TWI387602B - 與上皮生長因子受體（ｅｇｆｒ）結合之抗原結合分子，編碼該抗原結合分子之載體及其用途 - Google Patents
與上皮生長因子受體（ｅｇｆｒ）結合之抗原結合分子，編碼該抗原結合分子之載體及其用途 Download PDFInfo
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Families Citing this family (200)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| JP4334141B2 (ja) | 1998-04-20 | 2009-09-30 | グリカート バイオテクノロジー アクチェンゲゼルシャフト | 抗体依存性細胞傷害性を改善するための抗体のグリコシル化操作 |
| CA2455365C (en) | 2001-08-03 | 2014-07-29 | Glycart Biotechnology Ag | Antibody glycosylation variants having increased antibody-dependent cellular cytotoxicity |
| EP2402374A1 (en) | 2005-02-07 | 2012-01-04 | GlycArt Biotechnology AG | Antigen binding molecules that bind EGFR, vectors encoding same, and uses thereof |
| AR062223A1 (es) * | 2006-08-09 | 2008-10-22 | Glycart Biotechnology Ag | Moleculas de adhesion al antigeno que se adhieren a egfr, vectores que los codifican, y sus usos de estas |
| US8529901B2 (en) * | 2007-06-06 | 2013-09-10 | Hoffmann-La Roche, Inc. | Composition of a first non-labeled monoclonal antibody binding to a tumor antigen and a non-cross reactive second monoclonal antibody labeled with a NIR fluorescence label |
| US9266967B2 (en) | 2007-12-21 | 2016-02-23 | Hoffmann-La Roche, Inc. | Bivalent, bispecific antibodies |
| US20090162359A1 (en) | 2007-12-21 | 2009-06-25 | Christian Klein | Bivalent, bispecific antibodies |
| CN102164960A (zh) * | 2008-09-26 | 2011-08-24 | 罗氏格黎卡特股份公司 | 双特异性抗-egfr/抗-igf-1r抗体 |
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| BRPI1014089A2 (pt) | 2009-04-02 | 2016-04-19 | Roche Glycart Ag | anticorpos multiespecíficos que compreendem anticorpos de comprimento completo e fragmentos fab de cadeia simples |
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| US9676845B2 (en) | 2009-06-16 | 2017-06-13 | Hoffmann-La Roche, Inc. | Bispecific antigen binding proteins |
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| CA2783715A1 (en) * | 2009-12-29 | 2011-07-07 | F. Hoffmann-La Roche Ag | Novel antibody formulation |
| EP2523976B1 (en) * | 2010-01-11 | 2018-04-25 | Alexion Pharmaceuticals, Inc. | Biomarkers of immunomodulatory effects in humans treated with anti-cd200 antibodies |
| US20110200595A1 (en) * | 2010-02-18 | 2011-08-18 | Roche Glycart | TREATMENT WITH A HUMANIZED IgG CLASS ANTI EGFR ANTIBODY AND AN ANTIBODY AGAINST INSULIN LIKE GROWTH FACTOR 1 RECEPTOR |
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| CN101875697B (zh) * | 2010-04-15 | 2014-04-30 | 北京天广实生物技术股份有限公司 | 新型抗egfr人源抗体tgm10的设计及其应用 |
| CA2807278A1 (en) | 2010-08-24 | 2012-03-01 | F. Hoffmann - La Roche Ag | Bispecific antibodies comprising a disulfide stabilized - fv fragment |
| TW201302793A (zh) | 2010-09-03 | 2013-01-16 | Glaxo Group Ltd | 新穎之抗原結合蛋白 |
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| CN102153647B (zh) * | 2011-01-27 | 2012-07-04 | 中国人民解放军军事医学科学院生物工程研究所 | 一种抗egfr人源化抗体l3-h3及其编码基因与应用 |
| AU2012215572A1 (en) | 2011-02-10 | 2013-05-02 | Roche Glycart Ag | Improved immunotherapy |
| JP5764677B2 (ja) | 2011-02-28 | 2015-08-19 | エフ・ホフマン−ラ・ロシュ・アクチェンゲゼルシャフト | 抗原結合タンパク質 |
| CN103403025B (zh) | 2011-02-28 | 2016-10-12 | 弗·哈夫曼-拉罗切有限公司 | 单价抗原结合蛋白 |
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| JP5925893B2 (ja) | 2011-08-23 | 2016-05-25 | ロシュ グリクアート アーゲー | 二重特異性抗原結合分子 |
| WO2013026839A1 (en) | 2011-08-23 | 2013-02-28 | Roche Glycart Ag | Bispecific antibodies specific for t-cell activating antigens and a tumor antigen and methods of use |
| PT2748201T (pt) | 2011-08-23 | 2018-02-08 | Roche Glycart Ag | Moléculas de ligação ao antigénio biespecíficas que ativam as células t |
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| WO2013033008A2 (en) | 2011-08-26 | 2013-03-07 | Merrimack Pharmaceuticals, Inc. | Tandem fc bispecific antibodies |
| EP2758435A1 (en) * | 2011-09-23 | 2014-07-30 | Roche Glycart AG | Bispecific anti-egfr/anti igf-1r antibodies |
