The DNA-Binding Domain of Human PARP-1 Interacts with DNA Single-Strand Breaks as a Monomer through Its Second Zinc Finger-Reference-Cited by-同舟云学术

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The DNA-Binding Domain of Human PARP-1 Interacts with DNA Single-Strand Breaks as a Monomer through Its Second Zinc Finger

Published:2011-03 Issue:1 Volume:407 Page:149-170
ISSN:0022-2836
Container-title:Journal of Molecular Biology
language:en
Short-container-title:Journal of Molecular Biology

Author:

Eustermann Sebastian,Videler Hortense,Yang Ji-Chun,Cole Paul T.,Gruszka Dominika,Veprintsev Dmitry,Neuhaus David

Funder

Association of International Cancer Research

Publisher

Elsevier BV

Subject

Molecular Biology,Structural Biology

Reference69 articles.

1. Poly(ADP-ribosyl)ation reactions in the regulation of nuclear functions;D'Amours;Biochem. J.,1999

2. The PARP superfamily;Ame;Bioessays,2004

3. Poly(ADP-ribose) synthase is the major endogenous nonhistone acceptor for poly(ADP-ribose) in alkylated rat hepatoma cells;Adamietz;Eur. J. Biochem.,1987

4. Poly(ADP-ribosyl)ation of polynucleosomes causes relaxation of chromatin structure;Poirier;Proc. Natl Acad. Sci. USA,1982

5. ADP-ribosylation of chromosomal proteins and mouse mammary tumor virus gene expression. Glucocorticoids rapidly decrease endogenous ADP-ribosylation of nonhistone high mobility group 14 and 17 proteins;Tanuma;J. Biol. Chem.,1983

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