RU2522976C2 - Профилактика и лечение патологических состояний глаз, вызванных комплементом - Google Patents
Профилактика и лечение патологических состояний глаз, вызванных комплементом Download PDFInfo
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- RU2522976C2 RU2522976C2 RU2009147744/10A RU2009147744A RU2522976C2 RU 2522976 C2 RU2522976 C2 RU 2522976C2 RU 2009147744/10 A RU2009147744/10 A RU 2009147744/10A RU 2009147744 A RU2009147744 A RU 2009147744A RU 2522976 C2 RU2522976 C2 RU 2522976C2
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| JP2018536650A (ja) | 2015-10-30 | 2018-12-13 | ジェネンテック， インコーポレイテッド | 抗ｄ因子抗体変異体コンジュゲート及びその使用 |
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| WO2018136827A1 (en) | 2017-01-20 | 2018-07-26 | Vitrisa Therapeutics, Inc. | Stem-loop compositions and methods for inhibiting factor d |
| EP3580241A4 (en) * | 2017-02-10 | 2021-01-06 | The Trustees Of The University Of Pennsylvania | ANTIFACTOR D ANTIBODIES AND USES THEREOF |
| CN109632924B (zh) * | 2018-12-17 | 2022-02-08 | 上海市第一人民医院 | 人黄斑新生血管性疾病的血浆脂质标记物及其应用 |
| EP3999078A4 (en) * | 2019-07-18 | 2023-06-14 | Pandorum Technologies Private Limited | METHODS FOR CULTURING MESENCHYMATOUS STEM CELLS, PRODUCTS RELATED AND THEIR APPLICATIONS |
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|---|---|---|---|---|
| RU2232991C1 (ru) * | 2003-04-09 | 2004-07-20 | Государственное учреждение "Московский научно-исследовательский институт эпидемиологии и микробиологии им. Г.Н. Габричевского" | Способ определения функциональной активности фактора d комплемента человека |
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| US7419663B2 (en) | 1998-03-20 | 2008-09-02 | Genentech, Inc. | Treatment of complement-associated disorders |
| US7282565B2 (en) | 1998-03-20 | 2007-10-16 | Genentech, Inc. | PRO362 polypeptides |
| US8088386B2 (en) * | 1998-03-20 | 2012-01-03 | Genentech, Inc. | Treatment of complement-associated disorders |
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| AU2577799A (en) | 1998-02-09 | 1999-08-23 | Human Genome Sciences, Inc. | 45 human secreted proteins |
| US6956107B2 (en) | 1998-02-20 | 2005-10-18 | Tanox, Inc. | Inhibitors of complement activation |
| DE69939813D1 (de) * | 1998-02-20 | 2008-12-11 | Tanox Inc | Inhibitoren der komplement-aktivierung |
| NZ507435A (en) | 1998-03-10 | 2003-12-19 | Genentech Inc | Novel polypeptides and nucleic acids with homology to cornichon |
| WO2000012703A2 (en) | 1998-08-27 | 2000-03-09 | Incyte Pharmaceuticals, Inc. | Protein transport-associated molecules |
| IL142794A0 (en) | 1998-12-16 | 2002-03-10 | Genentech Inc | Secreted and transmembrane polypeptides and nucleic acids encoding the same |
| CN1330555A (zh) * | 1998-12-21 | 2002-01-09 | 路德维格癌症研究所 | 抗截短的vegf－d的抗体及其应用 |
| AU768230B2 (en) | 1998-12-22 | 2003-12-04 | Genentech Inc. | Methods and compositions for inhibiting neoplastic cell growth |
| CA2362427A1 (en) | 1999-03-08 | 2000-09-14 | Genentech, Inc. | Compositions and methods for the treatment of immune related diseases |
| IL145310A0 (en) | 1999-03-11 | 2003-01-12 | Rmf Dictagene Sa | Vascular adhesion molecules and modulation of their function |
| US6642353B1 (en) | 1999-03-17 | 2003-11-04 | Chugai Seiyaku Kabushiki Kaisha | Peptide ligands for the erythropoietin receptor |
| WO2001036102A1 (en) | 1999-11-02 | 2001-05-25 | Uliyanovsky Gosudarstvenny Tekhnichesky Universitet | Method for cleaning liquids of ferromagnetic particles and device for the implementation thereof |
| JP2003514541A (ja) | 1999-11-19 | 2003-04-22 | ヒューマン ジノーム サイエンシーズ， インコーポレイテッド | １８個のヒト分泌タンパク質 |
| CA2491610A1 (en) | 1999-12-01 | 2001-06-07 | Kevin P. Baker | Secreted and transmembrane polypeptides and nucleic acids encoding the same |
| JP2004516013A (ja) | 2000-07-20 | 2004-06-03 | ジェネンテック・インコーポレーテッド | 血管形成に関連する障害を診断及び治療するための組成物と方法 |
| AU2003258714A1 (en) | 2002-09-06 | 2004-03-29 | Cytos Biotechnology Ag | Immune modulatory compounds and methods |
| WO2006071856A2 (en) | 2004-12-23 | 2006-07-06 | Glycofi, Inc. | Immunoglobulins comprising predominantly a man5glcnac2 glycoform |
| KR20180002911A (ko) * | 2005-11-04 | 2018-01-08 | 제넨테크, 인크. | 안질환 치료를 위한 보체 경로 억제제의 용도 |
| US20070190057A1 (en) | 2006-01-23 | 2007-08-16 | Jian Wu | Methods for modulating mannose content of recombinant proteins |
| KR20140101873A (ko) * | 2006-11-02 | 2014-08-20 | 제넨테크, 인크. | 인간화 항-ｄ 인자 항체 |
| AR066660A1 (es) * | 2007-05-23 | 2009-09-02 | Genentech Inc | Prevencion y tratamiento de condiciones del ojo asociadas con su complemento |
| JP4349447B2 (ja) | 2007-07-19 | 2009-10-21 | トヨタ自動車株式会社 | インバータ制御装置および車両 |
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Patent Citations (1)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| RU2232991C1 (ru) * | 2003-04-09 | 2004-07-20 | Государственное учреждение "Московский научно-исследовательский институт эпидемиологии и микробиологии им. Г.Н. Габричевского" | Способ определения функциональной активности фактора d комплемента человека |
Non-Patent Citations (1)
| Title |
|---|
| PETRUKHIN K., "New therapeutic targets in atrophic age-related macular degeneration." Expert Opin Ther Targets. (2007); 11(5):625-39. UNDAR A. et al., "Novel Anti-Factor D Monoclonal Antibody Inhibits Complement and Leukocyte Activation in a Baboon Model of Cardiopulmonary Bypass." Ann Thorac Surg (2002);74:355-62. * |
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