Chemistry: molecular biology and microbiology – Enzyme – proenzyme; compositions thereof; process for... – Transferase other than ribonuclease
Reexamination Certificate
2006-11-14
2006-11-14
Hutson, Richard (Department: 1652)
Chemistry: molecular biology and microbiology
Enzyme , proenzyme; compositions thereof; process for...
Transferase other than ribonuclease
C435S183000, C435S193000, C435S320100, C435S252300, C435S325000, C536S023100, C536S023200, C536S023400, C530S350000
Reexamination Certificate
active
07135320
ABSTRACT:
The present invention relates generally to a newly identified adaptor protein FRS2 and related products and methods. FRS2 links protein kinases to activating partners in cells. The invention also relates to nucleic acid molecules encoding portions of FRS2, nucleic acid vectors containing FRS2 related nucleic acid molecules, recombinant cells containing such nucleic acid vectors, polypeptides purified from such recombinant cells, antibodies to such polypeptides, and methods of identifying compounds that enhance or block FRS2 interactions with natural binding partners. Also disclosed are methods for diagnosing abnormal conditions in an organism with FRS2 related molecules or compounds.
REFERENCES:
patent: 94/07913 (1994-04-01), None
patent: 95/09365 (1995-04-01), None
patent: 95/24426 (1995-09-01), None
patent: 96/18738 (1996-06-01), None
patent: 96/40115 (1996-12-01), None
Ngo et al., Computational Complexity, Protein Structure Prediction, and the Levinthal Paradox, in The Protein Folding Problem and Tertiary Structure Prediction, 1994, Merz et al. (ed.), Birkhauser, Boston, MA, pp. 433 and 492-495.
Ottilie et al., Multiple src-related kinase genes, srk 1-4, in the fresh water spongeSpongilla lacustris, Oncogene vol. 7, No. 8: 1625-1630, Aug. 1992.
Abe et al., “Molecular Characterization of a Novel Metabotropic Glutamate Receptor mGluR5 Coupled to Inositol Pohosphate/Ca2+ Signal,”J. Biol. Chem., vol. 267(19) 13361-13368. (1992).
Batzer et al., “Hierarchy of Binding Sites For Grb2 and Shc on the epidermal Growth Factor Receptor”,Mol. Cell. Biol., vol. 14:5192-5201, (1994).
Bellus et al., “A Recurrent Mutation In The Tyrosine Kinase Domain Of Fibroblast Growth Factor Receptor 3 Causes Hypochondroplasia”,Nature Genetics, vol. 10:357-359, (1995).
Blaikie et al., “A Region In Shc Distinct From The SH2 Domain Can Bind Tyrosine-phosphorylated Growth Factor Receptor”,The Journal of Biological Chemistry, vol. 269(51):32031-32034, (1994).
Clark et al., “C. Elegans Cell-Signalling Gene Sem-5 Encodes A Protein With SH2 and SH3 Domains,”Nature, vol. 356:340-344, (1992).
Curto et al., “Novel Recruitment Of Shc. Grb2, and Sos By Fibroblast Growth Factor Receptor-1 In V-Src-Transformed Cells,”Biochemical And Biophysical Research Communications, vol. 243:555-560, (1998).
Deng et al., “Murine FGFR-1 is Required For Early Postimplantation Growth and Axial Organization,”Genes&Dev/, vol. 8:3045-3057, (1994).
Devore et al., “An FGF Receptor Signaling Pathway Is Required For The Normal Cell Migrations Of The Sex Myoblasts in C. Elegans Hermaphrodites,”Cell, vol. 83:611-620, (1995).
Dikic et al., “Shc Binding To Nerve Growth Factor Receptor Is Mediated By The Phosphotyrosine Interaction Domain,”J. Biol. Chem., vol. 270:15125-15129, (1995).
Gustafson et al., “Phosphotyrosine-Dependent Ineraction Of SHC And Insulin Receptor Substrate 1 With The NPEY Motif Of The Insulin Receptor Via A Novel Non-SH2 Domain,”Mol. Cell. Biol., vol. 15:2500-2508, (1995).
Honegger et al., “Point Mutation At The ATP Binding Site Of EGF Receptor Abolishes Protein-Tyrosine Kinase Activity And Alters Cellular Routing,”Cell, vol. 51:199-209, (1987).
Jabs et al., “Jackson-Weiss And Crouzon syndromes Are Allelic With Mutations In Fibroblast Growth Factor Receptor 2”,Nature Genetics, vol. 8:275-279, (1994).
Klint et al., “Shc And A Novel 89-kDa Component Couple To The Grb-2 Sos Complex in Fibroblast Growth Factor-2 Stimulated Cells”,Journal Of Biological Chemistry, vol. 270(40):23337-23344, (1996).
