Insights into PARP inhibitors' selectivity using fluorescence polarization and surface plasmon resonance binding assays

Journal of Biomolecular Screening

Volumn 19, Issue 8, 2014, Pages 1212-1219

  Papeo, Gianluca ^a   Avanzi, Nilla ^a   Bettoni, Serena ^a   Leone, Antonella ^a   Paolucci, Mauro ^a   Perego, Rita ^a,b   Quartieri, Francesca ^a   Riccardi Sirtori, Federico ^a   Thieffine, Sandrine ^a   Montagnoli, Alessia ^a   Lupi, Rosita ^a,b  

^a NERVIANO MEDICAL SCIENCES   (Italy)

^b EVOTEC UK LTD   (United Kingdom)

Author keywords

fluorescence polarization (FP); HTS; PARP; selectivity; surface plasmon resonance (SPR)

Indexed keywords

8 HYDROXY 2 METHYL 4(3H) QUINAZOLINONE; FLUORESCENT DYE; N (5,6 DIHYDRO 6 OXO 2 PHENANTHRIDINYL) 2 DIMETHYLAMINOACETAMIDE; NICOTINAMIDE ADENINE DINUCLEOTIDE ADENOSINE DIPHOSPHATE RIBOSYLTRANSFERASE 1; NICOTINAMIDE ADENINE DINUCLEOTIDE ADENOSINE DIPHOSPHATE RIBOSYLTRANSFERASE 2; NICOTINAMIDE ADENINE DINUCLEOTIDE ADENOSINE DIPHOSPHATE RIBOSYLTRANSFERASE INHIBITOR; OLAPARIB; VELIPARIB; CELL CYCLE PROTEIN; NICOTINAMIDE ADENINE DINUCLEOTIDE ADENOSINE DIPHOSPHATE RIBOSYLTRANSFERASE; PARP1 PROTEIN, HUMAN; PARP2 PROTEIN, HUMAN; PARP3 PROTEIN, HUMAN; RECOMBINANT PROTEIN; TANKYRASE; TNKS PROTEIN, HUMAN;

ARTICLE; BINDING AFFINITY; BINDING ASSAY; BINDING SITE; CLONING; CONTROLLED STUDY; CROSS REACTION; DNA BINDING; DNA DAMAGE; DNA REPAIR; DRUG BINDING; DRUG SELECTIVITY; ENZYME ACTIVE SITE; EQUILIBRIUM CONSTANT; FLUORESCENCE POLARIZATION; HIGH THROUGHPUT SCREENING; LIGAND BINDING; PHARMACOPHORE; POLARIZATION; PRIORITY JOURNAL; PROTEIN PURIFICATION; SURFACE PLASMON RESONANCE; TITRIMETRY; ANTAGONISTS AND INHIBITORS; GENETICS; HUMAN; METABOLISM; PROCEDURES; REPRODUCIBILITY;

CELL CYCLE PROTEINS; FLUORESCENCE POLARIZATION; HIGH-THROUGHPUT SCREENING ASSAYS; HUMANS; POLY (ADP-RIBOSE) POLYMERASE-1; POLY(ADP-RIBOSE) POLYMERASE INHIBITORS; POLY(ADP-RIBOSE) POLYMERASES; RECOMBINANT PROTEINS; REPRODUCIBILITY OF RESULTS; SURFACE PLASMON RESONANCE; TANKYRASES;

EID: 84905594808     PISSN: 10870571     EISSN: 1552454X     Source Type: Journal    
DOI: 10.1177/1087057114538319     Document Type: Article

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