DE69722176T2 - Verfahren zur suche nach transdominanten effektorpeptiden und rna-molekülen - Google Patents
Verfahren zur suche nach transdominanten effektorpeptiden und rna-molekülen Download PDFInfo
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- DE69722176T2 DE69722176T2 DE69722176T DE69722176T DE69722176T2 DE 69722176 T2 DE69722176 T2 DE 69722176T2 DE 69722176 T DE69722176 T DE 69722176T DE 69722176 T DE69722176 T DE 69722176T DE 69722176 T2 DE69722176 T2 DE 69722176T2
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- C12N—MICROORGANISMS OR ENZYMES; COMPOSITIONS THEREOF; PROPAGATING, PRESERVING, OR MAINTAINING MICROORGANISMS; MUTATION OR GENETIC ENGINEERING; CULTURE MEDIA
- C12N2830/00—Vector systems having a special element relevant for transcription
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- C12N2830/00—Vector systems having a special element relevant for transcription
- C12N2830/80—Vector systems having a special element relevant for transcription from vertebrates
- C12N2830/85—Vector systems having a special element relevant for transcription from vertebrates mammalian
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- 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
- C12N2840/00—Vectors comprising a special translation-regulating system
- C12N2840/20—Vectors comprising a special translation-regulating system translation of more than one cistron
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- C—CHEMISTRY; METALLURGY
- C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
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- C12N2840/00—Vectors comprising a special translation-regulating system
- C12N2840/20—Vectors comprising a special translation-regulating system translation of more than one cistron
- C12N2840/203—Vectors comprising a special translation-regulating system translation of more than one cistron having an IRES
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- C12N2840/00—Vectors comprising a special translation-regulating system
- C12N2840/44—Vectors comprising a special translation-regulating system being a specific part of the splice mechanism, e.g. donor, acceptor
-
- G—PHYSICS
- G01—MEASURING; TESTING
- G01N—INVESTIGATING OR ANALYSING MATERIALS BY DETERMINING THEIR CHEMICAL OR PHYSICAL PROPERTIES
- G01N2500/00—Screening for compounds of potential therapeutic value
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- G—PHYSICS
- G01—MEASURING; TESTING
- G01N—INVESTIGATING OR ANALYSING MATERIALS BY DETERMINING THEIR CHEMICAL OR PHYSICAL PROPERTIES
- G01N2510/00—Detection of programmed cell death, i.e. apoptosis
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Applications Claiming Priority (5)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| US58991196A | 1996-01-23 | 1996-01-23 | |
| US08/589,109 US6365344B1 (en) | 1996-01-23 | 1996-01-23 | Methods for screening for transdominant effector peptides and RNA molecules |
| US589109 | 1996-01-23 | ||
| US589911 | 1996-01-23 | ||
| PCT/US1997/001048 WO1997027213A1 (en) | 1996-01-23 | 1997-01-23 | Methods for screening for transdominant effector peptides and rna molecules |
Publications (2)
| Publication Number | Publication Date |
|---|---|
| DE69722176D1 DE69722176D1 (de) | 2003-06-26 |
| DE69722176T2 true DE69722176T2 (de) | 2004-03-18 |
Family
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Family Applications (1)
| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| DE69722176T Expired - Lifetime DE69722176T2 (de) | 1996-01-23 | 1997-01-23 | Verfahren zur suche nach transdominanten effektorpeptiden und rna-molekülen |
Country Status (9)
| Country | Link |
|---|---|
| US (5) | US6455247B1 (enExample) |
| EP (2) | EP0877752B1 (enExample) |
| JP (2) | JP2000504220A (enExample) |
| AU (2) | AU725716C (enExample) |
| CA (1) | CA2244222A1 (enExample) |
| DE (1) | DE69722176T2 (enExample) |
| DK (1) | DK0877752T3 (enExample) |
| ES (1) | ES2200150T3 (enExample) |
| WO (2) | WO1997027212A1 (enExample) |
