CN113045650A - 抗-c5抗体及使用方法 - Google Patents
抗-c5抗体及使用方法 Download PDFInfo
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- CN113045650A CN113045650A CN202110290669.9A CN202110290669A CN113045650A CN 113045650 A CN113045650 A CN 113045650A CN 202110290669 A CN202110290669 A CN 202110290669A CN 113045650 A CN113045650 A CN 113045650A
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| RU2510400C9 (ru) | 2007-09-26 | 2014-07-20 | Чугаи Сейяку Кабусики Кайся | Способ модификации изоэлектрической точки антитела с помощью аминокислотных замен в cdr |
| US20110111406A1 (en) | 2008-04-11 | 2011-05-12 | Chugai Seiyaku Kabushiki Kaisha | Antigen-binding molecule capable of binding to two or more antigen molecules repeatedly |
| WO2012073992A1 (ja) | 2010-11-30 | 2012-06-07 | 中外製薬株式会社 | 複数分子の抗原に繰り返し結合する抗原結合分子 |
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| TW201817744A (zh) * | 2011-09-30 | 2018-05-16 | 日商中外製藥股份有限公司 | 具有促進抗原清除之FcRn結合域的治療性抗原結合分子 |
| JP6352634B2 (ja) | 2011-09-30 | 2018-07-04 | 中外製薬株式会社 | 標的抗原に対する免疫応答を誘導する抗原結合分子 |
| 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 |
| KR20230143201A (ko) | 2011-11-30 | 2023-10-11 | 추가이 세이야쿠 가부시키가이샤 | 면역 복합체를 형성하는 세포내로의 운반체(캐리어)를 포함하는 의약 |
| EP2813568B1 (en) | 2012-02-09 | 2025-04-23 | Chugai Seiyaku Kabushiki Kaisha | Modified fc region of antibody |
| TWI617578B (zh) | 2012-05-30 | 2018-03-11 | Chugai Pharmaceutical Co Ltd | 標的組織專一的抗原結合分子 |
| TWI855488B (zh) | 2012-08-24 | 2024-09-11 | 日商中外製藥股份有限公司 | FcγRIIb特異性Fc區域變異體 |
| US11267868B2 (en) | 2013-04-02 | 2022-03-08 | Chugai Seiyaku Kabushiki Kaisha | Fc region variant |
| MA40764A (fr) | 2014-09-26 | 2017-08-01 | Chugai Pharmaceutical Co Ltd | Agent thérapeutique induisant une cytotoxicité |
| AR103162A1 (es) | 2014-12-19 | 2017-04-19 | Chugai Pharmaceutical Co Ltd | Anticuerpos anti-c5 y métodos para su uso |
| AR103161A1 (es) | 2014-12-19 | 2017-04-19 | Chugai Pharmaceutical Co Ltd | Anticuerpos antimiostatina y regiones fc variantes así como métodos de uso |
| TW202248212A (zh) | 2015-02-05 | 2022-12-16 | 日商中外製藥股份有限公司 | 包含離子濃度依賴之抗原結合域的抗體、Fc區變體、IL-8結合抗體與其用途 |
| TW201718014A (zh) | 2015-10-12 | 2017-06-01 | 諾華公司 | C5抑制劑於移植相關微血管病之用途 |
| RU2742606C2 (ru) * | 2015-12-18 | 2021-02-09 | Чугаи Сейяку Кабусики Кайся | Антитела к с5 и способы их применения |
| EP3394098A4 (en) | 2015-12-25 | 2019-11-13 | Chugai Seiyaku Kabushiki Kaisha | ANTI-MYOSTATIN ANTIBODIES AND METHODS OF USE |
| EP3402816A1 (en) | 2016-01-11 | 2018-11-21 | Alexion Pharmaceuticals, Inc. | Dosage and administration of anti-c5 antibodies for treatment |
| SG11201809959PA (en) | 2016-05-10 | 2018-12-28 | Genentech Inc | Methods of decreasing trisulfide bonds during recombinant production of polypeptides |
| JP2019517473A (ja) | 2016-05-27 | 2019-06-24 | アレクシオン ファーマシューティカルズ インコーポレイテッドAlexion Pharmaceuticals, Inc. | 難治性全身型重症筋無力症の処置のための方法 |
| KR102667023B1 (ko) | 2016-06-14 | 2024-05-21 | 리제너론 파아마슈티컬스, 인크. | 항-c5 항체 및 이의 용도 |
| TWI610941B (zh) * | 2016-06-17 | 2018-01-11 | Chugai Seiyaku Kabushiki Kaisha | 抗c5抗體及使用方法 |
| EP3494991A4 (en) | 2016-08-05 | 2020-07-29 | Chugai Seiyaku Kabushiki Kaisha | COMPOSITION FOR THE PROPHYLAXIS OR TREATMENT OF IL-8 RELATED DISEASES |
| US20190328854A1 (en) * | 2016-08-29 | 2019-10-31 | The Cleveland Clinic Foundation | C5 immunization for autologous anti-c5 antibody production |
| WO2018109588A2 (en) * | 2016-12-16 | 2018-06-21 | Samsung Bioepis Co., Ltd | Stable aqueous anti-c5 antibody composition |
| WO2018139623A1 (en) | 2017-01-30 | 2018-08-02 | Chugai Seiyaku Kabushiki Kaisha | Anti-sclerostin antibodies and methods of use |
| TW202412841A (zh) * | 2017-01-31 | 2024-04-01 | 日商中外製藥股份有限公司 | 抗c5抗體在製造用於治療或預防c5相關疾病的醫藥組合物之用途 |
| US11578137B2 (en) * | 2017-03-06 | 2023-02-14 | The Trustees Of The University Of Pennsylvania | Anti-C5 antibodies and uses thereof |
| US11459382B2 (en) | 2017-05-22 | 2022-10-04 | Alexion Pharmaceuticals, Inc. | Dosage and administration of anti-C5 antibodies for treatment of protein-losing enteropathy in patients |
| PT3658184T (pt) * | 2017-07-27 | 2023-11-29 | Alexion Pharma Inc | Formulações de anticorpo anti-c5 de elevada concentração |
| EP3700928A1 (en) | 2017-10-26 | 2020-09-02 | Alexion Pharmaceuticals, Inc. | Dosage and administration of anti-c5 antibodies for treatment of paroxysmal nocturnal hemoglobinuria (pnh) and atypical hemolytic uremic syndrome (ahus) |
| JP7731196B2 (ja) * | 2017-11-14 | 2025-08-29 | 中外製薬株式会社 | 抗C1s抗体および使用方法 |
| EP3724226A1 (en) | 2017-12-13 | 2020-10-21 | Regeneron Pharmaceuticals, Inc. | Anti-c5 antibody combinations and uses thereof |
| AR115318A1 (es) | 2018-03-29 | 2020-12-23 | Genentech Inc | Modulación de la actividad lactogénica en células de mamífero |
| JP7165210B2 (ja) * | 2018-05-24 | 2022-11-02 | シグマ-アルドリッチ・カンパニー・リミテッド・ライアビリティ・カンパニー | タンパク質の定量分析 |
| JP7520725B2 (ja) | 2018-05-31 | 2024-07-23 | アレクシオン ファーマシューティカルズ, インコーポレイテッド | 小児患者における発作性夜間ヘモグロビン尿症(pnh)の治療のための抗c5抗体の用量および投与 |
| EP3802603A1 (en) | 2018-06-04 | 2021-04-14 | Alexion Pharmaceuticals, Inc. | Dosage and administration of anti-c5 antibodies for treatment of atypical hemolytic uremic syndrome (ahus) in pediatric patients |
| WO2020006266A1 (en) | 2018-06-28 | 2020-01-02 | Alexion Pharmaceuticals, Inc. | Methods of producing anti-c5 antibodies |
| SMT202400271T1 (it) * | 2018-08-01 | 2024-07-09 | Chugai Pharmaceutical Co Ltd | Composizione farmaceutica per l’uso nel trattamento o nella prevenzione di una patologia correlata a c5 |
| US12098190B2 (en) * | 2018-09-06 | 2024-09-24 | The Trustees Of The University Of Pennsylvania And | Humanized anti-C5 antibodies and uses thereof |
| US20220056115A1 (en) * | 2018-09-17 | 2022-02-24 | Kyoto University | Administration of an anti-c5 agent for treatment of hepatic injury or failure |
| US20200095307A1 (en) | 2018-09-21 | 2020-03-26 | Alexion Pharmaceuticals, Inc. | Compositions and methods for the treatment of neuromyelitis optica |
| EP4306128A3 (en) | 2018-10-30 | 2024-03-27 | Alexion Pharmaceuticals, Inc. | Subcutaneous dosage and administration of anti-c5 antibodies for treatment of paroxysmal nocturnal hemoglobinuria (pnh) |
