JP2009529917A - 標的ポリペプチドの同定方法および免疫学的疾患の治療のためのその使用 - Google Patents
標的ポリペプチドの同定方法および免疫学的疾患の治療のためのその使用 Download PDFInfo
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| CA2652570A1 (en) * | 2006-05-15 | 2007-11-22 | Viral Logic Systems Technology Corp. | Cd47 related compositions and methods for treating immunological diseases and disorders |
| US8377448B2 (en) * | 2006-05-15 | 2013-02-19 | The Board Of Trustees Of The Leland Standford Junior University | CD47 related compositions and methods for treating immunological diseases and disorders |
| US20090068635A1 (en) * | 2007-09-06 | 2009-03-12 | Muerhoff Anthony S | Indirectly labelled assay conjugates and methods of preparing and using same |
| EP2232258A4 (en) * | 2007-12-05 | 2011-01-05 | Govt Of The U S A As Represented By The Secretary Of The Dept Of Health & Human Services | IMPROVED VIRAL PROTEIN QUANTIFICATION AND VACCINE QUALITY CONTROL THEREWITH |
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| US8435961B2 (en) * | 2009-06-26 | 2013-05-07 | Massachusetts Institute Of Technology | Methods and compositions for increasing the activity of inhibitory RNA |
| US8268550B2 (en) * | 2009-06-26 | 2012-09-18 | Massachusetts Institute Of Technology | Compositions and methods for identification of PARP function, inhibitors, and activators |
| US20110097329A1 (en) | 2009-06-26 | 2011-04-28 | Massachusetts Institute Of Technology | Compositions and methods for treating cancer and modulating stress granule formation |
| CN104131035A (zh) | 2009-12-10 | 2014-11-05 | 瑞泽恩制药公司 | 生产重链抗体的小鼠 |
| EP2531859A4 (en) * | 2010-02-02 | 2013-07-31 | Jolla Inst Allergy Immunolog | Compositions and methods of modulating receptor protein tyrosine phosphatases |
| BR112016021572A2 (pt) | 2014-03-21 | 2017-10-03 | Regeneron Pharma | Métodos para preparar um animal não humano geneticamente modificado e para produzir proteínas de ligação, hibridoma, ácido nucleico, célula, e, proteína de ligação |
| EP3172228B1 (en) * | 2014-07-25 | 2019-02-27 | Theravectys | Lentiviral vectors for regulated expression of a chimeric antigen receptor molecule |
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| WO2005002526A2 (en) * | 2003-07-01 | 2005-01-13 | President And Fellows Of Harvard College | Method and compositions for treatment of viral infections |
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Family Cites Families (75)
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| US4411993A (en) | 1981-04-29 | 1983-10-25 | Steven Gillis | Hybridoma antibody which inhibits interleukin 2 activity |
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| US4952496A (en) | 1984-03-30 | 1990-08-28 | Associated Universities, Inc. | Cloning and expression of the gene for bacteriophage T7 RNA polymerase |
| JP2624470B2 (ja) | 1984-10-02 | 1997-06-25 | バイオジェン インコーポレイテッド | ストレプトアビジン様ポリペプチドの製造 |
| US5272254A (en) | 1984-10-02 | 1993-12-21 | Biogen Inc. | Production of streptavidin-like polypeptides |
| US4902614A (en) | 1984-12-03 | 1990-02-20 | Teijin Limited | Monoclonal antibody to human protein C |
| US5168062A (en) | 1985-01-30 | 1992-12-01 | University Of Iowa Research Foundation | Transfer vectors and microorganisms containing human cytomegalovirus immediate-early promoter-regulatory DNA sequence |
| US5011912A (en) | 1986-12-19 | 1991-04-30 | Immunex Corporation | Hybridoma and monoclonal antibody for use in an immunoaffinity purification system |
| US5091513A (en) | 1987-05-21 | 1992-02-25 | Creative Biomolecules, Inc. | Biosynthetic antibody binding sites |
