AU2009324354B2 - Amino acid sequences directed against the Angiopoietin/Tie system and polypeptides comprising the same for the treatment of diseases and disorders related to angiogenesis - Google Patents
Amino acid sequences directed against the Angiopoietin/Tie system and polypeptides comprising the same for the treatment of diseases and disorders related to angiogenesis Download PDFInfo
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- AU2009324354B2 AU2009324354B2 AU2009324354A AU2009324354A AU2009324354B2 AU 2009324354 B2 AU2009324354 B2 AU 2009324354B2 AU 2009324354 A AU2009324354 A AU 2009324354A AU 2009324354 A AU2009324354 A AU 2009324354A AU 2009324354 B2 AU2009324354 B2 AU 2009324354B2
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| DK2831111T3 (en) * | 2012-03-30 | 2019-04-29 | Boehringer Ingelheim Int | Ang2-binding molecules |
| EA201890895A1 (ru) | 2013-03-15 | 2019-02-28 | Зинджения, Инк. | Мультивалентные и моновалентные мультиспецифические комплексы и их применение |
| KR102131371B1 (ko) | 2013-07-02 | 2020-07-08 | 삼성전자주식회사 | Ang-2 특이적 항체 및 그의 용도 |
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| EP3194437B1 (en) | 2014-08-07 | 2021-01-20 | Novartis AG | Angiopoietin-like 4 (angptl4) antibodies and methods of use |
| MA41899A (fr) | 2015-04-07 | 2018-02-13 | Shire Human Genetic Therapies | Anticorps anti-flt-1 pour traiter la dystrophie musculaire de duchenne |
| JP6916776B2 (ja) * | 2015-07-29 | 2021-08-11 | アラーガン、インコーポレイテッドＡｌｌｅｒｇａｎ，Ｉｎｃｏｒｐｏｒａｔｅｄ | Ａｎｇ−２に対する重鎖のみ抗体 |
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| CA3049727C (en) * | 2017-01-13 | 2022-10-04 | Vasomune Therapeutics Inc. | An agent for promoting angiogenesis and methods and uses thereof |
| KR101955886B1 (ko) * | 2017-05-05 | 2019-03-12 | 주식회사 유비프로틴 | 안지오포이에틴-1 반감기를 증가시키는 방법 |
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| US7563443B2 (en) | 2004-09-17 | 2009-07-21 | Domantis Limited | Monovalent anti-CD40L antibody polypeptides and compositions thereof |
| CA2636854A1 (en) * | 2006-01-24 | 2007-08-02 | Domantis Limited | Ligands that bind il-4 and/or il-13 |
| AU2007227251A1 (en) | 2006-03-20 | 2007-09-27 | Amgen Fremont, Inc. | Antibodies directed to angiopoietin-like protein 4 and uses thereof |
| JP2010500876A (ja) * | 2006-08-18 | 2010-01-14 | アブリンクス エン．ヴェー． | Ｉｌ−６媒介性シグナル伝達に関連する疾患及び障害の治療のための、ｉｌ−６ｒに指向性を有するアミノ酸配列及びこれを含むポリペプチド |
| US20080213253A1 (en) * | 2007-01-12 | 2008-09-04 | Dyax Corp. | Combination therapy for the treatment of cancer |
| US20110091473A1 (en) * | 2007-10-22 | 2011-04-21 | Genmab A/S | Novel antibody therapies |
| MX2010005783A (es) * | 2007-11-27 | 2010-08-10 | Ablynx Nv | Secuencias de aminoacidos dirigidas contra citoquinas heterodimericas y/o sus receptores y polipeptidos que comprenden las mismas. |
| EP2285408B1 (en) * | 2008-06-05 | 2018-10-24 | Ablynx N.V. | Amino acid sequences directed against envelope proteins of a virus and polypeptides comprising the same for the treatment of viral diseases |
| CN102307902B (zh) | 2008-12-10 | 2016-02-24 | 埃博灵克斯股份有限公司 | 用于治疗与血管发生相关的疾病和病症的针对血管生成素/Tie系统的氨基酸序列和包括其的多肽 |
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2009
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- 2009-12-10 JP JP2011540102A patent/JP5823871B2/ja not_active Expired - Fee Related
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2016
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Patent Citations (1)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| US20050158829A1 (en) * | 2004-01-16 | 2005-07-21 | Fandl James P. | Fusion polypeptides capable of activating receptors |
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| AU2016204023A1 (en) | 2016-08-18 |
| US20120076796A1 (en) | 2012-03-29 |
| WO2010066836A2 (en) | 2010-06-17 |
| CN102307902B (zh) | 2016-02-24 |
| AU2016204023B2 (en) | 2018-02-01 |
| US20160368978A1 (en) | 2016-12-22 |
| US9822175B2 (en) | 2017-11-21 |
| US9382333B2 (en) | 2016-07-05 |
| JP2012511545A (ja) | 2012-05-24 |
| US20150093377A1 (en) | 2015-04-02 |
| AU2009324354A1 (en) | 2011-06-30 |
| CA2746395A1 (en) | 2010-06-17 |
| EP2364328A2 (en) | 2011-09-14 |
| JP5823871B2 (ja) | 2015-11-25 |
| CA2746395C (en) | 2019-07-09 |
| WO2010066836A3 (en) | 2010-08-05 |
| US8858940B2 (en) | 2014-10-14 |
| CN102307902A (zh) | 2012-01-04 |
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