| WO2020092546A1 (en) * | 2018-10-30 | 2020-05-07 | Alexion Pharmaceuticals, Inc. | Co-administration of a hyaluronidase and anti-c5 antibody for treatment of complement-associated conditions |
| KR20250016490A (ko) | 2019-01-25 | 2025-02-03 | 알렉시온 파마슈티칼스, 인코포레이티드 | 비정형 용혈성 요독증후군(ahus)의 치료를 위한 항-c5 항체의 복용량 및 투여 |
| CN113614106A (zh) | 2019-02-14 | 2021-11-05 | 亚力兄制药公司 | 抗c5抗体用于治疗全身型重症肌无力的剂量和施用 |
| WO2020213706A1 (en) * | 2019-04-19 | 2020-10-22 | Chugai Seiyaku Kabushiki Kaisha | Antibodies and compositions for use in detecting or capturing a polypeptide in a sample, and methods for detecting or capturing a polypeptide in a sample |
| BR112021019571A2 (pt) | 2019-04-19 | 2021-12-07 | Chugai Pharmaceutical Co Ltd | Receptor quimérico que reconhece o sítio de modificação do anticorpo |
| WO2020230834A1 (en) | 2019-05-15 | 2020-11-19 | Chugai Seiyaku Kabushiki Kaisha | An antigen-binding molecule, a pharmaceutical composition, and a method |
| US20220227851A1 (en) | 2019-05-24 | 2022-07-21 | Alexion Pharmaceuticals, Inc. | Methods of treating vitiligo using an anti-c5 antibody |
| TWI886140B (zh) | 2019-07-31 | 2025-06-11 | 瑞士商赫孚孟拉羅股份公司 | 藉由使用抗c5抗體克羅伐單抗(crovalimab)之治療或預防c5相關疾病之劑量及投藥療程 |
| CA3144921A1 (en) * | 2019-07-31 | 2021-02-04 | F. Hoffmann-La Roche Ag | Dosage and administration regimen for the treatment or prevention of c5-related diseases by the use of the anti-c5 antibody crovalimab |
| WO2021067526A1 (en) | 2019-10-02 | 2021-04-08 | Alexion Pharmaceuticals, Inc. | Complement inhibitors for treating drug-induced complement-mediated response |
| CN114867747A (zh) | 2019-12-09 | 2022-08-05 | 阿雷克森制药公司 | 用于治疗视神经脊髓炎谱系障碍的抗c5抗体 |
| US20230043576A1 (en) | 2019-12-23 | 2023-02-09 | Alexion Pharmaceuticals, Inc. | Methods of treating pregnancy-associated atypical hemolytic uremic syndrome using an anti-c5 antibody |
| CN111234016B (zh) * | 2020-02-23 | 2021-09-07 | 北京康普美特创新医药科技有限责任公司 | 一种抗补体c5分子的全人源单克隆抗体及应用 |
| CA3169908A1 (en) | 2020-03-26 | 2021-09-30 | Genentech, Inc. | Modified mammalian cells having reduced host cell proteins |
| KR20220161375A (ko) | 2020-03-31 | 2022-12-06 | 추가이 세이야쿠 가부시키가이샤 | 다중 특이성 항원 결합 분자를 제조하기 위한 방법 |
| CN113563467A (zh) * | 2020-04-28 | 2021-10-29 | 上海普铭生物科技有限公司 | 针对人补体蛋白c5的抗体及其应用 |
| US20230172930A1 (en) | 2020-05-12 | 2023-06-08 | Alexion Pharmaceuticals, Inc. | Use of complement factor d inhibitors alone or in combination with anti-c5 antibodies for treatment of paroxysmal nocturnal hemoglobinuria |
| CN115667925A (zh) | 2020-05-15 | 2023-01-31 | 阿雷克森制药公司 | 使用细胞外囊泡来检测补体激活的方法以及其用于评估和/或监测补体介导的疾病的治疗的用途 |
| BR112022024296A2 (pt) * | 2020-05-29 | 2023-04-25 | Amgen Inc | Formulações de anticorpos e seus usos |
| WO2021262329A1 (en) | 2020-06-24 | 2021-12-30 | Alexion Pharmaceuticals, Inc. | Subcutaneous (sc) administration of anti-c5 antibodies for treatment of complement-associated conditions |
| JP7674399B2 (ja) * | 2020-06-24 | 2025-05-09 | スタイドソン・(ベイジン)・バイオファーマシューティカルズ・カンパニー・リミテッド | C5aを特異的に認識する抗体およびその使用 |
| EP4172192A1 (en) | 2020-06-24 | 2023-05-03 | Genentech, Inc. | Apoptosis resistant cell lines |
| JP2023533030A (ja) * | 2020-07-09 | 2023-08-01 | アレクシオン ファーマシューティカルズ, インコーポレイテッド | 小児患者において発作性夜間血色素尿症(pnh)を治療するための抗c5抗体の投薬量及び投与 |
| KR20230047179A (ko) | 2020-08-13 | 2023-04-06 | 알렉시온 파마슈티칼스, 인코포레이티드 | 조혈 줄기세포 이식-연관 혈전성 미세혈관병증(hsct-tma)을 치료하기 위한 항-c5 항체의 복용량 및 투여 |
| CA3192344A1 (en) | 2020-08-28 | 2022-03-03 | Genentech, Inc. | Crispr/cas9 multiplex knockout of host cell proteins |
| EP4213940A1 (en) | 2020-09-21 | 2023-07-26 | Alexion Pharmaceuticals, Inc. | Dosage and administration of anti-c5 antibodies for treating c5-mediated glomerular nephritis (gn), including lupus nephritis (ln) and/or iga nephropathy (igan) |
| WO2022087339A1 (en) | 2020-10-23 | 2022-04-28 | Alexion Pharmaceuticals, Inc. | Methods of treating patients having complement disorders using anti-c5 antibodies |
| US20240092881A1 (en) | 2021-01-22 | 2024-03-21 | Alexion Pharmaceuticals, Inc. | Methods of treating complement mediated thrombotic microangiopathy using an anti-c5 antibody |
| CA3215965A1 (en) | 2021-04-19 | 2022-10-27 | Amy Shen | Modified mammalian cells |
| WO2022246259A1 (en) | 2021-05-21 | 2022-11-24 | Genentech, Inc. | Modified cells for the production of a recombinant product of interest |
| EP4155321A1 (en) | 2021-06-04 | 2023-03-29 | Chugai Seiyaku Kabushiki Kaisha | Anti-ddr2 antibodies and uses thereof |
| WO2022265915A1 (en) | 2021-06-14 | 2022-12-22 | Alexion Pharmaceuticals, Inc. | Dosage and administration of anti-c5 antibodies for treating dermatomyositis (dm) |
| US12448451B2 (en) | 2021-06-25 | 2025-10-21 | Chugai Seiyaku Kabushiki Kaisha | Anti-CTLA-4 antibody and use thereof |
| CR20240026A (es) * | 2021-06-25 | 2024-03-14 | Chugai Pharmaceutical Co Ltd | Anticuerpo anti-ctla-4 |
| WO2023287991A1 (en) | 2021-07-14 | 2023-01-19 | Alexion Pharmaceuticals, Inc. | Dosage and administration of anti-c5 antibodies for treatment of myasthenia gravis |
| WO2023023220A1 (en) | 2021-08-20 | 2023-02-23 | Alexion Pharmaceuticals, Inc. | Methods for treating sickle cell disease or beta thalassemia using a complement alternative pathway inhibitor |
| TW202404632A (zh) | 2022-04-04 | 2024-02-01 | 瑞士商赫孚孟拉羅股份公司 | 用於藉由使用抗c5抗體克羅伐單抗治療或預防格林-巴利症候群之劑量及投予方案 |
| TW202346339A (zh) | 2022-04-04 | 2023-12-01 | 瑞士商赫孚孟拉羅股份公司 | 藉由使用抗c5抗體克羅伐單抗之治療或預防格林-巴利症候群之劑量及投予方案 |
| CA3251727A1 (en) * | 2022-05-04 | 2023-11-09 | Alexion Pharmaceuticals, Inc. | COMPOSITIONS AND METHODS FOR THE TREATMENT OF A DISORDER ON THE SPECTRUM OF OPTICAL NEUROMYELITIS |
| EP4583911A1 (en) | 2022-09-06 | 2025-07-16 | Alexion Pharmaceuticals, Inc. | Diagnostic and prognostic biomarker profiles in patients with hematopoietic stem cell transplant-associated thrombotic microangiopathy (hsct-tma) |
| TW202426048A (zh) | 2022-09-06 | 2024-07-01 | 美商阿雷希昂製藥公司 | 用於治療造血幹細胞移植相關血栓性(hsct-tma)的抗c5抗體的補充劑量和投與 |
| TW202423479A (zh) | 2022-09-28 | 2024-06-16 | 美商阿雷希昂製藥公司 | 用於預防或最小化患有慢性腎病的患者中的心臟手術相關急性腎損傷(csa-aki)和/或隨後的主要不良腎事件(make)的抗c5抗體之劑量及投與 |
| WO2024238421A1 (en) | 2023-05-12 | 2024-11-21 | Alexion Pharmaceuticals, Inc. | Use of biomarkers for the identification and treatment of complement-mediated disorders |