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| CA2860369A1 (en) | 2012-03-02 | 2013-09-06 | Roche Glycart Ag | Predicitive biomarker for cancer treatment with adcc enhanced antibodies |
| EP2832363B1 (en) * | 2012-03-27 | 2018-09-19 | Green Cross Corporation | Epitopes of epidermal growth factor receptor surface antigen and use thereof |
| CA2872018A1 (en) * | 2012-05-17 | 2013-11-21 | Sorrento Therapeutics, Inc. | Antigen binding proteins that bind egfr |
| 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 |
| AU2013301582B2 (en) | 2012-08-07 | 2018-09-06 | Roche Glycart Ag | Composition comprising two antibodies engineered to have reduced and increased effector function |
| RU2015117393A (ru) | 2012-10-08 | 2016-12-10 | Роше Гликарт Аг | Лишенные fc антитела, содержащие два Fab-фрагмента, и способы их применения |
| AR094403A1 (es) * | 2013-01-11 | 2015-07-29 | Hoffmann La Roche | Terapia de combinación de anticuerpos anti-her3 |
| WO2014114595A1 (en) | 2013-01-23 | 2014-07-31 | Roche Glycart Ag | Predictive biomarker for cancer treatment with adcc-enhanced antibodies |
| RU2015140915A (ru) | 2013-02-26 | 2017-04-03 | Роше Гликарт Аг | Биспецифические антигенсвязывающие молекулы, активирующие т-клетки |
| EA201891502A1 (ru) | 2013-02-26 | 2018-12-28 | Роше Гликарт Аг | Биспецифические антигенсвязывающие молекулы, активирующие т-клетки |
| WO2014131711A1 (en) | 2013-02-26 | 2014-09-04 | Roche Glycart Ag | Bispecific t cell activating antigen binding molecules |
| MX2015011712A (es) | 2013-03-06 | 2016-04-04 | Merrimack Pharmaceuticals Inc | Anticerpos biespecificos fc en fila anti-c-met. |
| CN105229030A (zh) * | 2013-04-22 | 2016-01-06 | 葛莱高托普有限公司 | 用具有低岩藻糖基化的抗-egfr抗体的抗-癌治疗 |
| RU2016115866A (ru) | 2013-10-11 | 2017-11-16 | Ф. Хоффманн-Ля Рош Аг | Мультиспецифические антитела с обменянными доменами и одинаковыми вариабельными доменами легкой цепи |
| JP2016538283A (ja) | 2013-11-13 | 2016-12-08 | ザイムワークス，インコーポレイテッド | Ｅｇｆｒ及び／またはｈｅｒ２を標的にする一価抗原結合性構築物及びその使用 |
| SG11201607258SA (en) * | 2014-04-10 | 2016-10-28 | Obi Pharma Inc | Antibodies, pharmaceutical compositions and uses thereof |
| KR102411972B1 (ko) | 2014-08-04 | 2022-06-23 | 에프. 호프만-라 로슈 아게 | 이중특이적 t 세포 활성화 항원 결합 분자 |
| US9616114B1 (en) | 2014-09-18 | 2017-04-11 | David Gordon Bermudes | Modified bacteria having improved pharmacokinetics and tumor colonization enhancing antitumor activity |
| WO2016062851A1 (en) | 2014-10-23 | 2016-04-28 | Innate Pharma | Treatment of cancers using anti-nkg2a agents |
| RS60615B1 (sr) | 2014-11-20 | 2020-08-31 | Hoffmann La Roche | Zajednički laki lanci i postupci upotrebe |
| CN107074955B (zh) | 2014-11-20 | 2021-06-22 | 豪夫迈·罗氏有限公司 | 针对FolR1和CD3的T细胞活化性双特异性抗原结合分子 |
| LT3789402T (lt) | 2014-11-20 | 2022-09-26 | F. Hoffmann-La Roche Ag | Kompleksinė terapija, naudojant t ląsteles aktyvinančias bispecifines antigeną surišančias molekules ir pd-1 ašį surišančius antagonistus |
| PL3227332T3 (pl) | 2014-12-03 | 2020-06-15 | F. Hoffmann-La Roche Ag | Wielospecyficzne przeciwciała |
| US10676723B2 (en) | 2015-05-11 | 2020-06-09 | David Gordon Bermudes | Chimeric protein toxins for expression by therapeutic bacteria |
| AR106188A1 (es) | 2015-10-01 | 2017-12-20 | Hoffmann La Roche | Anticuerpos anti-cd19 humano humanizados y métodos de utilización |
| US20180282410A1 (en) | 2015-10-02 | 2018-10-04 | Hoffmann-La Roche Inc. | Anti-cd3xrob04 bispecific t cell activating antigen binding molecules |
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| EP3356417A1 (en) | 2015-10-02 | 2018-08-08 | H. Hoffnabb-La Roche Ag | Bispecific t cell activating antigen binding molecules binding mesothelin and cd3 |
| CN107949574A (zh) | 2015-10-02 | 2018-04-20 | 豪夫迈·罗氏有限公司 | 双特异性t细胞活化性抗原结合分子 |
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| WO2017055385A1 (en) | 2015-10-02 | 2017-04-06 | F. Hoffmann-La Roche Ag | Anti-cd3xgd2 bispecific t cell activating antigen binding molecules |
