CN101712722A - Glp-1融合蛋白 - Google Patents
Glp-1融合蛋白 Download PDFInfo
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- CN101712722A CN101712722A CN200910173888A CN200910173888A CN101712722A CN 101712722 A CN101712722 A CN 101712722A CN 200910173888 A CN200910173888 A CN 200910173888A CN 200910173888 A CN200910173888 A CN 200910173888A CN 101712722 A CN101712722 A CN 101712722A
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- A61P3/08—Drugs for disorders of the metabolism for glucose homeostasis
- A61P3/10—Drugs for disorders of the metabolism for glucose homeostasis for hyperglycaemia, e.g. antidiabetics
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- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
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- A61P5/48—Drugs for disorders of the endocrine system of the pancreatic hormones
- A61P5/50—Drugs for disorders of the endocrine system of the pancreatic hormones for increasing or potentiating the activity of insulin
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- A—HUMAN NECESSITIES
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- A61P9/00—Drugs for disorders of the cardiovascular system
- A61P9/10—Drugs for disorders of the cardiovascular system for treating ischaemic or atherosclerotic diseases, e.g. antianginal drugs, coronary vasodilators, drugs for myocardial infarction, retinopathy, cerebrovascula insufficiency, renal arteriosclerosis
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K14/00—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof
- C07K14/435—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from animals; from humans
- C07K14/575—Hormones
- C07K14/605—Glucagons
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K14/00—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof
- C07K14/435—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from animals; from humans
- C07K14/76—Albumins
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K14/00—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof
- C07K14/435—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from animals; from humans
- C07K14/76—Albumins
- C07K14/765—Serum albumin, e.g. HSA
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- C—CHEMISTRY; METALLURGY
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- C—CHEMISTRY; METALLURGY
- C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
- C12N—MICROORGANISMS OR ENZYMES; COMPOSITIONS THEREOF; PROPAGATING, PRESERVING, OR MAINTAINING MICROORGANISMS; MUTATION OR GENETIC ENGINEERING; CULTURE MEDIA
- C12N15/00—Mutation or genetic engineering; DNA or RNA concerning genetic engineering, vectors, e.g. plasmids, or their isolation, preparation or purification; Use of hosts therefor
- C12N15/09—Recombinant DNA-technology
- C12N15/11—DNA or RNA fragments; Modified forms thereof; Non-coding nucleic acids having a biological activity
- C12N15/62—DNA sequences coding for fusion proteins
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- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K2319/00—Fusion polypeptide
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- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
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- C07K—PEPTIDES
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- C07K2319/31—Fusion polypeptide fusions, other than Fc, for prolonged plasma life, e.g. albumin
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- C—CHEMISTRY; METALLURGY
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- C07K2319/70—Fusion polypeptide containing domain for protein-protein interaction
- C07K2319/735—Fusion polypeptide containing domain for protein-protein interaction containing a domain for self-assembly, e.g. a viral coat protein (includes phage display)
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| US25195400P | 2000-12-07 | 2000-12-07 | |
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| CNA018202322A Division CN1483041A (zh) | 2000-12-07 | 2001-11-29 | Glp-1融合蛋白 |
Publications (1)
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|---|---|
| CN101712722A true CN101712722A (zh) | 2010-05-26 |
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| CN200910173888A Pending CN101712722A (zh) | 2000-12-07 | 2001-11-29 | Glp-1融合蛋白 |
| CNA018202322A Pending CN1483041A (zh) | 2000-12-07 | 2001-11-29 | Glp-1融合蛋白 |
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| Application Number | Title | Priority Date | Filing Date |
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| CNA018202322A Pending CN1483041A (zh) | 2000-12-07 | 2001-11-29 | Glp-1融合蛋白 |
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| WO2018045872A1 (zh) * | 2016-09-06 | 2018-03-15 | 中国药科大学 | 一种多肽及其用途 |
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Families Citing this family (332)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| FR2686899B1 (fr) | 1992-01-31 | 1995-09-01 | Rhone Poulenc Rorer Sa | Nouveaux polypeptides biologiquement actifs, leur preparation et compositions pharmaceutiques les contenant. |
| GB9526733D0 (en) | 1995-12-30 | 1996-02-28 | Delta Biotechnology Ltd | Fusion proteins |
| US6444788B1 (en) | 1999-03-15 | 2002-09-03 | Novo Nordisk A/S | Ion exchange chromatography of GLP-1, analogs and derivatives thereof |
| US6924264B1 (en) * | 1999-04-30 | 2005-08-02 | Amylin Pharmaceuticals, Inc. | Modified exendins and exendin agonists |
| US6946134B1 (en) | 2000-04-12 | 2005-09-20 | Human Genome Sciences, Inc. | Albumin fusion proteins |
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| PT1695983E (pt) * | 2000-06-16 | 2009-05-05 | Lilly Co Eli | Análogos do peptídeo-1 do tipo glucagon |
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| WO2002059280A2 (en) | 2000-12-08 | 2002-08-01 | Alexion Pharmaceuticals, Inc. | Chronic lymphocytic leukemia cell line and its use for producing an antibody |
| AU2002228608A1 (en) * | 2000-12-13 | 2002-06-24 | Eli Lilly And Company | Amidated glucagon-like peptide-1 |
| US7507413B2 (en) | 2001-04-12 | 2009-03-24 | Human Genome Sciences, Inc. | Albumin fusion proteins |