Families Citing this family (139)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| US6140466A (en) | 1994-01-18 | 2000-10-31 | The Scripps Research Institute | Zinc finger protein derivatives and methods therefor |
| EP1405911A1 (en) * | 1994-07-20 | 2004-04-07 | The General Hospital Corporation | Interaction trap systems for detecting protein interactions |
| USRE39229E1 (en) | 1994-08-20 | 2006-08-08 | Gendaq Limited | Binding proteins for recognition of DNA |
| GB9824544D0 (en) | 1998-11-09 | 1999-01-06 | Medical Res Council | Screening system |
| US20050002902A1 (en) * | 1995-12-28 | 2005-01-06 | Liming Yu | Hybrid with interferon-alpha and an immunoglobulin Fc for treatment of tumors and viral infections |
| US6365344B1 (en) * | 1996-01-23 | 2002-04-02 | The Board Of Trustees Of The Leland Stanford Junior University | Methods for screening for transdominant effector peptides and RNA molecules |
| DE69722176T2 (de) | 1996-01-23 | 2004-03-18 | The Board Of Trustees Of The Leland Stanford Junior University, Palo Alto | Verfahren zur suche nach transdominanten effektorpeptiden und rna-molekülen |
| US5955275A (en) | 1997-02-14 | 1999-09-21 | Arcaris, Inc. | Methods for identifying nucleic acid sequences encoding agents that affect cellular phenotypes |
| US6060240A (en) * | 1996-12-13 | 2000-05-09 | Arcaris, Inc. | Methods for measuring relative amounts of nucleic acids in a complex mixture and retrieval of specific sequences therefrom |
| US6623922B1 (en) | 1997-02-14 | 2003-09-23 | Deltagen Proteomics | Methods for identifying, characterizing, and evolving cell-type specific CIS regulatory elements |
| GB9710809D0 (en) | 1997-05-23 | 1997-07-23 | Medical Res Council | Nucleic acid binding proteins |
| US6969584B2 (en) | 1997-06-12 | 2005-11-29 | Rigel Pharmaceuticals, Inc. | Combinatorial enzymatic complexes |
| DE19737562A1 (de) * | 1997-08-28 | 1999-05-06 | Otogene Biotechnologische Fors | Verfahren zur Identifizierung von Wechselwirkungen zwischen Proteinen bzw. Peptiden |
| WO1999024563A1 (en) * | 1997-11-07 | 1999-05-20 | Iconix Pharmaceuticals, Inc. | Surrogate genetics target characterization method |
| US6197502B1 (en) * | 1997-11-17 | 2001-03-06 | Cytos Biotechnology Ag | Expression cloning processes for the discovery characterization, and isolation of genes encoding polypeptides with a predetermined property |
| US6475726B1 (en) | 1998-01-09 | 2002-11-05 | Cubist Pharmaceuticals, Inc. | Method for identifying validated target and assay combinations for drug development |
| US6846625B1 (en) | 1998-01-09 | 2005-01-25 | Cubist Pharmaceuticals, Inc. | Method for identifying validated target and assay combination for drug development |
| US6410248B1 (en) | 1998-01-30 | 2002-06-25 | Massachusetts Institute Of Technology | General strategy for selecting high-affinity zinc finger proteins for diverse DNA target sites |
| DE19805334A1 (de) * | 1998-02-11 | 1999-08-12 | Otogene Biotechnologische Fors | Verfahren zur Entwicklung eines pharmazeutischen Wirkstoffes |
| WO1999041371A1 (en) * | 1998-02-13 | 1999-08-19 | Genetrace Systems, Inc. | Use of ribozymes for functionating genes |
| US6479626B1 (en) | 1998-03-02 | 2002-11-12 | Massachusetts Institute Of Technology | Poly zinc finger proteins with improved linkers |
| WO1999047656A2 (en) | 1998-03-17 | 1999-09-23 | Gendaq Limited | Nucleic acid binding proteins |
| AU3707099A (en) * | 1998-04-08 | 1999-11-01 | Max-Planck-Gesellschaft Zur Forderung Der Wissenschaften E.V. | Process for producing cell clone libraries |
| EP1070145A1 (en) * | 1998-04-09 | 2001-01-24 | Iconix Pharmaceuticals, Inc. | Methods for identifying genetic determinants associated with modulation of test compound activity |
| US6897031B1 (en) * | 1998-04-17 | 2005-05-24 | Rigel Pharmaceuticals, Inc. | Multiparameter FACS assays to detect alterations in exocytosis |
| US6461813B2 (en) * | 1998-09-21 | 2002-10-08 | Rigel Pharmaceuticals, Inc. | Multiparameter FACS assays to detect alterations in cell cycle regulation |
| US8334238B2 (en) * | 1998-04-17 | 2012-12-18 | Rigel, Inc. | Multiparameter FACS assays to detect alterations in cellular parameters and to screen small molecule libraries |
