UA128717C2 - Поліпшені антигензв'язуючі рецептори - Google Patents
Поліпшені антигензв'язуючі рецептори Download PDFInfo
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- UA128717C2 UA128717C2 UAA201910455A UAA201910455A UA128717C2 UA 128717 C2 UA128717 C2 UA 128717C2 UA A201910455 A UAA201910455 A UA A201910455A UA A201910455 A UAA201910455 A UA A201910455A UA 128717 C2 UA128717 C2 UA 128717C2
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| ES3000558T3 (en) | 2016-08-10 | 2025-02-28 | Univ Ajou Ind Academic Coop Found | Heterodimeric fc-fused cytokine and pharmaceutical composition comprising the same |
| AU2018308088B2 (en) | 2017-07-25 | 2025-05-29 | Truebinding, Inc. | Treating cancer by blocking the interaction of TIM-3 and its ligand |
| AU2019366956B2 (en) | 2018-10-23 | 2025-10-30 | Dragonfly Therapeutics, Inc. | Heterodimeric Fc-fused proteins |
| US20200223925A1 (en) * | 2018-12-21 | 2020-07-16 | Hoffmann-La Roche Inc. | Tumor-targeted superagonistic cd28 antigen binding molecules |
| WO2020127618A1 (en) | 2018-12-21 | 2020-06-25 | F. Hoffmann-La Roche Ag | Tumor-targeted agonistic cd28 antigen binding molecules |
| US20220152108A1 (en) * | 2019-03-18 | 2022-05-19 | Svenska Vaccinfabriken Produktion Ab | Chimeric antigen receptors directed to cells expressing the sodium taurocholate co-transporting receptor |
| CN114007643A (zh) | 2019-04-19 | 2022-02-01 | 中外制药株式会社 | 识别抗体改变部位的嵌合受体 |
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| US12281166B2 (en) | 2020-05-26 | 2025-04-22 | Truebinding, Inc. | Methods of treating inflammatory diseases by blocking Galectin-3 |
| EP3915576A1 (en) * | 2020-05-28 | 2021-12-01 | Fundació Privada Institut d'Investigació Oncològica de Vall-Hebron | Chimeric antigen receptors specific for p95her2 and uses thereof |
| JP2023531067A (ja) * | 2020-06-25 | 2023-07-20 | エフ・ホフマン－ラ・ロシュ・アクチェンゲゼルシャフト | 抗ｃｄ３／抗ｃｄ２８二重特異性抗原結合分子 |
| US20230322898A1 (en) | 2020-07-31 | 2023-10-12 | Chugai Seiyaku Kabushiki Kaisha | Pharmaceutical composition comprising cell expressing chimeric receptor |
| WO2022029051A1 (en) * | 2020-08-03 | 2022-02-10 | F. Hoffmann-La Roche Ag | Improved antigen binding receptors |
| AU2021329375A1 (en) | 2020-08-20 | 2023-04-20 | A2 Biotherapeutics, Inc. | Compositions and methods for treating ceacam positive cancers |
| CN111995689B (zh) * | 2020-08-27 | 2023-05-05 | 深圳市体内生物医药科技有限公司 | 一种基因修饰的免疫细胞及其制备方法和应用 |
| EP4237449A1 (en) * | 2020-10-28 | 2023-09-06 | F. Hoffmann-La Roche AG | Improved antigen binding receptors |
| CN117730102A (zh) | 2021-07-22 | 2024-03-19 | 豪夫迈·罗氏有限公司 | 异二聚体Fc结构域抗体 |
| AU2022397540A1 (en) * | 2021-11-25 | 2024-05-16 | F. Hoffmann-La Roche Ag | Improved antigen binding receptors |
| CN116162168A (zh) * | 2021-11-25 | 2023-05-26 | 信达细胞制药(苏州)有限公司 | 分子开关调控型嵌合抗原受体细胞和抗体的组合及其应用 |
| CN116284385A (zh) * | 2021-12-07 | 2023-06-23 | 信达细胞制药(苏州)有限公司 | 靶向bcma的p329g抗体及其与嵌合抗原受体细胞的组合和应用 |
| JP2025512797A (ja) * | 2022-03-25 | 2025-04-22 | エフ・ホフマン－ラ・ロシュ・アクチェンゲゼルシャフト | 改善されたキメラ受容体 |