| AU2002317599B2 (en) | 2001-07-31 | 2008-04-03 | The Government Of The United States Of America As Represented By The Secretary, Department Of Health And Human Services | GLP-1 exendin-4 peptide analogs and uses thereof |
| CA2458371A1 (en) * | 2001-08-23 | 2003-03-06 | Eli Lilly And Company | Glucagon-like peptide-1 analogs |
| US7176278B2 (en) | 2001-08-30 | 2007-02-13 | Biorexis Technology, Inc. | Modified transferrin fusion proteins |
| US8129504B2 (en) | 2001-08-30 | 2012-03-06 | Biorexis Technology, Inc. | Oral delivery of modified transferrin fusion proteins |
| HRP20040343A2 (en) * | 2001-10-18 | 2005-08-31 | Bristol-Myers Squibb Company | Human glucagon-like-peptide-1 mimics and their use in the treatment of diabetes and related conditions |
| EP1463752A4 (en) | 2001-12-21 | 2005-07-13 | Human Genome Sciences Inc | ALBUMIN FUSION PROTEINS |
| US20080194481A1 (en) * | 2001-12-21 | 2008-08-14 | Human Genome Sciences, Inc. | Albumin Fusion Proteins |
| EP2277910A1 (en) | 2001-12-21 | 2011-01-26 | Human Genome Sciences, Inc. | Albumin fusion proteins |
| EP1585959A4 (en) * | 2002-01-08 | 2007-11-14 | Lilly Co Eli | PEPTIDE-1 ANALOGUES OF EXTENSION GLUCAGON TYPE |
| US20030191056A1 (en) | 2002-04-04 | 2003-10-09 | Kenneth Walker | Use of transthyretin peptide/protein fusions to increase the serum half-life of pharmacologically active peptides/proteins |
| DE60331226D1 (de) | 2002-05-24 | 2010-03-25 | Medtronic Inc | Verfahren und dna-konstrukte zur produktion von polypeptiden mit hoher ausbeute |
| EP1545608A4 (en) * | 2002-06-28 | 2006-09-13 | Centocor Inc | CH1-DELETED MAMMED MUICETIC BODIES, COMPOSITIONS, METHODS AND APPLICATIONS |
| US9321832B2 (en) | 2002-06-28 | 2016-04-26 | Domantis Limited | Ligand |
| JP4873860B2 (ja) * | 2002-08-30 | 2012-02-08 | バイオレクシス ファーマシューティカル コーポレーション | 改変トランスフェリン融合タンパク質 |
| EP1688148A1 (en) * | 2002-12-03 | 2006-08-09 | Novo Nordisk A/S | Combination treatment using exendin-4 and thiazolidinediones |
| AU2003283216A1 (en) * | 2002-12-03 | 2004-06-23 | Novo Nordisk A/S | Combination treatment using exendin-4 and thiazolidinediones |
| US7655618B2 (en) | 2002-12-27 | 2010-02-02 | Diobex, Inc. | Compositions and methods for the prevention and control of insulin-induced hypoglycemia |
| NZ541365A (en) | 2002-12-27 | 2009-09-25 | Diobex Inc | Compositions and methods for the prevention and control of insulin-induced hypoglycemia |
| EP1582223A4 (en) * | 2003-01-10 | 2007-01-17 | Niigata Tlo Corp | VECTOR FOR GENE THERAPY AND METHOD FOR THE QUANTIFICATION OF A TARGET PROTEIN IN MAMMALIAN OR CULTURAL CELLS BY APPLYING THE VECTOR FOR GENE THERAPY |
| EP1594530A4 (en) | 2003-01-22 | 2006-10-11 | Human Genome Sciences Inc | HYBRID PROTEINS OF ALBUMIN |
| US20070059376A1 (en) * | 2003-02-06 | 2007-03-15 | Shinji Takeoka | Peptide conjugate |
| EA009366B1 (ru) * | 2003-03-19 | 2007-12-28 | Эли Лилли Энд Компани | Связанные с полиэтиленгликолем соединения гпп-1 |
| BRPI0408978B8 (pt) | 2003-04-08 | 2021-07-27 | Novo Nordisk As | processos para regenerar uma fase estacionária cromatográfica |
| WO2004089985A1 (en) * | 2003-04-11 | 2004-10-21 | Novo Nordisk A/S | Stable pharmaceutical compositions |
| EP1633384B1 (en) | 2003-05-15 | 2012-03-14 | Trustees Of Tufts College | Stable analogs of glp-1 |
| DE602004011770T2 (de) * | 2003-06-12 | 2009-02-05 | Eli Lilly And Co., Indianapolis | Fusionsproteine |
| ATE525395T1 (de) | 2003-06-12 | 2011-10-15 | Lilly Co Eli | Fusions proteine von glp-1-analoga |
| TW200526254A (en) * | 2003-09-19 | 2005-08-16 | Novo Nordisk As | Novel GLP-1 derivatives |
| JP2007537981A (ja) | 2003-09-19 | 2007-12-27 | ノボ ノルディスク アクティーゼルスカブ | 新規の血漿タンパク質親和性タグ |
| US20090238838A1 (en) * | 2003-11-13 | 2009-09-24 | Hanmi Pharm. Ind. Co. Ltd. | Insulinotropic peptide conjugate using an immunoglobulin fc |
| US8110665B2 (en) | 2003-11-13 | 2012-02-07 | Hanmi Holdings Co., Ltd. | Pharmaceutical composition comprising an immunoglobulin FC region as a carrier |
| US8263084B2 (en) * | 2003-11-13 | 2012-09-11 | Hanmi Science Co., Ltd | Pharmaceutical composition for treating obesity-related disease comprising insulinotropic peptide conjugate |
| ES2438098T3 (es) | 2003-11-13 | 2014-01-15 | Hanmi Science Co., Ltd. | Composición farmacéutica que comprende un Fc de inmunoglobulina como vehículo |
| KR101135244B1 (ko) * | 2007-11-29 | 2012-04-24 | 한미사이언스 주식회사 | 인슐린 분비 펩타이드 결합체를 포함하는 비만 관련질환 치료용 조성물 |
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| DE602004031455D1 (de) | 2003-12-09 | 2011-03-31 | Novo Nordisk As | Regulierung der nahrungspräferenz mit glp-1-agonisten |
| KR20060109940A (ko) * | 2003-12-18 | 2006-10-23 | 노보 노르디스크 에이/에스 | 알부민-유사제에 연결된 신규 glp-1 유사체 |
| US20060252693A1 (en) * | 2004-01-29 | 2006-11-09 | Wolfgang Glaesner | Glucagon-like peptide-1 analogs |
| CN1980687B (zh) * | 2004-02-09 | 2015-05-13 | 人类基因科学公司 | 清蛋白融合蛋白 |
| EP1729795B1 (en) * | 2004-02-09 | 2016-02-03 | Human Genome Sciences, Inc. | Albumin fusion proteins |
| EP1789440A4 (en) | 2004-02-11 | 2008-03-12 | Amylin Pharmaceuticals Inc | REASONS FOR THE FAMILY OF PANCREATIC POLYPEPTIDES AND POLYPEPTIDES CONTAINING THEM |
| IN2012DN03921A (enExample) * | 2004-02-11 | 2015-09-04 | Amylin Pharmaceuticals Inc | |
| US8076288B2 (en) | 2004-02-11 | 2011-12-13 | Amylin Pharmaceuticals, Inc. | Hybrid polypeptides having glucose lowering activity |
| EA011583B1 (ru) * | 2004-03-31 | 2009-04-28 | Сентокор, Инк. | Миметические антитела glp-1 человека, композиции, способы и применения |
| ES2887039T3 (es) | 2004-04-21 | 2021-12-21 | Alexion Pharma Inc | Conjugados para administración ósea y procedimiento de uso de estos para dirigir proteínas al hueso |
| CA2565300A1 (en) | 2004-05-13 | 2005-12-01 | Eli Lilly And Company | Fgf-21 fusion proteins |
| JP2008501765A (ja) | 2004-06-11 | 2008-01-24 | ノボ ノルディスク アクティーゼルスカブ | Glp−1アゴニストを用いた薬剤誘発性肥満の中和 |
| JP2008515856A (ja) | 2004-10-07 | 2008-05-15 | ノボ ノルディスク アクティーゼルスカブ | 遅延性glp−1化合物 |
| EP1799711B1 (en) | 2004-10-07 | 2012-06-20 | Novo Nordisk A/S | Protracted exendin-4 compounds |
| WO2006059106A2 (en) * | 2004-12-02 | 2006-06-08 | Domantis Limited | Bispecific domain antibodies targeting serum albumin and glp-1 or pyy |