| US7060433B1 (en) * | 1999-11-12 | 2006-06-13 | Rigel Pharmaceuticals, Inc. | Methods and compositions for screening using diphtheria toxin constructs |
| US7090976B2 (en) | 1999-11-10 | 2006-08-15 | Rigel Pharmaceuticals, Inc. | Methods and compositions comprising Renilla GFP |
| US20040002056A1 (en) * | 1998-05-12 | 2004-01-01 | Lorens James B. | Methods of screening for bioactive agents using cells transformed with self-inactivating viral vectors |
| US7001733B1 (en) * | 1998-05-12 | 2006-02-21 | Rigel Pharmaceuticals, Inc. | Methods and compositions for screening for modulations of IgE synthesis, secretion and switch rearrangement |
| US6413776B1 (en) | 1998-06-12 | 2002-07-02 | Galapagos Geonomics N.V. | High throughput screening of gene function using adenoviral libraries for functional genomics applications |
| DE19829495A1 (de) * | 1998-07-02 | 2000-01-05 | Jacques Paysan | Reagenzien und deren Anwendung zur Untersuchung von Wechselwirkungen zwischen zellulären Molekülen und deren Lokalisation in Zellen |
| EP1270746A1 (en) * | 1998-07-20 | 2003-01-02 | Inoxell A/S | Methods for the identification of ligand and target biomolecules |
| JP2002521652A (ja) * | 1998-07-20 | 2002-07-16 | ファーメクサ エイ/エス | リガンドおよびターゲット生体分子を同定するための新規な方法 |
| US6472151B1 (en) | 1998-08-19 | 2002-10-29 | Bristol-Myers Squibb Company | Method of screening for compounds that modulate the activity of a molecular target |
| AU5790199A (en) * | 1998-10-05 | 2000-04-26 | Duke University | Method and apparatus for detecting binding interactions (in vivo) |
| US7013219B2 (en) | 1999-01-12 | 2006-03-14 | Sangamo Biosciences, Inc. | Regulation of endogenous gene expression in cells using zinc finger proteins |
| US6453242B1 (en) | 1999-01-12 | 2002-09-17 | Sangamo Biosciences, Inc. | Selection of sites for targeting by zinc finger proteins and methods of designing zinc finger proteins to bind to preselected sites |
| US7070934B2 (en) | 1999-01-12 | 2006-07-04 | Sangamo Biosciences, Inc. | Ligand-controlled regulation of endogenous gene expression |
| US6534261B1 (en) | 1999-01-12 | 2003-03-18 | Sangamo Biosciences, Inc. | Regulation of endogenous gene expression in cells using zinc finger proteins |
| US6599692B1 (en) | 1999-09-14 | 2003-07-29 | Sangamo Bioscience, Inc. | Functional genomics using zinc finger proteins |
| US6720139B1 (en) | 1999-01-27 | 2004-04-13 | Elitra Pharmaceuticals, Inc. | Genes identified as required for proliferation in Escherichia coli |
| AU774332B2 (en) | 1999-03-12 | 2004-06-24 | Gpc Biotech Inc. | Methods and reagents for identifying synthetic genetic elements |
| AU3893000A (en) * | 1999-03-16 | 2000-10-04 | Dana-Farber Cancer Institute, Inc. | Lentiviral vector system for high quantity screening |
| US20030104526A1 (en) | 1999-03-24 | 2003-06-05 | Qiang Liu | Position dependent recognition of GNN nucleotide triplets by zinc fingers |
| US6794136B1 (en) | 2000-11-20 | 2004-09-21 | Sangamo Biosciences, Inc. | Iterative optimization in the design of binding proteins |
| US7030215B2 (en) | 1999-03-24 | 2006-04-18 | Sangamo Biosciences, Inc. | Position dependent recognition of GNN nucleotide triplets by zinc fingers |
| DE69918260T2 (de) * | 1999-03-29 | 2005-07-14 | Michael Blind | Methoden zur Identifizierung und Validierung von funktionellen Zielen mittels Intrameren oder in vivo Selektion |
| US6524797B1 (en) | 1999-05-10 | 2003-02-25 | Bernhard O. Palsson | Methods of identifying therapeutic compounds in a genetically defined setting |
| AU5303200A (en) * | 1999-05-25 | 2000-12-12 | Rigel Pharmaceuticals, Inc. | Identification of novel mechanisms of drug resistance |
| US6737240B1 (en) | 1999-05-25 | 2004-05-18 | Rigel Pharmaceuticals, Inc. | Methods of screening for a multi-drug resistance conferring peptide |
| EP1055929A1 (en) * | 1999-05-26 | 2000-11-29 | Tibotec N.V. | Means and methods for drug discovery and the phenotypic characterisation of cells |
| IL146743A0 (en) * | 1999-05-31 | 2002-07-25 | Novozymes As | Screening method for peptides |
