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Methods Mol Biol. 2011;780:83-91.

Noncovalent pADPr interaction with proteins and competition with RNA for binding to proteins.

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Epigenetics and Progenitor Cell Program, Fox Chase Cancer Center, Philadelphia, PA, USA.

Abstract

PARP1 can modify a variety of proteins through conserved domains in noncovalent manner. Since poly(ADP-ribose) is highly negatively charged and has a strong binding affinity for its target proteins, noncovalent binding by poly(ADP-ribose) modulates the protein activity during developmental processes. In this section, the methods including co-immunoprecipitation and dot-blot assay were illustrated for determining the specific interaction between poly(ADP-ribose) and proteins. Furthermore, the protocol for RNA EMSA was described to determine whether pADPr binding to hnRNPs can inhibit RNA-binding ability of human hnRNP A1.

PMID:: 21870256; [PubMed - indexed for MEDLINE]
PMCID:: PMC3164781

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Related citations in PubMed

Affinity-based assays for the identification and quantitative evaluation of noncovalent poly(ADP-ribose)-binding proteins. [Methods Mol Biol. 2011]
Affinity-based assays for the identification and quantitative evaluation of noncovalent poly(ADP-ribose)-binding proteins.
Gagné JP, Haince JF, Pic E, Poirier GG. Methods Mol Biol. 2011; 780:93-115.
Methods for purification of proteins associated with cellular poly(ADP-ribose) and PARP-specific poly(ADP-ribose). [Methods Mol Biol. 2011]
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Poly(ADP-ribosyl)ation of heterogeneous nuclear ribonucleoproteins modulates splicing. [Nucleic Acids Res. 2009]
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Review Importance of poly(ADP-ribose) glycohydrolase in the control of poly(ADP-ribose) metabolism. [Exp Cell Res. 2001]
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