MXPA06009072A - Proteinas de fusion de albumina. - Google Patents
Proteinas de fusion de albumina.Info
- Publication number
- MXPA06009072A MXPA06009072A MXPA06009072A MXPA06009072A MXPA06009072A MX PA06009072 A MXPA06009072 A MX PA06009072A MX PA06009072 A MXPA06009072 A MX PA06009072A MX PA06009072 A MXPA06009072 A MX PA06009072A MX PA06009072 A MXPA06009072 A MX PA06009072A
- Authority
- MX
- Mexico
- Prior art keywords
- fragment
- variant
- protein
- albumin
- albumin fusion
- Prior art date
Links
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Classifications
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- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K19/00—Hybrid peptides, i.e. peptides covalently bound to nucleic acids, or non-covalently bound protein-protein complexes
-
- 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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- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P3/00—Drugs for disorders of the metabolism
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- A—HUMAN NECESSITIES
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- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P31/00—Antiinfectives, i.e. antibiotics, antiseptics, chemotherapeutics
- A61P31/04—Antibacterial agents
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- A—HUMAN NECESSITIES
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- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
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- A61P37/00—Drugs for immunological or allergic disorders
- A61P37/02—Immunomodulators
- A61P37/06—Immunosuppressants, e.g. drugs for graft rejection
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- A61P37/00—Drugs for immunological or allergic disorders
- A61P37/08—Antiallergic agents
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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
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- A—HUMAN NECESSITIES
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- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P5/00—Drugs for disorders of the endocrine system
-
- 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
- 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
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61K—PREPARATIONS FOR MEDICAL, DENTAL OR TOILETRY PURPOSES
- A61K38/00—Medicinal preparations containing peptides
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K2319/00—Fusion polypeptide
- C07K2319/31—Fusion polypeptide fusions, other than Fc, for prolonged plasma life, e.g. albumin
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K2319/00—Fusion polypeptide
- C07K2319/35—Fusion polypeptide containing a fusion for enhanced stability/folding during expression, e.g. fusions with chaperones or thioredoxin
Landscapes
- Health & Medical Sciences (AREA)
- Life Sciences & Earth Sciences (AREA)
- Chemical & Material Sciences (AREA)
- Organic Chemistry (AREA)
- Genetics & Genomics (AREA)
- Engineering & Computer Science (AREA)
- General Health & Medical Sciences (AREA)
- Medicinal Chemistry (AREA)
- Bioinformatics & Cheminformatics (AREA)
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- Veterinary Medicine (AREA)
- Nuclear Medicine, Radiotherapy & Molecular Imaging (AREA)
- Pharmacology & Pharmacy (AREA)
- Public Health (AREA)
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- Chemical Kinetics & Catalysis (AREA)
- General Chemical & Material Sciences (AREA)
- Biochemistry (AREA)
- Zoology (AREA)
- Biophysics (AREA)
- Biomedical Technology (AREA)
- Immunology (AREA)
- Wood Science & Technology (AREA)
- General Engineering & Computer Science (AREA)
- Biotechnology (AREA)
- Proteomics, Peptides & Aminoacids (AREA)
- Toxicology (AREA)
- Gastroenterology & Hepatology (AREA)
- Microbiology (AREA)
- Oncology (AREA)
- Diabetes (AREA)
- Physics & Mathematics (AREA)
- Plant Pathology (AREA)
- Communicable Diseases (AREA)
- Endocrinology (AREA)
- Hematology (AREA)
- Pulmonology (AREA)
- Obesity (AREA)
- Virology (AREA)
- Transplantation (AREA)
Applications Claiming Priority (5)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| US54227404P | 2004-02-09 | 2004-02-09 | |
| US54990104P | 2004-03-05 | 2004-03-05 | |
| US55690604P | 2004-03-29 | 2004-03-29 | |
| US63660304P | 2004-12-17 | 2004-12-17 | |
| PCT/US2005/004041 WO2005077042A2 (en) | 2004-02-09 | 2005-02-09 | Albumin fusion proteins |
Publications (1)
| Publication Number | Publication Date |
|---|---|
| MXPA06009072A true MXPA06009072A (es) | 2007-03-29 |
Family
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Family Applications (1)
| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| MXPA06009072A MXPA06009072A (es) | 2004-02-09 | 2005-02-09 | Proteinas de fusion de albumina. |
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| Country | Link |
|---|---|
| US (3) | US7569384B2 (https=) |
| EP (1) | EP1729795B1 (https=) |
| JP (2) | JP5010923B2 (https=) |
| KR (1) | KR101184391B1 (https=) |
| CN (1) | CN102816241B (https=) |
| AU (2) | AU2005211725B2 (https=) |
| BR (1) | BRPI0507026A (https=) |
| CA (1) | CA2554089C (https=) |
| CY (1) | CY1117401T1 (https=) |
| DK (1) | DK1729795T3 (https=) |
| ES (1) | ES2567634T3 (https=) |
| HU (1) | HUE027902T2 (https=) |
| IL (1) | IL176894A (https=) |
| MA (1) | MA28565B1 (https=) |
| MX (1) | MXPA06009072A (https=) |
| NO (1) | NO20064059L (https=) |
| NZ (1) | NZ548612A (https=) |
| PL (1) | PL1729795T3 (https=) |
| SI (1) | SI1729795T1 (https=) |
| WO (1) | WO2005077042A2 (https=) |
Families Citing this family (208)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| GB9526733D0 (en) | 1995-12-30 | 1996-02-28 | Delta Biotechnology Ltd | Fusion proteins |
| US20050100991A1 (en) * | 2001-04-12 | 2005-05-12 | Human Genome Sciences, Inc. | Albumin fusion proteins |
| EP2213743A1 (en) | 2000-04-12 | 2010-08-04 | Human Genome Sciences, Inc. | Albumin fusion proteins |
| WO2005003296A2 (en) | 2003-01-22 | 2005-01-13 | Human Genome Sciences, Inc. | Albumin fusion proteins |
| AU2002364586A1 (en) | 2001-12-21 | 2003-07-30 | Delta Biotechnology Limited | Albumin fusion proteins |
| WO2003059934A2 (en) | 2001-12-21 | 2003-07-24 | Human Genome Sciences, Inc. | Albumin fusion proteins |
| US20080194481A1 (en) | 2001-12-21 | 2008-08-14 | Human Genome Sciences, Inc. | Albumin Fusion Proteins |
| US20060002935A1 (en) | 2002-06-28 | 2006-01-05 | Domantis Limited | Tumor Necrosis Factor Receptor 1 antagonists and methods of use therefor |
| WO2004096113A2 (en) * | 2003-04-28 | 2004-11-11 | Medical Instill Technologies, Inc. | Container with valve assembly for filling and dispensing substances, and apparatus and method for filling |
| HUE027902T2 (en) * | 2004-02-09 | 2016-11-28 | Human Genome Sciences Inc Corp Service Company | Albumin fusion proteins |
| EP2371390A3 (en) | 2004-10-08 | 2013-03-13 | Domantis Limited | Antagonists and methods of use therefor |
| WO2007021494A2 (en) * | 2005-08-12 | 2007-02-22 | Human Genome Sciences, Inc. | Albumin fusion proteins |