| CN107849137B (zh) | 2015-10-02 | 2021-11-26 | 豪夫迈·罗氏有限公司 | 双特异性抗ceaxcd3 t细胞活化性抗原结合分子 |
| WO2017055393A1 (en) | 2015-10-02 | 2017-04-06 | F. Hoffmann-La Roche Ag | Anti-cd3xtim-3 bispecific t cell activating antigen binding molecules |
| IL257696B2 (en) | 2015-12-09 | 2024-11-01 | Hoffmann La Roche | Type ii anti-cd20 antibody for reducing formation of anti-drug antibodies |
| KR20180097615A (ko) | 2016-01-08 | 2018-08-31 | 에프. 호프만-라 로슈 아게 | Pd-1 축 결합 길항물질 및 항-cea/항-cd3 이중특이성 항체를 사용하는 cea-양성 암의 치료 방법 |
| FI3433280T3 (fi) | 2016-03-22 | 2023-06-06 | Hoffmann La Roche | Proteaasin aktivoimia t-solubispesifisiä molekyylejä |
| BR112018016281A2 (pt) | 2016-03-22 | 2019-01-02 | F. Hoffmann-La Roche Ag | molécula biespecífica ativadora de célula t ativável por protease, polipeptídeo idiotipo-específico, composição farmacêutica, usos da molécula biespecífica e método de tratamento de uma doença em um indivíduo |
| US10753936B2 (en) | 2016-07-22 | 2020-08-25 | Van Andel Research Institute | Method of detecting the level of a glycan |
| WO2018060301A1 (en) | 2016-09-30 | 2018-04-05 | F. Hoffmann-La Roche Ag | Bispecific antibodies against cd3 |
| US11129906B1 (en) | 2016-12-07 | 2021-09-28 | David Gordon Bermudes | Chimeric protein toxins for expression by therapeutic bacteria |
| US11180535B1 (en) | 2016-12-07 | 2021-11-23 | David Gordon Bermudes | Saccharide binding, tumor penetration, and cytotoxic antitumor chimeric peptides from therapeutic bacteria |
| SG11201908784TA (en) | 2017-03-27 | 2019-10-30 | Hoffmann La Roche | Improved antigen binding receptor formats |
| AU2018241624B2 (en) | 2017-03-27 | 2024-01-25 | F. Hoffmann-La Roche Ag | Improved antigen binding receptors |
| PT3606946T (pt) | 2017-04-03 | 2022-10-17 | Hoffmann La Roche | Imunoconjugados de um anticorpo anti-pd-1 com uma il-2 mutante ou com il-15 |
| WO2018184965A1 (en) | 2017-04-03 | 2018-10-11 | F. Hoffmann-La Roche Ag | Immunoconjugates of il-2 with an anti-pd-1 and tim-3 bispecific antibody |
| BR112019018767A2 (pt) | 2017-04-03 | 2020-05-05 | Hoffmann La Roche | anticorpos, molécula de ligação ao antígeno biespecífica, um ou mais polinucleotídeos isolados, um ou mais vetores, célula hospedeira, método para produzir um anticorpo, composição farmacêutica, usos, método para tratar uma doença em um indivíduo e invenção |
| LT3606954T (lt) | 2017-04-05 | 2022-09-26 | F. Hoffmann-La Roche Ag | Anti-lag3 antikūnai |
| BR112019021411A2 (pt) | 2017-04-13 | 2020-05-05 | Hoffmann La Roche | métodos para tratar ou retardar a progressão do câncer e para melhorar a função, usos de um imunoconjugado, de um agonista, de um antagonista, composições, kit e invenção |
| GB201710836D0 (en) * | 2017-07-05 | 2017-08-16 | Ucl Business Plc | ROR1 Car T-Cells |
| CN107881160A (zh) * | 2017-08-11 | 2018-04-06 | 百奥泰生物科技(广州)有限公司 | 一种由基因组被编辑的cho宿主细胞产生的具有独特糖谱的重组抗体及其制备方法 |
| US11802154B2 (en) | 2017-12-20 | 2023-10-31 | Alexion Pharmaceuticals, Inc. | Humanized anti-CD200 antibodies and uses thereof |
| WO2019126133A1 (en) | 2017-12-20 | 2019-06-27 | Alexion Pharmaceuticals, Inc. | Liquid formulations of anti-cd200 antibodies |
| CN111527107B (zh) | 2017-12-21 | 2024-10-01 | 豪夫迈·罗氏有限公司 | 结合hla-a2/wt1的抗体 |
| JP7394058B2 (ja) | 2017-12-21 | 2023-12-07 | エフ・ホフマン－ラ・ロシュ・アクチェンゲゼルシャフト | 新規抗原結合部分の特異性試験のためのユニバーサルレポーター細胞アッセイ |
| JP2021508471A (ja) | 2017-12-29 | 2021-03-11 | エフ．ホフマン−ラ ロシュ アーゲーＦ． Ｈｏｆｆｍａｎｎ−Ｌａ Ｒｏｃｈｅ Ａｋｔｉｅｎｇｅｓｅｌｌｓｃｈａｆｔ | 抗ｖｅｇｆ抗体のｖｅｇｆ受容体遮断選択性を改善する方法 |
| MX2020008289A (es) | 2018-02-08 | 2020-09-25 | Genentech Inc | Moleculas biespecificas de union al antigeno y metodos de uso. |
| TWI829667B (zh) | 2018-02-09 | 2024-01-21 | 瑞士商赫孚孟拉羅股份公司 | 結合gprc5d之抗體 |
| MX2020010028A (es) | 2018-03-29 | 2020-10-14 | Genentech Inc | Actividad lactogenica modulada en celulas de mamifero. |
| JP7609771B2 (ja) * | 2018-06-01 | 2025-01-07 | エムユーエスシー ファウンデーション フォー リサーチ ディベロップメント | タンパク質と細胞のグリカン分析 |