| WO2024238422A1 (en) | 2023-05-12 | 2024-11-21 | Alexion Pharmaceuticals, Inc. | Use of a panel of lectins for detection of complement biomarkers in urine extracellular vesicles |
| WO2025006898A1 (en) * | 2023-06-29 | 2025-01-02 | Beam Therapeutics Inc. | Anti-idiotypic antibodies to cluster of differentiation 7-targeted binding domains and related compositions and methods |
| WO2025045250A1 (en) | 2023-09-03 | 2025-03-06 | Kira Pharmaceuticals (Us) Llc | Anti-human factor d antibody constructs and uses thereof |
| WO2025149667A1 (en) | 2024-01-12 | 2025-07-17 | Pheon Therapeutics Ltd | Antibody drug conjugates and uses thereof |
| WO2025166118A1 (en) | 2024-02-02 | 2025-08-07 | Alexion Pharmaceuticals, Inc. | Dosage and administration of anti-c5 antibodies for treating iga nephropathy (igan) |
| WO2025221479A1 (en) | 2024-04-16 | 2025-10-23 | Alexion Pharmaceuticals, Inc. | Biomarkers for monitoring effective treatment of neuromyelitis optica spectrum disorder (nmosd) with complement component c5 inhibitors |
Family Cites Families (276)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| JPS5144499B1 (cg-RX-API-DMAC7.html) | 1970-08-29 | 1976-11-29 | ||
| JPS5824836B2 (ja) | 1974-10-14 | 1983-05-24 | ノウミボウサイコウギヨウ カブシキガイシヤ | カサイナドノツウホウソウチ |
| US4769320A (en) | 1982-07-27 | 1988-09-06 | New England Medical Center Hospitals, Inc. | Immunoassay means and methods useful in human native prothrombin and human abnormal prothorombin determinations |
| CA1209907A (en) | 1982-04-12 | 1986-08-19 | Richard M. Bartholomew | Method of affinity purification employing monoclonal antibodies |
| US4689299A (en) | 1982-09-30 | 1987-08-25 | University Of Rochester | Human monoclonal antibodies against bacterial toxins |
| US4816567A (en) | 1983-04-08 | 1989-03-28 | Genentech, Inc. | Recombinant immunoglobin preparations |
| US4737456A (en) | 1985-05-09 | 1988-04-12 | Syntex (U.S.A.) Inc. | Reducing interference in ligand-receptor binding assays |
| US4676980A (en) | 1985-09-23 | 1987-06-30 | The United States Of America As Represented By The Secretary Of The Department Of Health And Human Services | Target specific cross-linked heteroantibodies |
| US6548640B1 (en) | 1986-03-27 | 2003-04-15 | Btg International Limited | Altered antibodies |
| JPS6350741A (ja) | 1986-08-20 | 1988-03-03 | Nippon Tectron Co Ltd | 蛍光偏光分析装置 |
| JPH06104071B2 (ja) | 1986-08-24 | 1994-12-21 | 財団法人化学及血清療法研究所 | 第▲ix▼因子コンホメ−シヨン特異性モノクロ−ナル抗体 |
| US4801687A (en) | 1986-10-27 | 1989-01-31 | Bioprobe International, Inc. | Monoclonal antibody purification process using protein A |
| 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. |
| US5004697A (en) | 1987-08-17 | 1991-04-02 | Univ. Of Ca | Cationized antibodies for delivery through the blood-brain barrier |
| US5606040A (en) | 1987-10-30 | 1997-02-25 | American Cyanamid Company | Antitumor and antibacterial substituted disulfide derivatives prepared from compounds possessing a methyl-trithio group |
| US5770701A (en) | 1987-10-30 | 1998-06-23 | American Cyanamid Company | Process for preparing targeted forms of methyltrithio antitumor agents |
| US5322678A (en) | 1988-02-17 | 1994-06-21 | Neorx Corporation | Alteration of pharmacokinetics of proteins by charge modification |
| US5750373A (en) | 1990-12-03 | 1998-05-12 | Genentech, Inc. | Enrichment method for variant proteins having altered binding properties, M13 phagemids, and growth hormone variants |
| ATE102631T1 (de) | 1988-11-11 | 1994-03-15 | Medical Res Council | Klonierung von immunglobulin sequenzen aus den variabelen domaenen. |
| US5530101A (en) | 1988-12-28 | 1996-06-25 | Protein Design Labs, Inc. | Humanized immunoglobulins |
| US5202253A (en) | 1988-12-30 | 1993-04-13 | Oklahoma Medical Research Foundation | Monoclonal antibody specific for protein C and antibody purification method |
| CA2006684C (en) | 1988-12-30 | 1996-12-17 | Charles T. Esmon | Monoclonal antibody against protein c |
| DE3920358A1 (de) | 1989-06-22 | 1991-01-17 | Behringwerke Ag | Bispezifische und oligospezifische, mono- und oligovalente antikoerperkonstrukte, ihre herstellung und verwendung |
| CA2026147C (en) | 1989-10-25 | 2006-02-07 | Ravi J. Chari | Cytotoxic agents comprising maytansinoids and their therapeutic use |
| US5208020A (en) | 1989-10-25 | 1993-05-04 | Immunogen Inc. | Cytotoxic agents comprising maytansinoids and their therapeutic use |
| US5959177A (en) | 1989-10-27 | 1999-09-28 | The Scripps Research Institute | Transgenic plants expressing assembled secretory antibodies |
| JPH0636741B2 (ja) | 1989-11-08 | 1994-05-18 | 帝人株式会社 | ヒト・プロテインcの分離方法 |
| US6150584A (en) | 1990-01-12 | 2000-11-21 | Abgenix, Inc. | Human antibodies derived from immunized xenomice |
| US6075181A (en) | 1990-01-12 | 2000-06-13 | Abgenix, Inc. | Human antibodies derived from immunized xenomice |
| CA2075927A1 (en) | 1990-02-16 | 1991-08-17 | Victor A. Raso | Hybrid reagents capable of selectively releasing molecules into cells |
| US5770429A (en) | 1990-08-29 | 1998-06-23 | Genpharm International, Inc. | Transgenic non-human animals capable of producing heterologous antibodies |
| US5571894A (en) | 1991-02-05 | 1996-11-05 | Ciba-Geigy Corporation | Recombinant antibodies specific for a growth factor receptor |
| ATE181575T1 (de) | 1991-04-25 | 1999-07-15 | Chugai Pharmaceutical Co Ltd | Rekombinierte humane antikörper gegen den humanen interleukin 6-rezeptor |
| DK0590058T3 (da) | 1991-06-14 | 2004-03-29 | Genentech Inc | Humaniseret heregulin-antistof |
| GB9114948D0 (en) | 1991-07-11 | 1991-08-28 | Pfizer Ltd | Process for preparing sertraline intermediates |
| WO1993006217A1 (en) | 1991-09-19 | 1993-04-01 | Genentech, Inc. | EXPRESSION IN E. COLI OF ANTIBODY FRAGMENTS HAVING AT LEAST A CYSTEINE PRESENT AS A FREE THIOL, USE FOR THE PRODUCTION OF BIFUNCTIONAL F(ab')2 ANTIBODIES |
| FI941572A7 (fi) | 1991-10-07 | 1994-05-27 | Oncologix Inc | Anti-erbB-2-monoklonaalisten vasta-aineiden yhdistelmä ja käyttömenete lmä |
