AU2006308614B2 - Novel activin receptor and uses thereof - Google Patents
Novel activin receptor and uses thereof Download PDFInfo
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- AU2006308614B2 AU2006308614B2 AU2006308614A AU2006308614A AU2006308614B2 AU 2006308614 B2 AU2006308614 B2 AU 2006308614B2 AU 2006308614 A AU2006308614 A AU 2006308614A AU 2006308614 A AU2006308614 A AU 2006308614A AU 2006308614 B2 AU2006308614 B2 AU 2006308614B2
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- activin
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- C07K2319/30—Non-immunoglobulin-derived peptide or protein having an immunoglobulin constant or Fc region, or a fragment thereof, attached thereto
Landscapes
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Priority Applications (1)
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| AU2011237541A AU2011237541B2 (en) | 2005-11-01 | 2011-10-19 | Novel activin receptor and uses thereof |
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| US73227005P | 2005-11-01 | 2005-11-01 | |
| US60/732,270 | 2005-11-01 | ||
| PCT/US2006/043044 WO2007053775A1 (en) | 2005-11-01 | 2006-11-01 | Novel activin receptor and uses thereof |
Related Child Applications (1)
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| CA (1) | CA2627200C (enExample) |
| ES (1) | ES2385581T3 (enExample) |
| WO (1) | WO2007053775A1 (enExample) |
Families Citing this family (55)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| RS52815B (sr) | 2002-12-20 | 2013-10-31 | Amgen Inc. | Vezivna sredstva koja inhibiraju miostatin |
| EP1771470B1 (en) | 2004-07-23 | 2013-06-26 | Acceleron Pharma Inc. | Actrii receptor polypeptides, methods and compositions |
| US8067562B2 (en) * | 2005-11-01 | 2011-11-29 | Amgen Inc. | Isolated nucleic acid molecule comprising the amino acid sequence of SEQ ID NO:1 |
| RS58231B1 (sr) | 2005-11-23 | 2019-03-29 | Acceleron Pharma Inc | Antagonisti aktivin-actriia i primene za stimulaciju rasta kostiju |
| US8128933B2 (en) | 2005-11-23 | 2012-03-06 | Acceleron Pharma, Inc. | Method of promoting bone growth by an anti-activin B antibody |
| CA2693178C (en) * | 2006-11-29 | 2018-12-04 | Nationwide Children's Hospital, Inc. | Myostatin inhibition for enhancing muscle and/or improving muscle function |
| MX2009006651A (es) | 2006-12-18 | 2009-08-26 | Acceleron Pharma Inc | Antagonistas de activina-actrii y usos para incrementar los niveles de globulos rojo. |
| US8895016B2 (en) | 2006-12-18 | 2014-11-25 | Acceleron Pharma, Inc. | Antagonists of activin-actriia and uses for increasing red blood cell levels |
| KR101526613B1 (ko) | 2007-02-01 | 2015-06-26 | 악셀레론 파마 인코포레이티드 | 액티빈-ａｃｔｒⅱａ 길항제 및 유방암을 치료 또는 예방하기 위한 이들의 용도 |
| TW201940502A (zh) | 2007-02-02 | 2019-10-16 | 美商艾瑟勒朗法瑪公司 | 衍生自ＡｃｔＲＩＩＢ的變體與其用途 |
| TW201808334A (zh) | 2007-02-09 | 2018-03-16 | 艾瑟勒朗法瑪公司 | 包含ＡｃｔＲＩＩａ-Ｆｃ融合蛋白的醫藥組合物；ＡｃｔＲＩＩａ-Ｆｃ融合蛋白於治療或預防與癌症相關的骨質流失之用途；ＡｃｔＲＩＩａ-Ｆｃ融合蛋白於治療或預防多發性骨髓瘤之用途 |
| TWI454479B (zh) * | 2007-03-06 | 2014-10-01 | Amgen Inc | 變異之活動素受體多肽及其用途 |