| US7846445B2 (en) * | 2005-09-27 | 2010-12-07 | Amunix Operating, Inc. | Methods for production of unstructured recombinant polymers and uses thereof |
| US7855279B2 (en) | 2005-09-27 | 2010-12-21 | Amunix Operating, Inc. | Unstructured recombinant polymers and uses thereof |
| JP2009509535A (ja) * | 2005-09-27 | 2009-03-12 | アムニクス， インコーポレイテッド | タンパク様薬剤およびその使用 |
| US20090099031A1 (en) * | 2005-09-27 | 2009-04-16 | Stemmer Willem P | Genetic package and uses thereof |
| US8202837B2 (en) * | 2005-11-04 | 2012-06-19 | Glaxosmithkline Llc | Methods for administering hypoglycemic agents |
| US20080280328A1 (en) * | 2005-11-18 | 2008-11-13 | Novozymes A/S | Glucoamylase Variants |
| EP1816201A1 (en) | 2006-02-06 | 2007-08-08 | CSL Behring GmbH | Modified coagulation factor VIIa with extended half-life |
| EP2007789B1 (en) | 2006-04-11 | 2015-05-20 | Novartis AG | Spirocyclic HCV/HIV inhibitors and their uses |
| WO2007127286A2 (en) | 2006-04-24 | 2007-11-08 | Medical Instill Technologies, Inc. | Needle penetrable and laser resealable lyophilization device and related method |
| WO2007146038A2 (en) * | 2006-06-07 | 2007-12-21 | Human Genome Sciences, Inc. | Albumin fusion proteins |
| TWI430806B (zh) * | 2006-09-13 | 2014-03-21 | Smithkline Beecham Corp | 用於投與長效降血糖藥劑之方法 |
| WO2008033413A2 (en) * | 2006-09-14 | 2008-03-20 | Human Genome Sciences, Inc. | Albumin fusion proteins |
| WO2008052043A2 (en) * | 2006-10-24 | 2008-05-02 | Cogenesys, Inc. | Opioid receptor agonist fusion proteins |
| MX2009005466A (es) | 2006-11-22 | 2009-08-17 | Adnexus A Bristol Myers Sqibb | Terapeuticos dirigidos a base de proteinas manipuladas para receptores de tirosina cinasas, incluyendo receptor de factor de crecimiento tipo insulina-i. |
| EP2450368A1 (en) | 2007-01-30 | 2012-05-09 | Epivax, Inc. | Regulatory t cell epitopes, compositions and uses thereof |
| EP2111228B1 (en) | 2007-02-02 | 2011-07-20 | Bristol-Myers Squibb Company | 10Fn3 domain for use in treating diseases associated with inappropriate angiogenesis |
| CA2688433A1 (en) | 2007-06-06 | 2008-12-11 | Domantis Limited | Methods for selecting protease resistant polypeptides |
| RU2361607C2 (ru) * | 2007-06-09 | 2009-07-20 | Государственное образовательное учреждение высшего профессионального образования "Челябинская государственная медицинская академия Федерального агентства по здравоохранению и социальному развитию Российской Федерации" | Способ локальной иммунотерапии гнойно-воспалительных заболеваний мягких тканей челюстно-лицевой области |
| US20100268055A1 (en) * | 2007-07-19 | 2010-10-21 | Arizona Board of Regents, a body corporate acting for and on behalf of Arizona State University | Self-Anchoring MEMS Intrafascicular Neural Electrode |
| JP2010536341A (ja) * | 2007-08-15 | 2010-12-02 | アムニクス， インコーポレイテッド | 生物学的に活性なポリペプチドの特性を改変するための組成物および方法 |
| CN101801460A (zh) * | 2007-09-05 | 2010-08-11 | 塞诺菲-安万特股份有限公司 | 尿酸氧化酶用于治疗或预防由局部缺血或再灌注事件引起的心脏疾病或间接后遗症的用途 |
| EP2050764A1 (en) | 2007-10-15 | 2009-04-22 | sanofi-aventis | Novel polyvalent bispecific antibody format and uses thereof |
| GB0723712D0 (en) * | 2007-12-04 | 2008-01-16 | Apitope Technology Bristol Ltd | Peptides |
| EP2072527A1 (en) | 2007-12-21 | 2009-06-24 | Altonabiotec AG | Fusion polypeptides comprising a SHBG dimerization component and uses thereof |
| US20110009497A1 (en) * | 2008-03-21 | 2011-01-13 | Fujifilm Corporation | Drug-containing composition |
| WO2009142773A2 (en) | 2008-05-22 | 2009-11-26 | Bristol-Myers Squibb Company | Multivalent fibronectin based scaffold domain proteins |
| US20110300127A1 (en) * | 2008-05-27 | 2011-12-08 | Fujifilm Corporation | Drug-containing composition |
| PT2373681T (pt) | 2008-12-10 | 2017-04-11 | Glaxosmithkline Llc | Composições farmacêuticas de albiglutida |
| US8680050B2 (en) * | 2009-02-03 | 2014-03-25 | Amunix Operating Inc. | Growth hormone polypeptides fused to extended recombinant polypeptides and methods of making and using same |
| ES2610356T3 (es) | 2009-02-03 | 2017-04-27 | Amunix Operating Inc. | Polipéptidos recombinantes extendidos y composiciones que comprenden los mismos |
| US8703717B2 (en) * | 2009-02-03 | 2014-04-22 | Amunix Operating Inc. | Growth hormone polypeptides and methods of making and using same |
| KR101722961B1 (ko) | 2009-02-11 | 2017-04-04 | 알부메딕스 에이/에스 | 알부민 변이체 및 접합체 |
| AU2010215479B2 (en) | 2009-02-19 | 2015-01-22 | Glaxo Group Limited | Improved anti-TNFR1 polypeptides, antibody variable domains & antagonists |
| EP2419120A4 (en) * | 2009-04-08 | 2016-01-06 | Univ California | HUMAN PROTEIN CONCERNS WITH CONTROLLED SERUM PHARMACOKINETICS |
| US20110182850A1 (en) | 2009-04-10 | 2011-07-28 | Trixi Brandl | Organic compounds and their uses |
| US8512690B2 (en) | 2009-04-10 | 2013-08-20 | Novartis Ag | Derivatised proline containing peptide compounds as protease inhibitors |
| KR101286721B1 (ko) * | 2009-06-05 | 2013-07-16 | 한국과학기술연구원 | 폴리-시스테인 펩티드 융합 재조합 알부민 및 이의 제조방법 |
| US9849188B2 (en) | 2009-06-08 | 2017-12-26 | Amunix Operating Inc. | Growth hormone polypeptides and methods of making and using same |
| WO2010144508A1 (en) * | 2009-06-08 | 2010-12-16 | Amunix Operating Inc. | Glucose-regulating polypeptides and methods of making and using same |
| JP2012532619A (ja) | 2009-07-16 | 2012-12-20 | グラクソ グループ リミテッド | Ｔｎｆｒ１を部分的に阻害するためのアンタゴニスト、用途および方法 |
| KR20120063475A (ko) | 2009-07-29 | 2012-06-15 | 글락소 그룹 리미티드 | 항-ｔｇｆ-베타 수용체 타입 ⅱ 단일 도메인 항체 |
| CA2771999A1 (en) | 2009-08-24 | 2011-03-10 | Amunix Operating Inc. | Coagulation factor vii compositions and methods of making and using same |
| JP2013507978A (ja) | 2009-10-27 | 2013-03-07 | グラクソ グループ リミテッド | 安定な抗ｔｎｆｒ１ポリペプチド、抗体可変ドメイン及びアンタゴニスト |
| EP2493921B1 (en) | 2009-10-30 | 2018-09-26 | Albumedix Ltd | Albumin variants |
| EA201200650A1 (ru) | 2009-10-30 | 2012-12-28 | Бёрингер Ингельхайм Интернациональ Гмбх | Курсы комбинированного лечения вируса гепатита с, включающие bi201335, интерферон-альфа и рибавирин |
| US20120308517A1 (en) | 2010-02-09 | 2012-12-06 | Digna Biotech, S.L. | Compositions for the treatment of infectious and tumoural diseases |
| JP2013520426A (ja) | 2010-02-18 | 2013-06-06 | ブリストル−マイヤーズ スクイブ カンパニー | Ｉｌ−２３に結合する、フィブロネクチンをベースとする足場ドメインタンパク質 |
| US8557961B2 (en) | 2010-04-02 | 2013-10-15 | Amunix Operating Inc. | Alpha 1-antitrypsin compositions and methods of making and using same |
| EP2556087A1 (en) | 2010-04-09 | 2013-02-13 | Novozymes Biopharma DK A/S | Albumin derivatives and variants |
| EP2558491B1 (en) | 2010-04-13 | 2018-07-04 | Bristol-Myers Squibb Company | Fibronectin based scaffold domain proteins that bind pcsk9 |
| US8691763B2 (en) | 2010-05-04 | 2014-04-08 | Glaxosmithkline Llc | Methods for treating or preventing cardiovascular disorders and providing cardiovascular protection |
| EP2571992B1 (en) * | 2010-05-21 | 2018-04-25 | Merrimack Pharmaceuticals, Inc. | Bi-specific fusion proteins |
| JP6023703B2 (ja) | 2010-05-26 | 2016-11-09 | ブリストル−マイヤーズ スクイブ カンパニーＢｒｉｓｔｏｌ−Ｍｙｅｒｓ Ｓｑｕｉｂｂ Ｃｏｍｐａｎｙ | 改善された安定性を有するフィブロネクチンをベースとする足場タンパク質 |
