Article ID Journal Published Year Pages File Type
10822559 Current Opinion in Structural Biology 2013 10 Pages PDF
Abstract
► PARP-1 zinc finger domains recognize exposed nucleotide bases as a DNA damage signal. ► The modular domain architecture of PARP-1 collapses onto DNA damage as a monomer. ► Interdomain communication is critical to PARP-1 activation in response to DNA damage. ► A destabilized PARP-1 catalytic domain has increased poly(ADP-ribosyl)ation activity.
Related Topics
Life Sciences Biochemistry, Genetics and Molecular Biology Biochemistry
Preview
PARP-1 mechanism for coupling DNA damage detection to poly(ADP-ribose) synthesis
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