| TWI881476B (zh) | 2018-12-21 | 2025-04-21 | 瑞士商赫孚孟拉羅股份公司 | 結合cd3之抗體 |
| EP3898671A1 (en) | 2018-12-21 | 2021-10-27 | F. Hoffmann-La Roche AG | Antibody that binds to vegf and il-1beta and methods of use |
| WO2020127618A1 (en) | 2018-12-21 | 2020-06-25 | F. Hoffmann-La Roche Ag | Tumor-targeted agonistic cd28 antigen binding molecules |
| US20200223925A1 (en) | 2018-12-21 | 2020-07-16 | Hoffmann-La Roche Inc. | Tumor-targeted superagonistic cd28 antigen binding molecules |
| JP2022516140A (ja) | 2018-12-26 | 2022-02-24 | インネート・ファルマ | 白血球免疫グロブリン様受容体２中和抗体 |
| TW202115124A (zh) | 2019-06-26 | 2021-04-16 | 瑞士商赫孚孟拉羅股份公司 | 結合至cea之新穎抗原結合分子 |
| WO2021001289A1 (en) | 2019-07-02 | 2021-01-07 | F. Hoffmann-La Roche Ag | Immunoconjugates comprising a mutant interleukin-2 and an anti-cd8 antibody |
| AR119382A1 (es) | 2019-07-12 | 2021-12-15 | Hoffmann La Roche | Anticuerpos de pre-direccionamiento y métodos de uso |
| AR119393A1 (es) | 2019-07-15 | 2021-12-15 | Hoffmann La Roche | Anticuerpos que se unen a nkg2d |
| CN114450306B (zh) | 2019-07-26 | 2024-04-05 | Abl生物公司 | 抗egfr/抗4-1bb双特异性抗体及其用途 |
| EP4004045A1 (en) | 2019-07-31 | 2022-06-01 | F. Hoffmann-La Roche AG | Antibodies binding to gprc5d |
| PE20220394A1 (es) | 2019-07-31 | 2022-03-18 | Hoffmann La Roche | Anticuerpos que se fijan a gprc5d |
| CR20220156A (es) | 2019-09-18 | 2022-05-23 | Genentech Inc | Anticuerpos anti-klk7, anticuerpos anti-klk5, anticuerpos multiespecíficos anti-klk5/klk7 y métodos de uso |
| PE20221282A1 (es) | 2019-12-18 | 2022-09-05 | Hoffmann La Roche | Anticuerpos que se unen a hla-a2/mage-a4 |
| CN111018990A (zh) * | 2020-02-10 | 2020-04-17 | 张喜田 | 一种新型的重组抗表皮生长因子受体单克隆抗体及其应用 |
| CN115315512A (zh) | 2020-03-26 | 2022-11-08 | 基因泰克公司 | 具有降低的宿主细胞蛋白质的经修饰的哺乳动物细胞 |
| EP4135848A2 (en) | 2020-04-15 | 2023-02-22 | F. Hoffmann-La Roche AG | Immunoconjugates |
| EP4149524A1 (en) | 2020-05-11 | 2023-03-22 | F. Hoffmann-La Roche AG | Combination therapy with modified pbmcs and an immunoconjugate |
| AR122569A1 (es) | 2020-06-08 | 2022-09-21 | Hoffmann La Roche | Anticuerpos anti-vhb y métodos de uso |
| WO2021255146A1 (en) | 2020-06-19 | 2021-12-23 | F. Hoffmann-La Roche Ag | Antibodies binding to cd3 and cea |
| TWI852680B (zh) | 2020-06-19 | 2024-08-11 | 瑞士商赫孚孟拉羅股份公司 | 與 cd3 及 cd19 結合之抗體 |
| WO2021255137A1 (en) | 2020-06-19 | 2021-12-23 | F. Hoffmann-La Roche Ag | Protease-activated t cell bispecific antibodies |
| WO2021255143A1 (en) | 2020-06-19 | 2021-12-23 | F. Hoffmann-La Roche Ag | Antibodies binding to cd3 and folr1 |
| AR122657A1 (es) | 2020-06-19 | 2022-09-28 | Hoffmann La Roche | Moléculas de unión al dominio fc de activación inmunitaria |
| AU2021291407A1 (en) | 2020-06-19 | 2022-09-29 | F. Hoffmann-La Roche Ag | Antibodies binding to CD3 |
| TW202216769A (zh) | 2020-06-23 | 2022-05-01 | 瑞士商赫孚孟拉羅股份公司 | 靶向ｈｅｒ２的激動性ｃｄ２８抗原結合分子 |
| IL299161A (en) | 2020-06-24 | 2023-02-01 | Genentech Inc | Cell lines resistant to apoptosis |
| 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 |
| PE20230434A1 (es) | 2020-07-10 | 2023-03-08 | Hoffmann La Roche | Anticuerpos que se unen a celulas cancerosas y dirigen radionucleotidos a dichas celulas |
| WO2022016037A1 (en) | 2020-07-17 | 2022-01-20 | Genentech, Inc. | Anti-notch2 antibodies and methods of use |
| WO2022029051A1 (en) | 2020-08-03 | 2022-02-10 | F. Hoffmann-La Roche Ag | Improved antigen binding receptors |
| KR20230056766A (ko) | 2020-08-28 | 2023-04-27 | 제넨테크, 인크. | 숙주 세포 단백질의 CRISPR/Cas9 다중 녹아웃 |
| CR20230114A (es) | 2020-09-04 | 2023-05-18 | Hoffmann La Roche | Anticuerpo que se une a vegf-a y ang2, y métodos de uso |
| AR123855A1 (es) | 2020-10-20 | 2023-01-18 | Genentech Inc | Anticuerpos anti-mertk conjugados con peg y métodos de uso |
| EP4237449A1 (en) | 2020-10-28 | 2023-09-06 | F. Hoffmann-La Roche AG | Improved antigen binding receptors |
| WO2022148853A1 (en) | 2021-01-11 | 2022-07-14 | F. Hoffmann-La Roche Ag | Immunoconjugates |