| US8501678B2 (en) | 2007-03-06 | 2013-08-06 | Atara Biotherapeutics, Inc. | Variant activin receptor polypeptides and uses thereof |
| EP2207562B1 (en) | 2007-09-18 | 2017-05-31 | Acceleron Pharma, Inc. | Activin-actriia antagonists and uses for decreasing or inhibiting fsh secretion |
| US8216997B2 (en) | 2008-08-14 | 2012-07-10 | Acceleron Pharma, Inc. | Methods for increasing red blood cell levels and treating anemia using a combination of GDF traps and erythropoietin receptor activators |
| HUE063136T2 (hu) | 2008-08-14 | 2023-12-28 | Acceleron Pharma Inc | GDF-Csapdák |
| EA201100832A1 (ru) | 2008-11-26 | 2011-12-30 | Амген Инк. | Варианты полипептидов рецептора iib активина и их применение |
| AU2013216639B2 (en) * | 2008-11-26 | 2016-05-05 | Amgen Inc. | Variants of activin IIB receptor polypeptides and uses thereof |
| CA2749544A1 (en) | 2009-01-13 | 2010-07-22 | Acceleron Pharma Inc. | Methods for increasing adiponectin |
| EA027071B1 (ru) * | 2009-04-27 | 2017-06-30 | Новартис Аг | АНТИТЕЛО К ActRIIB И СОДЕРЖАЩАЯ ЕГО КОМПОЗИЦИЯ |
| KR20120049214A (ko) | 2009-06-08 | 2012-05-16 | 악셀레론 파마 인코포레이티드 | 발열성 지방세포를 증가시키는 방법 |
| US8293881B2 (en) | 2009-06-12 | 2012-10-23 | Acceleron Pharma Inc. | Isolated nucleic acid encoding a truncated ActRIIB fusion protein |
| KR102170682B1 (ko) | 2009-08-13 | 2020-10-28 | 악셀레론 파마 인코포레이티드 | 적혈구 수준을 증가시키기 위한 ｇｄｆ 트랩과 에리트로포이에틴 수용체 활성인자의 병용 |
| EP2496247B1 (en) | 2009-11-03 | 2017-08-23 | Acceleron Pharma, Inc. | Methods for treating fatty liver disease |
| WO2011063018A1 (en) * | 2009-11-17 | 2011-05-26 | Acceleron Pharma Inc. | Actriib proteins and variants and uses therefore relating to utrophin induction for muscular dystrophy therapy |
| US20150359850A1 (en) | 2009-11-25 | 2015-12-17 | Santa Maria Biotherapeutics, Inc. | Administration of an anti-activin-a compound to a subject |
| NZ608206A (en) | 2010-08-16 | 2015-02-27 | Amgen Inc | Antibodies that bind myostatin, compositions and methods |
| CN103298832A (zh) | 2010-11-08 | 2013-09-11 | 阿塞勒隆制药公司 | Actriia结合剂及其用途 |
| KR20220075438A (ko) | 2011-10-17 | 2022-06-08 | 악셀레론 파마 인코포레이티드 | 비효율적 적혈구생성 치료를 위한 방법 및 조성물 |
| PE20142114A1 (es) | 2011-12-19 | 2015-01-04 | Amgen Inc | Polipeptidos de receptores de activina variantes, solos o en combinacion con quimioterapia, y sus usos |
| WO2014066486A2 (en) * | 2012-10-24 | 2014-05-01 | Celgene Corporation | Biomarker for use in treating anemia |
| MX366336B (es) | 2012-11-02 | 2019-07-05 | Celgene Corp | Antagonistas de activina - actrii y usos para el tratar trastornos oseos y otros. |
| US10092627B2 (en) | 2013-04-08 | 2018-10-09 | President And Fellows Of Harvard College | Methods and compositions for rejuvenating skeletal muscle stem cells |
| US10260068B2 (en) * | 2014-03-31 | 2019-04-16 | Sumitomo Dainippon Pharma Co., Ltd. | Prophylactic agent and therapeutic agent for fibrodysplasia ossificans progressiva |
| JP6649895B2 (ja) | 2014-04-18 | 2020-02-19 | アクセルロン ファーマ， インコーポレイテッド | 赤血球レベルを増加させ、そして鎌状赤血球症を処置するための方法 |