| AU2005209649B2 (en) * | 1999-05-31 | 2008-05-29 | Novozymes A/S | Screening method for peptides |
| AU2041901A (en) | 1999-11-09 | 2001-06-06 | Elitra Pharmaceuticals, Inc. | Genes essential for microbial proliferation and antisense thereto |
| EP1228233B1 (en) * | 1999-11-10 | 2007-01-10 | Rigel Pharmaceuticals, Inc. | Methods and compositions comprising renilla gfp |
| EP1236045B1 (en) | 1999-12-06 | 2005-11-09 | Sangamo Biosciences Inc. | Methods of using randomized libraries of zinc finger proteins for the identification of gene function |
| DK1242457T3 (da) * | 1999-12-28 | 2004-12-20 | Esbatech Ag | Intracellulære antistoffer [intracellulære antistoffer] med defineret struktur, der er stabil i et reducerende miljö, og anvendelse deraf |
| AU2001226935B2 (en) | 2000-01-24 | 2006-06-22 | Gendaq Limited | Nucleic acid binding polypeptides characterized by flexible linkers connected nucleic acid binding modules |
| US6582899B1 (en) * | 2000-02-15 | 2003-06-24 | Deltagen Proteomics, Inc. | Methods for identifying agents that cause a lethal phenotype, and agents thereof |
| AU2001247296A1 (en) * | 2000-03-06 | 2001-09-17 | Rigel Pharmaceuticals, Inc. | In vivo production of cyclic peptides |
| US7252952B2 (en) * | 2000-03-06 | 2007-08-07 | Rigel Pharmaceuticals, Inc. | In vivo production of cyclic peptides for inhibiting protein—protein interaction |
| US7378248B2 (en) * | 2000-03-06 | 2008-05-27 | Rigel Pharmaceuticals, Inc. | In vivo production of cyclic peptides for inhibiting protein-protein interaction |
| US7566765B2 (en) * | 2000-03-06 | 2009-07-28 | Rigel Pharmaceuticals, Inc. | Heterocyclic compounds containing a nine-membered carbon-nitrogen ring |
| AU2001289284A1 (en) * | 2000-04-04 | 2001-10-15 | Enanta Pharmaceuticals, Inc. | Methods for identifying peptide aptamers capable of altering a cell phenotype |
| US6762031B2 (en) * | 2000-06-16 | 2004-07-13 | University Of Medicine And Dentistry Of New Jersey | Targeting viral vectors to specific cells |
| US20030148924A1 (en) * | 2002-07-09 | 2003-08-07 | Tamar Tennenbaum | Methods and pharmaceutical compositions of healing wounds |
| US20040037828A1 (en) * | 2002-07-09 | 2004-02-26 | Bar-Ilan University | Methods and pharmaceutical compositions for healing wounds |
| WO2002009639A2 (en) * | 2000-07-31 | 2002-02-07 | Bar Ilan University | Methods and pharmaceutical compositions for healing wounds |
| US20060258562A1 (en) * | 2000-07-31 | 2006-11-16 | Healor Ltd. | Methods and pharmaceutical compositions for healing wounds |
| US20100129332A1 (en) * | 2000-07-31 | 2010-05-27 | Tamar Tennenbaum | Methods and pharmaceutical compositions for healing wounds |
| DE10060959A1 (de) * | 2000-12-06 | 2002-06-20 | Aventis Res & Tech Gmbh & Co | Verfahren zur Isolierung und Identifizierung von Effektoren |
| US7026462B2 (en) | 2000-12-07 | 2006-04-11 | Sangamo Biosciences, Inc. | Regulation of angiogenesis with zinc finger proteins |
| US7067317B2 (en) | 2000-12-07 | 2006-06-27 | Sangamo Biosciences, Inc. | Regulation of angiogenesis with zinc finger proteins |
| US7700274B2 (en) | 2000-12-22 | 2010-04-20 | Sagres Discovery, Inc. | Compositions and methods in cancer associated with altered expression of KCNJ9 |
| US7892730B2 (en) | 2000-12-22 | 2011-02-22 | Sagres Discovery, Inc. | Compositions and methods for cancer |
| US7820447B2 (en) | 2000-12-22 | 2010-10-26 | Sagres Discovery Inc. | Compositions and methods for cancer |
| US7645441B2 (en) | 2000-12-22 | 2010-01-12 | Sagres Discovery Inc. | Compositions and methods in cancer associated with altered expression of PRLR |
| EP1353941B1 (en) | 2001-01-22 | 2013-03-13 | Sangamo BioSciences, Inc. | Modified zinc finger binding proteins |
| AU2002338446A1 (en) * | 2001-01-23 | 2002-11-05 | University Of Rochester Medical Center | Methods of producing or identifying intrabodies in eukaryotic cells |
| AU2002255495A1 (en) * | 2001-02-02 | 2002-08-19 | University Of Rochester | Methods of identifying regulator molecules |
| JP2004530117A (ja) * | 2001-02-22 | 2004-09-30 | プラエシス ファーマシューティカルズ インコーポレーテッド | 生物プロセスを調節するペプチドを同定する方法 |
