Chemistry: natural resins or derivatives; peptides or proteins; – Proteins – i.e. – more than 100 amino acid residues
Reexamination Certificate
2006-07-18
2006-07-18
Brumback, Brenda (Department: 1646)
Chemistry: natural resins or derivatives; peptides or proteins;
Proteins, i.e., more than 100 amino acid residues
C530S300000
Reexamination Certificate
active
07078481
ABSTRACT:
The invention provides isolated nucleic acids molecules, designated PCIP nucleic acid molecules, which encode proteins that bind potassium channels and modulate potassium channel mediated activities. The invention also provides antisense nucleic acid molecules, recombinant expression vectors containing PCIP nucleic acid molecules, host cells into which the expression vectors have been introduced, and nonhuman transgenic animals in which a PCIP gene has been introduced or disrupted. The invention still further provides isolated PCIP proteins, fusion proteins, antigenic peptides and anti-PCIP antibodies. Diagnostic methods utilizing compositions of the invention are also provided.
REFERENCES:
patent: 6117989 (2000-09-01), Bandman et al.
patent: WO 97/31112 (1997-08-01), None
patent: WO 98/16185 (1998-04-01), None
patent: WO 99/49038 (1999-09-01), None
Voet et al. Biochemistry. 1990. John Wiley & Sons, Inc. pp. 126-128 and 228-234.
Adachi, Y. et al., “Identification and characterization of SET, a nuclear phosphoprotein encoded by the translocation break point in acute undifferentiated leukemia,”J. Biol. Chem.,269:2258-2262 (1994).
Bilbe, G., et al., “Restin: a novel intermediate filament-associated protein highly expressed in the Reed-Sternberg cells of Hodgkin's disease,”EMBO J.11 (6):2103-2113 (1992).
Bonaldo et al., GenBank Accession No. AA859724 [online], “Calcium-binding protein NCS-1” (Mar. 14, 1998).
Buxbaum, Joseph D. , et al., “Calsenilin: A calcium-binding protein that interacts with the presenilins and regulates the levels of a presenilin fragment”,Nature Medicine,vol. 4, No. 10, pp. 1177-1181 (1998).
Carrion, Angel M., et al., “Dream is a CA2+-regulated transcriptional repressor”,Nature,vol. 398, pp. 80-84 (1999).
Castagna, Michela et al. “Molecular Characteristics of Mammalian and Insect Amino Acid Transporters: Implications for Amino Acid Homeostatis”The Journal of Experimental Biology200:269-286 (1997).
Cunningham, E. et al., “Phosphatidylinositol transfer protein dictates the rate of inositol trisphosphate production by promoting the synthesis of PIP2.”Curr Biol.5(7):775-83 (1995).
DeCastro, E. et al., “Regulation of rhodopsin phosphorylation by a family of neuronal calcium sensors”Biochem Biophys Res Commun.;216(1):133-40 1995).
Dickeson,S.K., et al., “Isolation and sequence of cDNA clones encoding rat phosphatidylinositol transfer protein,”J. Biol. Chem.264 (28):16557-16564 (1989).
Dixon, J., “Role of the Kv4.3 K+ channel in ventricular muscle. A molecular correlate for the transient outward current”Circ Res:79(4) 659-68 (1996).
Endo T. A. et al “A new protein containing an SH2 domain that inhibits JAK kinase,”Nature387(6636) 921-4 1997.
Fukuda, J. et al., “Breakdown of cytoskeletal filaments selectively reduces Na and Ca spikes in cultured mammal neurones.”Nature294(5836):82-5 (1981).
Funkhouser, J.D.; Amino-terminal sequence of a phospholipid transfer protein from rat,lung, Biochem. Biophys. Res. Commun. 145:1310-1314 (1987).
Hoffman, D.A et al., “K+ channel regulation of signal propagation in dendrites of hippocampal pyramidal neurons,”Nature.387(6636):869-75 (1997).
Hoffman, D.A et al., “Downregulation of transient K+ channels in dendrites of hippocampal CA1 pyramidal neurons by activation of PKA and PKC,”J Neurosci.18(10):3521-8 (1998).
Honore, E. et al., “Different types of K+ channel current are generated by different levels of a single mRNA,”EMBO J.11(7):2465-71 (1992).
Hoppe-Seyler, “Purification and characterization of two putative HLA class II associated proteins: PHAPI and PHAPII,”Biol. Chem.,375:113-126 (1994).
Jan. L.Y. et al., “How might the diversity of potassium channels be generated?”Trends Neurosci.13(10):415-9 (1990).
Johnson, B.D et al., “A cytoskeletal mechanism for Ca2+ channel metabolic dependence and inactivation by intracellular Ca2+,”Neuron.10(5):797-804 (1993).
