CN1750844B - 凝集素途径特异性补体抑制剂在制备用于预防或抑制组织损伤的药物中的用途 - Google Patents
凝集素途径特异性补体抑制剂在制备用于预防或抑制组织损伤的药物中的用途 Download PDFInfo
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Images
Classifications
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- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K16/00—Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies
- C07K16/18—Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies against material from animals or humans
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- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P17/00—Drugs for dermatological disorders
- A61P17/02—Drugs for dermatological disorders for treating wounds, ulcers, burns, scars, keloids, or the like
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- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P43/00—Drugs for specific purposes, not provided for in groups A61P1/00-A61P41/00
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61K—PREPARATIONS FOR MEDICAL, DENTAL OR TOILETRY PURPOSES
- A61K39/00—Medicinal preparations containing antigens or antibodies
- A61K2039/505—Medicinal preparations containing antigens or antibodies comprising antibodies
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- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61K—PREPARATIONS FOR MEDICAL, DENTAL OR TOILETRY PURPOSES
- A61K38/00—Medicinal preparations containing peptides
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- Immunology (AREA)
- Biochemistry (AREA)
- Biophysics (AREA)
- Nuclear Medicine, Radiotherapy & Molecular Imaging (AREA)
- Molecular Biology (AREA)
- Dermatology (AREA)
- Medicines Containing Antibodies Or Antigens For Use As Internal Diagnostic Agents (AREA)
- Medicines That Contain Protein Lipid Enzymes And Other Medicines (AREA)
Abstract
Description
Claims (7)
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CN2004800045401A Expired - Fee Related CN1750844B (zh) | 2003-02-21 | 2004-02-20 | 凝集素途径特异性补体抑制剂在制备用于预防或抑制组织损伤的药物中的用途 |
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US (2) | US20060140939A1 (zh) |
EP (2) | EP1601377A4 (zh) |
JP (1) | JP2006518749A (zh) |
CN (2) | CN101897969B (zh) |
AU (1) | AU2004216176B2 (zh) |
CA (1) | CA2515453C (zh) |
HK (2) | HK1084603A1 (zh) |
MX (1) | MXPA05008570A (zh) |
WO (1) | WO2004075837A2 (zh) |
Families Citing this family (59)
Publication number | Priority date | Publication date | Assignee | Title |
---|---|---|---|---|
US6969601B2 (en) | 1997-04-03 | 2005-11-29 | Jensenius Jens Chr | MASP-2, a complement-fixing enzyme, and uses for it |
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US20070160645A1 (en) * | 2001-10-25 | 2007-07-12 | Jakob Vinten-Johansen | PostConditioning System And Method For The Reduction Of Ischemic-Reperfusion Injury In The Heart And Other Organs |
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AU2013201558B2 (en) * | 2004-06-10 | 2016-03-31 | Omeros Corporation | Methods for treating conditions associated with MASP-2-dependent complement activation |
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US7919094B2 (en) * | 2004-06-10 | 2011-04-05 | Omeros Corporation | Methods for treating conditions associated with MASP-2 dependent complement activation |
EP2465534B1 (en) * | 2004-06-10 | 2017-03-29 | Omeros Corporation | Methods for treating conditions associated with MASP-2 dependent complement activation |
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US8168584B2 (en) | 2005-10-08 | 2012-05-01 | Potentia Pharmaceuticals, Inc. | Methods of treating age-related macular degeneration by compstatin and analogs thereof |
