Chemistry: natural resins or derivatives; peptides or proteins; – Proteins – i.e. – more than 100 amino acid residues
Reexamination Certificate
2006-08-22
2006-08-22
Rawlings, Stephen L. (Department: 1643)
Chemistry: natural resins or derivatives; peptides or proteins;
Proteins, i.e., more than 100 amino acid residues
C536S023500
Reexamination Certificate
active
07094873
ABSTRACT:
An isolated polypeptide having negative regulating activity for a heat shock protein is provided. Also provided is an isolated nucleic acid encoding the polypeptide of the invention, methods for identifying inhibitors of the polypeptide and recombinant preparation of the polypeptide. Also provided are compositions such as inhibitor compositions.
REFERENCES:
patent: 4436815 (1984-03-01), Hershberger et al.
patent: 4440859 (1984-04-01), Rutter et al.
patent: 6043084 (2000-03-01), Scanlan et al.
patent: 6165767 (2000-12-01), Lal et al.
patent: 6218521 (2001-04-01), Obata
patent: 6338952 (2002-01-01), Young
patent: WO-9904265 (1999-01-01), None
Yang, X, et al, 1998, Human BAG-1/RAP46 protein is generated as four isoforms by alternative initiation and overexpressed in cancer cells, Oncogene, vol. 17, No. 8, pp. 981-989.
Takayama, S. et al, 1995, Cloning and functional analysis of BAG-1: a novel Bcl-2 binding protein with anti-cell death activity. Cell, vol. 80, No. 2, pp. 279-284.
Froesch, BA, et al, 1998, BAG-1L protein enhances androgen receptor function, Journal of Biological Chemistry, vol. 273, No. 19, pp. 11660-11666.
Cato, ACB, et al, 2001, BAG-1 family of cochaperones in the modulation of nuclear receptor action, Journal of Steroid Biochemistry & Molecular Biology, vol. 78, No. 5, pp. 379-388.
Prapapanich, V, et al, 1996, Mutational analysis of the hsp-70-interacting protein Hip, Molecular and Cellular Biology, vol. 16, No. 11, pp. 6200-6207.
Jiang, J., et al, 2001, CHIP is a U-box-dependent E3 ubiquitin ligase, Journal of Biological Chemistry, vol. 276, No. 46, pp. 42938-42944.
Prapapanich, V, et al, 1998, Mutation of Hip's carboxyl-terminal region inhibits a transitional stage of progesterone receptor assembly, Molecular and Cellular Biology, vol. 18, No. 2, pp. 944-952.
Bork, P, 2000, Powers and pitfalls in sequence analysis: the 70% hurdle, Genome Research, vol. 10, pp. 398-400.
Burgess, WH, et al, 1990, Possible dissociation of the heparin-binding and mitogenic activities of heparin-binding (acidic fibroblast) growth factor-1, J Cell Biology, vol. 111, pp. 2129-2138.
Lazar, E, et al, 1988, Transforming growth factor alpha: mutation of aspartic acid 47 and leucine 48 results in different biological activities, Molecular and Cellular Biology, vol. 8, pp. 1247-1252.
Bowie, JU, et al, 1990, Deciphering the message in protein sequences: tolerance to amino acid substitutions, Science, vol. 247, pp. 1306-1310.
Scanlan, MJ, Direct Submission, Dec. 23, 1997, Database GenBank Accession No. AF039689,Homo sapiensantigen NY-CO-7 (NY-CO-7) mRNA, complete cds.
Gura T. Science Nov. 7, 1997; 278: 1040-1.
Bergers G, et al. Cur Opin Genetics Develop 2000; 10: 120-7.
Skolnick, J, et al. Trends Biotechnol Jan. 2000; 18: 34-9.
De Plaen E, et al. Immunogenetics. 1994; 40: 360-9.
Tockman MS, et al. Cancer Res. 1992; 52 (Suppl.): 2711s-2718s.
Ward AM. Developmental Oncol. 1985; 21: 90-106.
Goebl M, et al. Trends Biochem Sci. May 1991;16 (5): 173-7.
Murata S, et al. EMBO Rep. Dec. 2001;2 (12): 1133-8.
Nickolay R, et al. J biol Chem. Jan. 23, 2004; 279 (4): 2673-8.
Murata S, et al. Int J Biochem Cell Biol. 2003; 35: 572-8.
Kampringa et al. (Mol. Cell. Biol. Jul. 2003; 23 (14): 4948-4958).
Luque et al. (Biochemistry. Nov. 19, 2002; 41 (46): 13663-13671.
Vucic et al. (J. Biol. Chem. Dec. 18, 1998; 273 (51): 33915-33921).
Takada et al. (Mol. Endocrinol. 2000; 14 (5): 733-740).
Guo et al. (Proc. Natl. Acad. Sci. USA. Jun. 22, 2004; 101 ;(25): 9205-9210).
Ballinger et al., “p35 is a Novel Protein Highly Expressed in Striated Muscle that Interacts with Members of the Heat Shock Protein Family,” Abstract 643, 71stAnnual Meeting of the American Heart Association, Nov. 8-11, Dallas,Supplement to Circulation,98(17):125 (Oct. 27, 1998).
