Visualization of poly(ADP-ribose) bound to PARG reveals inherent balance between exo- and endo-glycohydrolase activities

Nature Communications

Volumn 4, Issue , 2013, Pages

  Barkauskaite, Eva ^a   Brassington, Amy ^b   Tan, Edwin S ^c   Warwicker, Jim ^b   Dunstan, Mark S ^b   Banos, Benito ^a   Lafite, Pierre ^d   Ahel, Marijan ^e   Mitchison, Timothy J ^c   Ahel, Ivan ^a,f   Leys, David ^b  

^a UNIVERSITY OF MANCHESTER   (United Kingdom)

^b UNIVERSITY OF MANCHESTER   (United Kingdom)

^c HARVARD MEDICAL SCHOOL   (United States)

^d UNIVERSITÉ D'ORLÉANS   (France)

^e RUDER BO KOVI INSTITUTE   (Croatia)

^f UNIVERSITY OF OXFORD   (United Kingdom)

Author keywords

[No Author keywords available]

Indexed keywords

GLYCOSIDASE; POLY(ADENOSINE DIPHOSPHATE RIBOSE);

ENZYME ACTIVITY; GENOME; POLYMER; SUBSTRATE; VISUALIZATION;

ADENOSINE DIPHOSPHATE RIBOSYLATION; ARTICLE; BINDING AFFINITY; CATALYSIS; CONTROLLED STUDY; CRYSTAL STRUCTURE; ENZYME ACTIVITY; HUMAN; MOLECULAR MODEL;

EID: 84882412641     PISSN: None     EISSN: 20411723     Source Type: Journal    
DOI: 10.1038/ncomms3164     Document Type: Article

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