| TN2016000553A1 (en) | 2014-06-13 | 2018-04-04 | Acceleron Pharma Inc | Methods and compositions for treating ulcers |
| MA41052A (fr) | 2014-10-09 | 2017-08-15 | Celgene Corp | Traitement d'une maladie cardiovasculaire à l'aide de pièges de ligands d'actrii |
| IL252631B2 (en) | 2014-12-03 | 2024-06-01 | Celgene Corp | ACTIVIN-ACTRII antagonists and uses for the treatment of anemia |
| MA41119A (fr) | 2014-12-03 | 2017-10-10 | Acceleron Pharma Inc | Méthodes de traitement de syndromes myélodysplasiques et d'anémie sidéroblastique |
| MX2017013520A (es) * | 2015-04-22 | 2018-05-22 | Alivegen Usa Inc | Nuevas proteinas hibridas de bloqueo del ligando actriib para tratar enfermedades de atrofia muscular. |
| BR112018004981A2 (pt) * | 2015-09-15 | 2018-10-09 | Scholar Rock, Inc. | anticorpos anti-pró-miostatina/miostatina latente e usos destes. |
| US11123430B2 (en) | 2015-11-04 | 2021-09-21 | Acceleron Pharma Inc. | Methods for increasing red blood cell levels and treating ineffective erythropoiesis |
| CN108697793B (zh) | 2015-11-23 | 2023-08-01 | 阿塞勒隆制药公司 | 治疗眼睛疾病的方法 |
| IL293766B2 (en) | 2016-01-06 | 2023-08-01 | Harvard College | Treatment with gdf11 prevents weight gain, improves glucose loading and reduces hepatosteatosis |
| RS62011B1 (sr) | 2016-07-15 | 2021-07-30 | Acceleron Pharma Inc | Kompozicije koje sadrže polipeptide actriia za upotrebu u lečenju plućne hipertenzije |
| HUE067225T2 (hu) | 2016-07-27 | 2024-10-28 | Acceleron Pharma Inc | Mielofibrózis kezelésére szolgáló készítmények |
| JOP20190085A1 (ar) | 2016-10-20 | 2019-04-17 | Biogen Ma Inc | طرق علاج الضمور العضلي ومرض العظام باستخدام بروتينات احتجاز مركب ترابطي actriib هجين حديثة |
| EP3538123A4 (en) | 2016-11-10 | 2020-10-14 | Keros Therapeutics, Inc. | ACTIVIN RECEPTOR TYPE IIA VARIANTS AND THEIR METHODS OF USE |
| EP3706777B1 (en) | 2017-11-09 | 2024-05-22 | Keros Therapeutics, Inc. | Activin receptor type iia variants and methods of use thereof |
| CN120399032A (zh) | 2018-01-12 | 2025-08-01 | 科乐斯疗法公司 | 激活素受体iib型变体及其使用方法 |
| KR20250133994A (ko) | 2018-05-09 | 2025-09-09 | 케로스 테라퓨틱스, 인크. | 액티빈 수용체 유형 iia 변이체 및 그의 사용 방법 |
| CN109293763B (zh) * | 2018-10-26 | 2021-10-26 | 中国农业科学院特产研究所 | 水貂激活素b蛋白及其制备与应用 |
| JP2023518260A (ja) | 2020-03-20 | 2023-04-28 | ケロス セラピューティクス インコーポレイテッド | アクチビン受容体ｉｉ型キメラ及びその使用方法 |
| WO2021189010A1 (en) | 2020-03-20 | 2021-09-23 | Keros Therapeutics, Inc. | Methods of using activin receptor type iib variants |
| KR20250156167A (ko) * | 2023-03-09 | 2025-10-31 | 머크 샤프 앤드 돔 엘엘씨 | ActRIIa 폴리펩티드 변이체를 포함하는 제제 |
Citations (1)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| US6812339B1 (en) * | 2000-09-08 | 2004-11-02 | Applera Corporation | Polymorphisms in known genes associated with human disease, methods of detection and uses thereof |
Family Cites Families (41)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| US5567584A (en) | 1988-01-22 | 1996-10-22 | Zymogenetics, Inc. | Methods of using biologically active dimerized polypeptide fusions to detect PDGF |
