Chemistry: molecular biology and microbiology – Enzyme – proenzyme; compositions thereof; process for... – Transferase other than ribonuclease
Reexamination Certificate
2006-01-24
2006-01-24
Hutson, Richard (Department: 1652)
Chemistry: molecular biology and microbiology
Enzyme , proenzyme; compositions thereof; process for...
Transferase other than ribonuclease
C435S183000, C435S069100, C435S091100, C530S350000
Reexamination Certificate
active
06989260
ABSTRACT:
The invention provides a novel human poly(ADP-ribose) polymerase (hPARP2) polypeptides, polynucleotides encoding the polypeptides, expression constructs comprising the polynucleotides, and host cells transformed with the expression constructs. Also provided are methods for producing the hPARP2 polypeptides, antibodies that are immunoreactive with the hPARP2 polypeptides. In addition, there are provided methods for identifying specific binding partners of hPARP2, and more particularly methods for identifying binding partners that modulate biological activity of hPARP2. Methods of modulating biological activity of hPARP2 in vitro and in vivo are also provided.
REFERENCES:
patent: 3645090 (1972-02-01), Mochizuki et al.
patent: 3691016 (1972-09-01), Patel et al.
patent: 3940475 (1976-02-01), Gross
patent: 3969287 (1976-07-01), Jaworek et al.
patent: 4195128 (1980-03-01), Hildebrand et al.
patent: 4229537 (1980-10-01), Hodgins et al.
patent: 4247642 (1981-01-01), Hirohara et al.
patent: 4302204 (1981-11-01), Wahl et al.
patent: 4330440 (1982-05-01), Ayers et al.
patent: 4358535 (1982-11-01), Falkow et al.
patent: 4683195 (1987-07-01), Mullis et al.
patent: 4687732 (1987-08-01), Ward et al.
patent: 4703004 (1987-10-01), Hopp et al.
patent: 4711955 (1987-12-01), Ward et al.
patent: 4782137 (1988-11-01), Hopp et al.
patent: 4800195 (1989-01-01), Burgess et al.
patent: 4851431 (1989-07-01), Yehuda
patent: 4946778 (1990-08-01), Ladner et al.
patent: 4965188 (1990-10-01), Mullis et al.
patent: 5011912 (1991-04-01), Hopp et al.
patent: 5241060 (1993-08-01), Engelhardt et al.
patent: 5244787 (1993-09-01), Key et al.
patent: 5328824 (1994-07-01), Ward et al.
patent: 5580990 (1996-12-01), van den Berg et al.
patent: 5714327 (1998-02-01), Houthoff et al.
patent: 0 063 879 (1982-11-01), None
patent: 0 075 444 (1983-03-01), None
patent: 2 019 404 (1979-10-01), None
patent: 2 034 323 (1980-06-01), None
patent: WO 91/09955 (1991-07-01), None
patent: WO 92/20808 (1992-11-01), None
patent: WO 94/12650 (1994-06-01), None
patent: WO 99/11623 (1999-03-01), None
patent: WO 99/11649 (1999-03-01), None
patent: WO 99/64572 (1999-12-01), None
Alkhatid, et al., “Cloning and Expression of cDNA for Human Poly(ADP-ribose) Polymerase,”Proc. Natl. Acad. Sci. USA, vol. 84, pp. 1224-1228, Mar. 1987.
Althaus and Richter, “ADP-Ribosylation of Proteins: Enzymology and Biochemical Significance,”Molecular Biochemistry and Biophysics, Springer-Verlag (1987).
Amé, J.C., et al., “PARP-2, A Novel Mammalian DNA Damage-dependent Poly(ADP-Ribose) Polymerase,”J. Biol. Chem., 274(25):17860-17868 (1999).
Anderson, W.F., “Human Gene Therapy,”Nature, 392 (6679 Suppl.):25-30 (1998).
Ausubel, et al., (Eds.), “Screening of Recombinant DNA Libraries,”Current Protocols in Molecular Biology, John Wiley & Son, Chapter 6, pp. 6.0.3-6.4.10 (1994).
Babiychuk, et al., “Higher Plants Possess Two Structurally Different Poly(ADP-ribose) Polymerases,”The Plant Journal, vol. 15(5) pp. 635-645, Sep. 1998.
Banasik, et al., “Specific Inhibitors of Poly (ADP-Ribose) Synthetase and Mono (ADP-Ribosyl) transferase,”J. Biol. Chem., 267:1569-1575 (1992).
Barany, F., “The Ligase Chain Reaction in a PCR World,”PCR Methods and Applications, 1:5-16 (1991).
Benjamin and Gill, “Poly(ADP-ribose) Synthesis In Vitro Programmed by Damaged DNA,”J. Biol. Chem., 255:10502-8 (1980).
Berger and Kimmel, (Eds.) “Guide to Molecular Cloning Techniques, ”Methods in Enzymology, vol. 152, Title Page and Table of Contents Academic Press, San Diego, California (1987).
Berghammer, et al., “pADPRT-2: A Novel Mammalian Polymerizing (ADP-ribosyl) Transferase Gene Related to Truncated pADPRT Homologues in Plants andCaenorhabditis elegans,” FEBS Lett.449:259-263 (1999).