Ballinger et al., “Identification of CHIP, a Novel Striated Muscle-Restricted TPR-Containing Protein that Negatively Regulates Chaperone Functions,” Abstract 370.7 and Poster, Annual Meeting of Professional Research Scientists and American Association of Anatomists, Experimental Biology '99, Apr. 17-21, Washington, D.C.,The FASEB Journal, 13(4):A442, (Mar. 12, 1999).
Ballinger et al., “Identification of CHIP, a Novel Tetratricopeptide Repeat-Containing Protein That Interacts with Heat Shock Proteins and Negatively Regulates Chaperone Functions,”Molecular and Cellular Biology, 19(6):4535-4545 (Jun. 1999; available on line May 17, 1999).
Ballinger et al., “Ubiquitylation of HSC70 is Mediated by CHIP, a Novel Ubiquitylation Factor,” Abstract and oral presentation, Cold Spring Harbor Meeting on Molecular Chaperones & Heat Shock Response, May 3-7, Cold Spring Harbor, N.Y. (May 4, 2000).
Barr et al., “7-Deaza-2′-Deoxyguanosine-5′-Triphosphate: Enhanced Resolution in M13 Dideoxy Sequencing,”BioTechniques, 4(5):428-432 (1986).
Baumann et al., “Dexamethasone Regulates the Program of Secretory Glycoprotein Synthesis in Hepatoma Tissue Culture Cells,”The Journal of Cellular Biology, 85:1-8 (1980).
Benaroudj et al., “The COOH-terminal Peptide Binding Domain Is Essential for Self-association of the Molecular Chaperone HSC70,”The Journal of Biological Chemistry, 272(13):8744-8751 (1997).
“BLAST,” National Institutes of Health [online] United States, [retrieved Oct. 23, 2000]. Retrived from the Internet.
Boice et al., “A Mutational Study of the Peptide-binding Domain of Hsc70 Guided by Secondary Structure Prediction,”The Journal of Biological Chemistry, 272(40):24825-24831 (1997).
Braun et al., “The base of the proteasome regulatory particle exhibits chaperone-like activity,”Nature Cell Biology, 1:221-226 (Aug. 1999).
Broach, “[21] Construction of High Copy Yeast Vectors Using 2-μm Circle Sequences,”Methods in Enzymology: vol. 101 Recombinant DNA, pp. 307-325 (1983).
Carrello et al., “The Common Tetratricopeptide Repeat Acceptor Site for Steroid Receptor-associated Immunophilins and Hop Is Located in the Dimerization Domain of Hsp90,”The Journal of Biological Chemistry, 274(5):2682-2689 (Jan. 29, 1999).
Chakrabarti et al., “Vaccina Virus Expression Vector: Coexpression of β-Galactosidase Provides Visual Screening of Recombinant Virus Plaques,”Molecular and Cellular Biology, 5(12):3403-3409 (1985).
Chappell et al., “The ATPase Core of a Clathrin Uncoating Protein,”The Journal of Biological Chemistry, 262(2):746-751 (1987).
Chen et al., “Interactions of p60, a Mediator of Progesterone Receptor Assembly, with Heat Shock Proteins Hsp90 and Hsp70,”Molecular Endocrinology, 10(6):682-693 (1996).
Clewell et al., “Supercoiled Circular DNA-Protein Complex inEscherichia coli: Purification and Induced Conversion to an Open Circular DNA Form,”Proceedings of the National Academy of Sciences USA, 62:1159-1166 (1969).
Clewell, “Nature of Col E1Plasmid Replication inEscherichia coliin the Presence of Chlorampenicol,”Journal of Bacteriology, 110(2):667-676 (1972).
Cohen et al., “Nonchromosomal Antibiotic Resistance in Bacteria: Genetic Transformation ofEscherichia coliby R-Factor DNA,”Proceedings of the National Academy of Sciences USA, 69(8):2110-2114 (1972).
Connell et al., “CHIP's Interaction with HSP90 Regulates Glucocorticoid Receptor Function and Degradation,” Abstract and poster, Cold Spring Harbor Meeting on Molecular Chaperones & Heat Shock Response, May 3-7, Cold Spring Harbor, N.Y., 25 pages (May 4, 2000).
Connell et al., “The co-chaperone CHIP regulates protein triage decisions mediated by heat shock proteins,”Nature Cell Biology, 3(1):93-96 (2001).
Das et al., “The structure of the tetratricopeptide repeats of protein phosphatase 5: implications for TPR-mediated protein-protein interactions,”The EMBO Journal, 17(5):1192-1199 (1998).
De Boer et al., “Thetacpromoter: A functional hybrid derived from thetrpandlacpromoters,”Proceedings of the National Ac
Ballinger Carol A.
Patterson Winston Campbell
Board of Regents , The University of Texas System
Mueting Raasch & Gebhardt, P.A.
Rawlings Stephen L.
LandOfFree
Polypeptide that interacts with heat shock proteins does not yet have a rating. At this time, there are no reviews or comments for this patent.
If you have personal experience with Polypeptide that interacts with heat shock proteins, we encourage you to share that experience with our LandOfFree.com community. Your opinion is very important and Polypeptide that interacts with heat shock proteins will most certainly appreciate the feedback.
Profile ID: LFUS-PAI-O-3683446