| US5750375A (en) | 1988-01-22 | 1998-05-12 | Zymogenetics, Inc. | Methods of producing secreted receptor analogs and biologically active dimerized polypeptide fusions |
| US5885794A (en) | 1991-05-10 | 1999-03-23 | The Salk Institute For Biological Studies | Recombinant production of vertebrate activin receptor polypeptides and identification of receptor DNAs in the activin/TGF-β superfamily |
| US20050186593A1 (en) | 1991-05-10 | 2005-08-25 | The Salk Institute For Biological Studies | Cloning and recombinant production of CRF receptor(s) |
| US6162896A (en) | 1991-05-10 | 2000-12-19 | The Salk Institute For Biological Studies | Recombinant vertebrate activin receptors |
| US6153407A (en) | 1992-07-28 | 2000-11-28 | Beth Israel Deaconess Medical Center | Erythropoietin DNA having modified 5' and 3' sequences and its use to prepare EPO therapeutics |
| US5994618A (en) | 1997-02-05 | 1999-11-30 | Johns Hopkins University School Of Medicine | Growth differentiation factor-8 transgenic mice |
| US6465239B1 (en) | 1993-03-19 | 2002-10-15 | The John Hopkins University School Of Medicine | Growth differentiation factor-8 nucleic acid and polypeptides from aquatic species and non-human transgenic aquatic species |
| US6607884B1 (en) | 1993-03-19 | 2003-08-19 | The Johns Hopkins University School Of Medicine | Methods of detecting growth differentiation factor-8 |
| DE69432815T2 (de) | 1993-03-19 | 2003-12-11 | The Johns Hopkins University School Of Medicine, Baltimore | Wachstumsfaktor-8 |
| EP0756628B1 (en) * | 1994-04-29 | 2007-11-14 | Curis, Inc. | Morphogenic protein-specific cell surface receptors and uses therefor |
| US6891082B2 (en) | 1997-08-01 | 2005-05-10 | The Johns Hopkins University School Of Medicine | Transgenic non-human animals expressing a truncated activintype II receptor |
| US6656475B1 (en) | 1997-08-01 | 2003-12-02 | The Johns Hopkins University School Of Medicine | Growth differentiation factor receptors, agonists and antagonists thereof, and methods of using same |
| US6472179B2 (en) | 1998-09-25 | 2002-10-29 | Regeneron Pharmaceuticals, Inc. | Receptor based antagonists and methods of making and using |
| US6660843B1 (en) | 1998-10-23 | 2003-12-09 | Amgen Inc. | Modified peptides as therapeutic agents |
| ATE322681T1 (de) | 1999-01-21 | 2006-04-15 | Metamorphix Inc | Inhibitoren für wachstumdifferenzierungsfaktor und ihre anwendungen |
| JP4487376B2 (ja) | 2000-03-31 | 2010-06-23 | 味の素株式会社 | 腎疾患治療剤 |
| US20040223966A1 (en) | 2002-10-25 | 2004-11-11 | Wolfman Neil M. | ActRIIB fusion polypeptides and uses therefor |
| RS52815B (sr) | 2002-12-20 | 2013-10-31 | Amgen Inc. | Vezivna sredstva koja inhibiraju miostatin |
| EP2239273B1 (en) | 2003-11-13 | 2013-10-09 | Hanmi Science Co., Ltd. | A pharmaceutical composition comprosing an immunoglobulin fc as a carrier |
| US8110665B2 (en) | 2003-11-13 | 2012-02-07 | Hanmi Holdings Co., Ltd. | Pharmaceutical composition comprising an immunoglobulin FC region as a carrier |
| EP1771470B1 (en) | 2004-07-23 | 2013-06-26 | Acceleron Pharma Inc. | Actrii receptor polypeptides, methods and compositions |