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WO2007095154A2 (en) | 2006-02-10 | 2007-08-23 | The Brigham And Women's Hospital, Inc. | Lectin complement pathway assays and related compositions and methods |
HUE026042T2 (en) | 2006-10-10 | 2016-05-30 | Regenesance B V | Complement inhibition for improved nerve regeneration |
US8491870B2 (en) * | 2007-12-21 | 2013-07-23 | Lers Surgical, Llc | Method for detection and treatment of aneurysms |
HUP0900319A2 (en) * | 2009-05-25 | 2011-01-28 | Eotvos Lorand Tudomanyegyetem | New peptides, method of producing therof and use thereof |
CA2971474C (en) * | 2009-10-16 | 2022-11-22 | Omeros Corporation | Methods for treating disseminated intravascular coagulation by inhibiting masp-2 dependent complement activation |
CN103068396B (zh) * | 2010-03-02 | 2016-07-06 | 诺沃姆德治疗公司 | 抑制c5和备解素相互作用的抗-备解素抗体在制备抑制交替途径活化的药剂中的用途 |
WO2011112575A1 (en) * | 2010-03-08 | 2011-09-15 | Wake Forest University Health Sciences | Keratin biomaterials for treatment of ischemia |
PT2563813E (pt) | 2010-04-30 | 2015-11-26 | Alexion Pharma Inc | Anticorpos anti-c5a e métodos para utilização dos anticorpos |
WO2012006599A2 (en) * | 2010-07-09 | 2012-01-12 | Apellis Pharmaceuticals, Inc. | Compstatin analogs for treatment of rhinosinusitis and nasal polyposis |
US9644035B2 (en) * | 2011-04-08 | 2017-05-09 | Omeros Corporation | Methods for treating conditions associated with MASP-2 dependent complement activation |
ES2894342T3 (es) | 2011-04-08 | 2022-02-14 | Univ Leicester | Métodos para tratar afecciones asociadas con la activación de complemento dependiente de MASP-2 |
CN102304158B (zh) * | 2011-05-20 | 2014-07-30 | 中国人民解放军第二军医大学 | 酰化黄酮苷化合物及其在制备补体抑制剂药物中的应用 |
WO2013006449A2 (en) | 2011-07-01 | 2013-01-10 | The Trustees Of The University Of Pennsylvania | Anti-properdin antibodies and uses thereof |
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US10531655B2 (en) | 2011-12-02 | 2020-01-14 | The Regents Of The University Of California | Reperfusion protection solution and uses thereof |
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CN105051057B (zh) | 2012-11-15 | 2019-11-19 | 阿佩利斯制药公司 | 细胞反应性的、长效的或靶向的坎普他汀类似物及相关组合物和方法 |
KR102403299B1 (ko) | 2013-03-08 | 2022-06-03 | 체에스엘 베링 게엠베하 | 원격 허혈-재관류 손상의 치료 및 예방 |
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US9827245B2 (en) | 2013-03-15 | 2017-11-28 | KeraNetics, LLC | Keratin compositions comprising halofuginone |
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WO2018075474A1 (en) | 2016-10-17 | 2018-04-26 | Medical University Of South Carolina | Compositions and methods for treating central nervous system injury |
CA3059304A1 (en) | 2017-04-07 | 2018-10-11 | Apellis Pharmaceuticals, Inc. | Dosing regimens and related compositions and methods |
GB201800620D0 (en) | 2018-01-15 | 2018-02-28 | Univ Manchester | C3b Binding Polypeptide |
CN112638417A (zh) * | 2018-06-22 | 2021-04-09 | 奥默罗斯公司 | 用于治疗各种血栓性疾病和病症的抑制masp-2的组合物和方法 |
CN113395994A (zh) * | 2018-12-05 | 2021-09-14 | 格雷卡迪亚尔诊断有限公司 | 用于预防和/或治疗缺血和治疗缺血/再灌注损伤的方法和组合物 |
GB2583560A (en) | 2018-12-11 | 2020-11-04 | Admirx Inc | Fusion protein constructs for complement associated disease |
SG11202111419QA (en) * | 2019-04-24 | 2021-11-29 | Univ Pennsylvania | Bi-functional humanized anti-c5 antibodies and factor h fusion proteins and uses thereof |
EP3966226A1 (en) | 2019-05-07 | 2022-03-16 | Bayer Aktiengesellschaft | Masp inhibitory compounds and uses thereof |
EP4240750A1 (en) | 2020-11-04 | 2023-09-13 | Bayer Aktiengesellschaft | Masp inhibitory compounds and uses thereof |
EP4011904A1 (en) | 2020-12-14 | 2022-06-15 | Bayer Aktiengesellschaft | Masp inhibitory compounds and uses thereof |