| JP2013529627A (ja) | 2010-06-24 | 2013-07-22 | パンメド リミテッド | ヒドロキシクロロキンまたはヒドロキシクロロキンおよび抗ウイルス剤の組合せを使用するｃ型肝炎ウイルス関連疾患の処置 |
| WO2012013597A1 (de) * | 2010-07-28 | 2012-02-02 | Justus-Liebig-Universität Giessen | Stoffe und deren verwendung zur beeinflussung natriuretischer peptidrezeptoren |
| JP5909495B2 (ja) | 2010-10-08 | 2016-04-26 | ノバルティス アーゲー | スルファミドｎｓ３阻害剤のビタミンｅ製剤 |
| CN103380143B (zh) | 2010-12-22 | 2016-01-06 | 百时美施贵宝公司 | 结合il-23的基于纤连蛋白的支架结构域蛋白质 |
| WO2012093125A1 (en) | 2011-01-06 | 2012-07-12 | Glaxo Group Limited | Ligands that bind tgf-beta receptor ii |
| WO2012093704A1 (ja) * | 2011-01-07 | 2012-07-12 | 中外製薬株式会社 | 抗体の物性を改善させる方法 |
| US20120277155A1 (en) | 2011-02-25 | 2012-11-01 | Medtronic, Inc. | Therapy for kidney disease and/or heart failure |
| AU2012222833B2 (en) | 2011-03-03 | 2017-03-16 | Zymeworks Inc. | Multivalent heteromultimer scaffold design and constructs |
| CA2830660A1 (en) | 2011-05-05 | 2012-11-08 | Novozymes Biopharma Dk A/S | Albumin variants |
| EP2750697A4 (en) | 2011-09-02 | 2015-03-25 | Medtronic Inc | CHIMERIC NATRIURETIC PEPTIDE COMPOSITIONS AND METHOD FOR THE PRODUCTION THEREOF |
| JP2015504038A (ja) | 2011-10-31 | 2015-02-05 | ブリストル−マイヤーズ スクイブ カンパニーＢｒｉｓｔｏｌ−Ｍｙｅｒｓ Ｓｑｕｉｂｂ Ｃｏｍｐａｎｙ | 低減した免疫原性を有するフィブロネクチン結合ドメイン |
| EP2780364A2 (en) | 2011-11-18 | 2014-09-24 | Eleven Biotherapeutics, Inc. | Proteins with improved half-life and other properties |
| EP2822577B1 (en) | 2012-02-15 | 2019-02-06 | Bioverativ Therapeutics Inc. | Recombinant factor viii proteins |
| JP6256882B2 (ja) | 2012-02-15 | 2018-01-10 | アムニクス オペレーティング インコーポレイテッド | 第ｖｉｉｉ因子組成物、ならびに組成物の作製方法および用途 |
| JP6355563B2 (ja) | 2012-02-27 | 2018-07-11 | アムニクス オペレーティング インコーポレイテッド | Ｘｔｅｎ共役組成物およびそれを製造する方法 |
| US9603897B2 (en) | 2012-03-12 | 2017-03-28 | Massachusetts Institute Of Technology | Methods for treating tissue damage associated with ischemia with apolipoprotein D |
| WO2013137869A1 (en) | 2012-03-14 | 2013-09-19 | Boehringer Ingelheim International Gmbh | Combination therapy for treating hcv infection in an hcv-hiv coinfected patient population |
| DK2825556T3 (en) | 2012-03-16 | 2018-04-16 | Albumedix As | albumin Variants |
| JP2015512900A (ja) | 2012-03-28 | 2015-04-30 | ベーリンガー インゲルハイム インターナショナル ゲゼルシャフト ミット ベシュレンクテル ハフツング | 特別な患者の遺伝子亜型分集団のｈｃｖ感染症を治療するための併用療法 |
| US9844582B2 (en) | 2012-05-22 | 2017-12-19 | Massachusetts Institute Of Technology | Synergistic tumor treatment with extended-PK IL-2 and therapeutic agents |
| WO2014012082A2 (en) | 2012-07-13 | 2014-01-16 | Zymeworks Inc. | Multivalent heteromultimer scaffold design an constructs |
| EP2888279A1 (en) | 2012-08-22 | 2015-07-01 | Glaxo Group Limited | Anti lrp6 antibodies |
| ES2984405T3 (es) | 2012-09-13 | 2024-10-29 | Bristol Myers Squibb Co | Proteínas de dominio de andamio basadas en fibronectina que se unen a la miostatina |
| MX2015005363A (es) | 2012-11-08 | 2015-11-06 | Novozymes Biopharma Dk As | Variantes de albumina. |
| US20140205566A1 (en) | 2012-11-30 | 2014-07-24 | Novartis Ag | Cyclic nucleuoside derivatives and uses thereof |
| EP2951206A2 (en) | 2013-02-01 | 2015-12-09 | Bristol-Myers Squibb Company | Fibronectin based scaffold proteins |
| USRE48805E1 (en) * | 2013-03-06 | 2021-11-02 | Vision Global Holdings Ltd. | Method for cancer targeting treatment and detection of arginine using albumin-binding arginine deiminase fusion protein |
| US9255262B2 (en) * | 2013-03-06 | 2016-02-09 | Vision Global Holdings Ltd. | Albumin-binding arginine deminase and the use thereof |
| EP2964666B1 (en) | 2013-03-06 | 2020-11-18 | GlaxoSmithKline LLC | Host cells and methods of use |
| EP2968587A2 (en) | 2013-03-13 | 2016-01-20 | Bristol-Myers Squibb Company | Fibronectin based scaffold domains linked to serum albumin or a moiety binding thereto |
| US10344088B2 (en) | 2013-03-15 | 2019-07-09 | Glaxosmithkline Intellectual Property Development Limited | Antigen binding proteins |
| EP2992021B1 (en) | 2013-04-30 | 2020-07-22 | Intas Pharmaceuticals Limited | Novel cloning, expression & purification method for the preparation of ranibizumab |
| WO2015001049A1 (en) | 2013-07-04 | 2015-01-08 | Novartis Ag | O-mannosyltransferase deficient filamentous fungal cells and methods of use thereof |
| WO2015023890A1 (en) * | 2013-08-14 | 2015-02-19 | The Arizona Board Of Regents On Behalf Of The University Of Arizona | Glycosylated pacap/vip analogues with enhanced cns penetration for treatment of neurodegenerative diseases |
| TW202003554A (zh) | 2013-08-14 | 2020-01-16 | 美商百歐維拉提夫治療公司 | 因子ｖｉｉｉ－ｘｔｅｎ融合物及其用途 |
| CN105377882B (zh) * | 2014-03-06 | 2020-05-05 | 葛兰素史密斯克莱有限责任公司 | 宿主细胞和使用方法 |
| EP3157947A1 (en) | 2014-06-23 | 2017-04-26 | Novartis AG | Hsa-gdf-15 fusion polypeptide and use thereof |
| SG11201700446XA (en) | 2014-07-21 | 2017-02-27 | Glykos Finland Oy | Production of glycoproteins with mammalian-like n-glycans in filamentous fungi |
| CA2957717C (en) | 2014-08-12 | 2021-10-19 | Massachusetts Institute Of Technology | Synergistic tumor treatment with il-2 and integrin-binding-fc-fusion protein |
| WO2016025647A1 (en) | 2014-08-12 | 2016-02-18 | Massachusetts Institute Of Technology | Synergistic tumor treatment with il-2, a therapeutic antibody, and a cancer vaccine |
| US9616114B1 (en) | 2014-09-18 | 2017-04-11 | David Gordon Bermudes | Modified bacteria having improved pharmacokinetics and tumor colonization enhancing antitumor activity |
| CN107207379B (zh) | 2014-11-25 | 2021-08-10 | 百时美施贵宝公司 | 用于生物制品的18f-放射性标记的方法和组合物 |
| CA2969067A1 (en) | 2014-11-25 | 2016-06-02 | Bristol-Myers Squibb Company | Novel pd-l1 binding polypeptides for imaging |
| EP3967755B1 (en) | 2014-12-19 | 2024-03-27 | Inozyme Pharma, Inc. | Soluble npp1 for use in a method for treating pseudoxanthoma elasticum |
| EA035332B1 (ru) | 2015-04-24 | 2020-05-28 | ВАЙВ ХЕЛТКЕР ЮКей (№5) ЛИМИТЕД | Полипептиды, нацеленные на слияние вич |
| US10676723B2 (en) | 2015-05-11 | 2020-06-09 | David Gordon Bermudes | Chimeric protein toxins for expression by therapeutic bacteria |
| EA201890423A1 (ru) | 2015-08-03 | 2018-07-31 | Биовератив Терапьютикс Инк. | Слитые белки фактора ix, способы их получения и применения |
| JP7007261B2 (ja) | 2015-08-20 | 2022-01-24 | アルブミディクス リミティド | アルブミン変異体及びコンジュゲート |
| IL319047A (en) | 2015-08-28 | 2025-04-01 | Amunix Operating Inc | Chimeric polypeptide composition and methods for its preparation and use |
| CN117510633A (zh) | 2015-09-02 | 2024-02-06 | 伊缪泰普有限公司 | 抗lag-3抗体 |
| CA3183289A1 (en) * | 2015-09-08 | 2017-03-16 | Jcr Pharmaceuticals Co., Ltd. | Novel human serum albumin mutant |
| NZ740534A (en) * | 2015-09-18 | 2019-07-26 | Univ Miyazaki | Long-acting adrenomedullin derivative |
| CN108884147B (zh) | 2015-09-23 | 2024-02-27 | 百时美施贵宝公司 | 结合磷脂酰肌醇蛋白聚糖3的基于纤连蛋白的支架分子 |
| CN110498851B (zh) * | 2015-11-10 | 2022-10-11 | 孙嘉琳 | 一种抗肿瘤蛋白内皮抑素的衍生物及应用 |
| JP6946304B2 (ja) | 2015-12-22 | 2021-10-06 | ノバルティス アーゲー | 増殖分化因子１５（ｇｄｆ−１５）を使用して代謝障害を処置するまたは軽快させる方法 |
| CN108697768B (zh) * | 2015-12-23 | 2022-07-22 | 约翰霍普金斯大学 | 长效glp-1r激动剂作为神经系统病状和神经退行性病状的治疗方法 |