| WO1993008829A1 (en) | 1991-11-04 | 1993-05-13 | The Regents Of The University Of California | Compositions that mediate killing of hiv-infected cells |
| ATE295420T1 (de) | 1992-02-06 | 2005-05-15 | Chiron Corp | Marker für krebs und biosynthetisches bindeprotein dafür |
| GB9203459D0 (en) | 1992-02-19 | 1992-04-08 | Scotgen Ltd | Antibodies with germ-line variable regions |
| US5639641A (en) | 1992-09-09 | 1997-06-17 | Immunogen Inc. | Resurfacing of rodent antibodies |
| DK0752248T3 (da) | 1992-11-13 | 2000-11-13 | Idec Pharma Corp | Terapeutisk anvendelse af kimæriske og radioaktivt mærkede antistoffer mod humant B-lymfocytbegrænset differentieringsantig |
| US5635483A (en) | 1992-12-03 | 1997-06-03 | Arizona Board Of Regents Acting On Behalf Of Arizona State University | Tumor inhibiting tetrapeptide bearing modified phenethyl amides |
| US5780588A (en) | 1993-01-26 | 1998-07-14 | Arizona Board Of Regents | Elucidation and synthesis of selected pentapeptides |
| CA2162497A1 (en) | 1993-06-10 | 1994-12-22 | Sheila Connelly | Adenoviral vectors for treatment of hemophilia |
| CA2163345A1 (en) | 1993-06-16 | 1994-12-22 | Susan Adrienne Morgan | Antibodies |
| WO1996011020A1 (en) | 1994-10-07 | 1996-04-18 | Chugai Seiyaku Kabushiki Kaisha | Rheumatoid arthritis remedy containing il-6 antagonist as active ingredient |
| IL107742A0 (en) | 1993-11-24 | 1994-02-27 | Yeda Res & Dev | Chemically-modified binding proteins |
| US6074642A (en) | 1994-05-02 | 2000-06-13 | Alexion Pharmaceuticals, Inc. | Use of antibodies specific to human complement component C5 for the treatment of glomerulonephritis |
| US5773001A (en) | 1994-06-03 | 1998-06-30 | American Cyanamid Company | Conjugates of methyltrithio antitumor agents and intermediates for their synthesis |
| US6309636B1 (en) | 1995-09-14 | 2001-10-30 | Cancer Research Institute Of Contra Costa | Recombinant peptides derived from the Mc3 anti-BA46 antibody, methods of use thereof, and methods of humanizing antibody peptides |
| DE4436561C1 (de) | 1994-10-13 | 1996-03-14 | Deutsche Spezialglas Ag | Verfahren zur Veränderung der Durchbiegung von anodisch gebondeten flächigen Verbundkörpern aus Glas und Metall oder Halbleitermaterialien |
| CN100350973C (zh) | 1994-10-21 | 2007-11-28 | 岸本忠三 | 用于治疗il-6产生所致疾病的药物组合物 |
| US5789199A (en) | 1994-11-03 | 1998-08-04 | Genentech, Inc. | Process for bacterial production of polypeptides |
| US6485943B2 (en) | 1995-01-17 | 2002-11-26 | The University Of Chicago | Method for altering antibody light chain interactions |
| US5731168A (en) | 1995-03-01 | 1998-03-24 | Genentech, Inc. | Method for making heteromultimeric polypeptides |
| US5840523A (en) | 1995-03-01 | 1998-11-24 | Genetech, Inc. | Methods and compositions for secretion of heterologous polypeptides |
| US5869046A (en) | 1995-04-14 | 1999-02-09 | Genentech, Inc. | Altered polypeptides with increased half-life |
| US5712374A (en) | 1995-06-07 | 1998-01-27 | American Cyanamid Company | Method for the preparation of substantiallly monomeric calicheamicin derivative/carrier conjugates |
| US5714586A (en) | 1995-06-07 | 1998-02-03 | American Cyanamid Company | Methods for the preparation of monomeric calicheamicin derivative/carrier conjugates |
| US5830478A (en) | 1995-06-07 | 1998-11-03 | Boston Biomedical Research Institute | Method for delivering functional domains of diphtheria toxin to a cellular target |
| US6267958B1 (en) | 1995-07-27 | 2001-07-31 | Genentech, Inc. | Protein formulation |
| US5783186A (en) | 1995-12-05 | 1998-07-21 | Amgen Inc. | Antibody-induced apoptosis |
| GB9603256D0 (en) | 1996-02-16 | 1996-04-17 | Wellcome Found | Antibodies |
| IL127872A0 (en) | 1996-07-19 | 1999-10-28 | Amgen Inc | Analogs of cationic proteins |
| US5990286A (en) | 1996-12-18 | 1999-11-23 | Techniclone, Inc. | Antibodies with reduced net positive charge |
| US6277375B1 (en) | 1997-03-03 | 2001-08-21 | Board Of Regents, The University Of Texas System | Immunoglobulin-like domains with increased half-lives |
| US6884879B1 (en) | 1997-04-07 | 2005-04-26 | Genentech, Inc. | Anti-VEGF antibodies |
| US7365166B2 (en) | 1997-04-07 | 2008-04-29 | Genentech, Inc. | Anti-VEGF antibodies |
| AU7132798A (en) | 1997-04-17 | 1998-11-11 | Amgen, Inc. | Compositions comprising conjugates of stable, active, human ob protein with antibody fc chain and methods |
| US6171586B1 (en) | 1997-06-13 | 2001-01-09 | Genentech, Inc. | Antibody formulation |
| ATE296315T1 (de) | 1997-06-24 | 2005-06-15 | Genentech Inc | Galactosylierte glykoproteine enthaltende zusammensetzungen und verfahren zur deren herstellung |
| US6040498A (en) | 1998-08-11 | 2000-03-21 | North Caroline State University | Genetically engineered duckweed |
| ATE373712T1 (de) | 1997-10-03 | 2007-10-15 | Chugai Pharmaceutical Co Ltd | Natürlicher menschlicher antikörper |
| AU759779B2 (en) | 1997-10-31 | 2003-05-01 | Genentech Inc. | Methods and compositions comprising glycoprotein glycoforms |
| US6610833B1 (en) | 1997-11-24 | 2003-08-26 | The Institute For Human Genetics And Biochemistry | Monoclonal human natural antibodies |
| AU760562B2 (en) | 1997-12-05 | 2003-05-15 | Scripps Research Institute, The | Humanization of murine antibody |
| US6194551B1 (en) | 1998-04-02 | 2001-02-27 | Genentech, Inc. | Polypeptide variants |
| IL138608A0 (en) | 1998-04-02 | 2001-10-31 | Genentech Inc | Antibody variants and fragments thereof |
| KR20010042435A (ko) | 1998-04-03 | 2001-05-25 | 나가야마 오사무 | 인간조직인자(티에프)에 대한 인간형화항체 및인간형화항체의 제조방법 |
| PT1071700E (pt) | 1998-04-20 | 2010-04-23 | Glycart Biotechnology Ag | Modificação por glicosilação de anticorpos para melhorar a citotoxicidade celular dependente de anticorpos |
| GB9809951D0 (en) | 1998-05-08 | 1998-07-08 | Univ Cambridge Tech | Binding molecules |
| WO2000009560A2 (en) | 1998-08-17 | 2000-02-24 | Abgenix, Inc. | Generation of modified molecules with increased serum half-lives |
| US6475718B2 (en) | 1998-09-08 | 2002-11-05 | Schering Aktiengesellschaft | Methods and compositions for modulating the interaction between the APJ receptor and the HIV virus |
| KR100483494B1 (ko) | 1998-12-01 | 2005-04-15 | 프로테인 디자인 랩스 인코포레이티드 | 감마 인터페론에 대한 인간화 항체 |