Lowenstein et al., “The SH2 and SH3 Domain-Containing Protein GRB2 Links Receptor Tyrosine Kinases To Ras Signaling,”Cell, vol. 70:431-442, (1992).
Mohammadi et al., “Point Mutation In FGF Receptor Eliminates Phosphatidylinositol Hydrolysis Without Affecting Mitogenesis,”Nature, vol. 358:681-684, (1992).
Muenke et al., “A Common Mutation In The Fibroglast Growth Factor Receptor 1 Gene In Pfeiffer Syndrome,”Nature Genetics, vol. 8:269-274, (1994).
Nelsen, “Detection Of Acridinium Esters By Chemiluminescence,”Nonisotopic DNA Probe Techniques, ed. Larry J. Kricka, (San Diego: Academic Press, Inc.), pp. 275-310, (1992).
Pawson et al., “SH2 And SH3 Domains,”Current Biology, vol. 3(7):434-442, (1993).
Resh, “Myristylation And Palmitylation Of Src Family Members: The Fats Of The Matter,”Cell, vol. 76:411-413, (1994).
Rozakis-Adcock et al., “Association Of The Shc And Grb2/Sem5 SH2-Containing Proteins Is Implicated In Activation Of The Ras Pathway By Tyrosine Kinases,”Nature, vol. 360:689-692, (1992).
Rutland et al., “Identical Mutations In The FGFR2 Gene Cause Both Pfeiffer And Crouzon Syndrome Phenotypes,”Nature Genetics, vol. 9:173-176, (1995).
Sambrook et al.,Molecular Cloning: A Laboratory Manual, 2ndEdition, Cold Spring Harbor Laboratory Press, (1989), (Table of Contents).
Schlessinger, “SH2/SH3 Signaling Proteins,”Curr. Opin, Gen. Dev., vol. 4:25-30, (1994).
Schlessinger et al., “Growth Factor Signaling By Receptor Tyrosine Kinases,”Neuron, vol. 9:383-391, (1992).
Shiang et al., “Mutations In The Transmembrane Domain Of FGFR3 Cause The most Common Genetic Form Of Dwarfism, Achondroplasia,”Cell, vol. 78:335-342, (1994).
Skolnik et al., “The Function Of GRB2 In Linking The Insulin Receptor To Ras Signaling Pathways,”Science, vol. 260:1953-1955, (1993).
Spivak-Kroizman et al., “Point Mutation In The Fibroblast Grwoth Factor Receptor Eliminates 269:14419-Phosphatidylinositol Hydrolysis Without Affecting Neuronal Differentiation of PC12 Cells,”J. Biol. Chem., vol. 14423, (1994).
Sun et al., “Structure Of The Insulin Receptor Substrate IRS-1 Defines A Unique Signal Transduction Protein,”Nature, vol. 352:73-77, (1991).
Tavormina et al., “Another Mutation That Results In The Substitution Of An Unpaired Cysteine Residue In The Extracellular Domain Of FGFR3 In Thanatophoric Dysplasia Type I,”Hum. Mol. Genetics, vol. 4:2175-2177, (1995).
Vojtek et al., “Mammalian Ras Interacts Directly With The Serine/Threonine Kinase Raf,”Cell, vol. 74:205-214, (1993).
Wang et al., “Broadly Expressed SNT-Like Proteins Link FGF Receptor Stimulation To Activators Of Ras,”Oncogene, vol. 13:721-729, (1996).
Webster et al., “Constitutive Activation Of Fibroblast Growth Factor Receptor 3 By The Transmembrane Domain Point Mutation Found In Achondroplasia,”EMBO, vol. 15:520-527, (1996).
White et al., “Mutation Of The Insulin Receptor At Tyrosine 960 Inhibits Signal Transmission But Does Not Affect Its Tyrosine Kinase Activity,”Cell, vol. 54:641-649, (1988).
Yamaguchi et al., “FGFR-1 Is Required For Embryonic Growth And Mesodermal Patterning During Mouse Gastrulation,”Genes&Dev., vol. 8:3032-3044, (1994).
Dietrich, F.S., VAC8 Protein-Yeast (Saccharomyces cerevisiae), Genbank Accession No. S50446 (1999).
Raulf, F. Protein-Tyrosine Kinase (EC 2.7.1.112) 1-Freshwater Sponge(Spongilla lacustris), Genbank Accession No. S24550 (2000).
Kouhara Haruhiko
Lax Irit
Schlessinger Joseph
Spivak-Kroizman Taly
Foley & Lardner LLP
Hutson Richard
New York University
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