| WO2023242343A1 (en) | 2022-06-15 | 2023-12-21 | Immunoscape Pte. Ltd. | Human t cell receptors specific for antigenic peptides derived from mitogen-activated protein kinase 8 interacting protein 2 (mapk8ip2), epstein-barr virus or human endogenous retrovirus, and uses thereof |
| AR130387A1 (es) | 2022-09-08 | 2024-12-04 | Hoffmann La Roche | Receptores de linfocitos t recombinantes |
| EP4590322A1 (en) * | 2022-09-20 | 2025-07-30 | Dana-Farber Cancer Institute, Inc. | Reversible control of chimeric antigen receptor t cells |
| CN120548192A (zh) | 2023-01-20 | 2025-08-26 | 豪夫迈·罗氏有限公司 | 免疫缀合物 |
| WO2024251547A1 (en) | 2023-06-06 | 2024-12-12 | F. Hoffmann-La Roche Ag | Switch receptors |
| WO2024251132A1 (zh) * | 2023-06-06 | 2024-12-12 | 信达细胞制药(苏州)有限公司 | 一种包含bcma pg car-t细胞制剂和pg抗体制剂的药物组合制剂及其用途 |
| WO2025146286A1 (en) | 2024-01-04 | 2025-07-10 | Immunoscape Pte. Ltd. | Human t cell receptors and uses thereof |
| WO2025181329A1 (en) | 2024-03-01 | 2025-09-04 | Immunoscape Pte. Ltd. | Human t cell receptors and uses thereof |
| WO2025233304A1 (en) | 2024-05-08 | 2025-11-13 | F. Hoffmann-La Roche Ag | Recombinant fc domain – il7 variant polypeptides and combination therapy with membrane-anchored antigen binding polypeptides |
| CN119074926B (zh) * | 2024-08-29 | 2025-11-25 | 中国医学科学院阜外医院深圳医院(深圳市孙逸仙心血管医院) | 一种靶向fap的car-t细胞在制备治疗心肌炎慢性期心脏纤维化的药物中的应用 |
Family Cites Families (38)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| 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 |
| 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 |
| US5703055A (en) | 1989-03-21 | 1997-12-30 | Wisconsin Alumni Research Foundation | Generation of antibodies through lipid mediated DNA delivery |
| DE3920358A1 (de) | 1989-06-22 | 1991-01-17 | Behringwerke Ag | Bispezifische und oligospezifische, mono- und oligovalente antikoerperkonstrukte, ihre herstellung und verwendung |
| WO1992009690A2 (en) | 1990-12-03 | 1992-06-11 | Genentech, Inc. | Enrichment method for variant proteins with altered binding properties |
| US5571894A (en) | 1991-02-05 | 1996-11-05 | Ciba-Geigy Corporation | Recombinant antibodies specific for a growth factor receptor |
| EP0590058B1 (en) | 1991-06-14 | 2003-11-26 | Genentech, Inc. | HUMANIZED Heregulin ANTIBODy |
| GB9114948D0 (en) | 1991-07-11 | 1991-08-28 | Pfizer Ltd | Process for preparing sertraline intermediates |
| GB9304200D0 (en) | 1993-03-02 | 1993-04-21 | Sandoz Ltd | Improvements in or relating to organic compounds |
| FI941572L (fi) | 1991-10-07 | 1994-05-27 | Oncologix Inc | Anti-erbB-2-monoklonaalisten vasta-aineiden yhdistelmä ja käyttömenetelmä |
| ATE419355T1 (de) | 1992-02-06 | 2009-01-15 | Novartis Vaccines & Diagnostic | Marker für krebs und biosynthetisches bindeprotein dafür |
| JP3626187B2 (ja) | 1993-06-07 | 2005-03-02 | バイカル インコーポレイテッド | 遺伝子治療に適するプラスミド |
| AU723325B2 (en) | 1995-06-23 | 2000-08-24 | President And Fellows Of Harvard College | Transcriptional regulation of genes encoding vascular endothelial growth factor receptors |