| PL220113B1 (pl) | 1999-01-15 | 2015-08-31 | Genentech Inc | Wariant macierzystego polipeptydu zawierającego region Fc, polipeptyd zawierający wariant regionu Fc o zmienionym powinowactwie wiązania receptora Fc gamma (FcγR), polipeptyd zawierający wariant regionu Fc o zmienionym powinowactwie wiązania noworodkowego receptora Fc (FcRn), kompozycja, wyizolowany kwas nukleinowy, wektor, komórka gospodarza, sposób otrzymywania wariantu polipeptydu, zastosowanie wariantu polipeptydu i sposób otrzymywania wariantu regionu Fc |
| US6737056B1 (en) | 1999-01-15 | 2004-05-18 | Genentech, Inc. | Polypeptide variants with altered effector function |
| US6972125B2 (en) | 1999-02-12 | 2005-12-06 | Genetics Institute, Llc | Humanized immunoglobulin reactive with B7-2 and methods of treatment therewith |
| EP2278003B2 (en) | 1999-04-09 | 2020-08-05 | Kyowa Kirin Co., Ltd. | Method for controlling the activity of immunologically functional molecule |
| SK782002A3 (en) | 1999-07-21 | 2003-08-05 | Lexigen Pharm Corp | FC fusion proteins for enhancing the immunogenicity of protein and peptide antigens |
| US7125978B1 (en) | 1999-10-04 | 2006-10-24 | Medicago Inc. | Promoter for regulating expression of foreign genes |
| MXPA02003456A (es) | 1999-10-04 | 2002-10-23 | Medicago Inc | Metodo para regular la transcripcion de genes foraneos. |
| AU7950400A (en) | 1999-10-19 | 2001-04-30 | Kyowa Hakko Kogyo Co. Ltd. | Process for producing polypeptide |
| SE9903895D0 (sv) | 1999-10-28 | 1999-10-28 | Active Biotech Ab | Novel compounds |
| WO2001044463A1 (en) | 1999-12-15 | 2001-06-21 | Genentech, Inc. | Shotgun scanning, a combinatorial method for mapping functional protein epitopes |
| NZ518764A (en) | 1999-12-29 | 2004-02-27 | Immunogen Inc | Cytotoxic agents comprising modified doxorubicins and daunorubicins and their therapeutic use |
| EP1272647B1 (en) | 2000-04-11 | 2014-11-12 | Genentech, Inc. | Multivalent antibodies and uses therefor |
| AU2001266272B2 (en) | 2000-05-03 | 2005-09-15 | Medigene Ag | Cationic diagnostic, imaging and therapeutic agents associated with activated vascular sites |
| WO2002002641A1 (en) | 2000-06-16 | 2002-01-10 | Human Genome Sciences, Inc. | Antibodies that immunospecifically bind to blys |
| US7064191B2 (en) | 2000-10-06 | 2006-06-20 | Kyowa Hakko Kogyo Co., Ltd. | Process for purifying antibody |
| EA013563B1 (ru) | 2000-10-06 | 2010-06-30 | Киова Хакко Кирин Ко., Лтд. | Трансгенное животное, продуцирующее антитела с измененными углеводными цепями, способ получения антител и содержащее антитела лекарственное средство |
| US6946292B2 (en) | 2000-10-06 | 2005-09-20 | Kyowa Hakko Kogyo Co., Ltd. | Cells producing antibody compositions with increased antibody dependent cytotoxic activity |
| PT1325033E (pt) | 2000-10-10 | 2010-04-15 | Genentech Inc | Inibição da activação do complemento c5 para o tratamento e a prevenção da rejeição diferida de um xenoenxertos ou de uma rejeição vascular aguda |
| US6596541B2 (en) | 2000-10-31 | 2003-07-22 | Regeneron Pharmaceuticals, Inc. | Methods of modifying eukaryotic cells |
| MXPA03004793A (es) | 2000-11-30 | 2004-12-03 | Medarex Inc | Roedores transgenicos transcromosomales para elaborar anticuerpos humnanos. |
| PT1355919E (pt) | 2000-12-12 | 2011-03-02 | Medimmune Llc | Moléculas com semivida longa, composições que as contêm e suas utilizações |
| KR100927670B1 (ko) | 2001-04-13 | 2009-11-20 | 바이오겐 아이덱 엠에이 인코포레이티드 | Vla-1에 대한 항체들 |
| US7667004B2 (en) | 2001-04-17 | 2010-02-23 | Abmaxis, Inc. | Humanized antibodies against vascular endothelial growth factor |
| PT2208784E (pt) | 2001-06-22 | 2013-04-03 | Chugai Pharmaceutical Co Ltd | Inibidores da proliferação celular contendo um anticorpo anti-glipicano 3 |
| US20040161741A1 (en) | 2001-06-30 | 2004-08-19 | Elazar Rabani | Novel compositions and processes for analyte detection, quantification and amplification |
| HUP0700103A3 (en) | 2001-08-03 | 2012-09-28 | Glycart Biotechnology Ag | Antibody glycosylation variants having increased antibody-dependent cellular cytotoxicity |
| ATE360441T1 (de) | 2001-08-17 | 2007-05-15 | Tanox Inc | Komplement-inhibitoren die an c5 und c5a binden ohne die bildung von c5b zu hemmen |
| US20030049203A1 (en) | 2001-08-31 | 2003-03-13 | Elmaleh David R. | Targeted nucleic acid constructs and uses related thereto |
| US7320789B2 (en) | 2001-09-26 | 2008-01-22 | Wyeth | Antibody inhibitors of GDF-8 and uses thereof |
| JP2005532253A (ja) | 2001-10-25 | 2005-10-27 | ジェネンテック・インコーポレーテッド | 糖タンパク質組成物 |
| RU2318829C2 (ru) | 2001-11-14 | 2008-03-10 | Сентокор, Инк. | Антитела против il-6, композиции, способы и применение |
| US20040093621A1 (en) | 2001-12-25 | 2004-05-13 | Kyowa Hakko Kogyo Co., Ltd | Antibody composition which specifically binds to CD20 |
| US6684637B2 (en) | 2002-01-25 | 2004-02-03 | Sunpower, Inc. | Parallel slot heat exchanger |
| US20030224397A1 (en) | 2002-02-11 | 2003-12-04 | Genentech, Inc. | Antibody variants with faster antigen association rates |
| AR038568A1 (es) | 2002-02-20 | 2005-01-19 | Hoffmann La Roche | Anticuerpos anti-a beta y su uso |
| US20040110226A1 (en) * | 2002-03-01 | 2004-06-10 | Xencor | Antibody optimization |
| KR20050000380A (ko) | 2002-04-09 | 2005-01-03 | 교와 핫꼬 고교 가부시끼가이샤 | 게놈이 개변된 세포 |
| AU2003236018A1 (en) | 2002-04-09 | 2003-10-20 | Kyowa Hakko Kirin Co., Ltd. | METHOD OF ENHANCING ACTIVITY OF ANTIBODY COMPOSITION OF BINDING TO FcGamma RECEPTOR IIIa |
| AU2003236019A1 (en) | 2002-04-09 | 2003-10-20 | Kyowa Hakko Kirin Co., Ltd. | Drug containing antibody composition appropriate for patient suffering from Fc Gamma RIIIa polymorphism |
| EP1498490A4 (en) | 2002-04-09 | 2006-11-29 | Kyowa Hakko Kogyo Kk | PROCESS FOR PRODUCING ANTIBODY COMPOSITION |
| ATE503829T1 (de) | 2002-04-09 | 2011-04-15 | Kyowa Hakko Kirin Co Ltd | Zelle mit erniedrigter oder deletierter aktivität eines am gdp-fucosetransport beteiligten proteins |
| JPWO2003084569A1 (ja) | 2002-04-09 | 2005-08-11 | 協和醗酵工業株式会社 | 抗体組成物含有医薬 |
| EP1513879B1 (en) | 2002-06-03 | 2018-08-22 | Genentech, Inc. | Synthetic antibody phage libraries |
