JP2008501357A - 遺伝子改変された非ヒト哺乳動物および非ヒト細胞 - Google Patents
遺伝子改変された非ヒト哺乳動物および非ヒト細胞 Download PDFInfo
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| PT2374819T (pt) | 2003-05-12 | 2017-07-04 | Helion Biotech Aps | Anticorpos para masp-2 |
| PL2465534T3 (pl) * | 2004-06-10 | 2017-08-31 | Omeros Corporation | Sposoby leczenia stanów związanych z aktywacją dopełniacza zależną od masp-2 |
| US8840893B2 (en) | 2004-06-10 | 2014-09-23 | Omeros Corporation | Methods for treating conditions associated with MASP-2 dependent complement activation |
| US7919094B2 (en) * | 2004-06-10 | 2011-04-05 | Omeros Corporation | Methods for treating conditions associated with MASP-2 dependent complement activation |
| CN106390117A (zh) | 2009-10-16 | 2017-02-15 | 奥默罗斯公司 | 通过抑制masp‑2依赖性补体活化治疗弥散性血管内凝血的方法 |
| US9644035B2 (en) | 2011-04-08 | 2017-05-09 | Omeros Corporation | Methods for treating conditions associated with MASP-2 dependent complement activation |
| KR20220044616A (ko) | 2011-04-08 | 2022-04-08 | 유니버시티 오브 레스터 | Ｍａｓｐ-2 의존적 보체 활성화와 관련된 질병을 치료하는 방법 |
| EP2704743B1 (en) | 2011-05-04 | 2020-03-11 | Omeros Corporation | Compositions for inhibiting masp-2 dependent complement acitivation |
| CN112481302B (zh) * | 2021-02-05 | 2021-05-14 | 百奥赛图(北京)医药科技股份有限公司 | Masp2基因人源化的非人动物的构建方法及应用 |
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| EP1140171A4 (en) | 1998-12-15 | 2002-03-13 | Brigham & Womens Hospital | METHODS AND PRODUCTS FOR REGULATING THE COMPLEMENT ACTIVATION ASSOCIATED WITH THE LECTIN COMPLEMENT SYSTEM |
| US7273925B1 (en) | 1998-12-15 | 2007-09-25 | Brigham And Women's Hospital, Inc. | Methods and products for regulating lectin complement pathway associated complement activation |
| WO2001012212A1 (en) | 1999-08-13 | 2001-02-22 | The Brigham And Women's Hospital, Inc. | Inhibitors of the lectin complement pathway (lcp) and their use |
| EP2026073B1 (en) | 2000-04-29 | 2016-03-30 | University Of Iowa Research Foundation | Diagnostics and therapeutics for macular degeneration-related disorders |
| US20020094332A1 (en) | 2001-01-18 | 2002-07-18 | Alexion Pharmaceuticals | Method of prophylaxis against large myocardial infractions |
| US20030049260A1 (en) | 2001-07-26 | 2003-03-13 | Leonard Bell | Method of improving cognitive function |
| WO2003061765A1 (en) | 2002-01-22 | 2003-07-31 | Alexion Pharmaceuticals, Inc. | Method of prophylaxis against large myocardial infarctions |
| US20060275764A1 (en) | 2002-12-03 | 2006-12-07 | Aarhus Universitet | Method for determining predisposition to manifestation of immune system related diseases |
| US7361339B2 (en) | 2003-01-09 | 2008-04-22 | Alexion Pharmaceuticals, Inc. | Methods for reducing morality associated with acute myocardial infarction |
