | 2025-10-15 | Regeneron Pharmaceuticals, Inc. | Bispecific antigen-binding molecules and uses thereof |
| WO2025068957A1 (en) | 2023-09-29 | 2025-04-03 | Novartis Ag | Bispecific antibodies for use in lowering the risk of cardiovascular disease events in subjects known to be a carrier of clonal expansion of hematopoietic cell lines with somatic mutations |
| WO2025106469A1 (en) | 2023-11-14 | 2025-05-22 | Regeneron Pharmaceuticals, Inc. | Engineered heavy chain variable domains and uses thereof |
| WO2025122614A1 (en) | 2023-12-05 | 2025-06-12 | Regeneron Pharmaceuticals, Inc. | Il18 receptor agonists and methods of use thereof |
| WO2025122634A1 (en) | 2023-12-05 | 2025-06-12 | Voyager Therapeutics, Inc. | Compositions and methods for the treatment of tau-related disorders |
| WO2025133340A1 (en) * | 2023-12-21 | 2025-06-26 | Ludwig Institute For Cancer Research Ltd | Heterodimeric proteins comprising dimerization motifs and methods of using |
| WO2025199243A1 (en) | 2024-03-20 | 2025-09-25 | Regeneron Pharmaceuticals, Inc. | Trivalent multispecific binding molecules and methods of use thereof |
| WO2025231408A2 (en) | 2024-05-03 | 2025-11-06 | Janssen Biotech, Inc. | Methods for treating multiple myeloma with car-t cells and bispecific antibodies |
| WO2025231372A2 (en) | 2024-05-03 | 2025-11-06 | Janssen Biotech, Inc. | Methods for treating multiple myeloma with car-t cells and bispecific antibodies |
| WO2025240335A1 (en) | 2024-05-13 | 2025-11-20 | Regeneron Pharmaceuticals, Inc. | Fgfr3 binding molecules and methods of use thereof |
| WO2025245494A1 (en) | 2024-05-24 | 2025-11-27 | Regeneron Pharmaceuticals, Inc. | Tumor-targeted split il12 receptor agonists |
Family Cites Families (55)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| NL154598B (nl) | 1970-11-10 | 1977-09-15 | Organon Nv | Werkwijze voor het aantonen en bepalen van laagmoleculire verbindingen en van eiwitten die deze verbindingen specifiek kunnen binden, alsmede testverpakking. |
| US3817837A (en) | 1971-05-14 | 1974-06-18 | Syva Corp | Enzyme amplification assay |
| US3939350A (en) | 1974-04-29 | 1976-02-17 | Board Of Trustees Of The Leland Stanford Junior University | Fluorescent immunoassay employing total reflection for activation |
| US3996345A (en) | 1974-08-12 | 1976-12-07 | Syva Company | Fluorescence quenching with immunological pairs in immunoassays |
| US4275149A (en) | 1978-11-24 | 1981-06-23 | Syva Company | Macromolecular environment control in specific receptor assays |
| US4277437A (en) | 1978-04-05 | 1981-07-07 | Syva Company | Kit for carrying out chemically induced fluorescence immunoassay |
| US4366241A (en) | 1980-08-07 | 1982-12-28 | Syva Company | Concentrating zone method in heterogeneous immunoassays |
| ATE114723T1 (de) | 1987-03-02 | 1994-12-15 | Enzon Lab Inc | Organismus als träger für ''single chain antibody domain (scad)''. |
| US5091513A (en) | 1987-05-21 | 1992-02-25 | Creative Biomolecules, Inc. | Biosynthetic antibody binding sites |
| US5223409A (en) * | 1988-09-02 | 1993-06-29 | Protein Engineering Corp. | Directed evolution of novel binding proteins |
| EP1997891A1 (en) | 1988-09-02 | 2008-12-03 | Dyax Corporation | Generation and selection of recombinant varied binding proteins |
| WO1990005144A1 (en) | 1988-11-11 | 1990-05-17 | Medical Research Council | Single domain ligands, receptors comprising said ligands, methods for their production, and use of said ligands and receptors |
| US5530101A (en) * | 1988-12-28 | 1996-06-25 | Protein Design Labs, Inc. | Humanized immunoglobulins |
| US5143854A (en) | 1989-06-07 | 1992-09-01 | Affymax Technologies N.V. | Large scale photolithographic solid phase synthesis of polypeptides and receptor binding screening thereof |