| AU2005337493A1 (en) * | 2004-12-22 | 2007-04-26 | Centocor, Inc. | GLP-1 agonists, compositions, methods and uses |
| SI1831252T1 (sl) * | 2004-12-22 | 2009-12-31 | Lilly Co Eli | Formulacije analogov glp-1 fuzijskih proteinov |
| US20090016959A1 (en) * | 2005-02-18 | 2009-01-15 | Richard Beliveau | Delivery of antibodies to the central nervous system |
| TWI362392B (en) | 2005-03-18 | 2012-04-21 | Novo Nordisk As | Acylated glp-1 compounds |
| MX2007011307A (es) * | 2005-03-18 | 2007-10-08 | Novo Nordisk As | Compuestos de glp-1 extendidos. |
| JP2008546373A (ja) * | 2005-03-28 | 2008-12-25 | セントカー・インコーポレーテツド | ヒトglp−1ミメティボディ、組成物、方法および用途 |
| CA2606809C (en) * | 2005-05-06 | 2016-01-05 | Providence Health System | Trimeric ox40-immunoglobulin fusion protein and methods of use |
| DK1881850T3 (da) * | 2005-05-13 | 2011-01-03 | Lilly Co Eli | GLP-1-PEGylerede forbindelser |
| EP1920061A4 (en) * | 2005-07-27 | 2009-05-13 | Wang Qinghua | GLP / 1 / EXENDIN 4 IGG FC FUSION CONSTRUCTS FOR THE TREATMENT OF DIABETES |
| AU2006279276A1 (en) * | 2005-07-29 | 2007-02-15 | Amprotein Corporation | Chimeric therapeutic agents |
| WO2007016764A1 (en) * | 2005-08-06 | 2007-02-15 | Qinghua Wang | Composition and method for prevention and treatment of type i diabetes |
| AU2006279680B2 (en) * | 2005-08-11 | 2012-12-06 | Amylin Pharmaceuticals, Llc | Hybrid polypeptides with selectable properties |
| KR101399178B1 (ko) * | 2005-08-11 | 2014-06-18 | 아스트라제네카 파마수티컬스 엘피 | 선별가능한 특성을 갖는 하이브리드 폴리펩티드 |
| ES2336575T3 (es) * | 2005-09-22 | 2010-04-14 | Biocompatibles Uk Limited | Polipeptidos de fusion glp-1 (peptido-1 similar al glucagon) con resistencia aumentada a la peptidasa. |
| JPWO2007049695A1 (ja) * | 2005-10-26 | 2009-04-30 | 中外製薬株式会社 | 凝集性glp−1アナログおよび徐放性医薬組成物 |
| ES2586236T3 (es) * | 2005-11-04 | 2016-10-13 | Glaxosmithkline Llc | Procedimientos para administrar agentes hipoglucémicos |
| CN1962695B (zh) * | 2005-11-09 | 2011-08-31 | 浙江德清安平生物制药有限公司 | 类胰高血素肽-1融合蛋白及其制备和用途 |
| US8039432B2 (en) | 2005-11-09 | 2011-10-18 | Conjuchem, Llc | Method of treatment of diabetes and/or obesity with reduced nausea side effect |
| US20080280328A1 (en) * | 2005-11-18 | 2008-11-13 | Novozymes A/S | Glucoamylase Variants |
| JPWO2007063907A1 (ja) * | 2005-11-30 | 2009-05-07 | 塩野義製薬株式会社 | ペプチド糖鎖付加体およびそれを有効成分とする医薬 |
| WO2007075534A2 (en) | 2005-12-16 | 2007-07-05 | Nektar Therapeutics Al, Corporation | Polymer conjugates of glp-1 |
| US8841255B2 (en) | 2005-12-20 | 2014-09-23 | Duke University | Therapeutic agents comprising fusions of vasoactive intestinal peptide and elastic peptides |
| US20130172274A1 (en) | 2005-12-20 | 2013-07-04 | Duke University | Methods and compositions for delivering active agents with enhanced pharmacological properties |
| ES2779992T3 (es) | 2005-12-20 | 2020-08-21 | Univ Duke | Métodos y composiciones para suministrar agentes activos con propiedades farmacológicas potenciadas |
| AU2007207764B2 (en) | 2006-01-12 | 2012-06-07 | Alexion Pharmaceuticals, Inc. | Antibodies to OX-2/CD200 and uses thereof |
| US8946155B2 (en) | 2006-02-03 | 2015-02-03 | Opko Biologics Ltd. | Long-acting polypeptides and methods of producing and administering same |
| US8450269B2 (en) | 2006-02-03 | 2013-05-28 | Prolor Biotech Ltd. | Long-acting growth hormone and methods of producing same |
| US9458444B2 (en) | 2006-02-03 | 2016-10-04 | Opko Biologics Ltd. | Long-acting coagulation factors and methods of producing same |
| US9249407B2 (en) | 2006-02-03 | 2016-02-02 | Opko Biologics Ltd. | Long-acting coagulation factors and methods of producing same |
| US10221228B2 (en) | 2006-02-03 | 2019-03-05 | Opko Biologics Ltd. | Long-acting polypeptides and methods of producing and administering same |
| US8476234B2 (en) * | 2006-02-03 | 2013-07-02 | Prolor Biotech Inc. | Long-acting coagulation factors and methods of producing same |
| US8048849B2 (en) | 2006-02-03 | 2011-11-01 | Modigene, Inc. | Long-acting polypeptides and methods of producing same |
| US8759292B2 (en) | 2006-02-03 | 2014-06-24 | Prolor Biotech, Llc | Long-acting coagulation factors and methods of producing same |
| US10351615B2 (en) | 2006-02-03 | 2019-07-16 | Opko Biologics Ltd. | Methods of treatment with long-acting growth hormone |
| WO2007092252A2 (en) | 2006-02-03 | 2007-08-16 | Modigene Inc | Long-acting polypeptides and methods of producing same |
| US20150038413A1 (en) | 2006-02-03 | 2015-02-05 | Opko Biologics Ltd. | Long-acting polypeptides and methods of producing and administering same |
| US20140113860A1 (en) | 2006-02-03 | 2014-04-24 | Prolor Biotech Ltd. | Long-acting polypeptides and methods of producing and administering same |
| EP1816201A1 (en) * | 2006-02-06 | 2007-08-08 | CSL Behring GmbH | Modified coagulation factor VIIa with extended half-life |
| CN101003574B (zh) * | 2006-02-21 | 2010-12-15 | 大连帝恩生物工程有限公司 | 长效降血糖肽的重组表达及其在糖尿病治疗药物中的应用 |
| CA2800389A1 (en) | 2006-04-20 | 2007-11-01 | Amgen Inc. | Glp-1 compounds |
| ATE444741T1 (de) | 2006-05-10 | 2009-10-15 | Biocompatibles Uk Ltd | Glp-1 peptide enthaltende kugelförmige mikrokapseln, deren produktion und deren verwendung |
| WO2007139941A2 (en) | 2006-05-26 | 2007-12-06 | Amylin Pharmaceuticals, Inc. | Composition and methods for treatment of congestive heart failure |
| EP2046367A4 (en) * | 2006-06-07 | 2009-11-11 | Human Genome Sciences Inc | ALBUM INFUSION PROTEINS |
| EP2049567A2 (en) * | 2006-07-18 | 2009-04-22 | Centocor, Inc. | Human glp-1 mimetibodies, compositions, methods and uses |
| JP5102833B2 (ja) * | 2006-07-24 | 2012-12-19 | バイオレクシス ファーマシューティカル コーポレーション | エキセンディン融合タンパク質 |
| AU2007291501B2 (en) * | 2006-08-31 | 2012-07-12 | F. Hoffmann-La Roche Ag | Method for the production of insulin-like growth factor-I |
| CL2007002502A1 (es) | 2006-08-31 | 2008-05-30 | Hoffmann La Roche | Variantes del factor de crecimiento similar a insulina-1 humano (igf-1) pegilados en lisina; metodo de produccion; proteina de fusion que la comprende; y su uso para tratar la enfermedad de alzheimer. |
| CN101578373A (zh) * | 2006-09-06 | 2009-11-11 | 费斯生物制药公司 | 融合肽治疗组合物 |