| WO2003105757A2 (en) | 2002-06-12 | 2003-12-24 | Genencor International, Inc. | Methods and compositions for milieu-dependent binding of a targeted agent to a target |
| WO2003107009A2 (en) | 2002-06-12 | 2003-12-24 | Genencor International, Inc. | Methods for improving a binding characteristic of a molecule |
| ITMI20021527A1 (it) | 2002-07-11 | 2004-01-12 | Consiglio Nazionale Ricerche | Anticorpi anti componente c5 del complemento e loro uso |
| EP1539947A4 (en) | 2002-08-15 | 2006-09-06 | Epitomics Inc | HUMANIZED RABBIT ANTIBODIES |
| US7361740B2 (en) | 2002-10-15 | 2008-04-22 | Pdl Biopharma, Inc. | Alteration of FcRn binding affinities or serum half-lives of antibodies by mutagenesis |
| EP1944320A1 (en) | 2002-12-16 | 2008-07-16 | Genentech, Inc. | Immunoglobulin variants and uses thereof |
| EP1585767A2 (en) | 2003-01-16 | 2005-10-19 | Genentech, Inc. | Synthetic antibody phage libraries |
| JP2006517109A (ja) | 2003-02-07 | 2006-07-20 | プロテイン デザイン ラブス インコーポレイテッド | アンフィレグリン抗体ならびに癌および乾癬を処置するためのその使用 |
| ES2395126T3 (es) | 2003-02-28 | 2013-02-08 | Agenus Inc. | Uso de lectinas para promover la oligomerización de glicoproteínas y de moléculas antigénicas |
| PT1601697E (pt) | 2003-02-28 | 2007-09-04 | Lonza Biologics Plc | Purificação de anticorpos através de proteína a e cromatografia de troca iónica. |
| US7871607B2 (en) | 2003-03-05 | 2011-01-18 | Halozyme, Inc. | Soluble glycosaminoglycanases and methods of preparing and using soluble glycosaminoglycanases |
| US20060104968A1 (en) | 2003-03-05 | 2006-05-18 | Halozyme, Inc. | Soluble glycosaminoglycanases and methods of preparing and using soluble glycosaminogly ycanases |
| GB2401040A (en) | 2003-04-28 | 2004-11-03 | Chugai Pharmaceutical Co Ltd | Method for treating interleukin-6 related diseases |
| WO2005005462A2 (en) | 2003-06-05 | 2005-01-20 | Genentech, Inc. | Blys antagonists and uses thereof |
| AU2004273791A1 (en) | 2003-09-05 | 2005-03-31 | Genentech, Inc. | Antibodies with altered effector functions |
| JPWO2005035586A1 (ja) | 2003-10-08 | 2007-11-22 | 協和醗酵工業株式会社 | 融合蛋白質組成物 |
| JPWO2005035778A1 (ja) | 2003-10-09 | 2006-12-21 | 協和醗酵工業株式会社 | α1,6−フコシルトランスフェラーゼの機能を抑制するRNAを用いた抗体組成物の製造法 |
| WO2005035753A1 (ja) | 2003-10-10 | 2005-04-21 | Chugai Seiyaku Kabushiki Kaisha | 機能蛋白質を代替する二重特異性抗体 |
| SI1689777T1 (sl) | 2003-11-05 | 2007-08-31 | Ares Trading Sa | Postopek za äśiĺ äśenje il-18 vezavnega proteina |
| ME01775B (me) | 2003-11-05 | 2011-02-28 | Glycart Biotechnology Ag | Cd20 antitijela sa povećanim afinitetom vezivanja za fc receptor i efektornom funkcijom |
| KR101438983B1 (ko) | 2003-11-06 | 2014-09-05 | 시애틀 지네틱스, 인크. | 리간드에 접합될 수 있는 모노메틸발린 화합물 |
| CA2545603A1 (en) | 2003-11-12 | 2005-05-26 | Biogen Idec Ma Inc. | Neonatal fc receptor (fcrn)-binding polypeptide variants, dimeric fc binding proteins and methods related thereto |
| JPWO2005053742A1 (ja) | 2003-12-04 | 2007-06-28 | 協和醗酵工業株式会社 | 抗体組成物を含有する医薬 |
| PL2418220T3 (pl) | 2003-12-10 | 2017-12-29 | E. R. Squibb & Sons, L.L.C. | Przeciwciała przeciwko interferonowi alfa i ich zastosowania |
| MX350383B (es) | 2004-01-09 | 2017-09-04 | Pfizer | Anticuerpos contra madcam. |
| US20050169921A1 (en) | 2004-02-03 | 2005-08-04 | Leonard Bell | Method of treating hemolytic disease |
| US20070116710A1 (en) | 2004-02-03 | 2007-05-24 | Leonard Bell | Methods of treating hemolytic anemia |
| WO2005080429A2 (en) | 2004-02-11 | 2005-09-01 | Warner-Lambert Company Llc | Methods of treating osteoarthritis with anti-il-6 or anti-il6 receptor antibodies |
| EP1737890A2 (en) | 2004-03-24 | 2007-01-03 | Xencor, Inc. | Immunoglobulin variants outside the fc region |
| US20050260711A1 (en) | 2004-03-30 | 2005-11-24 | Deepshikha Datta | Modulating pH-sensitive binding using non-natural amino acids |
| WO2005097832A2 (en) | 2004-03-31 | 2005-10-20 | Genentech, Inc. | Humanized anti-tgf-beta antibodies |
| US7785903B2 (en) | 2004-04-09 | 2010-08-31 | Genentech, Inc. | Variable domain library and uses |
| EP2374817B1 (en) | 2004-04-13 | 2017-09-06 | F. Hoffmann-La Roche AG | Anti-P-selectin antibodies |
| WO2005112564A2 (en) | 2004-04-15 | 2005-12-01 | The Government Of The United States Of America As Represented By The Secretary Of The Department Of Health And Human Services | Germline and sequence variants of humanized antibodies and methods of making and using them |
| KR100620554B1 (ko) | 2004-06-05 | 2006-09-06 | 한국생명공학연구원 | Tag-72에 대한 인간화 항체 |
| AR049390A1 (es) | 2004-06-09 | 2006-07-26 | Wyeth Corp | Anticuerpos contra la interleuquina-13 humana y usos de los mismos |
| CN102532321B (zh) | 2004-06-18 | 2018-10-12 | Ambrx公司 | 新颖抗原结合多肽和其用途 |
| CA2572133A1 (en) | 2004-06-25 | 2006-01-12 | Medimmune, Inc. | Increasing the production of recombinant antibodies in mammalian cells by site-directed mutagenesis |
| 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 |
| US7572456B2 (en) | 2004-09-13 | 2009-08-11 | Macrogenics, Inc. | Humanized antibodies against West Nile Virus and therapeutic and prophylactic uses thereof |
| AU2005284006A1 (en) | 2004-09-14 | 2006-03-23 | Health Protection Agency | Vaccine |
| US7563443B2 (en) | 2004-09-17 | 2009-07-21 | Domantis Limited | Monovalent anti-CD40L antibody polypeptides and compositions thereof |
| TWI380996B (zh) | 2004-09-17 | 2013-01-01 | Hoffmann La Roche | 抗ox40l抗體 |
| CN104447992A (zh) | 2004-09-23 | 2015-03-25 | 健泰科生物技术公司 | 半胱氨酸改造的抗体和偶联物 |
| JO3000B1 (ar) | 2004-10-20 | 2016-09-05 | Genentech Inc | مركبات أجسام مضادة . |
| US7462697B2 (en) | 2004-11-08 | 2008-12-09 | Epitomics, Inc. | Methods for antibody engineering |
| US20070135620A1 (en) | 2004-11-12 | 2007-06-14 | Xencor, Inc. | Fc variants with altered binding to FcRn |
| EP1829961A4 (en) | 2004-12-22 | 2008-06-04 | Chugai Pharmaceutical Co Ltd | PROCESS FOR PREPARING ANTIBODY USING A CELL WHOSE FUCOSE CARRIER FUNCTION IS INHIBITED |
| MX2007007703A (es) | 2004-12-23 | 2007-08-14 | Novo Nordisk As | Ligandos de afinidad de union a anticuerpos. |
| GB0502358D0 (en) | 2005-02-04 | 2005-03-16 | Novartis Ag | Organic compounds |
| EP3623473A1 (en) | 2005-03-31 | 2020-03-18 | Chugai Seiyaku Kabushiki Kaisha | Process for production of polypeptide by regulation of assembly |