| US5270202A (en) | 1989-11-03 | 1993-12-14 | Syamal Raychaudhuri | Anti-idiotypic antibodies to human melanoma-associated proteoglycan antigen |
| US5427908A (en) | 1990-05-01 | 1995-06-27 | Affymax Technologies N.V. | Recombinant library screening methods |
| GB9206318D0 (en) | 1992-03-24 | 1992-05-06 | Cambridge Antibody Tech | Binding substances |
| GB9015198D0 (en) | 1990-07-10 | 1990-08-29 | Brien Caroline J O | Binding substance |
| ATE439435T1 (de) | 1991-03-01 | 2009-08-15 | Dyax Corp | Chimäres protein mit mikroprotein mit zwei oder mehr disulfidbindungen und ausgestaltungen davon |
| US5955341A (en) | 1991-04-10 | 1999-09-21 | The Scripps Research Institute | Heterodimeric receptor libraries using phagemids |
| US5858657A (en) | 1992-05-15 | 1999-01-12 | Medical Research Council | Methods for producing members of specific binding pairs |
| DE4122599C2 (de) | 1991-07-08 | 1993-11-11 | Deutsches Krebsforsch | Phagemid zum Screenen von Antikörpern |
| US5348867A (en) | 1991-11-15 | 1994-09-20 | George Georgiou | Expression of proteins on bacterial surface |
| WO1993010247A1 (en) | 1991-11-20 | 1993-05-27 | Ab Astra | PHASMID VECTOR IN $i(E.COLI) |
| US5412087A (en) | 1992-04-24 | 1995-05-02 | Affymax Technologies N.V. | Spatially-addressable immobilization of oligonucleotides and other biological polymers on surfaces |
| US5932448A (en) | 1991-11-29 | 1999-08-03 | Protein Design Labs., Inc. | Bispecific antibody heterodimers |
| ATE408012T1 (de) | 1991-12-02 | 2008-09-15 | Medical Res Council | Herstellung von autoantikörpern auf phagenoberflächen ausgehend von antikörpersegmentbibliotheken |
| WO1993015210A1 (en) | 1992-01-23 | 1993-08-05 | Merck Patent Gmbh | Monomeric and dimeric antibody-fragment fusion proteins |
| US5233409A (en) | 1992-02-25 | 1993-08-03 | Schwab Karl W | Color analysis of organic constituents in sedimentary rocks for thermal maturity |
| US6129914A (en) | 1992-03-27 | 2000-10-10 | Protein Design Labs, Inc. | Bispecific antibody effective to treat B-cell lymphoma and cell line |
| EP0672142B1 (en) | 1992-12-04 | 2001-02-28 | Medical Research Council | Multivalent and multispecific binding proteins, their manufacture and use |
| US5869337A (en) | 1993-02-12 | 1999-02-09 | President And Fellows Of Harvard College | Regulated transcription of targeted genes and other biological events |
| DE614989T1 (de) | 1993-02-17 | 1995-09-28 | Morphosys Proteinoptimierung | Verfahren für in vivo Selektion von Ligandenbindende Proteine. |
| US5605793A (en) | 1994-02-17 | 1997-02-25 | Affymax Technologies N.V. | Methods for in vitro recombination |
| US6165793A (en) | 1996-03-25 | 2000-12-26 | Maxygen, Inc. | Methods for generating polynucleotides having desired characteristics by iterative selection and recombination |
| US6117679A (en) | 1994-02-17 | 2000-09-12 | Maxygen, Inc. | Methods for generating polynucleotides having desired characteristics by iterative selection and recombination |
| US5525490A (en) | 1994-03-29 | 1996-06-11 | Onyx Pharmaceuticals, Inc. | Reverse two-hybrid method |
| US5738996A (en) | 1994-06-15 | 1998-04-14 | Pence, Inc. | Combinational library composition and method |
| US5824483A (en) | 1994-05-18 | 1998-10-20 | Pence Inc. | Conformationally-restricted combinatiorial library composition and method |
| US5695941A (en) | 1994-06-22 | 1997-12-09 | The General Hospital Corporation | Interaction trap systems for analysis of protein networks |
| CU22615A1 (es) | 1994-06-30 | 2000-02-10 | Centro Inmunologia Molecular | Procedimiento de obtención de anticuerpos monoclonales murinos menos inmunogénicos. anticuerpos monoclonales obtenidos |
| GB9500851D0 (en) | 1995-01-17 | 1995-03-08 | Bionvent International Ab | Method of selecting specific bacteriophages |
| US5731168A (en) | 1995-03-01 | 1998-03-24 | Genentech, Inc. | Method for making heteromultimeric polypeptides |