| MX2023008084A (es) | 2021-01-12 | 2023-07-13 | Hoffmann La Roche | Anticuerpos split que se unen a celulas cancerosas y dirigen radionuclidos a dichas celulas. |
| WO2022152701A1 (en) | 2021-01-13 | 2022-07-21 | F. Hoffmann-La Roche Ag | Combination therapy |
| WO2022169872A1 (en) | 2021-02-03 | 2022-08-11 | Genentech, Inc. | Multispecific binding protein degrader platform and methods of use |
| AR125074A1 (es) | 2021-03-12 | 2023-06-07 | Genentech Inc | Anticuerpos anti-klk7, anticuerpos anti-klk5, anticuerpos multiespecíficos anti-klk5 / klk7 y métodos de uso |
| JP2024512709A (ja) | 2021-03-30 | 2024-03-19 | エフ・ホフマン－ラ・ロシュ・アクチェンゲゼルシャフト | プロテアーゼ活性化ポリペプチド |
| IL307501A (en) | 2021-04-19 | 2023-12-01 | Hoffmann La Roche | Modified mammalian cells |
| MX2023012408A (es) | 2021-04-30 | 2023-10-31 | Hoffmann La Roche | Dosis para tratamiento conjunto con anticuerpo biespecifico anti-cd20/anti-cd3 y conjugado anticuerpo farmaco anti-cd79b. |
| EP4341385A1 (en) | 2021-05-21 | 2024-03-27 | Genentech, Inc. | Modified cells for the production of a recombinant product of interest |
| AR126009A1 (es) | 2021-06-02 | 2023-08-30 | Hoffmann La Roche | Moléculas agonistas de unión al antígeno cd28 que se dirigen a epcam |
| US20230048743A1 (en) | 2021-07-12 | 2023-02-16 | Genentech Inc. | Structures for Reducing Antibody-Lipase Binding |
| IL309856A (en) | 2021-07-14 | 2024-02-01 | Genentech Inc | Antibodies anti-C-C motif receptor 8 (CCR8) and methods of use |
| 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 |
| CN117794953A (zh) | 2021-08-03 | 2024-03-29 | 豪夫迈·罗氏有限公司 | 双特异性抗体及使用方法 |
| EP4416174A1 (en) | 2021-10-14 | 2024-08-21 | F. Hoffmann-La Roche AG | New interleukin-7 immunoconjugates |
| EP4429706A1 (en) | 2021-10-14 | 2024-09-18 | F. Hoffmann-La Roche AG | Alternative pd1-il7v immunoconjugates for the treatment of cancer |
| AU2022397540A1 (en) | 2021-11-25 | 2024-05-16 | F. Hoffmann-La Roche Ag | Improved antigen binding receptors |
| WO2023094569A1 (en) | 2021-11-26 | 2023-06-01 | F. Hoffmann-La Roche Ag | Combination therapy of anti-tyrp1/anti-cd3 bispecific antibodies and tyrp1-specific antibodies |
| AR127887A1 (es) | 2021-12-10 | 2024-03-06 | Hoffmann La Roche | Anticuerpos que se unen a cd3 y plap |
| CN116333117B (zh) * | 2021-12-16 | 2024-04-26 | 徕特康(苏州)生物制药有限公司 | 抗表皮生长因子受体抗体及其制备方法和用途 |
| CN116333116B (zh) * | 2021-12-16 | 2024-03-05 | 徕特康(苏州)生物制药有限公司 | 抗表皮生长因子受体抗体及其制备方法和用途 |
| US20230322958A1 (en) | 2022-01-19 | 2023-10-12 | Genentech, Inc. | Anti-Notch2 Antibodies and Conjugates and Methods of Use |
| JP2025508692A (ja) | 2022-02-11 | 2025-04-10 | 江▲蘇▼恒瑞医▲薬▼股▲フン▼有限公司 | 免疫複合体及びその使用 |
| 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 |
| AR129268A1 (es) | 2022-05-11 | 2024-08-07 | Hoffmann La Roche | Anticuerpo que se une a vegf-a e il6 y métodos de uso |
| CN120129693A (zh) | 2022-08-01 | 2025-06-10 | 旗舰创业创新第七有限责任公司 | 免疫调节蛋白及相关方法 |
| EP4594345A1 (en) | 2022-09-29 | 2025-08-06 | F. Hoffmann-La Roche AG | Protease-activated polypeptides |
| AU2023356326A1 (en) | 2022-10-06 | 2025-03-27 | Bicara Therapeutics Inc. | Multispecific proteins and related methods |
| AU2023356218A1 (en) | 2022-10-07 | 2025-04-24 | Genentech, Inc. | Methods of treating cancer with anti-c-c motif chemokine receptor 8 (ccr8) antibodies |
| TW202430211A (zh) | 2022-10-10 | 2024-08-01 | 瑞士商赫孚孟拉羅股份公司 | Ｇｐｒｃ５ｄ ｔｃｂ及ｉｍｉｄ之組合療法 |
| TW202423969A (zh) | 2022-10-10 | 2024-06-16 | 瑞士商赫孚孟拉羅股份公司 | Ｇｐｒｃ５ｄ ｔｃｂ及蛋白酶體抑制劑之組合療法 |
| TW202423970A (zh) | 2022-10-10 | 2024-06-16 | 瑞士商赫孚孟拉羅股份公司 | Ｇｐｒｃ５ｄ ｔｃｂ及ｃｄ３８抗體之組合療法 |
| CN120152989A (zh) | 2022-11-03 | 2025-06-13 | 豪夫迈·罗氏有限公司 | 抗cd19/抗cd28双特异性抗体的组合疗法 |
| WO2024100170A1 (en) | 2022-11-11 | 2024-05-16 | F. Hoffmann-La Roche Ag | Antibodies binding to hla-a*02/foxp3 |
| JP2025539760A (ja) | 2022-11-15 | 2025-12-09 | エフ・ホフマン－ラ・ロシュ・アクチェンゲゼルシャフト | 抗原結合分子 |
