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The structure and catalytic mechanism of a poly(ADP-ribose) glycohydrolase

The structure and catalytic mechanism of a poly(ADP-ribose) glycohydrolase

https://devfeature-collection.sl.nsw.gov.au/record/TN_cdi_pubmedcentral_primary_oai_pubmedcentral_nih_gov_3184140

The structure and catalytic mechanism of a poly(ADP-ribose) glycohydrolase

About this item

Full title

The structure and catalytic mechanism of a poly(ADP-ribose) glycohydrolase

Publisher

London: Nature Publishing Group UK

Journal title

Nature (London), 2011-09, Vol.477 (7366), p.616-620

Language

English

Formats

Publication information

Publisher

London: Nature Publishing Group UK

More information

Scope and Contents

Contents

Taking PAR apart
Proteins can be reversibly modified through the addition of repeating, polymerized ADP-ribose (PAR) subunits catalysed by poly(ADP-ribose) polymerase (PARP). Removal of PAR requires a glycohydrolase (PARG), which cleaves the ribose–ribose bond between subunits. Ivan Ahel and colleagues report that bacteria and fungi have a diver...

Alternative Titles

Full title

The structure and catalytic mechanism of a poly(ADP-ribose) glycohydrolase

Identifiers

Primary Identifiers

Record Identifier

TN_cdi_pubmedcentral_primary_oai_pubmedcentral_nih_gov_3184140

Permalink

https://devfeature-collection.sl.nsw.gov.au/record/TN_cdi_pubmedcentral_primary_oai_pubmedcentral_nih_gov_3184140

Other Identifiers

ISSN

0028-0836

E-ISSN

1476-4687

DOI

10.1038/nature10404

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