title: Affinity-based assays for the identification and quantitative evaluation of noncovalent poly(ADP-ribose)-binding proteins.
abstract: Poly(ADP-ribose) polymerases have been linked to several cellular functions, most of which being mediated through the dynamics of poly(ADP-ribose) (pADPr). In several pathways, pADPr is the effector molecule that regulates cellular signaling and dictates biological outcomes. pAPDr is a central molecule that is capable of promoting both cell survival through the maintenance of genome integrity and cell death that occurs by way of a signal-mediated apoptotic-like process. Thus, interactions with pADPr are extremely important in bringing about the balanced regulation that controls cell fate. Further clues regarding these functions are emerging from a growing list of proteins with which pADPr interacts. Here, we describe the current approaches for investigating noncovalent protein interactions with pADPr.
authors.affiliation: CHUQ Research Center (CHUL), Laval University, Quebec City, QC, Canada.
authors.forename: Jean-Philippe
authors.initials: JP
authors.lastname: Gagné
authors.forename: Jean-François
authors.initials: JF
authors.lastname: Haince
authors.forename: Emilie
authors.initials: E
authors.lastname: Pic
authors.forename: Guy G
authors.initials: GG
authors.lastname: Poirier
mesh_terms: D002352:Carrier Proteins / Q000235:genetics / Q000378:metabolism*; D024202:Electrophoretic Mobility Shift Assay; D047468:Immunoprecipitation; D013058:Mass Spectrometry; D011064:Poly Adenosine Diphosphate Ribose / Q000378:metabolism*; D011065:Poly(ADP-ribose) Polymerases / Q000235:genetics / Q000378:metabolism; D020349:Surface Plasmon Resonance
chemical_list: D002352:Carrier Proteins; D011064:Poly Adenosine Diphosphate Ribose; D011065:Poly(ADP-ribose) Polymerases