| JP2017165713A (ja) * | 2016-03-14 | 2017-09-21 | Ｊｃｒファーマ株式会社 | 血清アルブミン−２０ｋ成長ホルモン融合タンパク質 |
| US10994033B2 (en) | 2016-06-01 | 2021-05-04 | Bristol-Myers Squibb Company | Imaging methods using 18F-radiolabeled biologics |
| EP3471747A1 (en) | 2016-06-16 | 2019-04-24 | Alexion Pharmaceuticals, Inc. | Methods of treating myointimal proliferation |
| MX2019006444A (es) | 2016-12-02 | 2019-10-30 | Bioverativ Therapeutics Inc | Métodos de tratamiento de artropatía hemofílica utilizando factores de coagulación quiméricos. |
| US11180535B1 (en) | 2016-12-07 | 2021-11-23 | David Gordon Bermudes | Saccharide binding, tumor penetration, and cytotoxic antitumor chimeric peptides from therapeutic bacteria |
| US11129906B1 (en) | 2016-12-07 | 2021-09-28 | David Gordon Bermudes | Chimeric protein toxins for expression by therapeutic bacteria |
| US10350266B2 (en) | 2017-01-10 | 2019-07-16 | Nodus Therapeutics, Inc. | Method of treating cancer with a multiple integrin binding Fc fusion protein |
| AU2018207303A1 (en) | 2017-01-10 | 2019-07-25 | xCella Biosciences, Inc. | Combination tumor treatment with an integrin-binding-Fc fusion protein and immune modulator |
| US10767164B2 (en) | 2017-03-30 | 2020-09-08 | The Research Foundation For The State University Of New York | Microenvironments for self-assembly of islet organoids from stem cells differentiation |
| US12134790B2 (en) | 2017-09-27 | 2024-11-05 | Inozyme Pharma, Inc. | Methods of improving cardiovascular function and treating cardiovascular disease using a recombinant ectonucleotide pyrophosphatase phosphodiesterase (NPP1) |
| CN110090295B (zh) * | 2018-01-29 | 2022-12-23 | 武汉康理通科技有限公司 | Ephrin-B1在制备治疗炎症性肠病的药物中的用途 |
| WO2019152827A1 (en) * | 2018-02-02 | 2019-08-08 | AskGene Pharma, Inc. | Novel antibody-drug conjugates (adc), methods of making, and methods of use thereof |
| US20210113606A1 (en) | 2018-02-12 | 2021-04-22 | Biontech Rna Pharmaceuticals Gmbh | Treatment using cytokine encoding rna |
| AU2019271148B9 (en) | 2018-05-14 | 2025-05-29 | Werewolf Therapeutics, Inc. | Activatable interleukin-2 polypeptides and methods of use thereof |
| WO2019222296A1 (en) | 2018-05-14 | 2019-11-21 | Werewolf Therapeutics, Inc. | Activatable interleukin 12 polypeptides and methods of use thereof |
| PL3793588T3 (pl) | 2018-05-18 | 2025-09-01 | Bioverativ Therapeutics Inc. | Sposoby leczenia hemofilii a |
| EP3806889A4 (en) | 2018-06-18 | 2022-07-13 | Anwita Biosciences, Inc. | CYTOKI FUSION PROTEINS AND USES THEREOF |
| MX2021000801A (es) | 2018-07-24 | 2021-04-12 | BioNTech SE | Agonistas de il2. |
| US20220002370A1 (en) | 2018-09-27 | 2022-01-06 | Xilio Development, Inc. | Masked cytokine polypeptides |
| AU2019346335B2 (en) | 2018-09-28 | 2024-07-25 | Massachusetts Institute Of Technology | Collagen-localized immunomodulatory molecules and methods thereof |
| EP3914289A1 (en) | 2019-01-23 | 2021-12-01 | Massachusetts Institute of Technology | Combination immunotherapy dosing regimen for immune checkpoint blockade |
| US20220098252A1 (en) | 2019-01-25 | 2022-03-31 | Ospedale San Raffaele S.R.L. | Inhibitor of dux4 and uses thereof |
| EP4414033A3 (en) | 2019-02-08 | 2024-10-30 | Biontech Cell & Gene Therapies Gmbh | Treatment involving car-engineered t cells and cytokines |
| WO2020187848A1 (en) | 2019-03-18 | 2020-09-24 | Biontech Cell & Gene Therapies Gmbh | Lnterleukin-2 receptor (il2r) and interleukin-2 (il2) variants for specific activation of immune effector cells |
| WO2020200481A1 (en) | 2019-04-05 | 2020-10-08 | Biontech Rna Pharmaceuticals Gmbh | Treatment involving interleukin-2 (il2) and interferon (ifn) |
| EP3955957A1 (en) | 2019-04-15 | 2022-02-23 | Qwixel Therapeutics LLC | Fusion protein composition(s) comprising targeted masked type i interferons (ifna and ifnb) and an antibody against tumor antigen, for use in the treatment of cancer |
| CN111944036B (zh) * | 2019-05-14 | 2024-09-06 | 上海盖浦生物科技有限公司 | 一种增殖免疫细胞的突变体蛋白 |
| EP3969035A4 (en) | 2019-05-14 | 2023-06-21 | Werewolf Therapeutics, Inc. | SEPARATION UNITS AND METHODS AND THEIR USE |
| TW202115105A (zh) | 2019-06-24 | 2021-04-16 | 德商拜恩迪克Ｒｎａ製藥有限公司 | Ｉｌ２激動劑 |
| WO2020263399A1 (en) | 2019-06-26 | 2020-12-30 | Massachusetts Institute Of Technology | Immunomodulatory fusion protein-metal hydroxide complexes and methods thereof |
| RU2714392C1 (ru) * | 2019-07-09 | 2020-02-14 | Екатерина Олеговна Кудасова | Способ модификации поверхности метилметакрилата стоматологического протеза низкотемпературной газоразрядной плазмой кислорода низкого давления за счет изменения контактного угла смачивания по воде и свободной поверхностной энергии |
| KR20220044534A (ko) | 2019-08-13 | 2022-04-08 | 엘피스 바이오파마슈티컬즈 | 조작된 인터류킨-2 수용체 베타 효능제 |
| WO2021058091A1 (en) | 2019-09-24 | 2021-04-01 | Biontech Rna Pharmaceuticals Gmbh | Treatment involving therapeutic antibody and interleukin-2 (il2) |
| MX2022005666A (es) | 2019-11-14 | 2022-10-07 | Werewolf Therapeutics Inc | Polipeptidos de citocina activables y metodos de uso de los mismos. |
| WO2021129927A1 (en) | 2019-12-23 | 2021-07-01 | Biontech Cell & Gene Therapies Gmbh | Treatment with immune effector cells engineered to express an antigen receptor |
| WO2021129945A1 (en) | 2019-12-27 | 2021-07-01 | Biontech Cell & Gene Therapies Gmbh | In vitro and in vivo gene delivery to immune effector cells using nanoparticles functionalized with designed ankyrin repeat proteins (darpins) |
| WO2021174045A1 (en) | 2020-02-28 | 2021-09-02 | Bristol-Myers Squibb Company | Radiolabeled fibronectin based scaffolds and antibodies and theranostic uses thereof |
| US20230405046A1 (en) | 2020-03-16 | 2023-12-21 | Biontech Cell & Gene Therapies Gmbh | Antigen-specific t cell receptors and t cell epitopes |
| WO2021197589A1 (en) | 2020-03-31 | 2021-10-07 | BioNTech SE | Treatment involving non-immunogenic rna for antigen vaccination |
| CR20220596A (es) | 2020-05-26 | 2023-01-23 | Boehringer Ingelheim Int | Anticuerpos anti-pd-1 |
| JPWO2022030580A1 (https=) * | 2020-08-06 | 2022-02-10 | ||
| US20220288226A1 (en) * | 2020-08-27 | 2022-09-15 | Enosi Life Sciences Corp. | Methods and compositions to treat autoimmune diseases and cancer |
| KR102467827B1 (ko) * | 2020-08-31 | 2022-11-16 | 연세대학교 산학협력단 | 미생물 에어로졸화 과정 중 발생하는 손상 방지 방법 |
| CN112724259B (zh) * | 2020-11-16 | 2022-12-20 | 天津林达生物科技有限公司 | 人血清白蛋白与白介素2的融合蛋白及其用途 |
| WO2022115865A2 (en) | 2020-11-25 | 2022-06-02 | Xilio Development, Inc. | Tumor-specific cleavable linkers |
| WO2022135666A1 (en) | 2020-12-21 | 2022-06-30 | BioNTech SE | Treatment schedule for cytokine proteins |
| TW202245808A (zh) | 2020-12-21 | 2022-12-01 | 德商拜恩迪克公司 | 用於治療癌症之治療性ｒｎａ |
| WO2022135667A1 (en) | 2020-12-21 | 2022-06-30 | BioNTech SE | Therapeutic rna for treating cancer |
| CN112753846B (zh) * | 2021-01-27 | 2023-08-29 | 吉林农业大学 | 一种超持水大豆分离蛋白凝胶及其制备方法 |
| AU2022256732A1 (en) | 2021-04-12 | 2023-10-19 | Biontech Delivery Technologies Gmbh | Rna compositions comprising a buffer substance and methods for preparing, storing and using the same |