| AU2023404602A1 (en) | 2022-11-29 | 2025-05-29 | Jiangsu Hengrui Pharmaceuticals Co., Ltd. | Cldn18.2/4-1bb binding protein and medical use thereof |
| WO2024120516A1 (zh) | 2022-12-08 | 2024-06-13 | 南京诺唯赞生物科技股份有限公司 | 特异性结合rsv的抗体 |
| US20240360229A1 (en) | 2023-01-18 | 2024-10-31 | Genentech, Inc. | Multispecific antibodies and uses thereof |
| CN120548192A (zh) | 2023-01-20 | 2025-08-26 | 豪夫迈·罗氏有限公司 | 免疫缀合物 |
| CN120569410A (zh) | 2023-01-25 | 2025-08-29 | 豪夫迈·罗氏有限公司 | 与csf1r和cd3结合的抗体 |
| TW202438515A (zh) | 2023-02-06 | 2024-10-01 | 美商旗艦先鋒創新有限責任（Ｖｉｉ）公司 | 免疫調節組合物及相關方法 |
| CN120826234A (zh) | 2023-03-06 | 2025-10-21 | 豪夫迈·罗氏有限公司 | 抗EGFRvIII/抗CD3抗体与肿瘤靶向性4-1BB激动剂的组合疗法 |
| CN120858109A (zh) | 2023-03-10 | 2025-10-28 | 基因泰克公司 | 与蛋白酶的融合物及其用途 |
| WO2024206788A1 (en) | 2023-03-31 | 2024-10-03 | Genentech, Inc. | Anti-alpha v beta 8 integrin antibodies and methods of use |
| CN120917044A (zh) | 2023-04-03 | 2025-11-07 | 豪夫迈·罗氏有限公司 | 激动性拆分型抗体 |
| CN120882744A (zh) | 2023-04-03 | 2025-10-31 | 豪夫迈·罗氏有限公司 | 一体化激动性抗体 |
| AR132623A1 (es) | 2023-05-08 | 2025-07-16 | Hoffmann La Roche | PROTEÍNAS DE FUSIÓN DE INTERFERÓN a DIRIGIDAS Y MÉTODOS DE USO |
| AR132687A1 (es) | 2023-05-16 | 2025-07-23 | Hoffmann La Roche | Inmunoconjugados de il-2 regulados por pd-1 y sus usos |
| TW202502811A (zh) | 2023-06-01 | 2025-01-16 | 瑞士商赫孚孟拉羅股份公司 | 與ｂｃｍａ特異性結合之免疫刺激性抗原結合分子 |
| WO2024246083A1 (en) | 2023-06-01 | 2024-12-05 | F. Hoffmann-La Roche Ag | Bispecific antibodies targeting bcma and cd28 |
| US20250011450A1 (en) | 2023-06-22 | 2025-01-09 | Genentech, Inc. | Antibodies and uses thereof |
| WO2025024334A1 (en) | 2023-07-21 | 2025-01-30 | Marrow Therapeutics, Inc. | Hematopoietic cell targeting conjugates and related methods |
| WO2025021838A1 (en) | 2023-07-26 | 2025-01-30 | F. Hoffmann-La Roche Ag | Antibodies binding to cd3 |
| WO2025040567A1 (en) | 2023-08-18 | 2025-02-27 | F. Hoffmann-La Roche Ag | Protease activatable fc domain binding molecules |
| AR133909A1 (es) | 2023-09-25 | 2025-11-12 | Hoffmann La Roche | ANTICUERPO QUE SE UNE A C3bBb |
| WO2025099120A1 (en) | 2023-11-09 | 2025-05-15 | F. Hoffmann-La Roche Ag | Multispecific antibodies with conditional activity |
| WO2025125118A1 (en) | 2023-12-11 | 2025-06-19 | F. Hoffmann-La Roche Ag | Protease activatable fc domain binding molecules |
| WO2025125386A1 (en) | 2023-12-14 | 2025-06-19 | F. Hoffmann-La Roche Ag | Antibodies that bind to folr1 and methods of use |
| WO2025132503A1 (en) | 2023-12-20 | 2025-06-26 | F. Hoffmann-La Roche Ag | Antibodies binding to ceacam5 |
| WO2025133290A1 (en) | 2023-12-21 | 2025-06-26 | Temper Bio | Protein for immune regulation |
| WO2025133042A2 (en) | 2023-12-22 | 2025-06-26 | F. Hoffmann-La Roche Ag | Activatable fusion proteins and methods of use |
| WO2025149633A1 (en) | 2024-01-12 | 2025-07-17 | Laigo Bio B.V. | Bispecific antigen binding proteins |
| US20250375499A1 (en) | 2024-01-26 | 2025-12-11 | Flagship Pioneering Innovations Vii, Llc | Immunoreceptor inhibitory proteins and related methods |
| WO2025181189A1 (en) | 2024-03-01 | 2025-09-04 | F. Hoffmann-La Roche Ag | Antibodies binding to cd3 |
| WO2025202147A1 (en) | 2024-03-27 | 2025-10-02 | F. Hoffmann-La Roche Ag | Interleukin-7 immunoconjugates |
| WO2025215060A1 (en) | 2024-04-11 | 2025-10-16 | F. Hoffmann-La Roche Ag | Antibodies that specifically bind modified oligonucleotides |
| US20250353881A1 (en) | 2024-05-16 | 2025-11-20 | Flagship Pioneering Innovations Vii, Llc | Immunoreceptor inhibitory proteins and related methods |
| WO2025245111A1 (en) | 2024-05-22 | 2025-11-27 | Flagship Pioneering Innovations Vii, Llc | Immunoreceptor targeting proteins and related methods |
Family Cites Families (58)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| US2820404A (en) | 1954-11-23 | 1958-01-21 | Kwei Chung Shu | Photoprinting apparatus |
| US3773919A (en) | 1969-10-23 | 1973-11-20 | Du Pont | Polylactide-drug mixtures |
