Modification of the human thymine-DNA glycosylase by ubiquitin-like proteins facilitates enzymatic turnover

EMBO Journal

Volumn 21, Issue 6, 2002, Pages 1456-1464

  Hardeland, Ulrike ^a   Steinacher, Roland ^a   Jiricny, Josef ^a   Schär, Primo ^b  

^a DIVISION OF REPRODUCTIVE BIOLOGY   (United States)

^b UNIVERSITY OF ZURICH   (Switzerland)

Author keywords

DNA repair; SUMO conjugation; Thymine DNA glycosylase

Indexed keywords

DNA GLYCOSYLTRANSFERASE; PROTEIN DERIVATIVE; SUMO 1 PROTEIN; THYMINE; UBIQUITIN;

ARTICLE; BINDING AFFINITY; CONJUGATION; CONTROLLED STUDY; ENZYME ACTIVITY; ENZYME BINDING; ENZYME MECHANISM; ENZYME METABOLISM; ENZYME MODIFICATION; ENZYME PURIFICATION; ENZYME SUBSTRATE; HUMAN; HUMAN CELL; PRIORITY JOURNAL; PROTEIN INTERACTION;

BINDING SITES; DEOXYRIBONUCLEASE (PYRIMIDINE DIMER); DNA REPAIR; ENDODEOXYRIBONUCLEASES; HELA CELLS; HUMANS; LYSINE; RECOMBINANT FUSION PROTEINS; SMALL UBIQUITIN-RELATED MODIFIER PROTEINS; SUMO-1 PROTEIN; UBIQUITINS;

ZIZIPHUS MAURITIANA;

EID: 0037086643     PISSN: 02614189     EISSN: None     Source Type: Journal    
DOI: 10.1093/emboj/21.6.1456     Document Type: Article

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