Chemistry: molecular biology and microbiology – Animal cell – per se ; composition thereof; process of...
Reexamination Certificate
2008-03-18
2008-03-18
Saoud, Christine J. (Department: 1647)
Chemistry: molecular biology and microbiology
Animal cell, per se ; composition thereof; process of...
C435S069100, C435S252300, C435S320100, C530S350000, C536S023500
Reexamination Certificate
active
10842313
ABSTRACT:
The present invention provides novel polynucleotides encoding LTRPC3g, LTRPC3h, LTRPC3i, LTRPC3j, LTRPC3k, or LTRPC3l polypeptides, fragments and homologues thereof Also provided are vectors, host cells, antibodies, and recombinant and synthetic methods for producing said polypeptides. The invention further relates to diagnostic and therapeutic methods for applying these novel LTRPC3g, LTRPC3h, LTRPC3i, LTRPC3j, LTRPC3k, or LTRPC3l polypeptides to the diagnosis, treatment, and/or prevention of various diseases and/or disorders related to these polypeptides. The invention further relates to screening methods for identifying agonists and antagonists of the polynucleotides and polypeptides of the present invention.
REFERENCES:
patent: 5350836 (1994-09-01), Kopchick et al.
patent: 2003/0162189 (2003-08-01), Lee et al.
patent: 2003/0224450 (2003-12-01), Lee et al.
patent: WO01/32870 (2001-05-01), None
patent: WO02/46415 (2002-06-01), None
patent: WO02/077237 (2002-10-01), None
patent: WO03/012063 (2003-02-01), None
Jordt et al. (2000). Acid potentiation of the capsaicin receptor determined by a key extracellular site. Proc. Natl. Acad. Sci., USA 97(14):8134-8139.
Wells, J.A. (1990). Additivity of mutational effects in proteins. Biochemistry. 29(37):8509-8517.
Ngo et al. (1994). Computational complexity, protein structure prediction, and the Levinthal paradox. In Merz and Le Grand (Eds.) The Protein Folding Problem and Tertiary Structure Prediction. Birkhauser:Boston, pp. 492-495.
Skolnick et al. (2000). From genes to protein structure and function: novel applications of computational approaches in the genomic era. Trends in Biotech. 18(1):34-39.
Bork, A. (2000). Powers and pitfalls in sequence analysis: the 70% hurdle. Genome Res. 10:398-400.
Doerks et al. (1998). Protein annotation: detective work for function prediction. Trends in Genetics. 14(6):248-250.
Smith et al. (1997). The challenges of genome sequence annotation or The devil is in the details. Nature Biotech. 15:1222-1223.
Brenner, S.E. (1999). Errors in genome function. Trends in Genetics. 15(4):132-133.
Bork et al. (1996). Go hunting in sequence databases but watch out for the traps. Trends in Genetics. 12(10):425-427.
Altschul, et al., “Gapped Blast and PSI-BLAST: a new generation of protein database search programs”, Nucleic Acids Res., vol. 25 (17), pp. 3389-3402 (1997).
Blackshaw, et al., “Genomic Analysis of Mouse Retinal Development”, PLOS Biology, vol. 2(9), pp. 1411-1431 (2004).
Carninci, et al., “[2] High-Efficiency Full-Length cDNA Cloning”, Methods Enzy., vol. 303, pp. 19-44 (1999).
Carninci, et al., “Normalization and Subtraction of Cap-Trapper-Selected cDNAs to Prepare Full-Length cDNA Libraries for Rapid Discovery of New Genes”, Genome Res., vol. 10, pp. 1617-1630 (2000).
Caterina, et al., “Impaired Nociception and Pain Sensation in Mice Lacking the Capsaicin Receptor”, Science, vol. 288, pp. 306-313 (2000).
Caterina, et al., “A Capsaicin-Receptor Homologue with a High Threshold for Noxious Heat”, Nature, vol. 398, pp. 436-441 (1999).
Dambach, et al., “Role of CCR2 in Macrophage Migration Into the Liver During Acetaminophen-Induced Hepatotoxicity in the Mouse” Hepatology, vol. 35, pp. 1093-1103 (2002).
Duncan, et al., “Down-Regulation of the Novel Gene Melastatin Correlates with Potential for Melanoma Metastasis”, Cancer Research, vol. 58, pp. 1515-1520 (1998).
Eddy, Sean R., “Profile Hidden Markov Models”, Bioinformatics Review, vol. 14(9), pp. 755-763 (1998).
Freichel, et al., “Lack of an Endothelial Store-Operated Ca2+Current Impairs Agonist-Dependent Vasorelaxation in TRP4-/-Mice”, Nature Cell Biol., vol. 3, pp. 121-127 (2001).
Friedman, et al., “Cellular Calcium Transport in Renal Epithelia: Measurement, Mechanisms, and Regulation”, Physiological Rev., vol. 75(3), pp. 429-471 (1995).
