JP2010538017A5 - - Google Patents
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- JP2010538017A5 JP2010538017A5 JP2010523166A JP2010523166A JP2010538017A5 JP 2010538017 A5 JP2010538017 A5 JP 2010538017A5 JP 2010523166 A JP2010523166 A JP 2010523166A JP 2010523166 A JP2010523166 A JP 2010523166A JP 2010538017 A5 JP2010538017 A5 JP 2010538017A5
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| GB2523399B (en) | 2014-02-25 | 2019-03-13 | Orban Tihamer | A composition comprising ten overlapping peptide fragments of the entire preproinsulin sequence |
| US20160039876A1 (en) * | 2014-03-28 | 2016-02-11 | Claresa Levetan | Insulin independence among patients with diabetes utilizing an optimized hamster reg3 gamma peptide |
| 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 |
| 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 |
| 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 |
| WO2015158241A1 (en) * | 2014-04-18 | 2015-10-22 | National Institute Of Biological Sciences, Beijing | Reg3 therapeutics |
| PL3139948T3 (pl) * | 2014-05-07 | 2020-08-10 | Novo Nordisk A/S | Leczenie cukrzycy z zastosowaniem glp-1 i anty-il-21 |
| US9932381B2 (en) | 2014-06-18 | 2018-04-03 | Sanofi | Exendin-4 derivatives as selective glucagon receptor agonists |
| CN105727262B (zh) * | 2014-12-08 | 2020-08-25 | 华东师范大学 | 胰再生源蛋白在制备促进过度炎症伤口愈合的药物中的应用 |
| CN105732793A (zh) * | 2014-12-08 | 2016-07-06 | 华东师范大学 | 一种胰再生源蛋白衍生物及其应用 |
| AR105319A1 (es) | 2015-06-05 | 2017-09-27 | Sanofi Sa | Profármacos que comprenden un conjugado agonista dual de glp-1 / glucagón conector ácido hialurónico |
| TW201706291A (zh) | 2015-07-10 | 2017-02-16 | 賽諾菲公司 | 作為選擇性肽雙重ｇｌｐ－１／升糖素受體促效劑之新毒蜥外泌肽（ｅｘｅｎｄｉｎ－４）衍生物 |
| CN108366985B (zh) | 2015-08-28 | 2021-06-18 | 赛品制药有限责任公司 | 用于疾病治疗的方法 |
| CN109195983B (zh) * | 2016-03-10 | 2022-05-17 | 深圳君圣泰生物技术有限公司 | 胰岛新生多肽和类似物的缀合物及其方法 |
| US10772929B2 (en) * | 2017-05-11 | 2020-09-15 | Shenzhen Hightide Biopharmaceutical, Ltd. | Use of peptide compounds in treating acute pancreatitis |
| KR101995768B1 (ko) * | 2019-03-13 | 2019-07-03 | (주)엔솔바이오사이언스 | 신규 펩타이드 및 그 용도 |
| KR102503349B1 (ko) * | 2019-05-14 | 2023-02-23 | 프로벤션 바이오, 인코포레이티드 | 제1형 당뇨병을 예방하기 위한 방법 및 조성물 |
| MA56197A (fr) * | 2019-06-13 | 2022-04-20 | Regeneron Pharma | Procédés d'élimination de composants indésirables pendant des processus chromatographiques en plusieurs étapes |
| US12006366B2 (en) | 2020-06-11 | 2024-06-11 | Provention Bio, Inc. | Methods and compositions for preventing type 1 diabetes |
| CN117442585B (zh) * | 2023-12-25 | 2024-03-19 | 北京爱思益普生物科技股份有限公司 | 一种靶向胰腺癌的雷公藤红素递送体及其制备方法 |
Family Cites Families (76)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| US4444887A (en) | 1979-12-10 | 1984-04-24 | Sloan-Kettering Institute | Process for making human antibody producing B-lymphocytes |
| US4716111A (en) | 1982-08-11 | 1987-12-29 | Trustees Of Boston University | Process for producing human antibodies |
| 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 |
| US4757060A (en) | 1986-03-04 | 1988-07-12 | Bristol-Myers Company | Non-steroidal anti-inflammatory compositions protected against gastrointestinal injury with a combination of certain H1 and H2, receptor blockers |
| 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 |
| JPH01137994A (ja) | 1987-08-10 | 1989-05-30 | Shionogi & Co Ltd | ｒｅｇ蛋白質 |
| EP1997891A1 (en) | 1988-09-02 | 2008-12-03 | Dyax Corporation | Generation and selection of recombinant varied binding proteins |
| US5223409A (en) | 1988-09-02 | 1993-06-29 | Protein Engineering Corp. | Directed evolution of novel binding proteins |
| US5530101A (en) | 1988-12-28 | 1996-06-25 | Protein Design Labs, Inc. | Humanized immunoglobulins |
| US5028535A (en) | 1989-01-10 | 1991-07-02 | Biosite Diagnostics, Inc. | Threshold ligand-receptor assay |
| US5703055A (en) | 1989-03-21 | 1997-12-30 | Wisconsin Alumni Research Foundation | Generation of antibodies through lipid mediated DNA delivery |
