Three hybrid assay system

Details Three hybrid assay system Three hybrid assay system

2006-11-14

2006-11-14

Ketter, James (Department: 1636)

Chemistry: natural resins or derivatives; peptides or proteins;

Proteins, i.e., more than 100 amino acid residues

C435S006120, C536S023400, C514S712000

Reexamination Certificate

active

07135550

ABSTRACT:
The invention provides compositions and methods for isolating ligand binding polypeptides for a user-specified ligand, and for isolating small molecule ligands for a user-specified target polypeptide using an improved class of hybrid ligand compounds.

REFERENCES:
patent: 5468614 (1995-11-01), Fields et al.
patent: 5503977 (1996-04-01), Johnsson et al.
patent: 5525465 (1996-06-01), Haralambidis et al.
patent: 5585245 (1996-12-01), Johnsson et al.
patent: 5629157 (1997-05-01), Goodman et al.
patent: 5672508 (1997-09-01), Gyuris et al.
patent: 5714595 (1998-02-01), Mak et al.
patent: 5830462 (1998-11-01), Crabtree et al.
patent: 5834266 (1998-11-01), Crabtree et al.
patent: 5846722 (1998-12-01), Kauvar et al.
patent: 5846728 (1998-12-01), Haralambidis et al.
patent: 5869337 (1999-02-01), Crabtree et al.
patent: 5871753 (1999-02-01), Crabtree et al.
patent: 5955280 (1999-09-01), Vidal et al.
patent: 5965368 (1999-10-01), Vidal et al.
patent: 5994313 (1999-11-01), Crabtree et al.
patent: 6011018 (2000-01-01), Crabtree et al.
patent: 6015709 (2000-01-01), Natesan
patent: 6043082 (2000-03-01), Crabtree et al.
patent: 6046047 (2000-04-01), Crabtree et al.
patent: 6054436 (2000-04-01), Crabtree et al.
patent: 6063625 (2000-05-01), Crabtree et al.
patent: 6117680 (2000-09-01), Natesan et al.
patent: 6133456 (2000-10-01), Holt et al.
patent: 6140120 (2000-10-01), Crabtree et al.
patent: 6150527 (2000-11-01), Holt et al.
patent: 6165787 (2000-12-01), Crabtree et al.
patent: 6172208 (2001-01-01), Cook
patent: 6270964 (2001-08-01), Michnick et al.
patent: 6316418 (2001-11-01), Crabtree et al.
patent: 6326155 (2001-12-01), Maclennan et al.
patent: 6479653 (2002-11-01), Natesan et al.
patent: 6891021 (2005-05-01), Crabtree et al.
patent: 2002/0004202 (2002-01-01), Cornish
patent: 2002/0173474 (2002-11-01), Schreiber et al.
patent: 0646644 (1995-04-01), None
patent: WO 94/18317 (1994-08-01), None
patent: WO 96/02561 (1996-02-01), None
patent: WO 96/06097 (1996-02-01), None
patent: WO 96/13613 (1996-05-01), None
patent: WO 97/41255 (1997-11-01), None
patent: WO 98/07845 (1998-02-01), None
patent: WO-98/16835 (1998-04-01), None
patent: WO 98/25947 (1998-06-01), None
patent: WO-99/10510 (1999-03-01), None
patent: WO-00/01417 (2000-01-01), None
patent: WO-00/07018 (2000-02-01), None
patent: WO 01/53355 (2001-07-01), None
patent: WO 02/12902 (2002-02-01), None
patent: WO 02/059272 (2002-08-01), None
patent: WO-03/033499 (2003-04-01), None
The Merck Index, Seventh Edition, 1960, Stecher et al. eds., pp. 180, 430 and 677.
Bachmair, A. et al. In Vivo Half-Life of a Protein is a Function of its Amino-Terminal Residue. Science 234, 179-186 (1986).
Baker, R.T. et al. Ubiquitin-specific Proteases ofSaccharomyces cerevisiae. J. Biol. Chem. 267, 23364-23375 (1992).
Baker, R.T. & Varshavsky, A. Yeast N-terminal Amidase. J. Biol. Chem. 270, 12065-12074 (1995).
Bartel, B. et al. The recognition component of the N-end rule pathway. EMBO J. 9, 3179-3189 (1990).
Bartel, P.L. & Fields, S., eds. The yeast-two-hybrid system. Oxford University Press, New York, NY (1997).
Bergmann, K.E. et al. Bivalent Ligands as Probes of Estrogen Receptor Action. J. Steroid Biochem. Molec. Biol. 49, 139-152 (1994).
Dohmen, R.J. et al. The N-end rule is mediated by the UBC2(RAD6) ubiquitin-conjugating enzyme, PNAS 88, 7351-7355 (Aug. 1991).