| WO2006020884A2 (en) | 2004-08-12 | 2006-02-23 | Wyeth | Combination therapy for diabetes, obesity, and cardiovascular diseases using gdf-8 inhibitors |
| BRPI0516011A (pt) | 2004-09-24 | 2008-08-19 | Amgen Inc | moléculas fc modificadas |
| KR100754667B1 (ko) | 2005-04-08 | 2007-09-03 | 한미약품 주식회사 | 비펩타이드성 중합체로 개질된 면역글로불린 Ｆｃ 단편 및이를 포함하는 약제학적 조성물 |
| KR101084983B1 (ko) * | 2005-04-25 | 2011-11-18 | 가부시키가이샤 아루박 | 프린트헤드 유지 스테이션 |
| US8067562B2 (en) * | 2005-11-01 | 2011-11-29 | Amgen Inc. | Isolated nucleic acid molecule comprising the amino acid sequence of SEQ ID NO:1 |
| CL2007002567A1 (es) | 2006-09-08 | 2008-02-01 | Amgen Inc | Proteinas aisladas de enlace a activina a humana. |
| TW201940502A (zh) | 2007-02-02 | 2019-10-16 | 美商艾瑟勒朗法瑪公司 | 衍生自ＡｃｔＲＩＩＢ的變體與其用途 |
| TWI454479B (zh) | 2007-03-06 | 2014-10-01 | Amgen Inc | 變異之活動素受體多肽及其用途 |
| EP2578684B1 (en) | 2007-03-19 | 2016-02-24 | National Research Council Of Canada | Antagonists of ligands and uses thereof |
| EP2207562B1 (en) | 2007-09-18 | 2017-05-31 | Acceleron Pharma, Inc. | Activin-actriia antagonists and uses for decreasing or inhibiting fsh secretion |
| US8216997B2 (en) | 2008-08-14 | 2012-07-10 | Acceleron Pharma, Inc. | Methods for increasing red blood cell levels and treating anemia using a combination of GDF traps and erythropoietin receptor activators |
| HUE063136T2 (hu) | 2008-08-14 | 2023-12-28 | Acceleron Pharma Inc | GDF-Csapdák |
| EA201100832A1 (ru) | 2008-11-26 | 2011-12-30 | Амген Инк. | Варианты полипептидов рецептора iib активина и их применение |
| CA2749544A1 (en) | 2009-01-13 | 2010-07-22 | Acceleron Pharma Inc. | Methods for increasing adiponectin |
| KR20120049214A (ko) | 2009-06-08 | 2012-05-16 | 악셀레론 파마 인코포레이티드 | 발열성 지방세포를 증가시키는 방법 |
| US20120295814A1 (en) | 2010-01-08 | 2012-11-22 | The Brigham And Women's Hospital, Inc. | CA-125 Immune Complexes as Biomarkers of Ovarian Cancer |
| WO2011123691A1 (en) | 2010-03-31 | 2011-10-06 | Keryx Biopharmaceuticals, Inc. | Perifosine and capecitabine as a combined treatment for cancer |
| JP2012171705A (ja) * | 2011-02-17 | 2012-09-10 | Riso Kagaku Corp | 印刷装置 |
| JP6155653B2 (ja) * | 2013-01-17 | 2017-07-05 | 株式会社寺岡精工 | ラベルプリンタ |
-
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- 2006-10-31 US US11/590,962 patent/US8067562B2/en active Active
- 2006-11-01 EP EP06827481A patent/EP1943273B1/en active Active
- 2006-11-01 JP JP2008539077A patent/JP5349966B2/ja not_active Expired - Fee Related
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Patent Citations (1)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| US6812339B1 (en) * | 2000-09-08 | 2004-11-02 | Applera Corporation | Polymorphisms in known genes associated with human disease, methods of detection and uses thereof |
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| JP2013027391A (ja) | 2013-02-07 |
| JP5349966B2 (ja) | 2013-11-20 |
| US20160152683A1 (en) | 2016-06-02 |
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