Title : Arsenite interacts selectively with zinc finger proteins containing C3H1 or C4 motifs.

Pub. Date : 2011 Jul 1

PMID : 21550982






3 Functional Relationships(s)
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1 MALDI-TOF-MS analysis of peptides harboring site-directed substitutions of cysteine with histidine residues within the PARP-1 zinc finger revealed that arsenite bound to peptides containing three or four cysteine residues, but not to peptides with two cysteines, demonstrating arsenite binding selectivity. Cysteine poly(ADP-ribose) polymerase 1 Homo sapiens
2 MALDI-TOF-MS analysis of peptides harboring site-directed substitutions of cysteine with histidine residues within the PARP-1 zinc finger revealed that arsenite bound to peptides containing three or four cysteine residues, but not to peptides with two cysteines, demonstrating arsenite binding selectivity. Cysteine poly(ADP-ribose) polymerase 1 Homo sapiens
3 These findings demonstrate that PARP-1 is a direct molecular target of arsenite and that arsenite interacts selectively with zinc finger motifs containing three or more cysteine residues. Cysteine poly(ADP-ribose) polymerase 1 Homo sapiens