Grimm, et al., “Activation of the Melastatin-Related Cation Channel TRPM3 by D-erythro-Sphingosine”, Molecular Pharm., vol. 67 (3), pp. 798-805 (2005).
Grimm, et al., “Molecular and Functional Characterization of the Melastatin-related Cation Channel TRPM3”, JBC, vol. 278 (24), pp. 21493-21501 (2003).
Guo, et al., “Identification and Characterization of a Novel Polycystin Family Member, Polycystin-L2, in Mouse and Human: Sequence Expression, Alternative Splicing, and Chromosomal Localization”, Genomics, vol. 64, pp. 241-251 (2000).
Hara, et al., “LTRPC2 Ca2+-Permeable Channel Activated by Changes in Redox Status Confers Susceptibility to Cell Death”, Molecular Cell., vol. 9, pp. 163-173 (2002).
Hardie, et al. “The trp Gene Is Essential for a Light-Activated Ca2+Channel in Drosophilia Photoreceptors”, Neuron, vol. 8, pp. 643-651 (1992).
Harteneck, et al., “From worm to man: three subfamilies of TRP channels”, TINS, vol. 23 (4), pp. 159-166 (2000).
Henikoff, et al., “Amino Acid Substitution Matrices From Protein Blocks”, PNAS, vol. 89, pp. 10915-10919 (1992).
Henricksen, et al., “Inhibition of Flap Endonuclease 1 by Flap Secondary Structure and Relevance to Repeat Sequence Expansion”, JBC, vol. 275 (22), pp. 16420-16427 (2000).
Heymann, et al., “Conformations of the rhodopsin third cytoplasmic loop grafted onto bacteriorhodopsin”, Structure, vol. 8(6), pp. 643-653 (2000).
Hoenderop, et al., “Molecular Mechanism of Active Ca2+Reabsorption in the Distal Nephron”, Annu. Rev. Physiol., vol. 64, pp. 529-549 (2002).
Hoenderop, et al., “Molecular Identification of the Apical Ca2+Channel in 1,25-Dihydroxyvitamin D3-responsive Epithelia”, J. Biol. Chem., vol. 274(13), pp. 8375-8378 (1999).
Hunter, et al., “Chromosomal Localization and Genomic Characterization of the Mouse Melastatin Gene (Mlsn1)”, Genomics, vol. 54, pp. 116-123 (1998).
Inoue, et al., “The Transient Receptor Potential Protein Homologue TRP6 is the Essential Component of Vascular α1-Adrenoceptor-Activated Ca2+-Permeable Cation Channel”, Circ. Res., vol. 88, pp. 325-332 (2001).
Jin, et al., “The 3′→5′ Exonuclease of DNA Polymerase δ Can Substitute for the 5′ Flap Endonuclease Rad27/Fen1 in Processing Okazaki Fragments and Preventing Genome Instability”, PNAS, vol. 98(9), pp. 5122-5127 (2001).
Riken Genome Exploration Res. Group, “Functional annotation of a full-length mouse cDNA collection”, Nature, vol. 409, pp. 685-690 (2001).
Koticha, et al., “Plasma Membrane Targeting of SNAP-25 Increases its Local Concentration and is Necessary for SNARE Complex Formation and Regulated Exocytosis”, J. Cell Science, vol. 115, pp. 3341-3351 (2002).
Launay, et al., “TRPM4 Is a Ca2+-Activated Nonselective Cation Channel Mediating Cell Membrane Depolarization”, Cell, vol. 109, pp. 397-407 (2002).
Lee, et al., “Expression and Characterization of Human Transient Receptor Potential Melastatin 3 (hTRPM3)”, J. Biol. Chem., vol. 278(23), pp. 20890-20897 (2003).
Liman, et al., “TRP2: A Candidate Transduction Channel for Mammalian Pheromone Sensory Signaling”, PNAS, vol. 96, pp. 5791-5796 (1999).
Ma, et al., “Single Nucleotide Polymorphism Analyses of the Human Proliferating Cell Nuclear Antigen (PCNA) and Flap Endonuclease (FEN1) Genes”, Int. J. Cancer, vol. 88, pp. 938-942 (2000).
Ma, et al., “Protein Kinase C Activates Store-Operated Ca2+Channels in Human Glomerular Mesangial Cells”, J. Biol. Chem., vol. 276(28), pp. 25759-25765 (2001).
Matsumura, et al, “Single Solitary Metastasis of the Slowly Progressive Type of Renal Cell Carcinoma to the Choroid Plexus”, Neurol. Med. Chir., vol. 37, pp. 916-919 (1997).
McKemy, et al., “Identification of a cold receptor reveals a general role for TRP channels in thermosensation”, Nature, vol. 416, pp. 52-58 (2002).
Missiaen, et al., “Abnor
Blanar Michael A.
Chen Jian
Lee Ning
Levesque Paul C.
Sun Lucy
Bristol--Myers Squibb Company
D'Amico Stephen C.
Lockard Jon M
Saoud Christine J.
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