| TW200714313A (en) | 2005-04-08 | 2007-04-16 | Chugai Pharmaceutical Co Ltd | Antibodies that substitute for coagulation factor VIII |
| AU2006244445B2 (en) | 2005-05-05 | 2013-04-18 | Duke University | Anti-CD19 antibody therapy for autoimmune disease |
| AU2006283725B2 (en) | 2005-08-19 | 2012-02-16 | The Trustees Of The University Of Pennsylvania | Antagonist antibodies against GDF-8 and uses in treatment of ALS and other GDF-8-associated disorders |
| EP2465870A1 (en) | 2005-11-07 | 2012-06-20 | Genentech, Inc. | Binding polypeptides with diversified and consensus VH/VL hypervariable sequences |
| WO2007060411A1 (en) | 2005-11-24 | 2007-05-31 | Ucb Pharma S.A. | Anti-tnf alpha antibodies which selectively inhibit tnf alpha signalling through the p55r |
| JP2009517404A (ja) | 2005-11-28 | 2009-04-30 | メディミューン,エルエルシー | Hmgb1および/またはrageのアンタゴニストならびにその使用方法 |
| EP1973951A2 (en) | 2005-12-02 | 2008-10-01 | Genentech, Inc. | Binding polypeptides with restricted diversity sequences |
| RU2440824C2 (ru) | 2005-12-12 | 2012-01-27 | Ац Иммуне Са | Терапевтическая вакцина |
| DK3219328T3 (da) | 2005-12-29 | 2020-07-13 | Janssen Biotech Inc | Humane anti-il-23-antistoffer, sammensætninger, fremgangsmåder og anvendelser |
| JP5722524B2 (ja) | 2006-03-02 | 2015-05-20 | アレクシオン ファーマシューティカルズ, インコーポレイテッド | 補体活性を抑制することによる同種移植片の生存の延長 |
| CN104623692A (zh) | 2006-03-08 | 2015-05-20 | 阿切埃米克斯股份有限公司 | 治疗视觉失调中使用的补体结合适体和抗-c5药物 |
| AU2007225044C1 (en) | 2006-03-15 | 2018-03-29 | Alexion Pharmaceuticals, Inc. | Treatment of paroxysmal nocturnal hemoglobinuria patients by an inhibitor of complement |
| EP2009101B1 (en) | 2006-03-31 | 2017-10-25 | Chugai Seiyaku Kabushiki Kaisha | Antibody modification method for purifying bispecific antibody |
| KR101463631B1 (ko) | 2006-03-31 | 2014-11-19 | 추가이 세이야쿠 가부시키가이샤 | 항체의 혈중 동태를 제어하는 방법 |
| EP2738178A1 (en) | 2006-04-05 | 2014-06-04 | AbbVie Biotechnology Ltd | Antibody purification |
| TW200812616A (en) | 2006-05-09 | 2008-03-16 | Genentech Inc | Binding polypeptides with optimized scaffolds |
| EP2047863B1 (en) | 2006-06-08 | 2013-07-31 | Chugai Seiyaku Kabushiki Kaisha | Preventive or remedy for inflammatory disease |
| EP2059533B1 (en) | 2006-08-30 | 2012-11-14 | Genentech, Inc. | Multispecific antibodies |
| US8236313B2 (en) | 2006-10-06 | 2012-08-07 | The United States Of America, As Represented By The Secretary Of The Department Of Health And Human Services | Prevention of tissue ischemia, related methods and compositions |
| US20100034194A1 (en) | 2006-10-11 | 2010-02-11 | Siemens Communications Inc. | Eliminating unreachable subscribers in voice-over-ip networks |
| US20080226635A1 (en) | 2006-12-22 | 2008-09-18 | Hans Koll | Antibodies against insulin-like growth factor I receptor and uses thereof |
| CN101679486A (zh) | 2007-03-22 | 2010-03-24 | 诺瓦提斯公司 | C5抗原及其用途 |
| 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 |
| EP3543691A1 (en) | 2007-06-29 | 2019-09-25 | Quest Diagnostics Investments Incorporated | Analysis of amino acids in body fluid by liquid chromatography-mass spectrometry |
| PH12021552811A1 (en) | 2007-09-26 | 2022-11-21 | Chugai Pharmaceutical Co Ltd | Modified antibody constant region |
| MX2010003329A (es) | 2007-09-26 | 2010-04-27 | Chugai Pharmaceutical Co Ltd | Anticuerpo anti-receptor de il-6. |
| RU2510400C9 (ru) | 2007-09-26 | 2014-07-20 | Чугаи Сейяку Кабусики Кайся | Способ модификации изоэлектрической точки антитела с помощью аминокислотных замен в cdr |
| CL2008002873A1 (es) | 2007-09-28 | 2010-02-19 | Chugai Pharmaceutical Co Ltd | Anticuerpo anti-glipican 3/gpc3; composicion que lo comprende; agente anti-canceroso que lo comprende; acido nucleico que codifica dicho anticuerpo; celula hospedera aislada que comprende dicho acido nucleico; metodo para la preparacion de dicho anticuerpo |
| EP2261254A3 (en) | 2007-12-21 | 2011-04-13 | Amgen, Inc | Anti-amyloid antibodies and uses thereof |
| DK2235064T3 (en) | 2008-01-07 | 2016-01-11 | Amgen Inc | A process for the preparation of heterodimeric Fc molecules using electrostatic control effects |
| US20110111406A1 (en) | 2008-04-11 | 2011-05-12 | Chugai Seiyaku Kabushiki Kaisha | Antigen-binding molecule capable of binding to two or more antigen molecules repeatedly |
| WO2009139822A1 (en) | 2008-05-01 | 2009-11-19 | Amgen Inc. | Anti-hepcidin antibodies and methods of use |
| WO2009152354A1 (en) | 2008-06-14 | 2009-12-17 | Vytronus, Inc. | System and method for delivering energy to tissue |
| PL2328616T3 (pl) | 2008-08-05 | 2015-10-30 | Novartis Ag | Kompozycje i sposoby dla przeciwciał celujących białko dopełniacza C5 |
| TWI440469B (zh) | 2008-09-26 | 2014-06-11 | Chugai Pharmaceutical Co Ltd | Improved antibody molecules |
| BRPI0921237A2 (pt) | 2008-11-10 | 2015-09-22 | Alexion Pharma Inc | métodos e composições para o tratamento de distúrbios associados ao complemento |
| US20100292443A1 (en) | 2009-02-26 | 2010-11-18 | Sabbadini Roger A | Humanized platelet activating factor antibody design using anti-lipid antibody templates |
| CN102597005A (zh) | 2009-06-23 | 2012-07-18 | 阿雷克森制药公司 | 与补体蛋白质结合的双特异性抗体 |
| CN101875696B (zh) * | 2009-11-11 | 2012-02-08 | 中国人民解放军军事医学科学院生物工程研究所 | 一种抗体及其制备方法与应用 |
| EP2327725A1 (en) | 2009-11-26 | 2011-06-01 | InflaRx GmbH | Anti-C5a binding moieties with high blocking activity |
| CN102971342B (zh) | 2010-01-28 | 2016-08-03 | Ab生物科学公司 | 亲和力降低的新抗体和制备所述抗体的方法 |
| EP2542255B1 (en) * | 2010-03-01 | 2016-11-16 | Alexion Pharmaceuticals, Inc. | Compositions for treating degos' disease |
| TW201206466A (en) * | 2010-03-11 | 2012-02-16 | Rinat Neuroscience Corp | Antibodies with pH dependent antigen binding |
| SG183867A1 (en) | 2010-03-11 | 2012-10-30 | Rinat Neuroscience Corp | ANTIBODIES WITH pH DEPENDENT ANTIGEN BINDING |
| TWI667346B (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 |
| KR20130098161A (ko) | 2010-04-30 | 2013-09-04 | 알렉시온 파마슈티칼스, 인코포레이티드 | 인간에서 감소된 면역원성을 갖는 항체 |
| WO2012073992A1 (ja) | 2010-11-30 | 2012-06-07 | 中外製薬株式会社 | 複数分子の抗原に繰り返し結合する抗原結合分子 |
| CA2822288A1 (en) | 2010-12-22 | 2012-06-28 | Medimmune, Llc | Anti-c5/c5a/c5adesr antibodies and fragments |