| BR112023021654A2 (pt) | 2021-04-20 | 2023-12-26 | BioNTech SE | Vacina contra vírus |
| CA3218973A1 (en) * | 2021-05-14 | 2022-11-17 | Antlia Bioscience, Inc. | Modified b-type natriuretic peptide |
| TW202317620A (zh) | 2021-06-04 | 2023-05-01 | 德商百靈佳殷格翰國際股份有限公司 | 抗ＳＩＲＰα抗體 |
| CN113391067B (zh) * | 2021-06-16 | 2023-07-25 | 军事科学院军事医学研究院军事兽医研究所 | 抗尼帕病毒g蛋白抗体的间接elisa检测方法 |
| WO2023051926A1 (en) | 2021-09-30 | 2023-04-06 | BioNTech SE | Treatment involving non-immunogenic rna for antigen vaccination and pd-1 axis binding antagonists |
| EP4419136A1 (en) | 2021-10-21 | 2024-08-28 | BioNTech SE | Coronavirus vaccine |
| WO2023067193A2 (en) | 2021-10-22 | 2023-04-27 | BioNTech SE | Compositions for administration of different doses of rna |
| WO2023083434A1 (en) | 2021-11-09 | 2023-05-19 | BioNTech SE | Rna encoding peptidoglycan hydrolase and use thereof for treating bacterial infection |
| WO2023126053A1 (en) | 2021-12-28 | 2023-07-06 | BioNTech SE | Lipid-based formulations for administration of rna |
| WO2023141638A1 (en) * | 2022-01-21 | 2023-07-27 | The Methodist Hospital System | Methods for vascular regeneration and wound treatment |
| WO2023165681A1 (en) | 2022-03-01 | 2023-09-07 | BioNTech SE | Rna lipid nanoparticles (lnps) comprising a polyoxazoline and/or polyoxazine polymer |
| WO2023193892A1 (en) | 2022-04-05 | 2023-10-12 | BioNTech SE | Nucleic acid compositions comprising an inorganic polyphosphate and methods for preparing, storing and using the same |
| CN119731199A (zh) | 2022-05-10 | 2025-03-28 | 艾佩斯瑞生物制药公司 | 工程化的白细胞介素-2受体β降低结合的激动剂 |
| WO2024002985A1 (en) | 2022-06-26 | 2024-01-04 | BioNTech SE | Coronavirus vaccine |
| WO2024017479A1 (en) | 2022-07-21 | 2024-01-25 | BioNTech SE | Multifunctional cells transiently expressing an immune receptor and one or more cytokines, their use and methods for their production |
| AU2023317702A1 (en) | 2022-08-01 | 2025-01-09 | BioNTech SE | Nucleic acid compositions comprising amphiphilic oligo ethylene glycol (oeg)-conjugated compounds and methods of using such compounds and compositions |
| WO2024027910A1 (en) | 2022-08-03 | 2024-02-08 | BioNTech SE | Rna for preventing or treating tuberculosis |
| IL318534A (en) | 2022-08-03 | 2025-03-01 | BioNTech SE | RNA for preventing or treating tuberculosis |
| CN115960175A (zh) * | 2022-08-08 | 2023-04-14 | 江南大学 | 一种强化乳铁蛋白表达的毕赤酵母及其构建方法与应用 |
| WO2024080304A1 (ja) * | 2022-10-11 | 2024-04-18 | Ｊｃｒファーマ株式会社 | 血清アルブミンと生理活性を有する蛋白質との融合蛋白質 |
| WO2024080306A1 (ja) * | 2022-10-11 | 2024-04-18 | Ｊｃｒファーマ株式会社 | 血清アルブミンと生理活性を有する蛋白質との融合蛋白質 |
| EP4389762A1 (en) | 2022-12-23 | 2024-06-26 | Ospedale San Raffaele S.r.l. | Inhibitors of dux4 activity and their use in therapy. |
| WO2024153324A1 (en) | 2023-01-18 | 2024-07-25 | BioNTech SE | Rna formulations for pharmaceutical use |
| WO2024216212A1 (en) | 2023-04-14 | 2024-10-17 | BioNTech SE | Rna for preventing or treating tuberculosis |
| CN121398842A (zh) | 2023-04-14 | 2026-01-23 | 百欧恩泰欧洲股份公司 | 用于预防或治疗结核病的rna |
| WO2024213776A1 (en) | 2023-04-14 | 2024-10-17 | BioNTech SE | Rna for preventing or treating tuberculosis |
| AU2024308069A1 (en) | 2023-06-27 | 2026-02-05 | Firecyte Therapeutics, Inc. | Insulin-like growth factor binding protein like 1 (igfbpl1) compositions and methods of use thereof |
| WO2025021277A1 (en) | 2023-07-21 | 2025-01-30 | BioNTech SE | Agents and methods for targeted delivery of cytokines to immune cells |
| WO2025026866A1 (en) | 2023-07-28 | 2025-02-06 | BioNTech SE | Rna therapeutics with reduced toxicity |
| WO2025074337A1 (en) | 2023-10-06 | 2025-04-10 | Boehringer Ingelheim International Gmbh | Use of anti-sirp-alpha antibodies to treat a liver disease or disorder |
| WO2025074328A1 (en) | 2023-10-06 | 2025-04-10 | Boehringer Ingelheim International Gmbh | Use of anti-sirp-alpha antibodies to treat cancer |
| CN117511986B (zh) * | 2023-10-17 | 2026-04-10 | 广州立白企业集团有限公司 | 一种构建多基因改造酵母菌的方法及其应用 |
| WO2025106754A1 (en) | 2023-11-15 | 2025-05-22 | BioNTech SE | Coronavirus vaccine |
| WO2025181215A1 (en) | 2024-03-01 | 2025-09-04 | Boehringer Ingelheim International Gmbh | Antibodies to connective tissue growth factor (ctgf) and uses thereof |
| WO2026042012A1 (en) | 2024-08-19 | 2026-02-26 | Institute Of Molecular And Clinical Ophthalmology Basel (Iob) | Single domain antibodies and polypeptides containing same |
| WO2026082899A2 (en) | 2024-10-16 | 2026-04-23 | BioNTech SE | Rna for preventing or treating tuberculosis |
| CN120591344B (zh) * | 2025-06-13 | 2026-04-03 | 广州景旸生物科技有限公司 | Col3a1蛋白的制备方法及其应用 |
Family Cites Families (186)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| US4179337A (en) | 1973-07-20 | 1979-12-18 | Davis Frank F | Non-immunogenic polypeptides |
| US4002531A (en) | 1976-01-22 | 1977-01-11 | Pierce Chemical Company | Modifying enzymes with polyethylene glycol and product produced thereby |
| US4444887A (en) | 1979-12-10 | 1984-04-24 | Sloan-Kettering Institute | Process for making human antibody producing B-lymphocytes |
| US4714681A (en) | 1981-07-01 | 1987-12-22 | The Board Of Reagents, The University Of Texas System Cancer Center | Quadroma cells and trioma cells and methods for the production of same |
| US4474893A (en) | 1981-07-01 | 1984-10-02 | The University of Texas System Cancer Center | Recombinant monoclonal antibodies |
| US4716111A (en) | 1982-08-11 | 1987-12-29 | Trustees Of Boston University | Process for producing human antibodies |
| US4741900A (en) | 1982-11-16 | 1988-05-03 | Cytogen Corporation | Antibody-metal ion complexes |
| NZ207394A (en) | 1983-03-08 | 1987-03-06 | Commw Serum Lab Commission | Detecting or determining sequence of amino acids |
| GB8308235D0 (en) | 1983-03-25 | 1983-05-05 | Celltech Ltd | Polypeptides |
| US4816567A (en) | 1983-04-08 | 1989-03-28 | Genentech, Inc. | Recombinant immunoglobin preparations |
| US5807715A (en) | 1984-08-27 | 1998-09-15 | The Board Of Trustees Of The Leland Stanford Junior University | Methods and transformed mammalian lymphocyte cells for producing functional antigen-binding protein including chimeric immunoglobulin |
| EP0216846B2 (en) | 1985-04-01 | 1995-04-26 | Celltech Limited | Transformed myeloma cell-line and a process for the expression of a gene coding for a eukaryotic polypeptide employing same |
| US4980286A (en) | 1985-07-05 | 1990-12-25 | Whitehead Institute For Biomedical Research | In vivo introduction and expression of foreign genetic material in epithelial cells |
| US4676980A (en) | 1985-09-23 | 1987-06-30 | The United States Of America As Represented By The Secretary Of The Department Of Health And Human Services | Target specific cross-linked heteroantibodies |
| GB8601597D0 (en) | 1986-01-23 | 1986-02-26 | Wilson R H | Nucleotide sequences |
| US5225539A (en) | 1986-03-27 | 1993-07-06 | Medical Research Council | Recombinant altered antibodies and methods of making altered antibodies |
| GB8607679D0 (en) | 1986-03-27 | 1986-04-30 | Winter G P | Recombinant dna product |
| US4946778A (en) | 1987-09-21 | 1990-08-07 | Genex Corporation | Single polypeptide chain binding molecules |
