Data processing: measuring – calibrating – or testing – Measurement system in a specific environment – Chemical analysis
Reexamination Certificate
2006-07-04
2006-07-04
Brusca, John S. (Department: 1631)
Data processing: measuring, calibrating, or testing
Measurement system in a specific environment
Chemical analysis
C435S004000
Reexamination Certificate
active
07072771
ABSTRACT:
Poly(ADP-ribose) polymerase-1 (PARP-1) is a central signaling enzyme in a cell nucleus. PARP-1 is a target for the development of radio and chemo sensitizing agents in cancer treatment as well as providing protection from stroke. An SH3 domain and an SH3 ligand domain have now been discovered on the PARP-1 protein. These domains are involved in PARP-1 activation. This discovery makes possible the use of bioinformatics tools for the design of new drugs and strategies for drug target selection, specifically targeting the PARP-1 enzyme.
REFERENCES:
patent: 5032617 (1991-07-01), Lee et al.
patent: 5041653 (1991-08-01), Lee et al.
patent: 5215738 (1993-06-01), Lee et al.
patent: 5587384 (1996-12-01), Zhang et al.
patent: 5952169 (1999-09-01), Bürkle et al.
patent: 6074876 (2000-06-01), De Block
patent: 6100283 (2000-08-01), Griffin et al.
patent: 6121278 (2000-09-01), Jackson et al.
patent: 6201020 (2001-03-01), Zhang et al.
Jan Drenth, Principles of Protein X-ray Crystallography, 1995, Springer-Verlag, p. 16.
News Focus, Science, Nov. 1, 2002, vol. 298, pp. 948-950.
Amé J-C et al., “PARP-2, A novel mammalian DNA damage-dependent poly(ADP-ribose) polymerase.”J Biol Chem. 274(25): 17860-8 (1999).
Auer B et al., “Human nuclear NAD+ ADP-ribosyltransferase(polymerizing): organization of the gene.”DNA8(8): p. 575-80 (1989).
Bork P et al., A superfamily of conserved domains in DNA damage-responsive cell cycle checkpoint proteins.Faseb J. 11(1): 68-76 (1997).
Bousquet JA et al., “Circular dichroic investigation of the native and non-native conformational states of the growth factor receptor-binding protein 2 N-terminal src homology domain 3: effect of binding to a proline-rich peptide from guanine nucleotide exchange factor.”Biochemistry39, 7722-35 (2000).
Brannetti B et al., “SH3-SPOT: an algorithm to predict preferred ligands to different members of the SH3 gene family.”J Mol Biol298(2): 313-28 (2000).
Cherney, BW et al., “cDNA sequence, protein structure, and chromosonal location of the human gene for poly(ADP-ribose) polymerase.”Proc Natl Acad Sci U S A84(23): 8370-4 (1987).
Chong S et al., “Single column purification of free recombinant proteins using a self-clevable affinity tag derived from a protein splicing element.”Gene192(2):271-81 (Jun. 1997).
Dalgamo DC, Botfield MC & Rickles RJ, “SH3 domains and drug design: lignads, structure, and biological function.”Biopolymers43: 383-400 (1997).
de Murcia G & de Murcia JM, “Poly(ADP-ribose) polymerase: a molecular nick-sensor.”Trends Biochem Sci19(4): p. 172-6 (1994).
de Murcia JM, et al., “Requirement of poly(ADP-ribose) polymerase in recovery from DNA damage in mice and cells.”Proc Natl Acad Sci U S A94(14): 7303-7 (1997).
Decker P et al., “An improved non isotopic test to screen a large series of new inhibitor molecules of poly(ADP-ribose) polymerase activity for therapeutic applications.”Clin Cancer Res5, 1169-72 (1999).
DeDecker BS et al., “Allosteric drugs: thinking outside the active-site box.”Chem Biol 7(5): R103-7 (2000).
Deng CX & Brodie SG, “Roles fo BRCA1 and its interacting proteins.”Bioessays22(8): 728-37 (2000).
Garbay C et al., “Inhibitors of Ras signal transduction as antimuor agents.”Biochem. Pharmacol. 60(8): 1165-9 (Oct. 15, 2000).
Gradwohl G et al., “The second zinc-finger domain of poly(ADP-ribose) polymerase determines specificity for single-stranded breaks in DNA.”Proc Natl Acad Sci USA87,2990-4 (1990).
Ha HC, et al., “Poly(ADP-ribose) polymers-1 is required for efficient HIV-1 integration.”Proc Natl Acad Sci U S A. 98(6): 3364-8 (Mar. 13, 2001).
Hansson H et al., “Solution structure of the SH3 domain from Bruton's tyrosine kinase.”Biochemistry37(9): 2912-24 (Mar. 3, 1998).
Hansson H et al., “Intermolecular interactions between the SH3 domain and the proline-rich TH region of Bruton's tyrosine kinase.”FEBS Lett. 489(1): 67-70 (Jan. 26, 2001).