| US5132405A (en) | 1987-05-21 | 1992-07-21 | Creative Biomolecules, Inc. | Biosynthetic antibody binding sites |
| ATE120761T1 (de) | 1987-05-21 | 1995-04-15 | Creative Biomolecules Inc | Multifunktionelle proteine mit vorbestimmter zielsetzung. |
| GB8719042D0 (en) | 1987-08-12 | 1987-09-16 | Parker D | Conjugate compounds |
| GB8723661D0 (en) | 1987-10-08 | 1987-11-11 | British Bio Technology | Synthetic gene |
| US6018026A (en) | 1988-01-22 | 2000-01-25 | Zymogenetics, Inc. | Biologically active dimerized and multimerized polypeptide fusions |
| US5567584A (en) | 1988-01-22 | 1996-10-22 | Zymogenetics, Inc. | Methods of using biologically active dimerized polypeptide fusions to detect PDGF |
| US5223409A (en) | 1988-09-02 | 1993-06-29 | Protein Engineering Corp. | Directed evolution of novel binding proteins |
| GB8903022D0 (en) | 1989-02-10 | 1989-03-30 | Celltech Ltd | Chemical compounds |
| US5225538A (en) | 1989-02-23 | 1993-07-06 | Genentech, Inc. | Lymphocyte homing receptor/immunoglobulin fusion proteins |
| EP0438803B1 (en) | 1990-01-26 | 1997-03-12 | Immunomedics, Inc. | Vaccines against cancer and infectious diseases |
| US5567588A (en) | 1990-06-11 | 1996-10-22 | University Research Corporation | Systematic evolution of ligands by exponential enrichment: Solution SELEX |
| US5723286A (en) | 1990-06-20 | 1998-03-03 | Affymax Technologies N.V. | Peptide library and screening systems |
| US7253264B1 (en) | 1990-06-28 | 2007-08-07 | Sanofi-Arentideutschland GmbH | Immunoglobulin fusion proteins, their production and use |
| US20030064480A1 (en) | 1990-06-28 | 2003-04-03 | Leander Lauffer | Fusion proteins with immunoglobulin portions, the preparation and use thereof |
| EP0542810A1 (en) | 1990-08-02 | 1993-05-26 | B.R. Centre Limited | Methods for the production of proteins with a desired function |
| US5877397A (en) | 1990-08-29 | 1999-03-02 | Genpharm International Inc. | Transgenic non-human animals capable of producing heterologous antibodies of various isotypes |
| US6072039A (en) | 1991-04-19 | 2000-06-06 | Rohm And Haas Company | Hybrid polypeptide comparing a biotinylated avidin binding polypeptide fused to a polypeptide of interest |
| GB9112536D0 (en) | 1991-06-11 | 1991-07-31 | Celltech Ltd | Chemical compounds |
| GB9120467D0 (en) | 1991-09-26 | 1991-11-06 | Celltech Ltd | Anti-hmfg antibodies and process for their production |
| US5270170A (en) | 1991-10-16 | 1993-12-14 | Affymax Technologies N.V. | Peptide library and screening method |
| US5733731A (en) | 1991-10-16 | 1998-03-31 | Affymax Technologies N.V. | Peptide library and screening method |
| DE4135543A1 (de) | 1991-10-28 | 1993-04-29 | Boehringer Mannheim Gmbh | Rekombinantes core-streptavidin |
| AU676150B2 (en) | 1992-01-23 | 1997-03-06 | Merck Patent Gmbh | Monomeric and dimeric antibody-fragment fusion proteins |
| DE69312700T2 (de) | 1992-04-14 | 1998-02-19 | Cornell Res Foundation Inc | Makromoleküle auf basis von dendritischen polymeren und verfahren zur herstellung |
| EP0578515A3 (en) | 1992-05-26 | 1995-05-10 | Bristol Myers Squibb Co | Humanized monoclonal antibodies. |
| JPH07507449A (ja) | 1992-05-29 | 1995-08-24 | イー・アイ・デユポン・ドウ・ヌムール・アンド・カンパニー | バチルススブチリス（Ｂａｃｉｌｌｕｓｓｕｂｔｉｌｉｓ）からのストレプトアビジンの産生 |
| US5359039A (en) | 1993-07-09 | 1994-10-25 | Immunex Corporation | Isolated poxvirus A53R-equivalent tumor necrosis factor antagonists |
| US5922545A (en) | 1993-10-29 | 1999-07-13 | Affymax Technologies N.V. | In vitro peptide and antibody display libraries |