| GB8928874D0 (en) | 1989-12-21 | 1990-02-28 | Celltech Ltd | Humanised antibodies |
| WO1991010737A1 (en) | 1990-01-11 | 1991-07-25 | 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 |
| DE69133566T2 (de) | 1990-01-12 | 2007-12-06 | Amgen Fremont Inc. | Bildung von xenogenen Antikörpern |
| FR2661187B1 (fr) | 1990-04-20 | 1994-08-05 | Inst Nat Sante Rech Med | Proteine associee a la pancreatite aiguue. moyens pour le diagnostic de la pancreatite aiguue. |
| US5427908A (en) | 1990-05-01 | 1995-06-27 | Affymax Technologies N.V. | Recombinant library screening methods |
| GB9015198D0 (en) | 1990-07-10 | 1990-08-29 | Brien Caroline J O | Binding substance |
| US5698426A (en) | 1990-09-28 | 1997-12-16 | Ixsys, Incorporated | Surface expression libraries of heteromeric receptors |
| WO1992009690A2 (en) | 1990-12-03 | 1992-06-11 | Genentech, Inc. | Enrichment method for variant proteins with altered binding properties |
| DE69233750D1 (de) | 1991-04-10 | 2009-01-02 | Scripps Research Inst | Bibliotheken heterodimerer Rezeptoren mittels Phagemiden |
| DE69233482T2 (de) | 1991-05-17 | 2006-01-12 | Merck & Co., Inc. | Verfahren zur Verminderung der Immunogenität der variablen Antikörperdomänen |
| WO1992022324A1 (en) | 1991-06-14 | 1992-12-23 | Xoma Corporation | Microbially-produced antibody fragments and their conjugates |
| EP0590058B1 (en) | 1991-06-14 | 2003-11-26 | Genentech, Inc. | HUMANIZED Heregulin ANTIBODy |
| US5261752A (en) * | 1991-09-12 | 1993-11-16 | Nsk Ltd. | Bearing having passive pulser ring |
| US5565332A (en) | 1991-09-23 | 1996-10-15 | Medical Research Council | Production of chimeric antibodies - a combinatorial approach |
| ATE408012T1 (de) | 1991-12-02 | 2008-09-15 | Medical Res Council | Herstellung von autoantikörpern auf phagenoberflächen ausgehend von antikörpersegmentbibliotheken |
| DE69233204T2 (de) | 1991-12-13 | 2004-07-15 | Xoma Corp., Berkeley | Verfahren und materialien zur herstellung von modifizierten variablen antikörperdomänen und ihre therapeutische verwendung |
| GB9203459D0 (en) | 1992-02-19 | 1992-04-08 | Scotgen Ltd | Antibodies with germ-line variable regions |
| DK36392D0 (da) | 1992-03-19 | 1992-03-19 | Novo Nordisk As | Anvendelse af kemisk forbindelse |
| US5733743A (en) | 1992-03-24 | 1998-03-31 | Cambridge Antibody Technology Limited | Methods for producing members of specific binding pairs |
| US5639641A (en) | 1992-09-09 | 1997-06-17 | Immunogen Inc. | Resurfacing of rodent antibodies |
| WO1995015982A2 (en) | 1993-12-08 | 1995-06-15 | Genzyme Corporation | Process for generating specific antibodies |
| DK1231268T3 (da) | 1994-01-31 | 2005-11-21 | Univ Boston | Polyklonale antistofbiblioteker |
| 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 |
| WO1996019236A1 (en) | 1994-12-21 | 1996-06-27 | Yeda Research And Development Co. Ltd. | PEPTIDE p277 ANALOGS, AND PHARMACEUTICAL COMPOSITIONS COMPRISING THEM FOR TREATMENT OR DIAGNOSIS OF DIABETES |
| JP4111539B2 (ja) | 1995-02-22 | 2008-07-02 | イースタン・ヴァージニア・メディカル・スクール・オブ・ザ・メディカル・カレッジ・オブ・ハンプトン・ローズ | 膵島新生に関与するｉｎｇａｐタンパク質 |
| US5834590A (en) | 1995-02-22 | 1998-11-10 | Eastern Virginia Medical School Of The Medical College Of Hampton Roads | Ingap protein involved in pancreatic islet neogenesis |
| JP4312259B2 (ja) | 1995-04-27 | 2009-08-12 | アムジェン フレモント インク． | 免疫したゼノマウス（ＸｅｎｏＭｏｕｓｅ）に由来するヒト抗体 |
| EP0823941A4 (en) | 1995-04-28 | 2001-09-19 | Abgenix Inc | HUMAN ANTIBODIES DERIVED FROM IMMUNIZED XENO MOUSES |
| GB9601081D0 (en) | 1995-10-06 | 1996-03-20 | Cambridge Antibody Tech | Specific binding members for human transforming growth factor beta;materials and methods |
| 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 |
| US5916771A (en) | 1996-10-11 | 1999-06-29 | Abgenix, Inc. | Production of a multimeric protein by cell fusion method |
| DE69738539T2 (de) | 1996-12-03 | 2009-03-26 | Amgen Fremont Inc. | Vollkommen humane Antikörper die EGFR binden |