| WO2004075837A2 (en) * | 2003-02-21 | 2004-09-10 | Tanox, Inc. | Methods for preventing and treating tissue damage associated with ischemia-reperfusion injury |
| PT2374819T (pt) * | 2003-05-12 | 2017-07-04 | Helion Biotech Aps | Anticorpos para masp-2 |
| WO2005014849A2 (en) | 2003-07-03 | 2005-02-17 | Euro-Celtique, S.A. | Genes associated with responses to neuropathic pain |
| US7482376B2 (en) | 2003-07-03 | 2009-01-27 | 3-Dimensional Pharmaceuticals, Inc. | Conjugated complement cascade inhibitors |
| EP1670910A1 (en) | 2003-09-05 | 2006-06-21 | Natimmune A/S | Masp-2 crystal structure and uses thereof |
| WO2005123776A1 (en) | 2004-06-10 | 2005-12-29 | Omeros Corporation | Methods for treating conditions associated with lectin-dependent complement activation |
| PL2465534T3 (pl) | 2004-06-10 | 2017-08-31 | Omeros Corporation | Sposoby leczenia stanów związanych z aktywacją dopełniacza zależną od masp-2 |
-
2004
- 2004-06-10 GB GBGB0412966.4A patent/GB0412966D0/en not_active Ceased
-
2005
- 2005-06-08 WO PCT/GB2005/050086 patent/WO2005120222A2/en not_active Ceased
- 2005-06-08 ES ES05748982.5T patent/ES2535639T3/es not_active Expired - Lifetime
- 2005-06-08 EP EP05748982.5A patent/EP1766033B1/en not_active Expired - Lifetime
- 2005-06-08 US US11/570,087 patent/US8785717B2/en active Active
- 2005-06-08 JP JP2007526577A patent/JP2008501357A/ja active Pending
-
2014
- 2014-06-26 US US14/316,235 patent/US20150067897A1/en not_active Abandoned
-
2016
- 2016-11-10 US US15/348,162 patent/US10660317B2/en not_active Expired - Lifetime
Patent Citations (1)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| WO2002006460A2 (en) * | 2000-07-13 | 2002-01-24 | Jens Christian Jensenius | Masp-2, a complement-fixing enzyme, and uses for it |
Non-Patent Citations (7)
| Title |
|---|
| JPN6011003406, Ｉｎｔ． Ｉｍｍｕｎｏｐｈａｒｍａｃｏｌ．, 2002, ｖｏｌ． ２， ｎｏ． ９, １２２０ * |
| JPN6011003408, Ｊ． Ｅｘｐ． Ｍｅｄ．, 200405, ｖｏｌ． １９９, １２９５−１２９９ * |
| JPN6011003410, Ｊ． Ｉｍｍｕｎｏｌ．, 1999, ｖｏｌ． １６３, ６８４８−６８５９ * |
| JPN6011003411, Ｎｅｗ Ｅｎｇｌ． Ｊ． Ｍｅｄ．, 2003, ｖｏｌ． ３４９, ５５４−５６０ * |
| JPN6011003412, Ｊ． Ｉｍｍｕｎｏｌ．, 1999, ｖｏｌ． １６２, ３４８１−３４９０ * |
| JPN6011003413, Ｉｍｍｕｎｏｌ． Ｒｅｖ．, 200404, ｖｏｌ． １９８, １８５−２０２ * |
| JPN6011003414, Ｃｌｉｎ． Ｅｘｐ． Ｉｍｍｕｎｏｌ．, 200405, ｖｏｌ． １３６, ３０４−３１１ * |
Also Published As
| Publication number | Publication date |
|---|---|
| US10660317B2 (en) | 2020-05-26 |
| EP1766033B1 (en) | 2015-01-28 |
| WO2005120222A2 (en) | 2005-12-22 |
| ES2535639T3 (es) | 2015-05-13 |
| GB0412966D0 (en) | 2004-07-14 |
| US20090205058A1 (en) | 2009-08-13 |
| EP1766033A2 (en) | 2007-03-28 |
| WO2005120222A3 (en) | 2006-02-02 |
| US8785717B2 (en) | 2014-07-22 |
| US20150067897A1 (en) | 2015-03-05 |
| US20170127657A1 (en) | 2017-05-11 |
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