| US5773569A (en) | 1993-11-19 | 1998-06-30 | Affymax Technologies N.V. | Compounds and peptides that bind to the erythropoietin receptor |
| US5786331A (en) * | 1994-02-02 | 1998-07-28 | Affymax Technologies N.V. | Peptides and compounds that bind to the IL-1 receptor |
| US5608035A (en) | 1994-02-02 | 1997-03-04 | Affymax Technologies N.V. | Peptides and compounds that bind to the IL-1 receptor |
| US5880096A (en) | 1994-02-02 | 1999-03-09 | Affymax Technologies N.V. | Peptides and compounds that bind to the IL-1 receptor |
| US5869451A (en) | 1995-06-07 | 1999-02-09 | Glaxo Group Limited | Peptides and compounds that bind to a receptor |
| US6699843B2 (en) | 1995-06-07 | 2004-03-02 | Gilead Sciences, Inc. | Method for treatment of tumors using nucleic acid ligands to PDGF |
| US5746516A (en) | 1995-08-11 | 1998-05-05 | Hitachi Powdered Metals Co., Ltd. | Porous bearing system having internal grooves and electric motor provided with the same |
| US5871740A (en) * | 1995-09-29 | 1999-02-16 | Immunex Corporation | Methods of using poxvirus p35 as a chemokine inhibitor and compositions therefore |
| CA2267139A1 (en) | 1996-10-08 | 1998-04-16 | Ton Logtenberg | Methods and means for selecting peptides and proteins having specific affinity for a target |
| EP1707631A3 (en) * | 1996-11-20 | 2006-12-27 | Introgen Therapeutics, Inc. | An improved method for the production and purification of adenoviral vectors |
| DE69834179T2 (de) | 1997-02-21 | 2007-02-01 | Oxxon Therapeutics Ltd. | Rekombinantes pockenvirus das das lösliche chemokine-bindende protein kodierende gen a41l nicht exprimieren kann. |
| US6703015B1 (en) | 1999-09-03 | 2004-03-09 | Ramot At Tel-Aviv University Ltd. | Filamentous bacteriophage displaying an β-amyloid epitope |
| DE69939982D1 (de) * | 1998-08-07 | 2009-01-08 | Immunex Corp | B7l-1 moleküle |
| US7488590B2 (en) | 1998-10-23 | 2009-02-10 | Amgen Inc. | Modified peptides as therapeutic agents |
| US6660843B1 (en) | 1998-10-23 | 2003-12-09 | Amgen Inc. | Modified peptides as therapeutic agents |
| US6867289B1 (en) | 1998-10-26 | 2005-03-15 | Board Of Regents, The University Of Texas Systems | Thio-modified aptamer synthetic methods and compositions |
| GB9916703D0 (en) | 1999-07-16 | 1999-09-15 | Alcami Antonio | Viral protein binding compositions and methods |
| DK2796553T3 (da) | 2000-03-30 | 2019-09-30 | Whitehead Inst Biomedical Res | Rna-sekvensspecifikke formidlere af rna-interferens |
| CA2438628A1 (en) | 2001-02-19 | 2002-08-29 | Merck Patent Gesellschaft Mit Beschraenkter Haftung | Artificial proteins with reduced immunogenicity |
| CA2504413A1 (en) | 2001-03-22 | 2002-10-03 | Vlaams Interuniversitair Instituut Voor Biotechnologie Vzw | Methods and apparatus for gel-free qualitative and quantitative proteome analysis, and uses therefore |
| US6829539B2 (en) | 2001-04-13 | 2004-12-07 | The Institute For Systems Biology | Methods for quantification and de novo polypeptide sequencing by mass spectrometry |
| US6852486B2 (en) | 2001-07-12 | 2005-02-08 | Immunex Corp. | Viral proteins capable of binding LAR |
| US6680840B2 (en) | 2001-08-31 | 2004-01-20 | Hewlett-Packard Development Company, L.P. | Electro-mechanical interlock for hot-swappable power supplies and cards |
| FR2830020B1 (fr) * | 2001-09-25 | 2003-12-19 | Univ Victor Segalen Bordeaux 2 | Acide nucleique pour l'obtention d'un polynucleotide codant une proteine de detection et d'isolement d'un ligand "proie" et applications de cet acide nucleique |