| 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 |
| DE19735587B4 (de) | 1997-08-16 | 2012-03-22 | Eberhard-Karls-Universität Tübingen Universitätsklinikum | Peptid mit radioprotektiver Wirkung, dieses enthaltende kosmetische oder pharmazeutische Zusammensetzung, für dieses kodierende Nukleinsäure, Herstellungsverfahren für dieses Peptid und die Verwendung als radioprotektives Agens |
| US6311415B1 (en) | 1998-09-14 | 2001-11-06 | Lind Shoe Company | Bowling shoe with replaceable tip |
| EP1076066A1 (en) | 1999-07-12 | 2001-02-14 | Zealand Pharmaceuticals A/S | Peptides for lowering blood glucose levels |
| US6713058B2 (en) | 1999-09-14 | 2004-03-30 | Milkhaus Laboratory, Inc. | Methods for alleviating symptoms associated with neuropathic conditions comprising administration of low levels of antibodies |
| US6664230B1 (en) * | 2000-08-24 | 2003-12-16 | The Regents Of The University Of California | Orally administered peptides to ameliorate atherosclerosis |
| US20040132644A1 (en) * | 2001-10-16 | 2004-07-08 | The Procter & Gamble Company | Composition and method for treating diabetes |
| JPWO2003064462A1 (ja) * | 2002-02-01 | 2005-05-26 | 中外製薬株式会社 | Ｐｅｇ結合ｐｔｈ又はｐｅｇ結合ｐｔｈ誘導体 |
| US7166439B2 (en) | 2002-03-01 | 2007-01-23 | Gmp Endotherapeutics, Inc. | Assay for anti-INGAP antibodies |
| WO2003094958A1 (en) * | 2002-05-09 | 2003-11-20 | Medtronic Minimed, Inc. | Immunoprotective methods for beta cell neogenesis |
| WO2003105897A1 (en) | 2002-06-14 | 2003-12-24 | Novo Nordisk A/S | Combined use of a modulator of cd3 and a glp-1 compound |
| US6946151B2 (en) | 2002-11-12 | 2005-09-20 | Ayurvedic-Life International, Llc | Therapeutic compositions |
| WO2004055519A2 (en) * | 2002-12-17 | 2004-07-01 | Sinogenomax Co. Ltd. | Specific markers for pancreatic cancer |
| ES2332590T3 (es) * | 2003-01-15 | 2010-02-09 | International Institute Of Cancer Immunology, Inc. | Dimero peptidico. |
| JP2007525434A (ja) | 2003-03-19 | 2007-09-06 | アブジェニックス インコーポレイテッド | Ｔ細胞、免疫グロブリンドメインおよびムチンドメイン１（ｔｉｍ−１）抗原に対する抗体およびその使用。 |
| WO2005035761A1 (en) * | 2003-10-16 | 2005-04-21 | Compugen Ltd. | Splice variants of preproglucagon, glucagon-like peptide-1 and oxyntomodulin |
| US7576121B2 (en) | 2003-11-12 | 2009-08-18 | Phenomix Corporation | Pyrrolidine compounds and methods for selective inhibition of dipeptidyl peptidase-IV |
| AU2005213472A1 (en) | 2004-02-10 | 2005-08-25 | Santarus, Inc. | Combination of proton pump inhibitor, buffering agent, and nonsteroidal anti-inflammatory agent |
| CA2589800A1 (en) | 2004-12-02 | 2006-06-08 | Domantis Limited | Bispecific domain antibodies targeting serum albumin and glp-1 or pyy |
| WO2006096565A2 (en) * | 2005-03-04 | 2006-09-14 | Curedm Inc. | Methods and pharmaceutical compositions for treating type 1 diabetes mellitus and other conditions |
| US20090142338A1 (en) * | 2005-03-04 | 2009-06-04 | Curedm, Inc. | Methods and Compositions for Treating Type 1 and Type 2 Diabetes Mellitus and Related Conditions |
| EP2295066B1 (en) | 2005-05-25 | 2016-04-27 | CureDM Group Holdings, LLC | Peptides, derivatives and analogs thereof, and methods of using same |
| CA2608522A1 (en) | 2005-05-26 | 2006-11-30 | The Johns Hopkins University | Biomarkers for breast cancer |
| CN100429227C (zh) * | 2005-06-29 | 2008-10-29 | 常州制药厂有限公司 | Exendin4多肽片段 |
| US20090155799A1 (en) | 2006-03-02 | 2009-06-18 | Yusuke Nakamura | Methods for diagnosing pancreatic cancer using reg4 protein |
| WO2008064306A2 (en) * | 2006-11-22 | 2008-05-29 | Curedm, Inc. | Methods and compositions relating to islet cell neogenesis |
| PT2193142E (pt) | 2007-08-30 | 2015-04-22 | Curedm Group Holdings Llc | Composições e procedimentos de utilização de peptídeos pro-ilhota e seus análogos |
| US20110082080A1 (en) * | 2007-10-12 | 2011-04-07 | Curedm Group Holdings, Llc | Compositions and methods of using the human proislet peptide receptor |
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