Chemistry: natural resins or derivatives; peptides or proteins; – Proteins – i.e. – more than 100 amino acid residues – Blood proteins or globulins – e.g. – proteoglycans – platelet...
Reexamination Certificate
2003-06-16
2008-05-13
Romeo, David S (Department: 1647)
Chemistry: natural resins or derivatives; peptides or proteins;
Proteins, i.e., more than 100 amino acid residues
Blood proteins or globulins, e.g., proteoglycans, platelet...
C530S389100, C530S391300
Reexamination Certificate
active
07371828
ABSTRACT:
The present invention relates, in general, to an extracellular signal regulated kinase, ERK-5. In particular, the present invention relates to nucleic acid molecules coding for ERK-5; ERK-5 polypeptides; recombinant nucleic acid molecules; cells containing the recombinant nucleic acid molecules; antisense ERK-5 nucleic acid constructs; antibodies having binding affinity to an ERK-5 polypeptide; hybridomes containing the antibodies; nucleic acid probes for the detecting of ERK-5 nucleic acid; a method of detecting ERK-5 nucleic acid or polypeptide in a sample; kits containing nucleic acid probes or antibodies; a method of detecting a compound capable of binding to ERK-5 or a fragment thereof; a method of detecting an agonist or antagonist of ERK-5 activity; a method of agonizing or antagonizing ERK-5 associated activity in a mammal; a method of treating diabetes mellitus, skeletal muscle diseases, Alzheimer's disease, or peripheral neuropathies in a mammal with an agonist or antagonist of ERK-5 activity; and a pharmaceutical composition comprising an ERK-5 agonist or antagonist.
REFERENCES:
patent: 5219748 (1993-06-01), Yoshitaka et al.
patent: 5512473 (1996-04-01), Brent et al.
patent: WO 91/19008 (1991-12-01), None
patent: WO 92/13001 (1992-08-01), None
patent: WO 92/21641 (1992-12-01), None
patent: WO 92/21660 (1992-12-01), None
patent: WO 93/23569 (1993-11-01), None
Bogoyevitch et al. Counting on mitogen-activated protein kinases—ERKs 3, 4, 5, 6, 7 and 8. Cell Signal. Dec. 2004;16(12):1345-54.
Veach et al. Receptor/transporter-independent targeting of functional peptides across the plasma membrane. J Biol Chem. Mar. 19, 2004;279(12):11425-31.
Yokoyama et al. “Production of Monoclonal Antibodies,” Unit 2,5 in, Current protocols in immunology, edited by John E. Coligan et al. John Wiley & Sons Inc. 2006, pp. 2.5.1 and 2.5.13.
Sutcliffe et al. Antibodies that react with predetermined sites on proteins. Science. Feb. 11, 1983;219(4585):660-6.
Berzofsky JA. Intrinsic and extrinsic factors in protein antigenic structure. Science. Sep. 6, 1985;229(4717):932-40.
Sambrook et al.,Molecular Cloning: A Laboratory Manual Second Edition, vols. 1, 2, & 3, Cold Spring Harbor Laboratory Press, Cold Spring Harbor, New York, USA, Nov. 1989, p. 18.70.
Ahn et al., “Evidence for an Epidermal Growth Factor-stimulated Protein Kinase Cascae in Swiss 3T3 Cells,”The Journal of Biological Chemistry, 1990, pp. 11495-11501, vol. 265, No. 20.
Ahn et al., “Identification of Multiple Epidermal Growth Factor-stimulated Protein Serine/Threonine Kinases from Swiss 3T3 Cells,”Journal of Biological Chemistry, 1990, pp. 11487-11494, vol. 265, No. 20.
Ballou et al., “Protein Phosphatase 2A Inactivates the Mitogen-stimulated S6 Kinase from Swiss Mouse 3T3 Cells,”The Journal of Biological Chemistry, 1988, pp. 1188-1194, vol. 263, No. 3.
Borthwick et al., “Protein-serine kinase from rat epididymal adipose tissue phosphorylates and activates acetyl-CoA carboxylase,”Biochem. J., 1990, pp. 795-801, vol. 270.
Boulton et al., “An Insulin-Stimulated Protein Kinase Similar to Yeast Kinases Involved in Cell Cycle Control,”Science, 1990, pp. 64-67, vol. 249.
Boulton et al., “ERKs: A Family of Protein-Serine/Threonine Kinases That Are Activated and Tyrosine Phosphorylated in Response to Insulin and NGF,”Cell, 1991, pp. 663-675, vol. 65.
Boulton et al., “Purification and Properties of Extracellular Signal-Regulated Kinase 1, an Insulin-Stimulated Microtubule-Associated Protein 2 Kinase,”Biochemistry, 1991, pp. 278-286, vol. 30.
Boulton et al.,Cell Regulation, 1991, pp. 357-371, vol. 2.
Charles et al., “The growth factor-inducible immediate-early gene 3CH134 encodes a protein-tyrosine-phosphatase,”Proc. Natl. Acad. Sci. USA, 1993, pp. 5292-5296, vol. 90.
Chung et al., “Mitogen-activated Swiss mouse 3T3 RSK kinases I and II are related to pp44mpkfrom sea star oocytes and participate in the regulation of pp90rskactivity,”Proc. Natl. Acad. Sci. USA, 1991, pp. 4981-4985, vol. 88.