| PE20080840A1 (es) * | 2006-09-13 | 2008-08-27 | Smithkline Beecham Corp | Metodos para administrar agentes hipoglucemiantes de larga duracion |
| TWI428346B (zh) * | 2006-12-13 | 2014-03-01 | Imp Innovations Ltd | 新穎化合物及其等對進食行為影響 |
| JP2008169195A (ja) | 2007-01-05 | 2008-07-24 | Hanmi Pharmaceutical Co Ltd | キャリア物質を用いたインスリン分泌ペプチド薬物結合体 |
| RU2432361C2 (ru) * | 2007-01-05 | 2011-10-27 | КовЭкс Текнолоджиз Айэлэнд Лимитед | Соединения агонисты рецептора глюкагоноподобного белка-1 (glp-1r) |
| AU2011254001B2 (en) * | 2007-01-05 | 2012-08-02 | Covx Technologies Ireland Limited | Glucagon-like protein-1 receptor (GLP-1R) agonist compounds |
| US20090098130A1 (en) * | 2007-01-05 | 2009-04-16 | Bradshaw Curt W | Glucagon-like protein-1 receptor (glp-1r) agonist compounds |
| EP1972349A1 (en) * | 2007-03-21 | 2008-09-24 | Biocompatibles UK Limited | GLP-1 fusion peptides conjugated to polymer(s), their production and use |
| EP1975176A1 (en) * | 2007-03-27 | 2008-10-01 | Biocompatibles UK Limited | Novel glp-1 fusion peptides, their production and use |
| CA2682605A1 (en) | 2007-04-18 | 2008-10-30 | Zymogenetics, Inc. | Single chain fc, methods of making and methods of treatment |
| RU2440097C2 (ru) | 2007-04-23 | 2012-01-20 | Интарсия Терапьютикс, Инк. | Способ лечения диабета ii типа и ожирения, осмотическое устройство для доставки и способ его изготовления |
| JP2009019027A (ja) * | 2007-07-16 | 2009-01-29 | Hanmi Pharmaceutical Co Ltd | アミノ末端のアミノ酸が変異したインスリン分泌ペプチド誘導体 |
| BRPI0814645A2 (pt) | 2007-07-25 | 2015-01-27 | Alexion Pharma Inc | Métodos e composições para tratar de doença autoimune. |
| WO2009020802A2 (en) | 2007-08-03 | 2009-02-12 | Eli Lilly And Company | Treatment for obesity |
| JP5476304B2 (ja) | 2007-09-05 | 2014-04-23 | ノボ・ノルデイスク・エー/エス | グルカゴン様ペプチド−1誘導体及びそれらの医薬用途 |
| EP2190873B1 (en) | 2007-09-05 | 2015-07-22 | Novo Nordisk A/S | Truncated glp-1 derivatives and their therapeutical use |
| ES2532116T3 (es) | 2007-09-05 | 2015-03-24 | Novo Nordisk A/S | Péptidos derivados con A-B-C-D y sus usos terapéuticos |
| EP2200634B1 (en) | 2007-09-21 | 2015-02-11 | The Regents of The University of California | Targeted interferon demonstrates potent apoptotic and anti-tumor activities |
| CN101918027A (zh) * | 2007-11-02 | 2010-12-15 | 森托科尔奥索生物科技公司 | 半合成GLP-1肽-Fc融合构造、方法及其用途 |
| AU2009231439A1 (en) * | 2008-03-31 | 2009-10-08 | Glaxo Group Limited | Drug fusions and conjugates |
| BRPI0911266A2 (pt) * | 2008-04-03 | 2015-09-29 | Hoffmann La Roche | ensaio de fator de crescimento similar à insulina peguilado |
| CN101328221B (zh) * | 2008-04-14 | 2011-03-23 | 中国药科大学 | 一种降糖多肽融合蛋白及其衍生物的结构及用途 |
| WO2009158704A2 (en) | 2008-06-27 | 2009-12-30 | Duke University | Therapeutic agents comprising elastin-like peptides |
| KR101200659B1 (ko) | 2008-07-23 | 2012-11-12 | 한미사이언스 주식회사 | 세 말단 반응기를 갖는 비펩타이드성 중합체를 이용한 생리활성 폴리펩타이드 약물 결합체 |
| US8865868B2 (en) | 2008-08-06 | 2014-10-21 | Novo Nordisk Healthcare Ag | Conjugated proteins with prolonged in vivo efficacy |
| US20100075897A1 (en) * | 2008-09-23 | 2010-03-25 | Jinan University | Method for sustainedly releasing bioactive peptides and application thereof |
| CN102245642A (zh) | 2008-10-15 | 2011-11-16 | 安吉奥开米公司 | Glp-1激动剂的结合物及其用途 |
| BRPI0922689A2 (pt) | 2008-12-05 | 2018-11-06 | Angiochem Inc. | conjugados de neurotensina ou análogos de neurotensina e usos dos mesmos |
| EA026508B1 (ru) | 2008-12-05 | 2017-04-28 | Глэксо Груп Лимитед | Единичный вариабельный домен иммуноглобулина и выделенный устойчивый к протеазе полипептид, связывающие сывороточный альбумин человека |
| JP2012511586A (ja) | 2008-12-10 | 2012-05-24 | グラクソスミスクライン・リミテッド・ライアビリティ・カンパニー | 医薬組成物 |
| JP5816097B2 (ja) | 2009-01-22 | 2015-11-18 | ノヴォ・ノルディスク・ヘルス・ケア・アーゲー | 安定な成長ホルモン化合物 |
| SG172789A1 (en) | 2009-02-11 | 2011-08-29 | Novozymes Biopharma Dk As | Albumin variants and conjugates |
| WO2010096394A2 (en) | 2009-02-17 | 2010-08-26 | Redwood Biosciences, Inc. | Aldehyde-tagged protein-based drug carriers and methods of use |
| KR20110137819A (ko) | 2009-03-27 | 2011-12-23 | 글락소 그룹 리미티드 | 약물 융합체 및 컨쥬게이트 |
| ES2729261T3 (es) | 2009-04-20 | 2019-10-31 | Angiochem Inc | Tratamiento del cáncer de ovario utilizando un agente anticancerígeno conjugado con un análogo de Angiopep-2 |
| JP5932642B2 (ja) | 2009-07-02 | 2016-06-08 | アンジオケム インコーポレーテッド | 多量体ペプチドコンジュゲートおよびその使用 |
| US9663778B2 (en) | 2009-07-09 | 2017-05-30 | OPKO Biologies Ltd. | Long-acting coagulation factors and methods of producing same |
| US12203113B2 (en) | 2009-07-09 | 2025-01-21 | Opko Biologics Ltd. | Long-acting coagulation factors and methods of producing same |
| EP2461831B1 (en) | 2009-08-06 | 2018-11-21 | Novo Nordisk Health Care AG | Growth hormones with prolonged in-vivo efficacy |
| HUE054744T2 (hu) | 2009-08-14 | 2021-12-28 | Phasebio Pharmaceuticals Inc | Módosított vazoaktív intesztinális peptidek |
| CN101993485B (zh) | 2009-08-20 | 2013-04-17 | 重庆富进生物医药有限公司 | 促胰岛素分泌肽类似物同源二聚体及其用途 |
| CN101993496B (zh) * | 2009-08-20 | 2013-06-05 | 重庆富进生物医药有限公司 | 双重调节血糖血脂融合蛋白及其制法和用途 |
| CA2774552A1 (en) | 2009-09-30 | 2011-04-07 | Glaxo Group Limited | Drug fusions and conjugates with extended half life |
| WO2011043530A1 (ko) * | 2009-10-09 | 2011-04-14 | (주)알테오젠 | Glp-1 유사체의 융합체, 및 이를 유효성분으로 함유하는 당뇨병의 예방 또는 치료용 조성물 |
| CN102725312B (zh) * | 2009-10-20 | 2014-10-01 | 佐治亚州立大学研究基金会公司 | 用于糖尿病治疗和β细胞成像的蛋白药物 |
| JP2013509170A (ja) | 2009-10-30 | 2013-03-14 | ノボザイムス バイオファーマ デーコー アクティーゼルスカブ | アルブミン変異体 |
| CN102070717B (zh) * | 2009-11-19 | 2013-04-10 | 东莞太力生物工程有限公司 | 融合蛋白及其制备方法、编码该蛋白的dna序列、表达载体、宿主细胞、含有该蛋白的药物组合物 |
| CN102711795A (zh) | 2009-12-08 | 2012-10-03 | 泰华制药工业有限公司 | 用于治疗可卡因滥用的BChE白蛋白融合体 |
| CN118767115A (zh) | 2010-01-22 | 2024-10-15 | 诺沃—诺迪斯克保健股份有限公司 | 体内功效延长的生长激素 |
| US9211342B2 (en) | 2010-01-22 | 2015-12-15 | Novo Nordisk Healthcare Ag | Stable growth hormone compounds resistant to proteolytic degradation |
| AR081066A1 (es) | 2010-04-02 | 2012-06-06 | Hanmi Holdings Co Ltd | Conjugado de insulina donde se usa un fragmento de inmunoglobulina |
| US9981017B2 (en) | 2010-04-02 | 2018-05-29 | Hanmi Science Co., Ltd. | Insulin conjugate using an immunoglobulin fragment |