Bramlage, et al., “Designing Ribozymes for the Inhibition of Gene Expression,”Trends Biotechnol., 16:434-438 (1998).
Brüggemann, et al., “Strategies for Expressing Human Antibody Repertoires in Transgenic Mice,”Immunol. Today, 17:391-397 (1996).
Cane, et al., “Harnessing the Biosynthetic Code: Combinations, Permutations, and Mutations,”Science, 282:63-68 (1998).
Capecchi, M.R., “Altering the Genome by Homologous Recombination,”Science, 244:1288-1292 (1989).
Caruthers, M.H., “Gene Synthesis Machines: DNA Chemistry and Its Uses,”Science, 230:281-285 (1985).
Caruthers, et al., “Chemical Synthesis of Deoxyoligonucleotides and Deoxyoligonucleotide Analogs,”Methods Enzymol., 211:3-20 (1992).
Cherney, et al., “cDNA Sequence, Protein Structure, and Chronosomal Location of the Human Gene for Poly(ADP-ribose) Polymerase,”Proc. Natl. Acad. Sci. USA, vol. 84, pp. 8370-8374, Dec. 1987.
Clackson, et al., “Making Antibody Fragments Using Phage Display Libraries,”Nature, 352:624-628 (1991).
Cline, et al., “PCR Fidelity of Pfu DNA Polymerase and Other Thermostable DNA Polymerases,”Nucleic Acids. Res., 24:3546-3551 (1996).
Dall'Acqua, et al., “Antibody Engineering,”Curr. Opin. Struct. Biol., 8:443-450 (1998).
D'Amours, et al., “Purification of the Death Substrate Poly(ADP-ribose) Poymerase,”Anal. Biochem., 249:106-108 (1997).
David, et al., “Protein Iodination with Solid State Lactoperoxidase,”Biochemistry, 13:1014-1021 (1974).
Dayhoff inAtlas of Protein Sequence and Structure, National Biochemical Research Foundation, Washington, D.C. 5:124 (1972).
Delihas, et al., “Natural Antisense RNA/target RNA Interactions: Possible Models for Antisense Oligonucleotide Drug Design,”Nat. Biotechnol., 15:751-753 (1997).
Eguchi, Y., “Antisense RNA,”Annu. Rev. Biochem., 60:631-652 (1991).
Fritz, et al., “Effect of Transfection of Human Poly(ADP-ribose) Polymerase in Chinese Hamster Cells on Mutagen Resistance,”Mutation Res., 308:127-133 (1994).
Gatti, et al., “Localization of an Ataxia-telangiectasia Gene to Chromosome 11q22-23,”Nature, 336:577-580 (1988).
Gibson and Shillitoe, “Ribozymes: Their Functions and Strategies for Their Use,”Mol. Biotechnol., 7:125-137 (1997).
Harlow, et al., (Eds.)Antibodies: A Laboratory Manual, Chapter 6, Cold Spring Harbor Laboratory, Cold Spring Harbor, New York, NY, pp. 139-243 (1988).
Hodgkin, et al., “The NematodeCasnorhabditis elegansand Its Genome,”Science, 270:410 (1995).
Houston and Banks, “The Chemical-Biological Interface: Developments in Automated and Miniaturised Screening Technology,”Curr. Opin. Biotechnol., 8:734-740 (1997).
Hunter, et al., “Preparation of Iodine-131 Labelled Human Growth Hormone of High Specific Activity,”Nature, 194:495-496 (1962).
Huse, et al., “Generation of a Large Combinatorial Library of the Immunoglobulin Repertoire in Phage Lambda,”Science, 246:1275-1281 (1989).
Jayawickreme and Kost, “Gene Expression Systems in the Development of High-Throughput Screens,”Curr. Opin. Biotechnol., 8:629-634 (1997).
Johansson, M., “A Human Poly(ADP-Ribose) Polymerase Gene Family (ADPRTL): cDNA Cloning of Two Novel Poly(ADP-ribose) Polymerase Homologues,”Genomics, 57(3):442-445 (1999).
Johansson, M., EMBL/Genbank Data Libraries, Accession No. AF085734, Dec. 1999.
Köhler and Milstein, “Continuous Cultures of Fused Cells Secreting Antibody of Predefined Specificity,”Nature, 256:495-497 (1975).
Lagerström, et al., “Capture PCR: Efficient Amplification of DNA Fragments Adjacent to a Known Sequence in Human and YAC DNA,”PCR Methods Applic., 1:111-119 (1991).
Lamoyi, et al., “Preparation of F(ab')2Fragments From Mouse IgG of Various Subclasses,”J. Immunol. Meth., 56:235-243 (1983).
Landegren, et al., “A Ligase-Mediated Gene Detection Technique,”Science, 241:1077-1080 (1988).
Lavrovsky, et al., “Therapeutic Potential and Mechanism of Action of Oligonucle
Christenson Erik
DeMaggio Anthony J.
Goldman Phyllis S.
McElligott David L.
Hutson Richard
ICOS Corporation
Marshall & Gerstein & Borun LLP
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