| IL142481A0 (en) * | 2001-04-05 | 2002-03-10 | Yissum Res Dev Co | A method for identifying consitutively active mutants of mitogen activated protein kinases (mapk) and uses thereof |
| DE10119999A1 (de) * | 2001-04-23 | 2002-10-24 | Univ Heidelberg | Verfahren zur Identifizierung und Entwicklung von Substanzen oder Substanzgemischen die zelluläre Transport-, Prozessierungs- und Sekretionsprozesse beeinflussen |
| US20050255464A1 (en) * | 2001-07-19 | 2005-11-17 | Hagen Frederick S | Methods for the identification of peptidyl compounds interacting with extracellular target molecules |
| GB0118532D0 (en) * | 2001-07-30 | 2001-09-19 | Isis Innovation | Materials and methods relating to improved vaccination strategies |
| CN1633598A (zh) * | 2001-10-05 | 2005-06-29 | 科勒制药股份公司 | Toll样受体3信号传导的激动剂和拮抗剂 |
| WO2003038404A2 (en) * | 2001-11-01 | 2003-05-08 | Rensselaer Polytechnic Institute | In vitro metabolic engineering on microscale devices |
| AU2002361589A1 (en) * | 2001-11-06 | 2003-05-19 | Enanta Pharmaceuticals, Inc. | Methods and compositions for identifying peptide aptamers capable of altering a cell phenotype |
| US7262054B2 (en) | 2002-01-22 | 2007-08-28 | Sangamo Biosciences, Inc. | Zinc finger proteins for DNA binding and gene regulation in plants |
| AU2003205830A1 (en) | 2002-01-23 | 2003-09-02 | Mohamed Raafat El-Gewely | Molecular libraries |
| WO2003080808A2 (en) | 2002-03-21 | 2003-10-02 | Sagres Discovery, Inc. | Novel compositions and methods in cancer |
| US20030219723A1 (en) * | 2002-05-20 | 2003-11-27 | Lu Henry H. | Compositions and methods for screening and identifying anti-HCV agents |
| US20060121464A1 (en) * | 2002-06-07 | 2006-06-08 | Shophion Bioscience A/S | Screening methods |
| EP1539951A1 (en) * | 2002-06-21 | 2005-06-15 | Sinogenomax Co., Ltd. | Randomised dna libraries and double-stranded rna libraries, use and method of production thereof |
| US7361635B2 (en) | 2002-08-29 | 2008-04-22 | Sangamo Biosciences, Inc. | Simultaneous modulation of multiple genes |
| WO2004033715A1 (en) * | 2002-10-09 | 2004-04-22 | Novozymes A/S | A method for screening for an antimicrobial polypeptide |
| US20070099185A1 (en) * | 2002-11-04 | 2007-05-03 | Bioarctic Neuroscience Ab | Methods for the identification of agents that modulate the structure and processing of beta-amyloid precursor protein |
| JP2006505271A (ja) * | 2002-11-04 | 2006-02-16 | アイコジェネックス コーポレイション | 膜結合前駆タンパク質の構造およびプロセシングを調節する物質の同定のための方法 |
| EP1592708A2 (en) | 2003-02-14 | 2005-11-09 | Sagres Discovery, Inc. | Therapeutic gpcr targets in cancer |
| AU2004231997A1 (en) * | 2003-04-16 | 2004-11-04 | The University Of Mississippi | Immunostimulatory agents in botanicals |
| EP1625394A4 (en) * | 2003-04-23 | 2008-02-06 | Bioseek Inc | METHOD FOR ANALYZING BIOLOGICAL DATA PROFILES |
| GB0313173D0 (en) * | 2003-06-07 | 2003-07-16 | Givaudan Sa | Improvements in or related to organic compounds |
| RU2491952C2 (ru) * | 2003-07-15 | 2013-09-10 | Бар-Илан Юнивесити | Способы и фармакологические композиции для заживления ран |
| US7776584B2 (en) * | 2003-08-01 | 2010-08-17 | Genetix Limited | Animal cell colony picking apparatus and method |
| DK1651161T3 (da) | 2003-08-07 | 2012-01-30 | Healor Ltd | Farmaceutiske præparater og fremgangsmåder til at fremme sårheling |
| US20050052687A1 (en) * | 2003-08-12 | 2005-03-10 | Murata Kikai Kabushiki Kaisha | Image processing device and communication terminal device |
| CA2560751A1 (en) * | 2004-03-22 | 2005-10-06 | The Ohio State University Research Foundation | Methods for transfecting natural killer cells |
| US7745196B1 (en) | 2004-03-25 | 2010-06-29 | Rigel Pharmaceuticals, Inc. | Methods and compositions for identifying peptide modulators of cell surface receptors |
| EP1749022A2 (en) * | 2004-05-24 | 2007-02-07 | Rigel Pharmaceuticals, Inc. | Methods for cyclizing synthetic polymers |
| CA2567655C (en) | 2004-06-02 | 2015-06-30 | Diatech Pty Ltd | Binding moieties based on shark ignar domains |
| WO2006039630A2 (en) * | 2004-10-02 | 2006-04-13 | Indiana University Research & Technology Corporation | Materials and methods for identifying compounds that modulate the cell cycle |