| CA2217545A1 (en) | 1995-04-11 | 1996-10-17 | Marc Vidal | Reverse two-hybrid systems |
| CA2229043C (en) | 1995-08-18 | 2016-06-07 | Morphosys Gesellschaft Fur Proteinoptimierung Mbh | Protein/(poly)peptide libraries |
| US5695937A (en) | 1995-09-12 | 1997-12-09 | The Johns Hopkins University School Of Medicine | Method for serial analysis of gene expression |
| FR2741892B1 (fr) | 1995-12-04 | 1998-02-13 | Pasteur Merieux Serums Vacc | Procede de preparation d'une banque multicombinatoire de vecteurs d'expression de genes d'anticorps, banque et systemes d'expression d'anticorps "coliclonaux" obtenus |
| US6130037A (en) | 1996-04-25 | 2000-10-10 | Pence And Mcgill University | Biosensor device and method |
| US6083693A (en) | 1996-06-14 | 2000-07-04 | Curagen Corporation | Identification and comparison of protein-protein interactions that occur in populations |
| ATE284972T1 (de) | 1996-09-24 | 2005-01-15 | Cadus Pharmaceutical Corp | Verfahren und zusammensetzungen für die identifizierung von receptor effectoren |
| CA2304367C (en) | 1997-09-16 | 2009-06-09 | Fox Chase Cancer Center | An improved yeast interaction trap assay |
| JP2001522598A (ja) | 1997-11-10 | 2001-11-20 | ザ ジュネラル ホスピタル コーポレーション | タンパク質相互作用を記録するための検出システムおよび機能的関係 |
| BR9908082A (pt) | 1998-02-19 | 2000-10-31 | Harvard College | Proteìna de fusão do complexo de histocompatibilidade principal classe ii, conjugado dos domìnios de ligação do complexo de histocompatibilidade principal multimérico, processos para detectar células t tendo uma especificidade do complexo definido de mhc / peptìdeo, para conferir a um indivìduo imunidade adotiva a um complexo definido de mhc / peptìdeo, para estimular ou ativar as células t reativas a um complexo definido de mhc / peptìdeo, para seletivamente matar células t reativas a um complexo definido de mhc / peptìdeo, para tolerizar um indivìduo humano a um complexo definido de mhc / peptìdeo, e, ácido nucleico isolado |
| EP1109901B1 (en) | 1998-09-07 | 2006-10-25 | Glaxo Group Limited | GABA B RECEPTOR SUBTYPES GABA B-R1c AND GABA B-R2 AND HETERODIMERS THEREOF |
| EP1990409A3 (en) | 1999-07-20 | 2011-05-18 | MorphoSys AG | Bacteriophage |
-
2001
- 2001-08-01 US US09/921,144 patent/US6833441B2/en not_active Expired - Lifetime
-
2002
- 2002-07-31 CN CN200910149285A patent/CN101654483A/zh active Pending
- 2002-07-31 CN CNA02818596XA patent/CN1558916A/zh active Pending
- 2002-07-31 WO PCT/US2002/024582 patent/WO2003012069A2/en not_active Ceased
- 2002-07-31 EP EP02763414A patent/EP1421117B1/en not_active Expired - Lifetime
- 2002-07-31 JP JP2003517247A patent/JP2005506064A/ja not_active Withdrawn
- 2002-07-31 MX MXPA04001053A patent/MXPA04001053A/es active IP Right Grant
- 2002-07-31 CA CA2455237A patent/CA2455237C/en not_active Expired - Fee Related
-
2004
- 2004-08-03 US US10/911,127 patent/US7429652B2/en not_active Expired - Lifetime
-
2009
- 2009-09-14 JP JP2009211914A patent/JP2010053132A/ja active Pending
Cited By (4)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| JP2007008925A (ja) * | 2005-05-31 | 2007-01-18 | Canon Inc | 標的物質捕捉分子 |
| JP2011514807A (ja) * | 2008-03-03 | 2011-05-12 | グライコフィ, インコーポレイテッド | 下等真核生物中での組換えタンパク質の表面ディスプレイ |
| JP2013511268A (ja) * | 2009-11-18 | 2013-04-04 | ピエール、ファーブル、メディカマン | 新規なファージディスプレイベクター |
| JP2019501887A (ja) * | 2015-12-03 | 2019-01-24 | ユーシービー バイオファルマ エスピーアールエル | 多特異性抗体 |
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| MXPA04001053A (es) | 2005-02-17 |
| US6833441B2 (en) | 2004-12-21 |
| CN1558916A (zh) | 2004-12-29 |
| CN101654483A (zh) | 2010-02-24 |
| EP1421117A4 (en) | 2005-12-28 |
| WO2003012069A3 (en) | 2003-11-06 |
| WO2003012069A2 (en) | 2003-02-13 |
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