Patents Assigned to Odyssey Pharmaceuticals Inc.
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Publication number: 20130022999Abstract: The present invention describes a method for detecting biomolecular interactions said method comprising: (a) selecting an appropriate reporter molecule selected from the group consisting of a protein, a fluorescent protein, a luminescent protein and a phosphorescent protein; (b) effecting fragmentation of said reporter molecule such that said fragmentation results in reversible loss of reporter function; (c) fusing or attaching fragments of said reporter molecule separately to other molecules; followed by (d) reassociation of said reporter fragments through interactions of the molecules that are fused to said fragments; and (e) detecting said biomolecular interactions by reconstitution of activity of the reporter moleculeType: ApplicationFiled: June 4, 2012Publication date: January 24, 2013Applicant: Odyssey Pharmaceuticals, Inc.Inventors: Stephen William Watson Michnick, Joelle Nina Polletier, Ingrid Remy
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Publication number: 20110287950Abstract: We describe a strategy for designing and implementing protein-fragment complementation assays (PCAs) to detect biomolecular interactions in vivo and in vitro. The design, implementation and broad applications of this strategy are illustrated with a large number of enzymes with particular detail provided for the example of murine dihydrofolate reductase (DHFR). Fusion peptides consisting of N- and C-terminal fragments of murine DHFR fused to GCN4 leucine zipper sequences were coexpressed in Escherichia coli grown in minimal medium, where the endogenous DHFR activity was inhibited with trimethoprim. Coexpression of the complementary fusion products restored colony formation. Survival only occurred when both DHFR fragments were present and contained leucine-zipper forming sequences, demonstrating that reconstitution of enzyme activity requires assistance of leucine zipper formation. DHFR fragment-interface point mutants of increasing severity (Ile to Val, Ala and Gly) resulted in a sequential increase in E.Type: ApplicationFiled: August 1, 2011Publication date: November 24, 2011Applicant: Odyssey Pharmaceuticals, Inc.Inventors: Stephen William Watson Michnick, Joelle Nina Polletier, Ingrid Remy
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Publication number: 20080145315Abstract: The instant invention describes a method for detecting protein-protein interactions in living organisms and/or cells, said method comprising: (a) synthesizing probe protein fragments from a protein which enables fluorescent or luminescent detection by dissecting the gene coding for the fluorescent or luminescent protein into a least two fragments; (2) constructing fusion proteins consisting of the probe protein fragments linked to protein domains that are to be tested for interactions; (3) coexpressing the fusion proteins; and (d) detecting reconstitution of the fluorescence or luminescence signal.Type: ApplicationFiled: December 4, 2007Publication date: June 19, 2008Applicant: Odyssey Pharmaceuticals, Inc.Inventors: Stephen William Watson Michnick, Marnie MacDonald, John K. Westwick
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Publication number: 20070254373Abstract: The present invention is directed to Protein-fragment Complementation Assays (PCAs) and assay compositions based on fluorescent proteins. The invention provides methods for fragmenting fluorescent proteins and generating mutant fragments with desired spectral characteristics for PCA. The invention encompasses assays and compositions based on fluorescent proteins from the species Aequorea, Anemonia and Anthozoa. In particular, the invention is directed to fragments of mutant fluorescent proteins having improved spectral properties over the wild-type proteins. The invention encompasses fragments of mutant versions of A. Victoria green fluorescent protein (GFP), in particular yellow fluorescent proteins (EYFP and super-EYFP), ‘Venus’, cyan, ‘citrine’, blue, cyan-green, and photoactivatable variants of GFP The invention also encompasses red fluorescent PCAs based on Discosoma red fluorescent protein (RFP PCA)and a kindling fluorescent protein PCA (KFP1 PCA) derived from Anemonia sulcata.Type: ApplicationFiled: January 23, 2007Publication date: November 1, 2007Applicant: Odyssey Pharmaceuticals, Inc.Inventors: Stephen Michnick, Marnie MacDonald, Jane Lamerdin
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Publication number: 20070148682Abstract: We describe a strategy for designing and implementing protein-fragment complementation assays (PCAs) to detect biomolecular interactions in vivo and in vitro. The design, implementation and broad applications of this strategy are illustrated with a large number of enzymes with particular detail provided for the example of murine dihydrofolate reductase (DHFR). Fusion peptides consisting of N- and C-terminal fragments of murine DHFR fused to GCN4 leucine zipper sequences were coexpressed in Escherichia coli grown in minimal medium, where the endogenous DHFR activity was inhibited with trimethoprim. Coexpression of the complementary fusion products restored colony formation. Survival only occurred when both DHFR fragments were present and contained leucine-zipper forming sequences, demonstrating that reconstitution of enzyme activity requires assistance of leucine zipper formation. DHFR fragment-interface point mutants of increasing severity (Ile to Val, Ala and Gly) resulted in a sequential increase in E.Type: ApplicationFiled: January 8, 2007Publication date: June 28, 2007Applicant: Odyssey Pharmaceuticals, Inc.Inventors: Stephen Michnick, Joelle Pelletier, Ingrid Remy