| EP3300739A3 (en) | 2005-03-31 | 2018-07-18 | Agensys, Inc. | Antibodies and related molecules that bind to 161p2f10b proteins |
| EP1910557A2 (en) | 2005-04-07 | 2008-04-16 | Chiron Corporation | Cancer-related genes |
| AU2006235276A1 (en) | 2005-04-07 | 2006-10-19 | Novartis Vaccines And Diagnostics Inc. | CACNA1E in cancer diagnosis, detection and treatment |
| EP1940440A4 (en) * | 2005-08-29 | 2009-11-11 | Healor Ltd | METHOD AND COMPOSITIONS FOR THE PREVENTION AND TREATMENT OF DIABETIC AND AGED SKIN |
| US20090221441A1 (en) * | 2005-11-01 | 2009-09-03 | Rensselaer Polytechnic Institute | Three-dimensional cellular array chip and platform for toxicology assays |
| US8242057B2 (en) * | 2006-06-26 | 2012-08-14 | Cleveland Biolabs, Inc. | Methods for identifying modulators of apoptosis |
| US20100310542A1 (en) * | 2007-07-30 | 2010-12-09 | Healor Ltd. | Pharmaceutical Compositions for treating wouds and related methods |
| KR20130095835A (ko) * | 2009-02-24 | 2013-08-28 | 힐로 리미티드 | 여드름 및 기타 질환 치료용 비스파틴 치료제 |
| CA2760153A1 (en) * | 2009-04-27 | 2010-11-11 | Alex Chenchik | Reagents and methods for producing bioactive secreted peptides |
| WO2010136485A1 (en) * | 2009-05-28 | 2010-12-02 | Glaxo Group Limited | Antigen-binding proteins |
| AU2011204425A1 (en) | 2010-01-11 | 2012-08-02 | Healor Ltd. | Method for treatment of inflammatory disease and disorder |
| US20140234330A1 (en) | 2011-07-22 | 2014-08-21 | Amgen Inc. | Il-17 receptor a is required for il-17c biology |
| US20130164860A1 (en) | 2011-11-04 | 2013-06-27 | Technion Research & Development Foundation Ltd. | Affinity methods and compositions employing electronic control of ph |
| WO2013112881A1 (en) | 2012-01-27 | 2013-08-01 | Thomas Jefferson University | Mct protein inhibitor-related prognostic and therapeutic methods |
| WO2013116903A1 (en) | 2012-02-10 | 2013-08-15 | Phylogica Limited | Methods for the characterisation of interaction sites on target proteins |
| AU2013251310B2 (en) | 2012-04-27 | 2018-02-15 | Cytomx Therapeutics, Inc. | Activatable antibodies that bind epidermal growth factor receptor and methods of use thereof |
| GB2505237A (en) * | 2012-08-24 | 2014-02-26 | Stefan Grimm | Method of screening for therapeutic agents using cell lines including a reference cell line |
| US10022372B2 (en) | 2013-04-19 | 2018-07-17 | Thomas Jefferson University | Caveolin-1 related methods for treating glioblastoma with temozolomide |
| US9540440B2 (en) | 2013-10-30 | 2017-01-10 | Cytomx Therapeutics, Inc. | Activatable antibodies that bind epidermal growth factor receptor and methods of use thereof |
| US9737623B2 (en) | 2013-12-11 | 2017-08-22 | Cytomx Therapeutics, Inc. | Antibodies that bind activatable antibodies and methods of use thereof |
| CA2986388C (en) * | 2015-06-11 | 2024-02-27 | Genexine, Inc. | Modified interleukin-7 protein and uses thereof |
| CA2988588A1 (en) | 2015-06-12 | 2016-12-15 | Georgia State University Research Foundation, Inc. | Compositions and methods for treating opioid tolerance |
| KR102386735B1 (ko) | 2015-11-06 | 2022-04-14 | 주식회사 제넥신 | 변형된 인터루킨-7 융합 단백질의 제형 |
| CN108697764A (zh) | 2015-12-04 | 2018-10-23 | 格纳西尼有限公司 | 含有免疫球蛋白fc融合白细胞介素-7融合蛋白的用于预防或治疗流感病毒感染的药物组合物 |
| US11708399B2 (en) | 2015-12-04 | 2023-07-25 | Genexine, Inc. | Pharmaceutical composition comprising immunoglobulin Fc-fused interleukin-7 fusion protein for preventing or treating human papillomavirus-caused diseases |
| WO2022159936A1 (en) * | 2021-01-19 | 2022-07-28 | Hope Patents, Llc | A method for identifying peptide therapeutics to treat a variety of conditions |
Family Cites Families (44)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| US4618578A (en) | 1984-07-17 | 1986-10-21 | Chiron Corporation | Expression of glycoprotein D of herpes simplex virus |
| DE229046T1 (de) | 1985-03-30 | 1987-12-17 | Marc Genf/Geneve Ballivet | Verfahren zum erhalten von dns, rns, peptiden, polypeptiden oder proteinen durch dns-rekombinant-verfahren. |