Fields, S. & Song, O. A novel genetic system to detect protein-protein interactions. Nature 340, 245-246 (1989).
Gyrius, J. et al. cdl1, a Human G1 and S Phase Protein Phosphatase that Associates with Cdk2. Cell 75, 791-803 (1993).
Johnsson, N. & Varshavsky, A. Split ubiquitin as a sensor of protein interactions in vivo. PNAS 91, 10340-10344 (Oct. 1994).
Kwon, Y.T, et al. The mouse and human genes encoding the recognition component of the N-end rule pathway. PNAS 95, 7898-7903 (Jul. 1998).
Laser, H. et al. A new screen for protein interactions reveals that theSaccharomyces cerevisiaehigh mobility group proteins Nhp6A/B are involved in the regulation of the GAL 1 promoter. PNAS 97, 13732-13737 (Dec. 5, 2000).
Licitra, et al. A three-hybrid system for detecting small ligand-protein receptor interactions. PNAS 93, 12817-12821 (Nov. 1996).
Lin et al. J. Am. Chem. Soc. 122, 4247-4248 (2000).
Ozkaynak, E. et al. The yeast ubiquitin genes: a family of natural gene fusions. EMBO J. 6, 1429 (1987).
Reichel, C. et al. Enhanced green fluorescence by the expression of anAequorea victoriagreen fluorescent protein mutant in mono- and dicotyledonous plant cells. PNAS 93. 5888-5893 (Jun. 1996).
Stagljar, I. et al. A genetic system based on split-ubiquitin for the analysis of interactions between membrane proteins In vivo. PNAS 95, 5187-5192 (Apr. 1998).
Tobias, J.W. & Varshavsky, A. Cloning and Functional Analysis of the Ubiquitin-specific Protease Gene UBP1 ofSaccharomyces cerevisiae. J. Biol. Chem. 266, 12021-12028 (1991).
Varshavsky, A. The N-End Rule. Cell 725-735 (1992).
Yang, M. et al. Protein-peptide interactions analyzed with the yeast two-hybrid system. Nucleic Acid Res. 23, 1152-1156 (1995).
Zhu, L. & Hannon, G.J., eds. Yeast hybrid technologies. Biotechniques Press, Westborough, Ma (2000).
Amara, J.F., et al., “A versatile synthetic dimerizer for the regulation of protein—protein interactions.” PNAS 94: 10618-10623 (1997).
Baker, K., et al., “Chemical complementation: A reaction-independent genetic assay for enzyme catalysis.” PNAS 99(26): 16537-16543 (2002).
Bertozzi, C.R., et al., “The Synthesis of Heterobifunctional Linkers for the Conjugation of Ligands to Molecular Probes.” J. Org. Chem. 56: 4326-4329 (1991).
Griffith, E.C., et al., “Yeast Three-Hybrid System for Detecting Ligand-Receptor Interactions.” Methods in Enzymology 328: 89-103 (2000).
Henthorn, D.C., et al., “A GAL4-based yeast three-hybrid system for the identification of small molecule-target protein interactions.” Biochemical Pharmacology 63: 1619-1628 (2002).
MacBeath, G., et al., “Printing Proteins as Microassays for High-Throughput Function Determination.” Science 289: 1760-1763 (2000).
Spencer, D.M., et al., “Controlling Signal Transduction with Synthetic Ligands.” Science 262: 1019-1024 (1993).
Bierer et al., “Two district signal transmission pathways in T lymphocytes are inhibited by complexes formed between an immunophilin and either FK506 or rapamycin”. Proc. Natl. Acad. Sci., vol. 87 pp. 9231-9235 (1990).
Keenan et al., “Synthesis and Activity of Bivalent FKBP12 Ligands for the Regulated Dimerization of Proteins”, Bioorganic & Medicinal Chemistry vol. 6 pp. 1309-1335 (1998).
Lin et al., “Dexamethasone-Methotrexate: An Efficient Chemical Inducer of Protein DimerizationIn Vivo”, J. Am. Chem. Soc. vol. 122, pp. 4247-4248 (2000).
Matthews et al., “Dihydrofolate Reductase: X-ray Structure of the Binary complex with Methotrexate”, Science, vol. 197 pp. 452-455 (1977).
Sota et al., “Detection of Conformational Changes in an Immobilized Protein Using Surface Plasmon Resonance”, Analytical Chemistry, vol. 70, pp. 2019-2024 (1998).
ExPASy entry for Enzyme: EC 1.5.1.3., Dihydrofolate reductase, pp. 1-2, printed on Dec. 21, 2005.

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