| JP2873012B2 (ja) * | 1987-04-09 | 1999-03-24 | デルタ バイオテクノロジー リミテッド | 酵母ベクター |
| US5258498A (en) | 1987-05-21 | 1993-11-02 | Creative Biomolecules, Inc. | Polypeptide linkers for production of biosynthetic proteins |
| US4994560A (en) | 1987-06-24 | 1991-02-19 | The Dow Chemical Company | Functionalized polyamine chelants and radioactive rhodium complexes thereof for conjugation to antibodies |
| US5489425A (en) | 1987-06-24 | 1996-02-06 | The Dow Chemical Company | Functionalized polyamine chelants |
| GB8717430D0 (en) | 1987-07-23 | 1987-08-26 | Celltech Ltd | Recombinant dna product |
| PT88641B (pt) | 1987-10-02 | 1993-04-30 | Genentech Inc | Metodo para a preparacao de uma variante de adesao |
| GB8725529D0 (en) | 1987-10-30 | 1987-12-02 | Delta Biotechnology Ltd | Polypeptides |
| JPH01215289A (ja) | 1988-02-22 | 1989-08-29 | Toa Nenryo Kogyo Kk | 遺伝子組換えによる正常ヒト血清アルブミンａの製造方法 |
| GB8809129D0 (en) | 1988-04-18 | 1988-05-18 | Celltech Ltd | Recombinant dna methods vectors and host cells |
| CA1341373C (en) | 1988-06-24 | 2002-07-02 | Roberta C. Cheng | Macrocyclic bifunctional chelants, complexes thereof and their antibody conjugates |
| US5756065A (en) | 1988-06-24 | 1998-05-26 | The Dow Chemical Company | Macrocyclic tetraazacyclododecane conjugates and their use as diagnostic and therapeutic agents |
| ZA894792B (en) | 1988-06-24 | 1991-04-24 | Dow Chemical Co | Macrocyclic bifunctional chelants,complexes thereof and their antibody conjugates |
| US5274119A (en) | 1988-07-01 | 1993-12-28 | The Dow Chemical Company | Vicinal diols |
| US4925648A (en) | 1988-07-29 | 1990-05-15 | Immunomedics, Inc. | Detection and treatment of infectious and inflammatory lesions |
| FR2649991B2 (fr) | 1988-08-05 | 1994-03-04 | Rhone Poulenc Sante | Utilisation de derives stables du plasmide pkd1 pour l'expression et la secretion de proteines heterologues dans les levures du genre kluyveromyces |
| US5601819A (en) | 1988-08-11 | 1997-02-11 | The General Hospital Corporation | Bispecific antibodies for selective immune regulation and for selective immune cell binding |
| AU4216689A (en) | 1988-08-11 | 1990-03-05 | California Biotechnology, Inc. | Method for stabilizing heterologous protein expression and vectors for use therein |
| US5223409A (en) | 1988-09-02 | 1993-06-29 | Protein Engineering Corp. | Directed evolution of novel binding proteins |
| EP0436597B1 (en) | 1988-09-02 | 1997-04-02 | Protein Engineering Corporation | Generation and selection of recombinant varied binding proteins |
| US5349052A (en) | 1988-10-20 | 1994-09-20 | Royal Free Hospital School Of Medicine | Process for fractionating polyethylene glycol (PEG)-protein adducts and an adduct for PEG and granulocyte-macrophage colony stimulating factor |
| US5696239A (en) | 1988-10-31 | 1997-12-09 | The Dow Chemical Company | Conjugates possessing ortho ligating functionality and complexes thereof |
| US5342604A (en) | 1988-10-31 | 1994-08-30 | The Dow Chemical Company | Complexes possessing ortho ligating functionality |
| WO1990006952A1 (fr) | 1988-12-22 | 1990-06-28 | Kirin-Amgen, Inc. | Facteur de stimulation de colonies de granulocytes modifies chimiquement |
| US5530101A (en) | 1988-12-28 | 1996-06-25 | Protein Design Labs, Inc. | Humanized immunoglobulins |
| US5705363A (en) * | 1989-03-02 | 1998-01-06 | The Women's Research Institute | Recombinant production of human interferon τ polypeptides and nucleic acids |
| US5231020A (en) | 1989-03-30 | 1993-07-27 | Dna Plant Technology Corporation | Genetic engineering of novel plant phenotypes |
| US5324844A (en) | 1989-04-19 | 1994-06-28 | Enzon, Inc. | Active carbonates of polyalkylene oxides for modification of polypeptides |
| US5766883A (en) * | 1989-04-29 | 1998-06-16 | Delta Biotechnology Limited | Polypeptides |
| US5808003A (en) | 1989-05-26 | 1998-09-15 | Perimmune Holdings, Inc. | Polyaminocarboxylate chelators |
| ES2096590T3 (es) | 1989-06-29 | 1997-03-16 | Medarex Inc | Reactivos biespecificos para la terapia del sida. |
| US5413923A (en) | 1989-07-25 | 1995-05-09 | Cell Genesys, Inc. | Homologous recombination for universal donor cells and chimeric mammalian hosts |
| FR2650598B1 (fr) * | 1989-08-03 | 1994-06-03 | Rhone Poulenc Sante | Derives de l'albumine a fonction therapeutique |
| US5073627A (en) | 1989-08-22 | 1991-12-17 | Immunex Corporation | Fusion proteins comprising GM-CSF and IL-3 |
| KR100221066B1 (ko) | 1989-10-13 | 1999-10-01 | 스튜어트 엘.왓트 | 에리트로포이에틴 유사체와 그를 포함하는 제약학적 조성물 |
| US5667986A (en) * | 1989-10-18 | 1997-09-16 | Delta Biotechnology Limited | Yeast promoter for expressing heterologous polypeptides |
| GB8924021D0 (en) | 1989-10-25 | 1989-12-13 | Celltech Ltd | Recombinant dna method and vectors for the use therein |
| GB8928874D0 (en) | 1989-12-21 | 1990-02-28 | Celltech Ltd | Humanised antibodies |
| AU7247191A (en) | 1990-01-11 | 1991-08-05 | Molecular Affinities Corporation | Production of antibodies using gene libraries |
| US5780225A (en) | 1990-01-12 | 1998-07-14 | Stratagene | Method for generating libaries of antibody genes comprising amplification of diverse antibody DNAs and methods for using these libraries for the production of diverse antigen combining molecules |
| US6075181A (en) | 1990-01-12 | 2000-06-13 | Abgenix, Inc. | Human antibodies derived from immunized xenomice |
| WO1996033735A1 (en) | 1995-04-27 | 1996-10-31 | Abgenix, Inc. | Human antibodies derived from immunized xenomice |
| DE69120146T2 (de) | 1990-01-12 | 1996-12-12 | Cell Genesys Inc | Erzeugung xenogener antikörper |
| US5545618A (en) * | 1990-01-24 | 1996-08-13 | Buckley; Douglas I. | GLP-1 analogs useful for diabetes treatment |
| US5747334A (en) | 1990-02-15 | 1998-05-05 | The University Of North Carolina At Chapel Hill | Random peptide library |
| US5427908A (en) | 1990-05-01 | 1995-06-27 | Affymax Technologies N.V. | Recombinant library screening methods |
| GB9013017D0 (en) * | 1990-06-11 | 1990-08-01 | Mars Uk Ltd | Compounds |
| GB9015198D0 (en) | 1990-07-10 | 1990-08-29 | Brien Caroline J O | Binding substance |
| US5225341A (en) | 1990-07-19 | 1993-07-06 | The Regents Of The University Of California | Biologically safe plant transformation system using a ds transposon |
| US5202239A (en) * | 1990-08-07 | 1993-04-13 | Scios Nova Inc. | Expression of recombinant polypeptides with improved purification |
| US5661016A (en) | 1990-08-29 | 1997-08-26 | Genpharm International Inc. | Transgenic non-human animals capable of producing heterologous antibodies of various isotypes |
| US5545806A (en) | 1990-08-29 | 1996-08-13 | Genpharm International, Inc. | Ransgenic non-human animals for producing heterologous antibodies |
| ATE158021T1 (de) | 1990-08-29 | 1997-09-15 | Genpharm Int | Produktion und nützung nicht-menschliche transgentiere zur produktion heterologe antikörper |
| US5625126A (en) | 1990-08-29 | 1997-04-29 | Genpharm International, Inc. | Transgenic non-human animals for producing heterologous antibodies |