| CU22545A1 (es) | 1994-11-18 | 1999-03-31 | Centro Inmunologia Molecular | Obtención de un anticuerpo quimérico y humanizado contra el receptor del factor de crecimiento epidérmico para uso diagnóstico y terapéutico |
| US4816567A (en) | 1983-04-08 | 1989-03-28 | Genentech, Inc. | Recombinant immunoglobin preparations |
| EP0173494A3 (en) | 1984-08-27 | 1987-11-25 | The Board Of Trustees Of The Leland Stanford Junior University | Chimeric receptors by dna splicing and expression |
| US5225539A (en) | 1986-03-27 | 1993-07-06 | Medical Research Council | Recombinant altered antibodies and methods of making altered antibodies |
| US5530101A (en) | 1988-12-28 | 1996-06-25 | Protein Design Labs, Inc. | Humanized immunoglobulins |
| US5859205A (en) | 1989-12-21 | 1999-01-12 | Celltech Limited | Humanised antibodies |
| DK0531472T3 (da) | 1991-03-06 | 2003-12-01 | Merck Patent Gmbh | Humaniserede monoklonale antistoffer |
| EP0590058B1 (en) | 1991-06-14 | 2003-11-26 | Genentech, Inc. | HUMANIZED Heregulin ANTIBODy |
| GB9401182D0 (en) * | 1994-01-21 | 1994-03-16 | Inst Of Cancer The Research | Antibodies to EGF receptor and their antitumour effect |
| MX9800684A (es) | 1995-07-27 | 1998-04-30 | Genentech Inc | Formulacion de proteinas liofilizadas isotonicas estables. |
| US6001358A (en) | 1995-11-07 | 1999-12-14 | Idec Pharmaceuticals Corporation | Humanized antibodies to human gp39, compositions containing thereof |
| DE19746874A1 (de) | 1997-10-23 | 1999-04-29 | Qiagen Gmbh | Verfahren zur Isolierung und Reinigung von Nukleinsäuren an hydrophoben Oberflächen - insbesondere unter Verwendung hydrophober Membranen |
| JP4334141B2 (ja) | 1998-04-20 | 2009-09-30 | グリカート バイオテクノロジー アクチェンゲゼルシャフト | 抗体依存性細胞傷害性を改善するための抗体のグリコシル化操作 |
| US6737056B1 (en) | 1999-01-15 | 2004-05-18 | Genentech, Inc. | Polypeptide variants with altered effector function |
| US6322980B1 (en) | 1999-04-30 | 2001-11-27 | Aclara Biosciences, Inc. | Single nucleotide detection using degradation of a fluorescent sequence |
| CA2369292C (en) | 1999-04-09 | 2010-09-21 | Kyowa Hakko Kogyo Co. Ltd. | Method of modulating the activity of functional immune molecules |
| CN1308347C (zh) * | 1999-04-28 | 2007-04-04 | 德克萨斯大学董事会 | 用于通过选择性抑制vegf来治疗癌症的组合物和方法 |
| NZ523912A (en) | 2000-07-31 | 2005-03-24 | Biolex Inc | Expression of biologically active polypeptides in duckweed |
| US6946292B2 (en) | 2000-10-06 | 2005-09-20 | Kyowa Hakko Kogyo Co., Ltd. | Cells producing antibody compositions with increased antibody dependent cytotoxic activity |
| AU2002213357A1 (en) | 2000-10-20 | 2002-05-06 | Idec Pharmaceuticals Corporation | Variant igg3 rituxan r and therapeutic use thereof |
| PT1392359E (pt) * | 2001-05-11 | 2010-01-27 | Ludwig Inst For Cancer Res Ltd | Proteínas de ligação específica e suas utilizações |
| CZ200438A3 (cs) * | 2001-06-13 | 2004-06-16 | Genmab A/S | Název neuveden |
| US7321026B2 (en) | 2001-06-27 | 2008-01-22 | Skytech Technology Limited | Framework-patched immunoglobulins |
| WO2004006955A1 (en) | 2001-07-12 | 2004-01-22 | Jefferson Foote | Super humanized antibodies |
| CA2455365C (en) | 2001-08-03 | 2014-07-29 | Glycart Biotechnology Ag | Antibody glycosylation variants having increased antibody-dependent cellular cytotoxicity |
| US7084257B2 (en) | 2001-10-05 | 2006-08-01 | Amgen Inc. | Fully human antibody Fab fragments with human interferon-gamma neutralizing activity |
| ATE430580T1 (de) | 2001-10-25 | 2009-05-15 | Genentech Inc | Glycoprotein-zusammensetzungen |
| US20040093621A1 (en) | 2001-12-25 | 2004-05-13 | Kyowa Hakko Kogyo Co., Ltd | Antibody composition which specifically binds to CD20 |
| KR101001243B1 (ko) | 2001-12-27 | 2010-12-17 | 글리코파이, 인크. | 포유동물-유형 탄수화물 구조의 설계 방법 |
| US7432063B2 (en) | 2002-02-14 | 2008-10-07 | Kalobios Pharmaceuticals, Inc. | Methods for affinity maturation |
| US20040132101A1 (en) | 2002-09-27 | 2004-07-08 | Xencor | Optimized Fc variants and methods for their generation |
