CA2646391A1 - Methods for identifying polypeptide targets and uses thereof for treating immunological diseases - Google Patents
Methods for identifying polypeptide targets and uses thereof for treating immunological diseases Download PDFInfo
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- CA2646391A1 CA2646391A1 CA002646391A CA2646391A CA2646391A1 CA 2646391 A1 CA2646391 A1 CA 2646391A1 CA 002646391 A CA002646391 A CA 002646391A CA 2646391 A CA2646391 A CA 2646391A CA 2646391 A1 CA2646391 A1 CA 2646391A1
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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 |
| US20100204121A1 (en) | 2009-02-10 | 2010-08-12 | Romero Augustin T | Dietary supplements containing terpenoid acids of maslinic acid or oleanolic acid and process for enhancing muscle mass in mammals |
| 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 |
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| WO2019040899A1 (en) * | 2017-08-25 | 2019-02-28 | Ichan School Of Medicine At Mount Sinai | FUSION PROTEINS COMPRISING DETECTABLE MARKERS, NUCLEIC ACID MOLECULES, AND METHOD OF TRACKING A CELL |
| US11974552B2 (en) * | 2018-08-02 | 2024-05-07 | The University Of Toledo | Transgenic C57BL6-BTBR mouse with a humanized MHC II gene that expresses GAD65 |
Family Cites Families (78)
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| US4376110A (en) | 1980-08-04 | 1983-03-08 | Hybritech, Incorporated | Immunometric assays using monoclonal antibodies |
| 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 |
| WO2004003509A2 (en) * | 2002-06-28 | 2004-01-08 | Genepharm, Inc. | A method to identify specific interaction between ligand and receptor |
| US20040265799A1 (en) * | 2003-06-24 | 2004-12-30 | Compugen Ltd. | Human-virus homologous sequences and uses thereof |
| WO2005002526A2 (en) * | 2003-07-01 | 2005-01-13 | President And Fellows Of Harvard College | Method and compositions for treatment of viral infections |
| US7238478B2 (en) * | 2003-11-13 | 2007-07-03 | Stratagene California | Compositions and methods for protein isolation |
| 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
Also Published As
| Publication number | Publication date |
|---|---|
| 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 |
| PT2005185E (pt) | 2011-01-27 |
| EP2275816A2 (en) | 2011-01-19 |
| US8293500B2 (en) | 2012-10-23 |
| EP2005185A2 (en) | 2008-12-24 |
| JP2009529917A (ja) | 2009-08-27 |
| 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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