| US5633425A (en) | 1990-08-29 | 1997-05-27 | Genpharm International, Inc. | Transgenic non-human animals capable of producing heterologous antibodies |
| US5814318A (en) | 1990-08-29 | 1998-09-29 | Genpharm International Inc. | Transgenic non-human animals for producing heterologous antibodies |
| US5698426A (en) | 1990-09-28 | 1997-12-16 | Ixsys, Incorporated | Surface expression libraries of heteromeric receptors |
| DK0553244T4 (da) | 1990-10-05 | 2005-08-01 | Celldex Therapeutics Inc | Målrettet immunostimulering med bispecifikke reagenser |
| JPH07108232B2 (ja) | 1990-10-09 | 1995-11-22 | エム・ディ・リサーチ株式会社 | ペプチド又は蛋白質の製造方法 |
| WO1992008802A1 (en) | 1990-10-29 | 1992-05-29 | Cetus Oncology Corporation | Bispecific antibodies, method of production, and uses thereof |
| CA2095633C (en) | 1990-12-03 | 2003-02-04 | Lisa J. Garrard | Enrichment method for variant proteins with altered binding properties |
| ATE414768T1 (de) | 1991-04-10 | 2008-12-15 | Scripps Research Inst | Bibliotheken heterodimerer rezeptoren mittels phagemiden |
| CA2108451A1 (en) | 1991-04-26 | 1992-10-27 | Beverley J. Randle | Novel antibodies, and methods for their use |
| US5646012A (en) * | 1991-04-30 | 1997-07-08 | Rhone-Poulenc Rorer S.A. | Yeast promoter and use thereof |
| EP0519596B1 (en) | 1991-05-17 | 2005-02-23 | Merck & Co. Inc. | A method for reducing the immunogenicity of antibody variable domains |
| WO1992022324A1 (en) | 1991-06-14 | 1992-12-23 | Xoma Corporation | Microbially-produced antibody fragments and their conjugates |
| US5565332A (en) | 1991-09-23 | 1996-10-15 | Medical Research Council | Production of chimeric antibodies - a combinatorial approach |
| PT1024191E (pt) | 1991-12-02 | 2008-12-22 | Medical Res Council | Produção de auto-anticorpos a partir de reportórios de segmentos de anticorpo e exibidos em fagos |
| US5428139A (en) | 1991-12-10 | 1995-06-27 | The Dow Chemical Company | Bicyclopolyazamacrocyclophosphonic acid complexes for use as radiopharmaceuticals |
| FR2686620B1 (fr) * | 1992-01-27 | 1995-06-23 | Rhone Poulenc Rorer Sa | Serum-albumine humaine, preparation et utilisation. |
| 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. |
| PT627940E (pt) | 1992-03-05 | 2003-07-31 | Univ Texas | Utilizacao de imunoconjugados para o diagnostico e/ou terapia de tumores vascularizados |
| US5733743A (en) | 1992-03-24 | 1998-03-31 | Cambridge Antibody Technology Limited | Methods for producing members of specific binding pairs |
| US5573905A (en) | 1992-03-30 | 1996-11-12 | The Scripps Research Institute | Encoded combinatorial chemical libraries |
| DK0598877T3 (da) | 1992-06-09 | 2000-02-21 | Hoppe Ag | Falle og dørlås |
| US5505931A (en) | 1993-03-04 | 1996-04-09 | The Dow Chemical Company | Acid cleavable compounds, their preparation and use as bifunctional acid-labile crosslinking agents |
| DK0955062T3 (da) | 1992-07-31 | 2007-09-17 | Genentech Inc | Vandig formulering indeholdende humant væksthormon |
| US5639641A (en) | 1992-09-09 | 1997-06-17 | Immunogen Inc. | Resurfacing of rodent antibodies |
| US5441050A (en) | 1992-12-18 | 1995-08-15 | Neoprobe Corporation | Radiation responsive surgical instrument |
| DK82893D0 (da) * | 1993-07-08 | 1993-07-08 | Novo Nordisk As | Peptid |
| US5512459A (en) | 1993-07-20 | 1996-04-30 | Bionebraska, Inc. | Enzymatic method for modification or recombinant polypeptides |
| GB9317618D0 (en) | 1993-08-24 | 1993-10-06 | Royal Free Hosp School Med | Polymer modifications |
| US5643575A (en) | 1993-10-27 | 1997-07-01 | Enzon, Inc. | Non-antigenic branched polymer conjugates |
| WO1995015982A2 (en) | 1993-12-08 | 1995-06-15 | Genzyme Corporation | Process for generating specific antibodies |
| US5705483A (en) * | 1993-12-09 | 1998-01-06 | Eli Lilly And Company | Glucagon-like insulinotropic peptides, compositions and methods |
| DK144093D0 (https=) * | 1993-12-23 | 1993-12-23 | Novo Nordisk As | |
| DE69534347T2 (de) | 1994-01-31 | 2006-05-24 | Trustees Of Boston University, Boston | Bibliotheken aus Polyklonalen Antikörpern |
| US5516637A (en) | 1994-06-10 | 1996-05-14 | Dade International Inc. | Method involving display of protein binding pairs on the surface of bacterial pili and bacteriophage |
| US5985660A (en) | 1994-06-15 | 1999-11-16 | Systemix, Inc. | Method of identifying biological response modifiers involved in dendritic and/or lymphoid progenitor cell proliferation and/or differentiation |
| US5639642A (en) * | 1994-06-16 | 1997-06-17 | Novo Nordisk A/S | Synthetic leader peptide sequences |
| US5623054A (en) | 1994-06-23 | 1997-04-22 | The General Hospital Corporation | Crucifer AFT proteins and uses thereof |
| US5574008A (en) * | 1994-08-30 | 1996-11-12 | Eli Lilly And Company | Biologically active fragments of glucagon-like insulinotropic peptide |
| US5512549A (en) * | 1994-10-18 | 1996-04-30 | Eli Lilly And Company | Glucagon-like insulinotropic peptide analogs, compositions, and methods of use |
| WO1996034096A1 (en) | 1995-04-28 | 1996-10-31 | Abgenix, Inc. | Human antibodies derived from immunized xenomice |
| US5804162A (en) | 1995-06-07 | 1998-09-08 | Alliance Pharmaceutical Corp. | Gas emulsions stabilized with fluorinated ethers having low Ostwald coefficients |
| US5811097A (en) | 1995-07-25 | 1998-09-22 | The Regents Of The University Of California | Blockade of T lymphocyte down-regulation associated with CTLA-4 signaling |
| GB9526733D0 (en) * | 1995-12-30 | 1996-02-28 | Delta Biotechnology Ltd | Fusion proteins |
| US6110707A (en) * | 1996-01-19 | 2000-08-29 | Board Of Regents, The University Of Texas System | Recombinant expression of proteins from secretory cell lines |
| WO1997026321A2 (en) | 1996-01-19 | 1997-07-24 | Board Of Regents, The University Of Texas System | Recombinant expression of proteins from secretory cell lines |
| US6087129A (en) * | 1996-01-19 | 2000-07-11 | Betagene, Inc. | Recombinant expression of proteins from secretory cell lines |
| JP2978435B2 (ja) | 1996-01-24 | 1999-11-15 | チッソ株式会社 | アクリロキシプロピルシランの製造方法 |
| DE69740176D1 (de) | 1996-03-01 | 2011-05-26 | Novo Nordisk As | Appetithemmendes Peptid, Zusammensetzung und Verwendung |
| US5912229A (en) * | 1996-03-01 | 1999-06-15 | Novo Nordisk Als | Use of a pharmaceutical composition comprising an appetite-suppressing peptide |
| AU5711196A (en) | 1996-03-14 | 1997-10-01 | Human Genome Sciences, Inc. | Apoptosis inducing molecule i |
| CA2248868A1 (en) | 1996-03-22 | 1997-09-25 | Human Genome Sciences, Inc. | Apoptosis inducing molecule ii |
| US6300065B1 (en) * | 1996-05-31 | 2001-10-09 | Board Of Trustees Of The University Of Illinois | Yeast cell surface display of proteins and uses thereof |
| US6110703A (en) * | 1996-07-05 | 2000-08-29 | Novo Nordisk A/S | Method for the production of polypeptides |
| WO1998005782A1 (en) * | 1996-08-02 | 1998-02-12 | Zymogenetics, Inc. | Testis-specific insulin homolog polypeptides |
| US6458924B2 (en) * | 1996-08-30 | 2002-10-01 | Novo Nordisk A/S | Derivatives of GLP-1 analogs |
| US6277819B1 (en) | 1996-08-30 | 2001-08-21 | Eli Lilly And Company | Use of GLP-1 or analogs in treatment of myocardial infarction |
