Title : Role of zinc-finger motif in redox regulation of human replication protein A.

Pub. Date : 2001 Aug

PMID : 11554452






3 Functional Relationships(s)
Download
Sentence
Compound Name
Protein Name
Organism
1 The inhibitory effect of o-phenanthroline on RPA-ssDNA interaction was reversed by Zn(II), but not by other divalent cations, suggesting that Zn(II) is the unique metal coordinating the zinc-finger cysteines in redox regulation of RPA-ssDNA interaction. Zinc replication protein A1 Homo sapiens
2 The inhibitory effect of o-phenanthroline on RPA-ssDNA interaction was reversed by Zn(II), but not by other divalent cations, suggesting that Zn(II) is the unique metal coordinating the zinc-finger cysteines in redox regulation of RPA-ssDNA interaction. Zinc replication protein A1 Homo sapiens
3 The inhibitory effect of o-phenanthroline on RPA-ssDNA interaction was reversed by Zn(II), but not by other divalent cations, suggesting that Zn(II) is the unique metal coordinating the zinc-finger cysteines in redox regulation of RPA-ssDNA interaction. Zinc replication protein A1 Homo sapiens