Chemistry: molecular biology and microbiology – Measuring or testing process involving enzymes or...
Reexamination Certificate
2007-12-04
2007-12-04
Canella, Karen A. (Department: 1642)
Chemistry: molecular biology and microbiology
Measuring or testing process involving enzymes or...
Reexamination Certificate
active
11253190
ABSTRACT:
The present invention relates to methods of identifying modulators of an interaction between 53BP1 and histone H3 (H3). The present invention also relates to methods of use of inhibitors of an interaction between 53BP1 and H3. The present invention further relates to fragments of 53BP1 and H3, as well as other methods and uses.
REFERENCES:
Bowie et al (Science, 1990, 257:1306-1310).
Lazar et al (Molecular and Cellular Biology, 1988, 8:1247-1252).
Burgess et al (J of Cell Bio. 111:2129-2138, 1990).
Anderson et al., “Phosphorylation and rapid relocalization of 53BP1 to nuclear foci upon DNA damage,”Molecular and Cellular Biology(2001) 21(5):1719-1729.
Bakkenist et al., “DNA damage activates ATM through intermolecular autophosphorylation and dimer dissociation,”Nature(2003) 421(6922):499-506.
Bergendahl et al., “Luminescence resonance energy transfer-based high-throughput screening assay for inhibitors of essential protein-protein interactions in bacterial RNA polymerase,”Appl Environ Microbiol.(2003) 69(3):1492-1498.
Boulton et al., “Combined functional genomic maps of theC. elegansDNA damage response,”Science(2002) 295(5552):127-131.
Boute et al., “The use of resonance energy transfer in high-throughput screening: BRET versus FRET,”Trends Pharmacol Sci.(2002) 23(8):351-354.
Brahms et al., “Symmetrical dimethylation of arginine residues in spliceosomal Sm protein B/B″ and the Sm-like protein LSm4 and their interaction with the SMN protein,”RNA(2001) 7:1531-1542.
Celeste et al., “Histone H2AX phosphorylation is dispensable for the initial recognition of DNA breaks,”Nature Cell Biology(2003) 5(7):675-679.
Charier et al., “The Tudor tandem of 53BPI: a new structural motif involved in DNA and RG-rich peptide binding,”Structure(2004) 12(9):1551-1562.
Cunningham et al., “Label-free assays on the BIND system,”J. Biomol Screen(2004) 9(6):481-490.
Feng et al., “Methylation of H3-Lysine 79 Is Mediated by a New Family of HMTases without a SET Domain,”Current Biology(2002) 12(12)1052-1058.
Friesen et al., “SMN, the product of the spinal muscular atrophy gene, binds preferentially to dimethylarginine-containing protein targets,”Molecular Cell(2001) 7(5):1111-1117.
Gadek “Strategies and methods in the identification of antagonists of protein-protein interactions,”Biotechniques(2003) Suppl:21-24.
Gadek et al., “Small molecule antagonists of proteins,”Biochem Pharmacol(2003) 65(1):1-8.
Game et al., “X-ray survival characteristics and genetic analysis for nine Saccharomyces deletion mutants that show altered radiation sensitivity,”Genetics(2005) 169(1):51-63.
Huyen et al., “Structural differences in the DNA binding domains of human p53 and itsC. elegansortholog Cep-1,”Structure(2004) 12(7):1237-1243.
Iwabuchi et al., “Potential role for 53BP1 in the DNA end-joining repair through direct interaction with DNA,”The Journal of Biological Chemistry(2003) 278(38):36487-36495.
Kannouche et al., “Interaction of human DNA polymerase eta with monoubiquitinated PCNA: a possible mechanism for the polymerase switch in response to DNA damage,”Molecular Cell(2004) 14(4):491-500.
Kay et al., “High-throughput screening strategies to identify inhibitors of protein-protein interactions,”Mol. Divers.(1996) 1(2):139-140.
Kouzarides, “Histone methylation in transcriptional control,”Current Opinion in Genetics and Development(2002) 12(2)198-209.