| EP2679681B2 (en) | 2011-02-25 | 2023-11-15 | Chugai Seiyaku Kabushiki Kaisha | FcgammaRIIB-specific FC antibody |
| CA2836857C (en) | 2011-05-21 | 2019-12-03 | Macrogenics, Inc. | Cd3-binding molecules capable of binding to human and non-human cd3 |
| CN103826659A (zh) * | 2011-06-20 | 2014-05-28 | 圣路易斯大学 | 用于治疗的靶向神经肌肉接头 |
| 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 |
| TW201817744A (zh) | 2011-09-30 | 2018-05-16 | 日商中外製藥股份有限公司 | 具有促進抗原清除之FcRn結合域的治療性抗原結合分子 |
| US20150299313A1 (en) | 2011-10-05 | 2015-10-22 | Chugai Seiyaku Kabushiki Kaisha | Antigen-binding molecule for promoting clearance from plasma of antigen comprising suger chain receptor-binding domain |
| KR20230143201A (ko) | 2011-11-30 | 2023-10-11 | 추가이 세이야쿠 가부시키가이샤 | 면역 복합체를 형성하는 세포내로의 운반체(캐리어)를 포함하는 의약 |
| TWI682939B (zh) | 2012-02-24 | 2020-01-21 | 日商中外製藥股份有限公司 | 經FcγRIIB促進抗原消失之抗原結合分子 |
| RU2644684C2 (ru) * | 2012-03-16 | 2018-02-13 | Регенерон Фармасьютикалз, Инк. | Антитела со встроенным в легкие цепи гистидином и генетически модифицированные отличные от человека животные для их получения |
| HUE045537T2 (hu) | 2012-03-16 | 2019-12-30 | Regeneron Pharma | PH-érzékeny immunglobulin-szekvenciákat expresszáló rágcsálók |
| US9453076B2 (en) * | 2012-03-29 | 2016-09-27 | Novimmune S.A. | Anti-TLR4 antibodies and uses thereof |
| TWI619729B (zh) * | 2012-04-02 | 2018-04-01 | 再生元醫藥公司 | 抗-hla-b*27抗體及其用途 |
| ES2856272T3 (es) | 2012-05-30 | 2021-09-27 | Chugai Pharmaceutical Co Ltd | Molécula de unión a antígenos para eliminar antígenos agregados |
| TWI596115B (zh) | 2012-08-13 | 2017-08-21 | 再生元醫藥公司 | 具有pH-依賴性結合特性之抗-PCSK9抗體 |
| US9133269B2 (en) | 2012-08-24 | 2015-09-15 | Anaptysbio, Inc. | Humanized antibodies directed against complement protein C5 |
| TW201418707A (zh) | 2012-09-21 | 2014-05-16 | Alexion Pharma Inc | 補體組分c5拮抗劑之篩選分析 |
| KR101638931B1 (ko) | 2013-01-31 | 2016-07-12 | 서울대학교산학협력단 | 보체 관련 질환의 예방 및 치료를 위한 c5 항체 및 방법 |
| US9321686B2 (en) | 2013-03-15 | 2016-04-26 | Forta Corporation | Reinforcement fiber coating compositions, methods of making and treating, and uses for improved adhesion to asphalt and portland cement concrete |
| WO2014144080A2 (en) | 2013-03-15 | 2014-09-18 | Amgen Inc. | Human antigen binding proteins that bind to proprotein convertase subtilisin kexin type 9 |
| ES2768648T3 (es) | 2013-03-29 | 2020-06-23 | Alexion Pharma Inc | Composiciones y métodos para aumentar la semivida en suero de un agente terapéutico dirigido a C5 del complemento |
| US11267868B2 (en) | 2013-04-02 | 2022-03-08 | Chugai Seiyaku Kabushiki Kaisha | Fc region variant |
| WO2015023972A1 (en) | 2013-08-16 | 2015-02-19 | Alexion Pharmaceuticals, Inc. | Treatment of graft rejection by administering a complement inhibitor to an organ prior to transplant |
| JP6382641B2 (ja) | 2013-09-11 | 2018-08-29 | 株式会社東芝 | 非水電解質電池及び非水電解質電池の製造方法 |
| CA2939626C (en) | 2014-02-20 | 2023-01-17 | Allergan, Inc. | Complement component c5 antibodies |
| NZ631007A (en) | 2014-03-07 | 2015-10-30 | Alexion Pharma Inc | Anti-c5 antibodies having improved pharmacokinetics |
| JP2016024424A (ja) | 2014-07-24 | 2016-02-08 | 株式会社リコー | 情報処理システム、情報処理装置、情報処理方法、及びプログラム |
| AR103162A1 (es) | 2014-12-19 | 2017-04-19 | Chugai Pharmaceutical Co Ltd | Anticuerpos anti-c5 y métodos para su uso |
| EP3247723A1 (en) | 2015-01-22 | 2017-11-29 | Chugai Seiyaku Kabushiki Kaisha | A combination of two or more anti-c5 antibodies and methods of use |
| TW202248212A (zh) | 2015-02-05 | 2022-12-16 | 日商中外製藥股份有限公司 | 包含離子濃度依賴之抗原結合域的抗體、Fc區變體、IL-8結合抗體與其用途 |
| CA2972393A1 (en) | 2015-02-27 | 2016-09-01 | Chugai Seiyaku Kabushiki Kaisha | Composition for treating il-6-related diseases |
| WO2016160756A2 (en) | 2015-03-31 | 2016-10-06 | Alexion Pharmaceuticlas, Inc. | Identifying and treating subpopulations of paroxysmal nocturnal hemoglobinuria (pnh) patents |
| US20180311299A1 (en) | 2015-05-01 | 2018-11-01 | Alexion Pharmaceuticals, Inc. | Efficacy of an anti-c5 antibody in the prevention of antibody mediated rejection in sensitized recipients of a kidney transplant |
| JP2018520139A (ja) | 2015-06-26 | 2018-07-26 | アレクシオン ファーマシューティカルズ, インコーポレイテッド | エクリズマブまたはエクリズマブバリアントでのワクチン接種に従って患者を処置するための方法 |
| TW201718014A (zh) | 2015-10-12 | 2017-06-01 | 諾華公司 | C5抑制劑於移植相關微血管病之用途 |
| RU2742606C2 (ru) | 2015-12-18 | 2021-02-09 | Чугаи Сейяку Кабусики Кайся | Антитела к с5 и способы их применения |
| US10233252B2 (en) | 2015-12-21 | 2019-03-19 | Wisconsin Alumni Research Foundation | pH-dependent antibodies targeting the transferrin receptor and methods of use thereof to deliver a therapeutic agent |
| EP3402816A1 (en) | 2016-01-11 | 2018-11-21 | Alexion Pharmaceuticals, Inc. | Dosage and administration of anti-c5 antibodies for treatment |
| MA53248A (fr) | 2016-01-25 | 2022-02-16 | Takeda Pharmaceuticals Co | Anticorps anti-c5 à commutation ph améliorée |
| KR102667023B1 (ko) | 2016-06-14 | 2024-05-21 | 리제너론 파아마슈티컬스, 인크. | 항-c5 항체 및 이의 용도 |
| TWI610941B (zh) | 2016-06-17 | 2018-01-11 | Chugai Seiyaku Kabushiki Kaisha | 抗c5抗體及使用方法 |
| TW202412841A (zh) | 2017-01-31 | 2024-04-01 | 日商中外製藥股份有限公司 | 抗c5抗體在製造用於治療或預防c5相關疾病的醫藥組合物之用途 |
| KR20240151866A (ko) | 2017-03-14 | 2024-10-18 | 파이브 프라임 테라퓨틱스, 인크. | 산성 pH에서 VISTA에 결합하는 항체 |
| MX2019010802A (es) | 2017-03-16 | 2019-10-30 | Medimmune Ltd | Anticuerpos anti-par2 y usos de los mismos. |
| ES2893769T3 (es) | 2017-04-03 | 2022-02-10 | Inflarx Gmbh | Tratamiento de enfermedades inflamatorias con inhibidores de la actividad de C5a |
| EP3700928A1 (en) | 2017-10-26 | 2020-09-02 | Alexion Pharmaceuticals, Inc. | Dosage and administration of anti-c5 antibodies for treatment of paroxysmal nocturnal hemoglobinuria (pnh) and atypical hemolytic uremic syndrome (ahus) |
| MX2020005547A (es) | 2017-12-04 | 2020-08-20 | Ra Pharmaceuticals Inc | Moduladores de la actividad del complemento. |
| SMT202400271T1 (it) | 2018-08-01 | 2024-07-09 | Chugai Pharmaceutical Co Ltd | Composizione farmaceutica per l’uso nel trattamento o nella prevenzione di una patologia correlata a c5 |
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