Jacobson MK & Jacobson EL, “Discovering new ADP-ribose polymer cycles: protecting the genome and more.”Trends Biochem Sci. 24(11): 415-7 (Nov. 1999).
Jagtap P et al., “Novel phenanthridinone inhibitros of poly (adenosine 5'-diphosphate-ribose) synthetase: potent cytoprotective and antishock agents.”Crit. Care Med. 30(5):1071-82 (May 2002).
Johansson M, “A human poly(ADP-ribose) polymerase gene family (ADPRTL): cDNA cloning of two novel poly(ADP-ribose) polymerase homologues.”Genomics, 57(3): 442-5 (1999).
Juarez-Salinas H et al., “Simultaneous determination of linear and branched residues in poly(ADP-ribose).”Anal Biochem131(2): 410-8 (1983).
Kardinal C et al., “Rational development of cell-penetrating high affinity SH3 domain binding peptides that selectively disrupt the signal transduction of Crk family adapters.”Ann. NY Acad. Sci.886: 289-92 (1999).
Kawamura T et al., “An alternative form of poly(ADP-ribose) polymerase in Drosophila melanogaster and its ectopic expression in rat-1 cells.”Biochem Biophys Res Commun251(1): 35-40 (1998).
Kickhoefer VA et al., “The 193-kD vault protein, VPARP, is a novel poly(ADP-ribose) polymerase.”J Cell Biol146(5): 917-28 (1999).
Kim JW et al., “Inhibition of homodimerization of poly(ADP-ribose) polymerase by its C-terminal cleavage products produced during apoptosis.”J Biol Chem275(11): 8121-5 (2000).
Kuriyan J & Cowburn D, “Modular peptide recognition domains in eukaryotic signaling.”Annu Rev Biophys Biomol Struct26: 259-88 (1997).
Kurosaki T et al., Primary structrue of human poly(ADP-ribose) synthetase as deduced from cDNA sequence.J Biol Chem262(33): 15990-7 (1987).
Los M et al., “Activation and caspase-mediated inhibition of PARP: A molecular switch between fibroblast necrosis and apoptosis in death receptor signaling.”Molecular Biology of the Cell 13:978-988 (Mar. 2002).
Mabley JG et al., “Inhibition of poly (ADP-ribose) synthetase by gene disruption or inhibition with 5-iodo-6-amino-1,2-benzopyrone protects mice from multiple-low-dose-streptozotocin-induced diabetes.”Br. J. Pharmacol. 133(6): 909-19 (Jul. 2001).
Macias MJ, Wiesner S & Sudol M, “WW and SH3 domains, two different scaffolds to recognize proline-rich ligands.”FEBS Lett513(1): 30-7 (2002).
Marintchev A et al., “Solution structure of the single-strand break repair protein XRCCI N-terminal domain.”Nat Struct Biol6(9): 884-93 (1999).
Mendoza-Alvarez H & Alvarez-Gonzalez R, “Poly(ADP-ribose) polymerase is a catalytic dimer and the automodification reaction is intermolecular.”J Biol Chem268(30): 22575-80 (1993).
Mosser EA et al., “Physical and functional interactions between the transactivation domain of the hematopoietic transcription factor NF-E2 and WWdomains.”Biochemistry37: 13686-95 (1998).
Nguyen JT et al., “Improving SH3 domain ligand selectivity using a non-natural scaffold.”Chem Biol. 7(7): 463-73 (2000).
Nicholson DW et al., “Identification and Inhibition of the ICE/CED-3 protease necessary for mammalian apoptosis.”Nature376(6535): 37-43 (1995).
Perkins E et al., “Novel inhibitors of poly(adp-ribose) polymerase/parp 1 and parp2 identified using a cell-based screen in yeast.”Cancer Res61(10): 4175-83 (May 15, 2001).
Pieper A et al., “Poly(ADP-ribosyl)ation basally activated by DNA strand breaks reflects glutamate-nitric oxide neurotransmission.”Proc Natl Acad Sci U S A97(4): 1845-50 (Feb. 15, 2000).
Politou AS et al., “The SH3 domain of nebulin binds selectively to type II peptides: theoretical prediction and experimental validation.”J Mol Biol316(2): 305-15 (2002).
Rolli V et al., “Random mutagenesis of the poly(ADP-ribose) polymerase catalytic domain reveals amino acids involoved in polymer branching.
Brusca John S.
University of Kentucky Research Foundation
LandOfFree
Selective PARP-1 targeting for designing chemo/radio... does not yet have a rating. At this time, there are no reviews or comments for this patent.
If you have personal experience with Selective PARP-1 targeting for designing chemo/radio..., we encourage you to share that experience with our LandOfFree.com community. Your opinion is very important and Selective PARP-1 targeting for designing chemo/radio... will most certainly appreciate the feedback.
Profile ID: LFUS-PAI-O-3600159