| WO2011124718A1 (en) | 2010-04-09 | 2011-10-13 | Novozymes A/S | Albumin derivatives and variants |
| CN101875700B (zh) * | 2010-04-09 | 2012-09-26 | 无锡和邦生物科技有限公司 | 一种增加促胰岛素分泌肽融合蛋白生物活性的方法 |
| WO2011123943A1 (en) | 2010-04-09 | 2011-10-13 | Mount Sinai Hospital | Methods for treating disorders of the gastrointestinal tract using a glp-1 agonist |
| JP5827218B2 (ja) | 2010-04-30 | 2015-12-02 | 株式会社三和化学研究所 | 生理活性物質等の生体内安定性向上のためのペプチド及び生体内安定性が向上した生理活性物質 |
| US8691763B2 (en) | 2010-05-04 | 2014-04-08 | Glaxosmithkline Llc | Methods for treating or preventing cardiovascular disorders and providing cardiovascular protection |
| WO2011153642A1 (en) * | 2010-06-10 | 2011-12-15 | Angiochem Inc. | Leptin and leptin analog conjugates and fusion proteins and uses thereof |
| CN101891823B (zh) | 2010-06-11 | 2012-10-03 | 北京东方百泰生物科技有限公司 | 一种Exendin-4及其类似物融合蛋白 |
| WO2011162830A2 (en) * | 2010-06-24 | 2011-12-29 | Biousian Biosystems, Inc. | Glucagon-like peptide-1 glycopeptides |
| EP2588490B1 (en) | 2010-07-02 | 2017-02-22 | Angiochem Inc. | Short and d-amino acid-containing polypeptides for therapeutic conjugates and uses thereof |
| CN102311501A (zh) * | 2010-07-08 | 2012-01-11 | 天津药物研究院 | 含有glp-1或其类似物的融合蛋白、制备方法及其应用 |
| CN101906158B (zh) * | 2010-07-14 | 2013-10-23 | 中国药科大学 | 一种聚乙二醇化降糖多肽及其制法和用途 |
| KR101382593B1 (ko) | 2010-07-21 | 2014-04-10 | 한미사이언스 주식회사 | 신규한 지속형 글루카곤 결합체 및 이를 포함하는 비만 예방 및 치료용 약학적 조성물 |
| CN102532323B (zh) * | 2010-12-09 | 2014-07-23 | 天津药物研究院 | 一种多肽复合物、药物组合物、其制备方法和应用 |
| RS60321B1 (sr) | 2010-12-16 | 2020-07-31 | Novo Nordisk As | Čvrste kompozicije koje sadrže glp-1 agonist i so n-(8-(2- hidroksibenzoil)amino)kaprilne kiseline |
| CN102533655A (zh) * | 2010-12-21 | 2012-07-04 | 青岛黄海制药有限责任公司 | 高效表达人源重组蛋白GLP1/Fc的CHO-S细胞株及其建立方法 |
| WO2012088608A1 (en) * | 2010-12-27 | 2012-07-05 | Enobia Canada Limited Partnership | Compositions comprising natriuretic peptides and methods of use thereof |
| WO2012097333A2 (en) | 2011-01-14 | 2012-07-19 | Redwood Bioscience, Inc. | Aldehyde-tagged immunoglobulin polypeptides and method of use thereof |
| EP2682128B1 (en) | 2011-02-28 | 2017-11-08 | National Cerebral and Cardiovascular Center | Atrial natriuretic peptide or brain natriuretic peptide for use in preventing metastasis |
| JP6101638B2 (ja) | 2011-03-03 | 2017-03-22 | ザイムワークス,インコーポレイテッド | 多価ヘテロマルチマー足場設計及び構築物 |
| WO2012136790A1 (en) | 2011-04-07 | 2012-10-11 | Glaxo Group Limited | Compositions comprising fusion proteins or conjugates with an improved half -life |
| WO2012136792A2 (en) | 2011-04-07 | 2012-10-11 | Glaxo Group Limited | Cck compositions |
| DK2696687T3 (en) | 2011-04-12 | 2017-02-06 | Novo Nordisk As | Double-acylated GLP-1 derivatives |
| EP2717902B1 (en) | 2011-06-06 | 2018-01-24 | Phasebio Pharmaceuticals, Inc. | Use of modified vasoactive intestinal peptides in the treatment of hypertension |
| IN2013MN02442A (enExample) * | 2011-06-28 | 2015-06-12 | Inhibrx Llc | |
| US10400029B2 (en) | 2011-06-28 | 2019-09-03 | Inhibrx, Lp | Serpin fusion polypeptides and methods of use thereof |
| CA2839619C (en) | 2011-06-28 | 2021-11-16 | Inhibrx Llc | Serpin fusion polypeptides and methods of use thereof |
| WO2013004607A1 (en) | 2011-07-01 | 2013-01-10 | Bayer Intellectual Property Gmbh | Relaxin fusion polypeptides and uses thereof |
| MX2014000316A (es) | 2011-07-08 | 2014-02-19 | Bayer Ip Gmbh | Proteinas de fusion liberadoras de relaxina y usos de las mismas. |
| JP6038795B2 (ja) | 2011-08-19 | 2016-12-07 | 国立研究開発法人国立循環器病研究センター | ナトリウム利尿ペプチド受容体gc−aアゴニスト及びgc−bアゴニストを組み合わせてなる悪性腫瘍の増悪防止用医薬 |
| CN103765213B (zh) * | 2011-08-25 | 2016-08-17 | 美迪恩斯生命科技株式会社 | 胰高血糖素样肽-1的测定法及其中使用的试剂盒 |
| US9758560B2 (en) | 2011-09-06 | 2017-09-12 | Novo Nordisk A/S | GLP-1 derivatives |
| KR20130049671A (ko) | 2011-11-04 | 2013-05-14 | 한미사이언스 주식회사 | 생리활성 폴리펩타이드 결합체 제조 방법 |
| EP2780364A2 (en) | 2011-11-18 | 2014-09-24 | Eleven Biotherapeutics, Inc. | Proteins with improved half-life and other properties |
| WO2013083826A2 (en) | 2011-12-09 | 2013-06-13 | Novo Nordisk A/S | Glp-1 agonists |
| KR101895047B1 (ko) * | 2011-12-30 | 2018-09-06 | 한미사이언스 주식회사 | 면역글로불린 단편을 이용한 위치 특이적 글루카곤 유사 펩타이드-2 약물 결합체 |
| CN104204218A (zh) | 2012-01-26 | 2014-12-10 | 安姆根有限公司 | 生长分化因子15 (gdf-15)多肽 |
| AR090281A1 (es) | 2012-03-08 | 2014-10-29 | Hanmi Science Co Ltd | Proceso mejorado para la preparacion de un complejo polipeptidico fisiologicamente activo |
| WO2013135896A1 (en) | 2012-03-16 | 2013-09-19 | Novozymes Biopharma Dk A/S | Albumin variants |
| PL2827885T3 (pl) | 2012-03-22 | 2019-01-31 | Novo Nordisk A/S | Kompozycje peptydów GLP-1 i ich otrzymywanie |
| HUE042757T2 (hu) | 2012-03-22 | 2019-07-29 | Novo Nordisk As | Szállító szert tartalmazó készítmények és elõállításuk |
| PE20142405A1 (es) | 2012-04-19 | 2015-01-25 | Opko Biolog Ltd | Variantes de oxintomodulina de accion prolongada y metodos de produccion de las mismas |
| CA2873536A1 (en) | 2012-05-16 | 2013-11-21 | Glaxo Group Limited | Polypeptide loaded poca nanoparticles for oral administration |
| CN108524919A (zh) | 2012-05-17 | 2018-09-14 | 延伸生物科学股份有限公司 | 用于改进的药物递送的载体 |
| US10052366B2 (en) | 2012-05-21 | 2018-08-21 | Alexion Pharmaceuticsl, Inc. | Compositions comprising alkaline phosphatase and/or natriuretic peptide and methods of use thereof |
| CA2869786A1 (en) | 2012-06-08 | 2013-12-12 | Alkermes, Inc. | Fusion polypeptides comprising mucin-domain polypeptide linkers |
| WO2013189988A1 (en) | 2012-06-20 | 2013-12-27 | Novo Nordisk A/S | Tablet formulation comprising a peptide and a delivery agent |
| WO2014012082A2 (en) | 2012-07-13 | 2014-01-16 | Zymeworks Inc. | Multivalent heteromultimer scaffold design an constructs |
| AR091902A1 (es) | 2012-07-25 | 2015-03-11 | Hanmi Pharm Ind Co Ltd | Formulacion liquida de un conjugado de insulina de accion prolongada |
| AR094821A1 (es) * | 2012-07-25 | 2015-09-02 | Hanmi Pharm Ind Co Ltd | Formulación líquida de un conjugado de péptido insulinotrópico de acción prolongada |
| AR092862A1 (es) * | 2012-07-25 | 2015-05-06 | Hanmi Pharm Ind Co Ltd | Formulacion liquida de insulina de accion prolongada y un peptido insulinotropico y metodo de preparacion |