Cicirelli et al., “Activation of Multiple Protein Kinases during the Burst in Protein Phosphorylation That Precedes the First Meiotic Cell Division in Xenopus Oocytes,”The Journal of Biological Chemistry, 1988, pp. 2009-2019, vol. 263, No. 4.
Cobb et al.,Cell Regulation, 1991, pp. 965-978, vol. 2.
Cooper et al., “Diverse Mitogenic Agents Induce the Phosphorylation of Two Related 42,000-Dalton Proteins on Tyrosine in Quiescent Chick Cells,”Molecular and Cellular Biology, 1984, pp. 30-37, vol. 4, No. 1.
Dent et al., “The molecular mechanism by which insulin stimulates glycogen synthesis in mammalian skeletal muscle,”Nature, 1990, pp. 302-308, vol. 348.
Duerr et al., “MsERK1: A Mitogen-Activated protein Kinase from a Flowering Plant,”The Plant Cell, 1993, pp. 87-96, vol. 5.
Ershler et al.,Gene, 1993, pp. 305-306, vol. 124.
Ferrell and Martin, “Identification of a 42-Kilodalton Phosphotyrosyl Protein as a Serine (Threonine) Protein Kinase by Renaturation,”Molecular and Cellular Biology, 1990, pp. 3020-3026, vol. 10, No. 6.
Gotoh et al., “In vitro effects of microtubule dynamics of purified Xenopus M phase-activated MAP kinase,”Nature, 1991, pp. 251-254, vol. 349.
Gotoh et al., “Xenopus M phase MAP kinase: isolation of its cDNA and activation by MPF,”The EMBO Journal, 1991, pp. 2661-2668, vol. 10, No. 9.
Gregory et al., “An Insulin-stimulated Ribosomal Protein S6 Kinase from Rabbit Liver,”The Journal of Biological Chemistry, 1989, pp. 18397-18401, vol. 264, No. 31.
Hanks et al., “The Protein Kinase Family: Conserved Features and Deduced Phylogeny of the Catalytic Domains,”Science, 1988, pp. 42-52, vol. 241.
Her et al., “Sequence of pp42/MAP kinase, a serine/theronine kinase regulated by tyrosine phosphorylation,”Nucleic Acids Research, 1991, p. 3743, vol. 19, No. 13.
Hoshi et al., “Activation of Ca2+-inhibitable Protein Kinase That Phosphorylates Microtuble-associated Protein 2 in Vitro by Growth Factors, Phorbol Esters, and Serum in Quieschen Cultured Human Fibroblasts,”Journal of Biological Chemistry, 1988, pp. 5396-5401, vol. 263.
Kozak et al., :An analysis of 5′-noncoding sequences from 699 vertebrate messenger RNAs,Nucleic Acids Research, 1987, pp. 8125-8148, vol. 15.
Kyriakis and Avruch, “pp54 Microtubule-associated Protein 2 Kinase: A Novel Serine/Threonine Protein Kinase Regulated by Phosphorylation and Stimulated by Poly-L-L-ysine,”Journal Biological Chemistry, 1990, pp. 17355-17363, vol. 265.
Kyriakis et al., “pp54 Microtubule-associated Protein-2 Kinase Requires Both Tyrosine an Serine/Threonine Phosphorylation for Activity,”Journal Biological Chemistry, 1991, pp. 10043-10046, vol. 226.
Needleman and Wunsch, “A General Method Applicable to the Search for Similarities in the Amino Acid Sequence of Two Proteins,”J. Mol. Biol., 1970, pp. 443-453, vol. 48.
Northwood et al., “Isolation and Characterization of Two Growth Factor-stimulated Protein Kinases That Phosphorylate the Epidermal Growth Factor Receptor at Threonine 669,”Journal of Biological Chemistry, 1991, pp. 15266-15276, vol. 266.
Owaki et al., “Extracellular Signal-Regulated Kinases in T Cell Characterization of Human ERK1 and ER2 cDNAs1,2,” Biochemical and Biophysical Research Communications, 1992, pp. 1416-1422, vol. 183.
Payne et al., “Identification of the regulatory phosphorylation sites in pp42/mitogen-activated protein kinase (MAP kinase),”EMBO J., 1991, pp. 885-892, vol. 10.
Posada and Cooper, “Requirements for Phosphorylation of MAP Kinase During Meiosis in Xenopus Oocytes,”Science, 1992, pp. 212-215, vol. 255.
Posada et al., “Tyrosine Phosphorylation and Activation of Homologous Protein Kinases during Oocyte Maturation and Mitogenic Activation of Fibroblasts,”Mo
Lechner Cornelia
Moller Niels P.
Ullrich Axel
Foley & Lardner LLP
Max-Planck-Gesellschaft zur Forderung der Wissenschaften E.V.
Romeo David S
LandOfFree
Extracellular signal-regulated kinase sequences and methods... does not yet have a rating. At this time, there are no reviews or comments for this patent.
If you have personal experience with Extracellular signal-regulated kinase sequences and methods..., we encourage you to share that experience with our LandOfFree.com community. Your opinion is very important and Extracellular signal-regulated kinase sequences and methods... will most certainly appreciate the feedback.
Profile ID: LFUS-PAI-O-3985181