| EP1485492B1 (en) | 2002-03-19 | 2011-12-21 | Stichting Dienst Landbouwkundig Onderzoek | Gntiii (udp-n-acetylglucosamine:beta-d mannoside beta(1,4)-n-acetylglucosaminyltransferase iii) expression in plants |
| US8420353B2 (en) | 2002-03-22 | 2013-04-16 | Aprogen, Inc. | Humanized antibody and process for preparing same |
| CN100367698C (zh) | 2002-03-28 | 2008-02-06 | 先进微装置公司 | 同步数据检测单元及方法 |
| US20030190689A1 (en) | 2002-04-05 | 2003-10-09 | Cell Signaling Technology,Inc. | Molecular profiling of disease and therapeutic response using phospho-specific antibodies |
| CN1930288B (zh) | 2002-04-09 | 2012-08-08 | 协和发酵麒麟株式会社 | 基因组被修饰的细胞 |
| WO2003085119A1 (en) | 2002-04-09 | 2003-10-16 | Kyowa Hakko Kogyo Co., Ltd. | METHOD OF ENHANCING ACTIVITY OF ANTIBODY COMPOSITION OF BINDING TO FcϜ RECEPTOR IIIa |
| WO2003084570A1 (en) | 2002-04-09 | 2003-10-16 | Kyowa Hakko Kogyo Co., Ltd. | DRUG CONTAINING ANTIBODY COMPOSITION APPROPRIATE FOR PATIENT SUFFERING FROM FcϜRIIIa POLYMORPHISM |
| JPWO2003085118A1 (ja) | 2002-04-09 | 2005-08-11 | 協和醗酵工業株式会社 | 抗体組成物の製造方法 |
| ES2362419T3 (es) | 2002-04-09 | 2011-07-05 | Kyowa Hakko Kirin Co., Ltd. | Células con depresión o deleción de la actividad de la proteína que participa en el transporte de gdp-fucosa. |
| US20040132097A1 (en) | 2002-06-19 | 2004-07-08 | Bacus Sarah S. | Method for predicting response to epidermal growth factor receptor-directed therapy |
| DE60333201D1 (de) | 2002-09-12 | 2010-08-12 | Greenovation Biotech Gmbh | Verfahren zur herstellung von proteinen |
| RU2325186C2 (ru) * | 2002-09-27 | 2008-05-27 | Ксенкор, Инк. | АНТИТЕЛО, СОДЕРЖАЩЕЕ Fc-ВАРИАНТНУЮ ЧАСТЬ (ВАРИАНТЫ), ФАРМАЦЕВТИЧЕСКАЯ КОМПОЗИЦИЯ, СОДЕРЖАЩАЯ АНТИТЕЛО, И СПОСОБ ЛЕЧЕНИЯ МЛЕКОПИТАЮЩЕГО |
| US6938692B2 (en) | 2002-12-17 | 2005-09-06 | Halliburton Energy Services, Inc. | Permeable cement composition and method for preparing the same |
| WO2004057002A2 (en) | 2002-12-20 | 2004-07-08 | Greenovation Biotech Gmbh | Production of heterologous glycosylated proteins in bryophyte cells |
| EP1587540B1 (en) | 2003-01-09 | 2021-09-15 | MacroGenics, Inc. | IDENTIFICATION AND ENGINEERING OF ANTIBODIES WITH VARIANT Fc REGIONS AND METHODS OF USING SAME |
| PL224786B1 (pl) | 2003-01-22 | 2017-01-31 | Glycart Biotechnology Ag | Wyizolowany kwas nukleinowy, ssaczy wektor ekspresyjny, komórki gospodarza, fuzja polipeptydowa i sposób jej wytwarzania, sposoby in vitro i ex vivo modyfikowania profilu glikozylacji polipeptydu wytwarzanego przez komórki gospodarza |
| ME01775B (me) | 2003-11-05 | 2011-02-28 | Glycart Biotechnology Ag | Cd20 antitijela sa povećanim afinitetom vezivanja za fc receptor i efektornom funkcijom |
| EP1701979A2 (en) * | 2003-12-03 | 2006-09-20 | Xencor, Inc. | Optimized antibodies that target the epidermal growth factor receptor |
| AU2004297616B2 (en) * | 2003-12-04 | 2008-12-18 | Xencor, Inc. | Methods of generating variant proteins with increased host string content and compositions thereof |
| EP2402374A1 (en) * | 2005-02-07 | 2012-01-04 | GlycArt Biotechnology AG | Antigen binding molecules that bind EGFR, vectors encoding same, and uses thereof |
| US20100068163A1 (en) * | 2005-07-13 | 2010-03-18 | L'oreal | Keratin Fibre Coating Composition Comprising a Liquid Fatty Phase and a Tackifying Resin |
| WO2007031875A2 (en) | 2005-08-26 | 2007-03-22 | Glycart Biotechnology Ag | Modified antigen binding molecules with altered cell signaling activity |
| AR062223A1 (es) * | 2006-08-09 | 2008-10-22 | Glycart Biotechnology Ag | Moleculas de adhesion al antigeno que se adhieren a egfr, vectores que los codifican, y sus usos de estas |
| US20100291593A1 (en) * | 2007-07-13 | 2010-11-18 | Powell William C | Method of identifying diagnostic reagents |
| CN102164960A (zh) * | 2008-09-26 | 2011-08-24 | 罗氏格黎卡特股份公司 | 双特异性抗-egfr/抗-igf-1r抗体 |
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