Poly(ADP-ribose) Polymerase

Approaches to Detect PARP-1 Activation In vivo, In situ, and In vitro.- Quantification of Poly(ADP-ribose) In vitro: Determination of the (ADP-ribose) Chain Length and Branching Pattern.- Assay for Protein Modification by Poly-ADP-Ribose In vitro.- Identification of Distinct Amino Acids as ADP-ribose Acceptor Sites by Mass Spectrometry.- Non-covalent Protein Interaction with Poly(ADP-ribose).- Non-covalent pADPr Interaction with Protein and Competition with RNA for Binding to Proteins.- Affinity-based Assays for the Identification and Quantitative Evaluation of Non-covalent Poly(ADP-ribose)-binding Proteins.- Detecting and Quantifying pADPr In vivo.- Purification of Recombinant Poly(ADP-ribose) Polymerases.- Methods for Purification of Proteins Associated with Cellular poly(ADP-risbose) and PARP-specific Poly(ADP-ribose).- Purification and Characterization of Poly(ADP-ribosyl)ated DNA Replication/Repair Complexes.- PARP1 Genomics: Chromatin Immuno-precipitation Approach using Anti-PARP1 Antibody (ChIP and ChIP-seq).- Purification of Human PARP-1 and PARP-1 Domains from E. coli for Structural and Biochemical Analysis.- Regulation of Chromatin Structure by PARP-1.- The Use of PARP Inhibitors in Cancer Therapy: Use as Adjuvant with Chemotherapy or Radiotherapy, Use as a Single Agent in Susceptible Patients; Techniques used to Identify Susceptible Agents.- Quantification of PARP Activity in Human Tissues: Ex vivo Assays in Blood Cells, and Immunohistochemistry in Human Biopsies.- Assay for Hypermethilation of the BRCA1 Gene Promoter in Tumor Cells to Predict Sensitivity to PARP-Inhibitor Therapy.- Generation of Poly(ADP-ribosyl)ation Deficient Mutants of the Transcription Factor, CTCF.- Phenotypic Characterization of Parp-1 and Parp-2 Deficient Mice and Cells.- Poly(ADP-ribosyl)ation Pathways in Mammals: The Advantage of Murine PARG Null Mutation.- Genetic Approaches to Targeting Multiple PARP Genes in a Mammalian Genome.- Approaches to Separate and Identify