| US7825227B2 (en) * | 2002-05-09 | 2010-11-02 | Prolexys Pharmaceuticals, Inc. | Method for purification of a protein complex and identification of its components |
| US8029803B2 (en) | 2002-06-20 | 2011-10-04 | Paladin Labs, Inc. | Chimeric antigens for eliciting an immune response |
| US20040265799A1 (en) * | 2003-06-24 | 2004-12-30 | Compugen Ltd. | Human-virus homologous sequences and uses thereof |
| WO2005121178A2 (en) * | 2004-06-08 | 2005-12-22 | Wisconsin Alumni Research Foundation | Immunoaffinity chromatography polyol-responsive monoclonal antibodies |
| US20070134234A1 (en) | 2005-09-29 | 2007-06-14 | Viral Logic Systems Technology Corp. | Immunomodulatory compositions and uses therefor |
| ATE485517T1 (de) | 2006-03-22 | 2010-11-15 | Viral Logic Systems Technology | Verfahren zur identifizierung von polypeptid- targets |
| TWI497333B (zh) | 2011-06-14 | 2015-08-21 | Giant Mfg Co Ltd | 自行車適配產生方法、自行車適配系統與電腦程式產品 |
| US9104666B2 (en) | 2012-09-04 | 2015-08-11 | Oracle International Corporation | Controlling access to a large number of electronic resources |
-
2007
- 2007-03-22 AT AT07753924T patent/ATE485517T1/de active
- 2007-03-22 JP JP2009501596A patent/JP2009529917A/ja active Pending
- 2007-03-22 CA CA002646391A patent/CA2646391A1/en not_active Abandoned
- 2007-03-22 DK DK07753924.5T patent/DK2005185T3/da active
- 2007-03-22 ES ES07753924T patent/ES2354954T3/es active Active
- 2007-03-22 WO PCT/US2007/007340 patent/WO2007109370A2/en not_active Ceased
- 2007-03-22 PL PL07753924T patent/PL2005185T3/pl unknown
- 2007-03-22 EP EP07753924A patent/EP2005185B1/en not_active Not-in-force
- 2007-03-22 EP EP11155067A patent/EP2322931A3/en not_active Withdrawn
- 2007-03-22 DE DE602007009954T patent/DE602007009954D1/de active Active
- 2007-03-22 EP EP10186919A patent/EP2275816A3/en not_active Withdrawn
- 2007-03-22 US US11/728,329 patent/US8293500B2/en not_active Expired - Fee Related
- 2007-03-22 PT PT07753924T patent/PT2005185E/pt unknown
- 2007-03-22 AU AU2007227218A patent/AU2007227218A1/en not_active Abandoned
-
2012
- 2012-09-14 US US13/616,694 patent/US20130129748A1/en not_active Abandoned
Patent Citations (3)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| WO2004003509A2 (en) * | 2002-06-28 | 2004-01-08 | Genepharm, Inc. | A method to identify specific interaction between ligand and receptor |
| WO2005002526A2 (en) * | 2003-07-01 | 2005-01-13 | President And Fellows Of Harvard College | Method and compositions for treatment of viral infections |
| US20050106663A1 (en) * | 2003-11-13 | 2005-05-19 | Stratagene | Compositions and methods for protein isolation |
Cited By (1)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| JP2019501631A (ja) * | 2015-10-23 | 2019-01-24 | アポジェニックス アーゲー | 一本鎖ｇｉｔｒ受容体アゴニストタンパク質 |
Also Published As
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|---|---|
| EP2005185B1 (en) | 2010-10-20 |
| EP2322931A2 (en) | 2011-05-18 |
| WO2007109370A3 (en) | 2007-12-13 |
| EP2275816A3 (en) | 2011-06-29 |
| DK2005185T3 (da) | 2011-01-31 |
| CA2646391A1 (en) | 2007-09-27 |
| PT2005185E (pt) | 2011-01-27 |
| EP2275816A2 (en) | 2011-01-19 |
| US8293500B2 (en) | 2012-10-23 |
| EP2005185A2 (en) | 2008-12-24 |
| AU2007227218A1 (en) | 2007-09-27 |
| ES2354954T3 (es) | 2011-03-21 |
| DE602007009954D1 (de) | 2010-12-02 |
| US20070264654A1 (en) | 2007-11-15 |
| PL2005185T3 (pl) | 2011-05-31 |
| EP2322931A3 (en) | 2011-08-31 |
| WO2007109370A2 (en) | 2007-09-27 |
| ATE485517T1 (de) | 2010-11-15 |
| HK1126856A1 (en) | 2009-09-11 |
| US20130129748A1 (en) | 2013-05-23 |
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