| US6737056B1 (en) | 1999-01-15 | 2004-05-18 | Genentech, Inc. | Polypeptide variants with altered effector function |
| US20030180714A1 (en) | 1999-12-15 | 2003-09-25 | Genentech, Inc. | Shotgun scanning |
| CA2488441C (en) | 2002-06-03 | 2015-01-27 | Genentech, Inc. | Synthetic antibody phage libraries |
| PT1572744E (pt) | 2002-12-16 | 2010-09-07 | Genentech Inc | Variantes de imunoglobulina e utilizações destas |
| US20050079574A1 (en) | 2003-01-16 | 2005-04-14 | Genentech, Inc. | Synthetic antibody phage libraries |
| US7785903B2 (en) | 2004-04-09 | 2010-08-31 | Genentech, Inc. | Variable domain library and uses |
| BR122019012028B1 (pt) | 2004-04-13 | 2023-09-26 | F. Hoffmann-La Roche Ag | Anticorpos anti-p-selectina, molécula de ácido nucléico, vetor, e composição |
| DE602005011617D1 (de) | 2004-05-19 | 2009-01-22 | Medigene Ltd | Hochaffiner ny-eso-t-zellen-rezeptor |
| TWI380996B (zh) | 2004-09-17 | 2013-01-01 | Hoffmann La Roche | 抗ｏｘ４０ｌ抗體 |
| EP2402374A1 (en) | 2005-02-07 | 2012-01-04 | GlycArt Biotechnology AG | Antigen binding molecules that bind EGFR, vectors encoding same, and uses thereof |
| EP2465870A1 (en) | 2005-11-07 | 2012-06-20 | Genentech, Inc. | Binding polypeptides with diversified and consensus VH/VL hypervariable sequences |
| US20070237764A1 (en) | 2005-12-02 | 2007-10-11 | Genentech, Inc. | Binding polypeptides with restricted diversity sequences |
| WO2007134050A2 (en) | 2006-05-09 | 2007-11-22 | Genentech, Inc. | Binding polypeptides with optimized scaffolds |
| CN100592373C (zh) | 2007-05-25 | 2010-02-24 | 群康科技(深圳)有限公司 | 液晶显示面板驱动装置及其驱动方法 |
| WO2010012829A1 (en) | 2008-07-31 | 2010-02-04 | Helmholtz Zentrum München Deutsches Forschungszentrum Für Gesundheit Und Umwelt (Gmbh) | Her2/neu specific t cell receptors |
| KR20160044598A (ko) | 2011-03-29 | 2016-04-25 | 로슈 글리카트 아게 | 항체 Fc 변이체 |
| JP2016528167A (ja) | 2013-04-29 | 2016-09-15 | エフ．ホフマン−ラ ロシュ アーゲーＦ． Ｈｏｆｆｍａｎｎ−Ｌａ Ｒｏｃｈｅ Ａｋｔｉｅｎｇｅｓｅｌｌｓｃｈａｆｔ | ヒトＦｃＲｎ結合改変抗体及び使用方法 |
| KR102266819B1 (ko) * | 2013-04-29 | 2021-06-18 | 에프. 호프만-라 로슈 아게 | Fc-수용체 결합 개질된 비대칭 항체 및 이의 사용 방법 |
| US10144770B2 (en) * | 2013-10-17 | 2018-12-04 | National University Of Singapore | Chimeric receptors and uses thereof in immune therapy |
| WO2015142675A2 (en) | 2014-03-15 | 2015-09-24 | Novartis Ag | Treatment of cancer using chimeric antigen receptor |
| US20170151283A1 (en) * | 2014-05-23 | 2017-06-01 | The Trustees Of The University Of Pennsylvania | Compositions and methods for treating antibody resistance |
| MX2017003062A (es) * | 2014-09-09 | 2017-12-14 | Unum Therapeutics | Receptores quimericos y usos de los mismos en terapia inmune. |
| KR102558502B1 (ko) | 2014-12-05 | 2023-07-20 | 시티 오브 호프 | Ｃｓ1 표적화된 키메라 항원 수용체-변형된 ｔ 세포 |
| CN114891102A (zh) | 2015-10-29 | 2022-08-12 | 豪夫迈·罗氏有限公司 | 抗变体Fc区抗体及使用方法 |
| SG11201908784TA (en) | 2017-03-27 | 2019-10-30 | Hoffmann La Roche | Improved antigen binding receptor formats |
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