| US6006753A (en) * | 1996-08-30 | 1999-12-28 | Eli Lilly And Company | Use of GLP-1 or analogs to abolish catabolic changes after surgery |
| AU4199597A (en) | 1996-09-09 | 1998-04-02 | Novo Nordisk A/S | A cdna and peptide with relation to cancer and weight loss |
| AU7364696A (en) | 1996-09-18 | 1998-04-14 | Human Genome Sciences, Inc. | Human tumor necrosis factor receptor-like genes |
| US5916771A (en) | 1996-10-11 | 1999-06-29 | Abgenix, Inc. | Production of a multimeric protein by cell fusion method |
| EP1306092A3 (en) | 1996-11-05 | 2003-05-07 | Eli Lilly & Company | Use of GLP-1 and analogs administered peripherally, in regulation of obesity |
| 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 |
| DE69732572T2 (de) | 1996-11-12 | 2005-12-29 | Novo Nordisk A/S | Verwendung von glp-1 peptiden |
| CA2722378C (en) | 1996-12-03 | 2015-02-03 | Amgen Fremont Inc. | Human antibodies that bind tnf.alpha. |
| EP0954589A1 (en) | 1997-01-24 | 1999-11-10 | Novo Nordisk A/S | Synthetic leader peptide sequences |
| WO1998032466A1 (en) | 1997-01-29 | 1998-07-30 | Polymasc Pharmaceuticals Plc | Pegylation process |
| US20030049618A1 (en) * | 1997-03-07 | 2003-03-13 | Ruben Steven M. | 186 human secreted proteins |
| US6420526B1 (en) * | 1997-03-07 | 2002-07-16 | Human Genome Sciences, Inc. | 186 human secreted proteins |
| US20060084082A1 (en) * | 1997-03-07 | 2006-04-20 | Human Genome Sciences, Inc. | 186 human secreted proteins |
| US20030175858A1 (en) * | 1997-03-07 | 2003-09-18 | Ruben Steven M. | 186 human secreted proteins |
| US20030065139A1 (en) * | 1998-03-19 | 2003-04-03 | Craig A. Rosen | Secreted protein hmmbd35 |
| US5981488A (en) * | 1997-03-31 | 1999-11-09 | Eli Lillly And Company | Glucagon-like peptide-1 analogs |
| BRPI9809391B8 (pt) | 1997-04-14 | 2021-05-25 | Amgen Res Munich Gmbh | processo para a produção de um receptor de antígeno anti-humano, anticorpo humano e composição farmacêutica |
| US6235883B1 (en) | 1997-05-05 | 2001-05-22 | Abgenix, Inc. | Human monoclonal antibodies to epidermal growth factor receptor |
| GB9713412D0 (en) | 1997-06-26 | 1997-08-27 | Delta Biotechnology Ltd | Improved protein expression strains |
| NZ503343A (en) | 1997-09-17 | 2002-09-27 | Genentech Inc | Secreted and transmembrane polypeptides and use to induce apoptosis of tumour cells |
| CA2309541C (en) | 1997-11-03 | 2011-01-11 | Human Genome Sciences, Inc. | Vegi, an inhibitor of angiogenesis and tumor growth |
| WO1999043706A1 (en) | 1998-02-27 | 1999-09-02 | Novo Nordisk A/S | Derivatives of glp-1 analogs |
| US7205280B2 (en) * | 1998-03-11 | 2007-04-17 | Cognosci, Inc. | Methods of suppressing microglial activation |
| DE69933216T2 (de) * | 1998-06-15 | 2007-09-20 | GTC Biotherapeutics, Inc., Framingham | Erythropoietin-analog-menschliches serum-albumin fusionsprotein |
| MY155270A (en) | 1998-09-24 | 2015-09-30 | Lilly Co Eli | Use of glp-1 or analogs in treatment of stroke |
| US7259136B2 (en) | 1999-04-30 | 2007-08-21 | Amylin Pharmaceuticals, Inc. | Compositions and methods for treating peripheral vascular disease |
| US6514500B1 (en) * | 1999-10-15 | 2003-02-04 | Conjuchem, Inc. | Long lasting synthetic glucagon like peptide {GLP-!} |
| BR0010750A (pt) | 1999-05-17 | 2002-02-26 | Conjuchem Inc | Peptìdeos insulinotrópicos de longa duração |
| CA2376641A1 (en) | 1999-07-19 | 2001-01-25 | Aaron Morris | Chimeric polypeptides of serum albumin and uses related thereto |
| US20020048571A1 (en) | 1999-07-19 | 2002-04-25 | Jeno Gyuris | Chimeric polypeptides of serum albumin and uses related thereto |
| EP2213743A1 (en) | 2000-04-12 | 2010-08-04 | Human Genome Sciences, Inc. | Albumin fusion proteins |
| CN103356996A (zh) | 2000-05-19 | 2013-10-23 | 埃米林药品公司 | Glp-1用于制备治疗急性冠脉综合征的药物的用途 |
| NZ519752A (en) | 2000-10-20 | 2005-04-29 | Amylin Pharmaceuticals Inc | Treatment of hibernating myocardium and diabetic cardiomyopathy with a GLP-1 peptide |
| US7101561B2 (en) * | 2000-12-01 | 2006-09-05 | Innogenetics N.V. | Purified hepatitis C virus envelope proteins for diagnostic and therapeutic use |
| IL155812A0 (en) * | 2000-12-07 | 2003-12-23 | Lilly Co Eli | Glp-1 fusion proteins |
| WO2002097038A2 (en) | 2001-05-25 | 2002-12-05 | Human Genome Sciences, Inc. | Chemokine beta-1 fusion proteins |
| AU2002322403A1 (en) | 2001-08-23 | 2003-03-10 | Eli Lilly And Company | Glucagon-like peptide-1 analogs |
| WO2003042354A2 (en) * | 2001-09-04 | 2003-05-22 | Aventis Pharmaceuticals Inc. | Abrogen polypeptides, nucleic acids encoding them and methods for using them to inhibit angiogenesis |
| AU2002332041A1 (en) * | 2001-10-05 | 2003-04-22 | Human Genome Sciences, Inc. | Albumin fusion proteins |
| ES2411007T3 (es) * | 2001-10-10 | 2013-07-04 | Novo Nordisk A/S | Remodelación y glicoconjugación de péptidos |
| AU2002364586A1 (en) * | 2001-12-21 | 2003-07-30 | Delta Biotechnology Limited | Albumin fusion proteins |
| WO2003059934A2 (en) * | 2001-12-21 | 2003-07-24 | Human Genome Sciences, Inc. | Albumin fusion proteins |
| WO2003054182A2 (en) * | 2001-12-21 | 2003-07-03 | Nexia Biotechnologies, Inc. | Production of butyrylcholinesterases in transgenic mammals |
| KR101271635B1 (ko) * | 2001-12-21 | 2013-06-12 | 휴먼 게놈 사이언시즈, 인코포레이티드 | 알부민 융합 단백질 |
| WO2005003296A2 (en) * | 2003-01-22 | 2005-01-13 | Human Genome Sciences, Inc. | Albumin fusion proteins |
| US20080167238A1 (en) * | 2001-12-21 | 2008-07-10 | Human Genome Sciences, Inc. | Albumin Fusion Proteins |
| WO2003084563A1 (en) | 2002-04-04 | 2003-10-16 | Novo Nordisk A/S | Glp-1 agonist and cardiovascular complications |
| CN1241946C (zh) * | 2002-07-01 | 2006-02-15 | 美国福源集团 | 对多种细胞具刺激增生作用的人血清白蛋白重组融合蛋白 |
| DK1641823T3 (da) | 2003-06-12 | 2011-12-12 | Lilly Co Eli | GLP-1-analog fusionsproteiner |
| HUE027902T2 (en) | 2004-02-09 | 2016-11-28 | Human Genome Sciences Inc Corp Service Company | Albumin fusion proteins |
| US20070270339A1 (en) * | 2004-04-23 | 2007-11-22 | Serono, Inc. | Use of GPCR54 Ligands for the Treatment of Infertility |
| CA2599594A1 (en) | 2004-12-24 | 2006-07-13 | Amylin Pharmaceuticals, Inc. | Use of glp-1 and agonists thereof to prevent cardiac myocyte apoptosis |
| DK1888103T3 (da) | 2005-04-11 | 2012-04-23 | Amylin Pharmaceuticals Inc | Anvendelse af glp-1, exendin og agonister deraf til forsinkelse eller forhindring af kardial remodellering |
| WO2007021494A2 (en) | 2005-08-12 | 2007-02-22 | Human Genome Sciences, Inc. | Albumin fusion proteins |
| WO2007139941A2 (en) | 2006-05-26 | 2007-12-06 | Amylin Pharmaceuticals, Inc. | Composition and methods for treatment of congestive heart failure |
| WO2007146038A2 (en) | 2006-06-07 | 2007-12-21 | Human Genome Sciences, Inc. | Albumin fusion proteins |
| WO2008019143A2 (en) | 2006-08-04 | 2008-02-14 | Amylin Pharmaceuticals, Inc | Use of exendins and glp-i receptor agonists for altering lipoprotein particle size and subclass composition |
| JP5005450B2 (ja) * | 2007-07-13 | 2012-08-22 | 本田技研工業株式会社 | 燃料給油管の口元内部構造 |
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