| US6492107B1 (en) | 1986-11-20 | 2002-12-10 | Stuart Kauffman | Process for obtaining DNA, RNA, peptides, polypeptides, or protein, by recombinant DNA technique |
| US4980281A (en) | 1988-02-10 | 1990-12-25 | Housey Gerard M | Method of screening for protein inhibitors and activators |
| US5688655A (en) | 1988-02-10 | 1997-11-18 | Ict Pharmaceuticals, Inc. | Method of screening for protein inhibitors and activators |
| US5266464A (en) | 1988-02-10 | 1993-11-30 | Ict Pharmaceuticals, Inc. | Method of screening for protein inhibitors and activators |
| CN1038306A (zh) | 1988-03-21 | 1989-12-27 | 维吉恩公司 | 重组反转录病毒 |
| DE68927933T2 (de) * | 1988-09-02 | 1997-08-14 | Dyax Corp | Herstellung und auswahl von rekombinantproteinen mit verschiedenen bindestellen |
| CA2009996A1 (en) * | 1989-02-17 | 1990-08-17 | Kathleen S. Cook | Process for making genes encoding random polymers of amino acids |
| US5283173A (en) | 1990-01-24 | 1994-02-01 | The Research Foundation Of State University Of New York | System to detect protein-protein interactions |
| DE4002897A1 (de) | 1990-02-01 | 1991-08-08 | Behringwerke Ag | Herstellung und verwendung von genbanken synthetischer menschlicher antikoerper ("synthetische human-antikoerper-bibliotheken") |
| EP0515516B1 (en) | 1990-02-15 | 2002-01-16 | University of North Carolina | Methods for identifying heterofunctional fusion proteins |
| US5747334A (en) | 1990-02-15 | 1998-05-05 | The University Of North Carolina At Chapel Hill | Random peptide library |
| JP2706568B2 (ja) | 1990-05-01 | 1998-01-28 | アイシス・ファーマシューティカルス・インコーポレーテッド | 新規な薬物および試薬の同定 |
| US5639595A (en) * | 1990-05-01 | 1997-06-17 | Isis Phamaceuticals, Inc. | Identification of novel drugs and reagents |
| US5723286A (en) * | 1990-06-20 | 1998-03-03 | Affymax Technologies N.V. | Peptide library and screening systems |
| US5650489A (en) | 1990-07-02 | 1997-07-22 | The Arizona Board Of Regents | Random bio-oligomer library, a method of synthesis thereof, and a method of use thereof |
| CA2092195C (en) | 1990-09-21 | 2000-04-18 | Douglas J. Jolly | Retroviral packaging cell line |
| US5770434A (en) | 1990-09-28 | 1998-06-23 | Ixsys Incorporated | Soluble peptides having constrained, secondary conformation in solution and method of making same |
| US5217889A (en) | 1990-10-19 | 1993-06-08 | Roninson Igor B | Methods and applications for efficient genetic suppressor elements |
| US5223408A (en) * | 1991-07-11 | 1993-06-29 | Genentech, Inc. | Method for making variant secreted proteins with altered properties |
| WO1993003143A1 (en) | 1991-08-07 | 1993-02-18 | Anderson W French | Retroviral vectors containing internal ribosome entry sites |
| US5733731A (en) * | 1991-10-16 | 1998-03-31 | Affymax Technologies N.V. | Peptide library and screening method |
| US5270170A (en) * | 1991-10-16 | 1993-12-14 | Affymax Technologies N.V. | Peptide library and screening method |
| US5395750A (en) | 1992-02-28 | 1995-03-07 | Hoffmann-La Roche Inc. | Methods for producing proteins which bind to predetermined antigens |
| WO1993023569A1 (en) | 1992-05-11 | 1993-11-25 | Ribozyme Pharmaceuticals, Inc. | Method and reagent for inhibiting viral replication |
| CA2145063A1 (en) | 1992-09-22 | 1994-03-31 | Cambridge Genetics Limited | Recombinant viruses displaying a nonviral polypeptide on their external surface |
| WO1994018219A1 (en) | 1993-02-02 | 1994-08-18 | The Scripps Research Institute | Methods for producing antibody libraries using universal or randomized immunoglobulin light chains |
| US6140120A (en) * | 1993-02-12 | 2000-10-31 | Board Of Trustees Of Leland Stanford Jr. University | Regulated transcription of targeted genes and other biological events |
| EP0689601B1 (en) * | 1993-02-22 | 2006-10-04 | The Rockefeller University | Production of high titer helper-free retroviruses by transient transfection |
| EP0688358A4 (en) | 1993-03-12 | 1997-10-01 | Univ Creighton | IMPROVED VECTORS FOR GENTHERAPY |
| WO1994029469A2 (en) | 1993-06-07 | 1994-12-22 | Vical Incorporated | Plasmids suitable for gene therapy |