Lacoste et al., “Disruptor of telomeric silencing-1 is a chromatin-specific histone H3 methyltransferase,”The Journal of Biological Chemistry(2002) 277(34):30421-30424.
Luger et al., “Crystal structure of the nucleosome core particle at 2.8 A resolution,”Nature(1997) 389(6648):251-260.
Mochan et al., “53BP1 and NFBD1/MDC1-Nbs1 function in parallel interacting pathways activating ataxia-telangiectasia mutated (ATM) in response to DNA damage,”Cancer Research(2003) 63(24):8586-8591.
Mozziconacci et al., “Nucleosome gaping supports a functional structure for the 30nm chromatin fiber,”Journal of Structural Biology(2003) 143(1):72-76.
Pierceall et al., “Affinity capillary electrophoresis analyses of protein-protein interactions in target-directed drug discovery,”Methods Mol. Biol.(2004) 261:187-198.
Rappold et al., “Tumor suppressor p53 binding protein 1 (53BP1) is involved in DNA damage-signaling pathways,”The Journal of Cell Biology(2001) 153(3):613-620.
Rogakou et al., “Megabase chromatin domains involved in DNA double-strand breaks in vivo,”J Cell Biol(1999) 146(5):905-916.
Saka et al., “Damage and replication checkpoint control in fission yeast is ensured by interactions of Crb2, a protein with BRCT motif, with Cut5 and Chk1,”Genes&Development(1997) 11(24):3387-3400.
San-Segundo et al., “Role for the silencing protein Dot1 in meiotic checkpoint control,”Mol Biol Cell(2000) 11(10):3601-3615.
Schultz et al., “p53 binding protein 1 (53BP1) is an early participant in the cellular response to DNA double-strand breaks,”The Journal of Cell Biology(2000) 151(7):1381-1390.
Selenko et al., “SMN tudor domain structure and its interaction with the Sm proteins,”Nat Struct Biol(2001) 8(1):27-31.
Sprangers et al., “High-resolution X-ray and NMR structures of the SMN Tudor domain: conformational variation in the binding site for symmetrically dimethylated arginine residues,”J Mol Biol(2003) 327(2):507-520.
Theobald et al., “Nucleic acid recognition by OB-fold proteins,”Annu Rev Biophys Biomol Struct(2003) 32:115-133.
Van Leeuwen et al., “Dot1p modulates silencing in yeast by methylation of the nucleosome core,”Cell(2002) 109(6):745-756.
Ward et al., “Accumulation of checkpoint protein 53BP1 at DNA breaks involves its binding to phosphorylated histone H2AX,”The Journal of Biological Chemistry(2003) 278(22):19579-19582.
Weinert et al., “The RAD9 gene controls the cell cycle response to DNA damage inSaccharomyces cerevisiae,”Science(1988) 241(4863):317-322.
Willson et al., “Isolation and characterization of theSchizosaccharomyces pomberhp9 gene: a gene required for the DNA damage checkpoint but not the replication checkpoint,”Nucleic Acids Research(1997) 25(11):2138-2146.
Xia et al., “Negative cell cycle regulation and DNA damage-inducible phosphorylation of the BRCT protein 53BP1,”The Journal of Biological Chemistry(2001) 276(4):2708-2718.
Huyen et al., “Methylated lysine 79 of histone H3 targets 53BP1 to DNA double-strand breaks,”Nature(2004) 432(7015):406-411.
Ward et al., “53BP1 is required for class switch recombination,”J Cell Biol(2004) 165(4):459-464.
Canella Karen A.
Halazonetis Thanos D.
Joyce Catherine
Pepper Hamilton LLP
LandOfFree
Methods of identifying an agent that modulates an... does not yet have a rating. At this time, there are no reviews or comments for this patent.
If you have personal experience with Methods of identifying an agent that modulates an..., we encourage you to share that experience with our LandOfFree.com community. Your opinion is very important and Methods of identifying an agent that modulates an... will most certainly appreciate the feedback.
Profile ID: LFUS-PAI-O-3875030