AU2022263683A1 (en) * | 2021-04-25 | 2023-11-23 | Jiangsu Hengrui Pharmaceuticals Co., Ltd. | Anti-masp2 antibody, antigen-binding fragment thereof and medical use thereof |
Citations (2)
Publication number | Priority date | Publication date | Assignee | Title |
---|---|---|---|---|
WO2001040451A2 (en) * | 1999-12-02 | 2001-06-07 | Jens Christian Jensenius | Masp-3, a complement-fixing enzyme, and uses for it |
WO2002006460A2 (en) * | 2000-07-13 | 2002-01-24 | Jens Christian Jensenius | Masp-2, a complement-fixing enzyme, and uses for it |
Family Cites Families (11)
Publication number | Priority date | Publication date | Assignee | Title |
---|---|---|---|---|
US4816567A (en) | 1983-04-08 | 1989-03-28 | Genentech, Inc. | Recombinant immunoglobin preparations |
US6458360B1 (en) | 1990-04-25 | 2002-10-01 | The Johns Hopkins University | Soluble complement regulatory molecules |
US6267958B1 (en) | 1995-07-27 | 2001-07-31 | Genentech, Inc. | Protein formulation |
US6086868A (en) * | 1997-04-30 | 2000-07-11 | Schering Corporation | Method for treating or preventing ischemia-reperfusion injury |
US6171586B1 (en) | 1997-06-13 | 2001-01-09 | Genentech, Inc. | Antibody formulation |
JP2002532079A (ja) * | 1998-12-15 | 2002-10-02 | ザ ブライハム アンド ウイミンズ ホスピタル, インコーポレイテッド | 補体活性化に関連するレクチン補体経路を調節するための方法および産物 |
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 |
CA2360233A1 (en) * | 1999-02-09 | 2000-08-17 | 3-Dimensional Pharmaceuticals, Inc. | Methods of treating c1s-mediated diseases and conditions, and compounds and compositions therefor |
AU781805B2 (en) * | 1999-08-13 | 2005-06-16 | Brigham And Women's Hospital | Inhibitors of the lectin complement pathway (LCP) and their use |
CA2433353C (en) | 2000-12-28 | 2017-03-21 | Altus Biologics, Inc. | Crystals of whole antibodies and fragments thereof and methods for making and using them |
US7361339B2 (en) | 2003-01-09 | 2008-04-22 | Alexion Pharmaceuticals, Inc. | Methods for reducing morality associated with acute myocardial infarction |
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2004
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Patent Citations (2)
Publication number | Priority date | Publication date | Assignee | Title |
---|---|---|---|---|
WO2001040451A2 (en) * | 1999-12-02 | 2001-06-07 | Jens Christian Jensenius | Masp-3, a complement-fixing enzyme, and uses for it |
WO2002006460A2 (en) * | 2000-07-13 | 2002-01-24 | Jens Christian Jensenius | Masp-2, a complement-fixing enzyme, and uses for it |
Non-Patent Citations (2)
Title |
---|
Morito Endo et al.Glomerular deposition of mannose-binding lectin(MBL)indicates a novel mechanism of complement activation inIgA nephropathy.Nephrology Dialysis Transplantation13.1998,(13),1984-1990. * |
Steen Vang Petersen et al.Control of the classical and the MBL pathway of complementactivation.Molecular Immunology37.2000,3(7),803-811. * |
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US20060140939A1 (en) | 2006-06-29 |
MXPA05008570A (es) | 2005-11-04 |
WO2004075837A2 (en) | 2004-09-10 |
HK1150751A1 (zh) | 2012-01-13 |
EP2422812A1 (en) | 2012-02-29 |
EP1601377A4 (en) | 2009-07-15 |
AU2004216176B2 (en) | 2008-04-03 |
CN101897969A (zh) | 2010-12-01 |
CN101897969B (zh) | 2014-04-02 |
JP2006518749A (ja) | 2006-08-17 |
CN1750844A (zh) | 2006-03-22 |
AU2004216176A1 (en) | 2004-09-10 |
HK1084603A1 (en) | 2006-08-04 |
CA2515453C (en) | 2013-09-24 |
US20090017031A1 (en) | 2009-01-15 |
CA2515453A1 (en) | 2004-09-10 |
EP1601377A2 (en) | 2005-12-07 |
WO2004075837A3 (en) | 2005-06-02 |
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