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Publication number: 20040038298Abstract: We describe a strategy for designing and implementing protein-fragment complementation assays (PCAs) to detect biomolecular interactions in vivo and in vitro. The design, implementation and broad applications of this strategy are illustrated with a large number of enzymes with particular detail provided for the example of murine dihydrofolate reductase (DHFR). Fusion peptides consisting of N- and C-terminal fragments of murine DHFR fused to GCN4 leucine zipper sequences were coexpressed in Escherichia coli grown in minimal medium, where the endogenous DHFR activity was inhibited with trimethoprim. Coexpression of the complementary fusion products restored colony formation. Survival only occurred when both DHFR fragments were present and contained leucine-zipper forming sequences, demonstrating that reconstitution of enzyme activity requires assistance of leucine zipper formation. DHFR fragment-interface point mutants of increasing severity (Ile to Val, Ala and Gly) resulted in a sequential increase in E.Type: ApplicationFiled: January 29, 2003Publication date: February 26, 2004Applicant: Odyssey Pharmaceuticals, Inc.Inventors: Stephen William Waston Michnick, Joelle Nina Pelletier, Ingrid Remy
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Publication number: 20030049688Abstract: We describe a strategy for designing and implementing protein-fragment complementation assays (PCAs) to detect biomolecular interactions in vivo and in vitro. The design, implementation and broad applications of this strategy are illustrated with a large number of enzymes with particular detail provided for the example of murine dihydrofolate reductase (DHFR). Fusion peptides consisting of N- and C-terminal fragments of murine DHFR fused to GCN4 leucine zipper sequences were coexpressed in Escherichia coli grown in minimal medium, where the endogenous DHFR activity was inhibited with trimethoprim. Coexpression of the complementary fusion products restored colony formation. Survival only occurred when both DHFR fragments were present and contained leucine-zipper forming sequences, demonstrating that reconstitution of enzyme activity requires assistance of leucine zipper formation. DHFR fragment-interface point mutants of increasing severity (Ile to Val, Ala and Gly) resulted in a sequential increase in E.Type: ApplicationFiled: May 24, 2002Publication date: March 13, 2003Applicant: Odyssey Pharmaceuticals, Inc.Inventors: Stephen William Watson Michnick, Joelle Nina Pelletier, Ingrid Remy
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Patent number: 6428951Abstract: We describe a strategy for designing and implementing protein-fragment complementation assays (PCAs) to detect biomolecular interactions in vivo and in vitro. The design, implementation and broad applications of this strategy are illustrated with a large number of enzymes with particular detail provided for the example of murine dihydrofolate reductase (DHFR). Fusion peptides consisting of N- and C-terminal fragments of murine DHFR fused to-GCN4 leucine zipper sequences were coexpressed in Escherichia coli grown in minimal medium, where the endogenous DHFR activity was inhibited with trimethoprim. Coexpression of the complementary fusion products restored colony formation. Survival only occurred when both DHFR fragments were present and contained leucine-zipper forming sequences, demonstrating that reconstitution of enzyme activity requires assistance of leucine zipper formation. DHFR fragment-interface point mutants of increasing severity (lie to Val, Ala and Gly) resulted in a sequential increase in E.Type: GrantFiled: February 7, 2000Date of Patent: August 6, 2002Assignee: Odyssey Pharmaceuticals, Inc.Inventors: Stephen William Watson Michnick, Joelle Nina Pelletier, Ingrid Remy
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Patent number: 6294330Abstract: The invention provides a general protein-fragment complementation assays to detect biomolecular interactions in vivo and in vitro. The protein-complemetation assay/universal reporter system can be used to detect and screen an agonist and an antagonist of a membrane receptor system. The assay can be used to study protein-protein, protein-DNA, protein-RNA, protein-carbohydrate, and protein-small molecule interactions. The assay can be used to screen cDNA libraries for binding of a target protein with unknown proteins or libraries of small organic molecules for biological activity.Type: GrantFiled: July 30, 1998Date of Patent: September 25, 2001Assignee: Odyssey Pharmaceuticals Inc.Inventors: Stephen William Watson Michnick, Ingrid Remy
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Patent number: 6270964Abstract: We describe a strategy for designing and implementing protein-fragment complementation assays (PCAs) to detect biomolecular interactions in vivo and in vitro. The design, implementation and broad applications of this strategy are illustrated with a large number of enzymes with particular detail provided for the example of murine dihydrofolate reductase (DHFR). Fusion peptides consisting of N- and C-terminal fragments of murine DHFR fused to GCN4 leucine zipper sequences were coexpressed in Escherichia coli grown in minimal medium, where the endogenous DHFR activity was inhibited with trimethoprim. Coexpression of the complementary fusion products restored colony formation. Survival only occurred when both DHFR fragments were present and contained leucine-zipper forming sequences, demonstrating that reconstitution of enzyme activity requires assistance of leucine zipper formation. DHFR fragment-interface point mutants of increasing severity (lle to Val, Ala and Gly) resulted in a sequential increase in E.Type: GrantFiled: February 2, 1998Date of Patent: August 7, 2001Assignee: Odyssey Pharmaceuticals Inc.Inventors: Stephen William Watson Michnick, Joelle Nina Pelletier, Ingrid Remy