| JPH09500625A (ja) * | 1993-07-09 | 1997-01-21 | スミスクライン・ビーチャム・コーポレイション | 環状セミランダムペプチドライブラリー |
| WO1995004824A1 (en) * | 1993-08-05 | 1995-02-16 | Medvet Science Pty. Ltd. | Generation of dna libraries and retroviral vectors for same |
| WO1995011998A1 (en) | 1993-10-26 | 1995-05-04 | United Biomedical, Inc. | Structured synthetic antigen libraries as diagnostics, vaccines and therapeutics |
| US6303574B1 (en) * | 1994-07-22 | 2001-10-16 | The University Of North Carolina At Chapel Hill | Scr SH3 binding peptides and methods of isolating and using same |
| WO1996023899A1 (en) * | 1995-02-01 | 1996-08-08 | University Of Massachusetts Medical Center | Methods of selecting a random peptide that binds to a target protein |
| US20010053523A1 (en) | 1995-06-02 | 2001-12-20 | M&E Biotech A/S. | Method for identification of biologically active peptides and nucleic acids |
| DE69610310T2 (de) * | 1995-06-02 | 2001-03-15 | M&E Biotech A/S, Horsholm | Verfahren zur identifikation von biologisch aktiven peptiden und nukleinsäuren |
| US5698396A (en) | 1995-06-07 | 1997-12-16 | Ludwig Institute For Cancer Research | Method for identifying auto-immunoreactive substances from a subject |
| CA2233316C (en) * | 1995-09-29 | 2010-12-14 | Indiana University Foundation | Methods for enhanced virus-mediated dna transfer using molecules with virus- and cell-binding domains |
| DE69722176T2 (de) * | 1996-01-23 | 2004-03-18 | The Board Of Trustees Of The Leland Stanford Junior University, Palo Alto | Verfahren zur suche nach transdominanten effektorpeptiden und rna-molekülen |
| US5955275A (en) * | 1997-02-14 | 1999-09-21 | Arcaris, Inc. | Methods for identifying nucleic acid sequences encoding agents that affect cellular phenotypes |
| JP2002521652A (ja) | 1998-07-20 | 2002-07-16 | ファーメクサ エイ/エス | リガンドおよびターゲット生体分子を同定するための新規な方法 |
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1997
- 1997-01-23 DE DE69722176T patent/DE69722176T2/de not_active Expired - Lifetime
- 1997-01-23 JP JP9526969A patent/JP2000504220A/ja active Pending
- 1997-01-23 US US08/787,738 patent/US6455247B1/en not_active Expired - Lifetime
- 1997-01-23 US US08/789,333 patent/US6153380A/en not_active Expired - Lifetime
- 1997-01-23 EP EP97903068A patent/EP0877752B1/en not_active Expired - Lifetime
- 1997-01-23 AU AU17078/97A patent/AU725716C/en not_active Ceased
- 1997-01-23 EP EP02026164A patent/EP1295952A3/en not_active Withdrawn
- 1997-01-23 CA CA002244222A patent/CA2244222A1/en not_active Abandoned
- 1997-01-23 WO PCT/US1997/001019 patent/WO1997027212A1/en not_active Ceased
- 1997-01-23 WO PCT/US1997/001048 patent/WO1997027213A1/en not_active Ceased
- 1997-01-23 JP JP52698297A patent/JP2001509661A/ja not_active Ceased
- 1997-01-23 ES ES97903068T patent/ES2200150T3/es not_active Expired - Lifetime
- 1997-01-23 AU AU17074/97A patent/AU1707497A/en not_active Abandoned
- 1997-01-23 DK DK97903068T patent/DK0877752T3/da active
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2001
- 2001-07-27 US US09/916,940 patent/US6737241B2/en not_active Expired - Fee Related
- 2001-07-30 US US09/918,601 patent/US20020146710A1/en not_active Abandoned
- 2001-07-31 US US09/919,635 patent/US20030104384A1/en not_active Abandoned
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| US20020146710A1 (en) | 2002-10-10 |
| AU1707897A (en) | 1997-08-20 |
| US6455247B1 (en) | 2002-09-24 |
| AU1707497A (en) | 1997-08-20 |
| AU725716B2 (en) | 2000-10-19 |
| US20030104384A1 (en) | 2003-06-05 |
| EP1295952A3 (en) | 2003-07-09 |
| WO1997027212A1 (en) | 1997-07-31 |
| DK0877752T3 (da) | 2003-09-15 |
| JP2001509661A (ja) | 2001-07-24 |
| EP0877752B1 (en) | 2003-05-21 |
| CA2244222A1 (en) | 1997-07-31 |
| AU725716C (en) | 2003-02-20 |
| US6153380A (en) | 2000-11-28 |
| EP1295952A2 (en) | 2003-03-26 |
| JP2000504220A (ja) | 2000-04-11 |
| DE69722176D1 (de) | 2003-06-26 |
| ES2200150T3 (es) | 2004-03-01 |
| EP0877752A1 (en) | 1998-11-18 |
| US20020127564A1 (en) | 2002-09-12 |
| HK1016997A1 (en) | 1999-11-12 |
| WO1997027213A1 (en) | 1997-07-31 |
| US6737241B2 (en) | 2004-05-18 |
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