| UA116217C2 (uk) | 2012-10-09 | 2018-02-26 | Санофі | Пептидна сполука як подвійний агоніст рецепторів glp1-1 та глюкагону |
| RU2670063C2 (ru) | 2012-11-08 | 2018-10-17 | Альбумедикс А/С | Варианты альбумина |
| EP2922867B1 (en) | 2012-11-20 | 2021-07-21 | OPKO Biologics Ltd. | Method of increasing the hydrodynamic volume of polypeptides by attaching to gonadotrophin carboxy terminal peptides |
| WO2014089354A1 (en) | 2012-12-07 | 2014-06-12 | The Regents Of The University Of California | Cd138-targeted interferon demonstrates potent apoptotic and anti-tumor activities |
| HRP20181300T1 (hr) | 2012-12-21 | 2018-10-05 | Sanofi | Derivati eksendina-4 kao dvostruki glp1/gip- ili trostruki glp1/gip/glukagon agonisti |
| MX2015009141A (es) | 2013-01-15 | 2016-03-16 | Teva Pharma | Formulaciones de albu-bche, preparacion y usos de las mismas. |
| US11045523B2 (en) | 2013-04-05 | 2021-06-29 | Novo Nordisk Healthcare Ag | Formulation of growth hormone albumin-binder conjugate |
| KR20210086717A (ko) | 2013-05-02 | 2021-07-08 | 노보 노르디스크 에이/에스 | Glp-1 화합물의 경구 투여 |
| WO2014194100A1 (en) | 2013-05-29 | 2014-12-04 | The Regents Of The University Of California | Anti-cspg4 fusions with interferon for the treatment of malignancy |
| CN104277112B (zh) * | 2013-07-04 | 2018-01-26 | 嘉和生物药业有限公司 | 长效降血糖融合蛋白 |
| CN105980400B (zh) * | 2013-07-31 | 2021-05-07 | 美国安进公司 | 生长分化因子15(gdf-15)构建体 |
| CN103408669B (zh) * | 2013-08-01 | 2016-01-20 | 江苏泰康生物医药有限公司 | Glp-1类似物融合蛋白,及其制备方法和用途 |
| CN104371019B (zh) | 2013-08-13 | 2019-09-10 | 鸿运华宁(杭州)生物医药有限公司 | 一种能与glp-1r特异性结合的抗体及其与glp-1的融合蛋白质 |
| HK1226084A1 (zh) * | 2013-08-16 | 2017-09-22 | Medimmune Limited | 用於治疗糖尿病的gip和glp-1受体双重激动剂 |
| WO2015054427A1 (en) | 2013-10-10 | 2015-04-16 | Beth Israel Deaconess Medical Center, Inc. | Tm4sf1 binding proteins and methods of using same |
| US20150158926A1 (en) | 2013-10-21 | 2015-06-11 | Opko Biologics, Ltd. | Long-acting polypeptides and methods of producing and administering same |
| EP3080156A1 (en) * | 2013-12-10 | 2016-10-19 | F. Hoffmann-La Roche AG | Use of the binding domain of a subunit of a multi-subunit structure for targeted delivery of pharmaceutically active entities to the multi-subunit structure |
| EP3080154B1 (en) | 2013-12-13 | 2018-02-07 | Sanofi | Dual glp-1/gip receptor agonists |
| WO2015086728A1 (en) | 2013-12-13 | 2015-06-18 | Sanofi | Exendin-4 peptide analogues as dual glp-1/gip receptor agonists |
| EP3080149A1 (en) | 2013-12-13 | 2016-10-19 | Sanofi | Dual glp-1/glucagon receptor agonists |
| TW201609796A (zh) | 2013-12-13 | 2016-03-16 | 賽諾菲公司 | 非醯化之艾塞那肽-4(exendin-4)胜肽類似物 |
| SG11201608120TA (en) * | 2014-03-31 | 2016-11-29 | Hanmi Pharm Ind Co Ltd | Method for improving solubility of protein and peptide by using immunoglobulin fc fragment linkage |
| TW201625670A (zh) | 2014-04-07 | 2016-07-16 | 賽諾菲公司 | 衍生自exendin-4之雙重glp-1/升糖素受體促效劑 |
| TW201625669A (zh) | 2014-04-07 | 2016-07-16 | 賽諾菲公司 | 衍生自艾塞那肽-4(Exendin-4)之肽類雙重GLP-1/升糖素受體促效劑 |
| TW201625668A (zh) | 2014-04-07 | 2016-07-16 | 賽諾菲公司 | 作為胜肽性雙重glp-1/昇糖素受體激動劑之艾塞那肽-4衍生物 |
| NO2776305T3 (enExample) * | 2014-04-23 | 2018-01-27 | ||
| WO2015165480A1 (en) | 2014-04-30 | 2015-11-05 | Institute For Research In Biomedicine | Human cytomegalovirus vaccine compositions and method of producing the same |
| ES2818824T3 (es) | 2014-05-08 | 2021-04-14 | Phasebio Pharmaceuticals Inc | Composiciones que comprenden una proteína de fusión de VIP-ELP para su uso en el tratamiento de fibrosis quística |
| US9932381B2 (en) | 2014-06-18 | 2018-04-03 | Sanofi | Exendin-4 derivatives as selective glucagon receptor agonists |
| WO2016007873A1 (en) | 2014-07-11 | 2016-01-14 | The Regents Of The University Of Michigan | Compositions and methods for treating craniosynostosis |
| CN104558198A (zh) * | 2014-07-25 | 2015-04-29 | 成都贝爱特生物科技有限公司 | GLP-1类似物和amylin类似物的融合蛋白制备及其用途 |
| CN104257696B (zh) * | 2014-09-04 | 2017-08-25 | 西安国誉生物科技有限公司 | 一种降糖稳糖酵母菌粉及其制备方法和应用 |
| ES2685987T3 (es) | 2014-09-05 | 2018-10-15 | University Of Copenhagen | Análogos de péptidos gip |
| CN107108713A (zh) * | 2014-10-10 | 2017-08-29 | 诺和诺德股份有限公司 | 稳定的基于glp‑1的glp‑1/胰高血糖素受体共激动剂 |
| CN104327187B (zh) * | 2014-10-11 | 2018-06-08 | 上海兴迪金生物技术有限公司 | 一种重组人GLP-1-Fc融合蛋白 |
| US9616109B2 (en) | 2014-10-22 | 2017-04-11 | Extend Biosciences, Inc. | Insulin vitamin D conjugates |
| US9789197B2 (en) | 2014-10-22 | 2017-10-17 | Extend Biosciences, Inc. | RNAi vitamin D conjugates |
| WO2016065042A1 (en) | 2014-10-22 | 2016-04-28 | Extend Biosciences, Inc. | Therapeutic vitamin d conjugates |
| CN107207597A (zh) * | 2014-11-06 | 2017-09-26 | 儿研所儿童医学中心 | 用于癌症和自身免疫疾病的免疫疗法 |
| BR112017011900A2 (pt) | 2014-12-05 | 2018-02-27 | Alexion Pharma Inc | tratamento de ataques com fosfatase alcalina recombinante |
| CN107108718B (zh) * | 2014-12-08 | 2022-07-22 | 北京强新生物科技有限公司 | 可溶性通用的增强adcc的合成融合基因和融合肽的技术及其应用 |
| PH12017501089B1 (en) | 2014-12-10 | 2022-06-22 | Opko Biologics Ltd | Methods of producing long acting ctp-modified growth hormone polypeptides |
| WO2016118577A1 (en) * | 2015-01-22 | 2016-07-28 | Medimmune, Llc | Thymosin-beta-four fusion proteins |
| CA2973883A1 (en) | 2015-01-28 | 2016-08-04 | Alexion Pharmaceuticals, Inc. | Methods of treating a subject with an alkaline phosphatase deficiency |
| CN114652817A (zh) | 2015-02-09 | 2022-06-24 | 费斯生物制药公司 | 用于治疗肌肉疾病和病症的方法和组合物 |
| AU2016218759B2 (en) | 2015-02-11 | 2021-11-25 | Gmax Biopharm Llc. | Stabilized solution preparation of pharmaceutical GLP-1R antibody fusion protein |
| CA2981517A1 (en) * | 2015-04-01 | 2016-10-06 | The Scripps Research Institute | Methods and compositions related to gpcr agonist polypeptides |
| MX2017012966A (es) | 2015-04-10 | 2018-06-06 | Amgen Inc | Muteinas de interleuquina 2 para la expansion de celulas t regulatorias. |
| AR105616A1 (es) | 2015-05-07 | 2017-10-25 | Lilly Co Eli | Proteínas de fusión |
| AR105319A1 (es) | 2015-06-05 | 2017-09-27 | Sanofi Sa | Profármacos que comprenden un conjugado agonista dual de glp-1 / glucagón conector ácido hialurónico |
| CN107921143B (zh) | 2015-06-15 | 2021-11-19 | 安吉奥开米公司 | 用于治疗软脑膜癌病的方法 |
| AU2016280867B2 (en) | 2015-06-19 | 2020-02-27 | Opko Biologics Ltd. | Long-acting coagulation factors and methods of producing same |
