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Cited by 182

The DOI matches its Crossref record; 1 of the 1 references it cites were found in a registry or an index.

A Shuttle Mechanism for DNA‐Protein Interactions: The Regulation of Poly(ADP‐ribose) Polymerase

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ZAHRADKA, Peter, EBISUZAKI, Kaney·1982·European Journal of Biochemistry

Abstract

Previously it had been shown that poly(ADP‐ribose) polymerase requires DNA for its activity and that this enzyme is auto‐poly(ADP‐ribosyl)ated. The studies reported here indicate that this self‐modification inhibits the enzyme and decreases its affinity for DNA, as shown by sucrose gradient density centrifugation. The coupling of poly(ADP‐ribose) polymerase with poly(ADP‐ribose) glycohydrolase reactivates the polymerase by degrading poly(ADP‐ribose) and restoring the polymerase‐DNA complex. The assay of polymerase in the presence of glycohydrolase was made possible by use of a double‐label assay involving release of 14 C‐labelled nicotinamide and the incorporation of 3 H‐labelled ADP‐ribose from NAD+. These results provide the basis for a shuttle mechanism in which the polymerase can be moved on and off DNA by the action of these two enzymes. Mg 2+ and histone HI appear to activate the polymerase by increasing the affinity of the polymerase for DNA.

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Crossref · 10.1111/j.1432-1033.1982.tb06912.x

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Metadata

Authors
ZAHRADKA, P., & EBISUZAKI, K.
Venue
European Journal of Biochemistry
Publisher
Wiley
Published
1982-10
Volume
127
Issue
3
Pages
579-585
ISSN
  • 0014-2956 (ISSN-L)
  • 1432-1033
OpenAlex
W1565928793
Cited by
182
References
1
FWCI
2.62
Type
journal article
Language
en
Open access
bronze

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CoChat. (2026). Citation check: A Shuttle Mechanism for DNA‐Protein Interactions: The Regulation of Poly(ADP‐ribose) Polymerase. https://app.cochat.ai/papers/10.1111/j.1432-1033.1982.tb06912.x
The paper
ZAHRADKA, P., & EBISUZAKI, K. (1982). A Shuttle Mechanism for DNA‐Protein Interactions: The Regulation of Poly(ADP‐ribose) Polymerase. European Journal of Biochemistry. https://doi.org/10.1111/j.1432-1033.1982.tb06912.x

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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).

Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.