Kaab, S. et al , “Molecular basis of transient outward potassium current downregulation in human heart failure: a decrease in Kv4.3 mRNA correlates with a reduction in current density”Circulation.98(14):1383-93 (1998).
Kim, E. et al. “Clustering of Shaker-type K+channels by interaction with a family of membrane-associated guanylate kinases”Nature378:85-88 (Nov. 2, 1995).
Levin, G. et al., “Phosphorylation of a K+ channel alpha subunit modulates the inactivation conferred by a beta subunit. Involvement of cytoskeleton,”J Biol Chem.271(46):29321-8 (1996).
Li, M., et al., “The myeloid leukemia-associated protein SET is a potent inhibitor of protein phosphatase 2A,”J. Biol. Chem.271 (19):11059-11062 (1996).
Lombardi, Stephen J. et al. “Structure-Activity Relationships of the Kvβ1 Inactivation Domain and Its Putative Receptor Probed Using Peptide Analogs of Voltage-gated Potassium Channel α and β-Supunits”The Journal of Biological Chemistry273(46) 30092-30096 (Nov. 13, 1998).
Masiakowski, P et al Nerve growth factor induces the genes for two proteins related to a family of calcium-binding proteins in PC12 cells,Proc Natl Acad Sci U S A.85(4):1277-81 (1988).
Nagase, T. et al., “Prediction of the coding sequences of unidentified human genes. XI. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro,”DNA Res.5 (5):277-286 (1998).
Nagata, K. et al., “Replication factor encoded by a putative oncogene, set, associated with myeloid leukemogenesis,”Proc Natl. Acad. Sci. U.S.A.,92:4279-4283 (1995).
Naka, T. et al., “Structure and function of a new STAT-induced STAT inhibitor,”Nature.387(6636):924-9 (1997).
Nakamura, T.Y. et al., “Modulation of Kv4 channels, key component of rat ventricular transient outward K+ channel current, by PKC,”Am J Physiol.273(4 Pt 2):H1775-86 (1997).
National Cancer Institute-Cancer Genome Aanatomy Project, GenBank Accession No. AI038858 [online], “. . . Homo sapiens cDNA clone Image:1659605 3' similar to SW:VIS3_Rat P35333 Visinin-like Protein” (Jul. 1, 1998).
Nerbonne, J., “Regulation of voltage-gated K+ channel expression in the developing mammalian myocardium”,J Neurobiol.;37(1):37-59. (1998)Review.
Panaretou, C. et al., “Characterization of p150, an adaptor protein for the human phosphatidylinositol (Ptdins) 3-kinase. Substrate presentation by phosphatidylinositol transfer protein to the p150.Ptdins 3-kinase complex,”J Biol Chem.272(4):2477-85 (1997).
Pierre,P., et al., “CLIP-170 links endocytic vesicles to microtubules,”Cell70 (6):887-900 (1992).
Pongs, O. et al., “Regulation of the activity of voltage-gated potassium channels by beta subunits”Sem. Neurosci.7:137-146 (1995).
Prevarskaya, N.B. et al., “Role of tyrosine phosphorylation in potassium channel activation. Functional association with prolactin receptor and JAK2 tyrosine kinase,”J Biol. Chem.270(41):24292-9 (1995).
Scannevin, R.H. and Trimmer, J.S. “Cytoplasmic Domains of Voltage-Sensitive K+Channels Involved in Mediating Protein-Protein Interactions”Biochemical and Biophysical Research Communications232:585-589 (1997).
Serodio, P. et al., “Cloning of a Novel Component of A-Type K+Channels Operating at Subthreshold Potential with Unique Expression in Heart and Brian”Journal of Neurophysiology,vol. 75, No. 5, pp. 2174-2179 (1996).
Sheng, M. et al., “Subcellular segregation of two A-type K+ channel proteins in rat central neurons,”Neuron.9(2):271-84 (1992).
Sheng, M. and Kim, E. “Ion channel associated proteins”Current Opinion in Neurobiology6:602-608 (1996).
Simon, H.U. et al., “Molecular characterization of hNRP, a cDNA encoding a human nucleosome-assembly-protein-I-related gene product involved in the induction of cell p
An Wenqian
Betty Maria
Ling Huai-Ping
Rhodes Kenneth
Brumback Brenda
Mandragouras Amy E.
Marie Laccotripe Zacharakis Lahive & Cockfield LLP
Millennium Pharmaceuticals Inc.
Murphy Joseph F.
LandOfFree
Potassium channel interactors and uses therefor does not yet have a rating. At this time, there are no reviews or comments for this patent.
If you have personal experience with Potassium channel interactors and uses therefor, we encourage you to share that experience with our LandOfFree.com community. Your opinion is very important and Potassium channel interactors and uses therefor will most certainly appreciate the feedback.
Profile ID: LFUS-PAI-O-3570570