| AR105284A1 (es) | 2015-07-10 | 2017-09-20 | Sanofi Sa | Derivados de exendina-4 como agonistas peptídicos duales específicos de los receptores de glp-1 / glucagón |
| AU2016308624B2 (en) | 2015-08-17 | 2022-06-23 | Alexion Pharmaceuticals, Inc. | Manufacturing of alkaline phosphatases |
| EP3337816B1 (en) | 2015-08-20 | 2024-02-14 | Albumedix Ltd | Albumin variants and conjugates |
| JP6951825B2 (ja) | 2015-09-04 | 2021-10-20 | ザ スクリプス リサーチ インスティテュート | インスリン免疫グロブリン融合タンパク質 |
| JP6868617B2 (ja) | 2015-09-28 | 2021-05-12 | アレクシオン ファーマシューティカルズ, インコーポレイテッド | 低ホスファターゼ血症の組織非特異的アルカリホスファターゼ(tnsalp)酵素補充療法に有効な投薬計画の特定 |
| WO2017074466A1 (en) | 2015-10-30 | 2017-05-04 | Alexion Pharmaceuticals, Inc. | Methods for treating craniosynostosis in a patient |
| CN105367664B (zh) * | 2015-11-04 | 2019-09-20 | 成都贝爱特生物科技有限公司 | 激活GLP-1受体和Amylin受体双功能作用的融合蛋白制备及其用途 |
| CA3071494C (en) | 2015-11-24 | 2021-12-14 | Transfert Plus, S.E.C. | Peptide compounds and peptide conjugates for the treatment of cancer through receptor-mediated chemotherapy |
| US11065306B2 (en) | 2016-03-08 | 2021-07-20 | Alexion Pharmaceuticals, Inc. | Methods for treating hypophosphatasia in children |
| US11186832B2 (en) | 2016-04-01 | 2021-11-30 | Alexion Pharmaceuticals, Inc. | Treating muscle weakness with alkaline phosphatases |
| WO2017173395A1 (en) | 2016-04-01 | 2017-10-05 | Alexion Pharmaceuticals, Inc. | Methods for treating hypophosphatasia in adolescents and adults |
| JP2019515677A (ja) | 2016-04-26 | 2019-06-13 | アール.ピー.シェーラー テクノロジーズ エルエルシー | 抗体複合体ならびにそれを作製および使用する方法 |
| US10988744B2 (en) | 2016-06-06 | 2021-04-27 | Alexion Pharmaceuticals, Inc. | Method of producing alkaline phosphatase |
| KR102618424B1 (ko) | 2016-07-11 | 2023-12-26 | 옵코 바이오로직스 리미티드 | 지속성 응고 인자 vii 및 그 제조 방법 |
| CN106046176B (zh) | 2016-08-16 | 2019-09-10 | 中国药科大学 | 一种高活性长效降糖融合蛋白及其制备方法与医药用途 |
| JP7018933B2 (ja) | 2016-08-18 | 2022-02-14 | アレクシオン ファーマシューティカルズ, インコーポレイテッド | 気管気管支軟化症の治療方法 |
| WO2018112282A1 (en) | 2016-12-14 | 2018-06-21 | Ligandal, Inc. | Compositions and methods for nucleic acid and/or protein payload delivery |
| CN107033234B (zh) * | 2017-01-03 | 2018-06-26 | 北京凯因科技股份有限公司 | 酰化的glp-1衍生物 |
| JP2020505029A (ja) * | 2017-01-25 | 2020-02-20 | メディミューン,エルエルシー | リラキシン融合ポリペプチドおよびその使用 |
| CN110719786A (zh) | 2017-03-31 | 2020-01-21 | 阿雷克森制药公司 | 用于治疗成人和青少年的低磷酸酯酶症(hpp)的方法 |
| CN108727486A (zh) * | 2017-04-24 | 2018-11-02 | 舒泰神(北京)生物制药股份有限公司 | 长效神经生长因子、制备方法及其组合物 |
| US20200157151A1 (en) | 2017-05-24 | 2020-05-21 | Transfert Plus, S.E.C. | Peptide compounds, conjugate compounds and uses thereof for treating inflammatory diseases |
| JP2020521784A (ja) | 2017-05-31 | 2020-07-27 | ユニバーシティ オブ コペンハーゲン | 長時間作用性gipペプチド類似体 |
| MX2020001525A (es) | 2017-08-24 | 2020-03-20 | Novo Nordisk As | Composiciones de peptido similar al glucagon tipo 1 (glp-1) y sus usos. |
| WO2019067499A1 (en) | 2017-09-27 | 2019-04-04 | Alexion Pharmaceuticals, Inc. | BIOMARKER SIGNATURE FOR PREDICTING A TUMOR RESPONSE TO ANTI-CD200 THERAPY |
| EA202090971A1 (ru) | 2017-11-21 | 2020-08-07 | Эли Лилли Энд Компани | Способы применения и композиции, содержащие дулаглутид |
| CN115109166B (zh) * | 2017-11-24 | 2025-07-18 | 浙江道尔生物科技有限公司 | 一种治疗代谢疾病的多结构域活性蛋白 |
| CN113603794B (zh) * | 2018-01-11 | 2024-01-16 | 安源医药科技(上海)有限公司 | 用于调节血糖和脂质的增效型双功能蛋白 |
| WO2019140021A1 (en) | 2018-01-12 | 2019-07-18 | Eli Lilly And Company | Combination therapy |
| CN110092835A (zh) * | 2018-01-30 | 2019-08-06 | 上海惠盾生物技术有限公司 | 一种glp-1类似物-col3a1融合蛋白 |
| CN111683676B (zh) | 2018-02-02 | 2024-06-18 | 诺和诺德股份有限公司 | 包含glp-1激动剂、n-(8-(2-羟基苯甲酰基)氨基)辛酸的盐和润滑剂的固体组合物 |
| US11913039B2 (en) | 2018-03-30 | 2024-02-27 | Alexion Pharmaceuticals, Inc. | Method for producing recombinant alkaline phosphatase |
| KR20250065720A (ko) | 2018-04-05 | 2025-05-13 | 썬 파마슈티칼 인더스트리스 리미티드 | 신규한 glp-1 유사체 |
| MX2020010659A (es) | 2018-04-09 | 2020-10-28 | Amgen Inc | Proteinas de fusion del factor de diferenciacion de crecimiento 15. |
| WO2019200594A1 (zh) | 2018-04-19 | 2019-10-24 | 杭州先为达生物科技有限公司 | 酰化的glp-1衍生物 |
| EP3833377B1 (en) | 2018-08-10 | 2023-11-22 | Alexion Pharmaceuticals, Inc. | Bone healing at implants using alkaline phosphatase |
| MY205905A (en) | 2018-10-22 | 2024-11-20 | Janssen Pharmaceutica Nv | Glucagon like peptide 1 (glp1)-growth differentiation factor 15 (gdf15) fusion proteins and uses thereof |
| CA3114803A1 (en) * | 2018-10-24 | 2020-04-30 | Shire-Nps Pharmaceuticals, Inc. | Glp-2 fusion polypeptides and uses for treating and preventing gastrointestinal conditions |
| US12297250B2 (en) | 2018-12-03 | 2025-05-13 | Antag Therapeutics Aps | Modified GIP peptide analogues |
| WO2020118843A1 (zh) * | 2018-12-12 | 2020-06-18 | 四川利通科创生物医药科技有限公司 | 一种glp-1突变体及其制备方法和用途 |
| TW202024134A (zh) | 2018-12-21 | 2020-07-01 | 大陸商江蘇恆瑞醫藥股份有限公司 | 雙特異性蛋白 |
| CA3177693A1 (en) | 2019-04-05 | 2020-10-05 | Eli Lilly And Company | Therapeutic uses of dulaglutide |
| EP4065585B1 (en) | 2019-11-25 | 2025-08-20 | Alkermes, Inc. | Substituted macrocyclic compounds and related methods of treatment |
| MX2022007114A (es) | 2019-12-09 | 2022-07-11 | Alexion Pharma Inc | Polipeptidos de fosfatasa alcalina y metodos de uso de los mismos. |
| IL294520A (en) | 2020-02-18 | 2022-09-01 | Novo Nordisk As | Pharmaceutical formulations |
| JPWO2021167107A1 (enExample) | 2020-02-22 | 2021-08-26 | ||
| CA3190396A1 (en) * | 2020-08-24 | 2022-03-03 | James M. Wilson | Viral vectors encoding glp-1 receptor agonist fusions and uses thereof in treating metabolic diseases in felines |
| US12122817B2 (en) * | 2020-09-22 | 2024-10-22 | Serpentide Inc. | Long-lasting GLP1 analogue drug for type-2 diabetes |
| US11760747B2 (en) | 2020-12-21 | 2023-09-19 | Alkermes, Inc. | Substituted piperidino compounds and related methods of treatment |
| CN114685644A (zh) * | 2020-12-29 | 2022-07-01 | 苏州康宁杰瑞生物科技有限公司 | 一种人glp-1多肽变体及其应用 |
| BR112023016048A2 (pt) | 2021-02-12 | 2023-11-14 | Alexion Pharma Inc | Polipeptídeos de fosfatase alcalina e métodos de uso dos mesmos |
| TW202305012A (zh) | 2021-03-22 | 2023-02-01 | 日商肽夢想股份有限公司 | c-Met 蛋白質結合肽複合物 |
| WO2022202816A1 (ja) | 2021-03-22 | 2022-09-29 | ペプチエイド株式会社 | ペプチド及びペプチドを含む組成物 |
| CN117440972A (zh) | 2021-03-24 | 2024-01-23 | 奥克梅斯公司 | Upar抗体和具有所述抗体的融合蛋白 |
| AU2022294601A1 (en) | 2021-06-18 | 2023-12-14 | Peptidream Inc. | Ghr-binding pending peptide and composition comprising same |
| WO2023022234A1 (ja) | 2021-08-19 | 2023-02-23 | ペプチドリーム株式会社 | ヒトトランスフェリンレセプター結合ペプチド |
| US20240390508A1 (en) | 2021-08-21 | 2024-11-28 | Takeda Pharmaceutical Company Limited | Human transferrin receptor binding peptide-drug conjugate |
| IL311025A (en) | 2021-08-24 | 2024-04-01 | Peptidream Inc | Human transferrin receptor-binding antibody-peptide conjugate |
| WO2023054712A1 (ja) | 2021-09-30 | 2023-04-06 | ペプチドリーム株式会社 | ペプチド |
| CN113801853B (zh) * | 2021-11-19 | 2022-03-15 | 山东兴瑞生物科技有限公司 | Exendin-4融合基因修饰的MSC及其应用 |
| AU2023246202A1 (en) | 2022-03-30 | 2024-10-17 | Peptidream Inc | Peptide complex having trkb binding activity |
| US20250361274A1 (en) | 2022-06-15 | 2025-11-27 | Peptidream Inc. | Peptide and peptide-containing agent |
| CN117836330A (zh) | 2022-06-23 | 2024-04-05 | 广州银诺医药集团股份有限公司 | 一种改进的glp-1受体激动剂的融合蛋白和应用 |
| IL319526A (en) | 2022-09-30 | 2025-05-01 | Extend Biosciences Inc | Long-acting parathyroid hormone |
| WO2024123812A1 (en) | 2022-12-05 | 2024-06-13 | Shattuck Labs, Inc. | Fusion proteins for the treatment of cardiometabolic diseases |
| TW202434613A (zh) | 2023-02-17 | 2024-09-01 | 日商肽夢想股份有限公司 | 人類運鐵蛋白受體結合肽 |
| TW202440649A (zh) | 2023-03-30 | 2024-10-16 | 大陸商廣州銀諾醫藥集團股份有限公司 | 一種包含glp-1 融合蛋白的藥物製劑及其用途 |
| TW202504632A (zh) | 2023-06-07 | 2025-02-01 | 日商肽夢想股份有限公司 | 靶向磷脂醯肌醇蛋白聚糖-3之肽組成物及其用途 |
Family Cites Families (32)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| GB8725529D0 (en) | 1987-10-30 | 1987-12-02 | Delta Biotechnology Ltd | Polypeptides |
| US5766883A (en) * | 1989-04-29 | 1998-06-16 | Delta Biotechnology Limited | Polypeptides |
| ATE92107T1 (de) | 1989-04-29 | 1993-08-15 | Delta Biotechnology Ltd | N-terminale fragmente von menschliches serumalbumin enthaltenden fusionsproteinen. |
| FR2650598B1 (fr) * | 1989-08-03 | 1994-06-03 | Rhone Poulenc Sante | Derives de l'albumine a fonction therapeutique |
| FR2686899B1 (fr) * | 1992-01-31 | 1995-09-01 | Rhone Poulenc Rorer Sa | Nouveaux polypeptides biologiquement actifs, leur preparation et compositions pharmaceutiques les contenant. |
| FR2686900B1 (fr) * | 1992-01-31 | 1995-07-21 | Rhone Poulenc Rorer Sa | Nouveaux polypeptides ayant une activite de stimulation des colonies de granulocytes, leur preparation et compositions pharmaceutiques les contenant. |
| CN1149887A (zh) * | 1994-04-22 | 1997-05-14 | 科里克萨有限公司 | 刺激和增强保护性免疫反应和il-12产生的化合物和方法 |
| US5990077A (en) * | 1995-04-14 | 1999-11-23 | 1149336 Ontario Inc. | Glucagon-like peptide-2 and its therapeutic use |
| US5925351A (en) * | 1995-07-21 | 1999-07-20 | Biogen, Inc. | Soluble lymphotoxin-β receptors and anti-lymphotoxin receptor and ligand antibodies as therapeutic agents for the treatment of immunological disease |
| GB9526733D0 (en) | 1995-12-30 | 1996-02-28 | Delta Biotechnology Ltd | Fusion proteins |
| US6750334B1 (en) * | 1996-02-02 | 2004-06-15 | Repligen Corporation | CTLA4-immunoglobulin fusion proteins having modified effector functions and uses therefor |
| MY120425A (en) * | 1996-07-26 | 2005-10-31 | Novartis Ag | Fusion polypeptides |
| ES2319936T5 (es) | 1996-08-08 | 2013-06-24 | Amylin Pharmaceuticals, Inc. | Regulación de la motilidad gastrointestinal |
| CZ300837B6 (cs) * | 1996-08-30 | 2009-08-26 | Novo Nordisk A/S | Deriváty GLP-1(7-37) nebo jeho analogy, farmaceutický prostredek je obsahující a jejich použití |
| UA65549C2 (uk) * | 1996-11-05 | 2004-04-15 | Елі Ліллі Енд Компані | Спосіб регулювання ожиріння шляхом периферійного введення аналогів та похідних glp-1 (варіанти) та фармацевтична композиція |
| US6190909B1 (en) * | 1997-04-17 | 2001-02-20 | Millennium Pharmaceuticals, Inc. | TH2-specific gene |
| EP0887061A1 (en) * | 1997-06-28 | 1998-12-30 | The Procter & Gamble Company | Faecal collector |
| AU749914B2 (en) | 1997-08-08 | 2002-07-04 | Amylin Pharmaceuticals, Inc. | Novel exendin agonist compounds |
| NZ504258A (en) | 1997-11-14 | 2002-12-20 | Amylin Pharmaceuticals Inc | Exendin 3 and 4 agonist compounds for the treatment of diabetes |
| EP1032587B2 (en) | 1997-11-14 | 2013-03-13 | Amylin Pharmaceuticals, Inc. | Novel exendin agonist compounds |
| DE69936446T2 (de) | 1998-02-13 | 2008-03-06 | Amylin Pharmaceuticals, Inc., San Diego | Inotropische und diuretische effekte von exendin und glp-1 |
| DE69942306D1 (de) * | 1998-02-27 | 2010-06-10 | Novo Nordisk As | Abkömmlinge von glp-1 analogen |
| EP1062240B1 (en) * | 1998-02-27 | 2010-04-28 | Novo Nordisk A/S | N-terminally modified glp-1 derivatives |
| DE69916811T2 (de) * | 1998-02-27 | 2005-04-14 | Novo Nordisk A/S | Glp-1 derivate mit einem helix-gehalt über 25 %, die partiell strukturierte mizellenartige aggregate bilden |
| WO1999043708A1 (en) | 1998-02-27 | 1999-09-02 | Novo Nordisk A/S | Glp-1 derivatives of glp-1 and exendin with protracted profile of action |
| AU775422B2 (en) * | 1998-06-15 | 2004-07-29 | Gtc Biotherapeutics, Inc. | Erythropoietin analog-human serum albumin fusion |
| AU775076B2 (en) * | 1998-12-10 | 2004-07-15 | Bristol-Myers Squibb Company | Protein scaffolds for antibody mimics and other binding proteins |
| CN1191273C (zh) * | 1999-05-17 | 2005-03-02 | 康久化学公司 | 长效促胰岛肽 |
| US6514500B1 (en) * | 1999-10-15 | 2003-02-04 | Conjuchem, Inc. | Long lasting synthetic glucagon like peptide {GLP-!} |
| AU2001261024A1 (en) | 2000-04-12 | 2001-10-30 | Delta Biotechnology Limited | Albumin fusion proteins |
| EP2277910A1 (en) | 2001-12-21 | 2011-01-26 | Human Genome Sciences, Inc. | Albumin fusion proteins |
| EP1463752A4 (en) | 2001-12-21 | 2005-07-13 | Human Genome Sciences Inc | ALBUMIN FUSION PROTEINS |
-
2001
- 2001-11-29 MX MXPA03005036A patent/MXPA03005036A/es active IP Right Grant
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- 2001-11-29 EA EA200300644A patent/EA005584B1/ru not_active IP Right Cessation
- 2001-11-29 SI SI200130878T patent/SI1355942T1/sl unknown
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