Strikingly different properties of uracil-DNA glycosylases UNG2 and SMUG1 may explain divergent roles in processing of genomic uracil

DNA Repair

Volumn 11, Issue 6, 2012, Pages 587-593

  Doseth, Berit ^a   Ekre, Cecilie ^a   Slupphaug, Geir ^a   Krokan, Hans E ^a   Kavli, Bodil ^a  

^a NORWEGIAN UNIVERSITY OF SCIENCE AND TECHNOLOGY   (Norway)

Author keywords

Activation induced cytidine deaminase; Cytosine deamination; Hot spot sequence; Substrate specificity; Uracil DNA glycosylase

Indexed keywords

CYTOSINE DEAMINASE; DNA (APURINIC OR APYRIMIDINIC SITE) LYASE; DOUBLE STRANDED DNA; MAGNESIUM ION; POTASSIUM CHLORIDE; REPLICATION FACTOR A; SINGLE STRAND SELECTIVE MONOFUNCTIONAL URACIL DNA GLYCOSYLASE 1; SODIUM CHLORIDE; UNCLASSIFIED DRUG; URACIL; URACIL DNA GLYCOSIDASE; URACIL DNA GLYCOSIDASE UNG2;

ANTIBODY SPECIFICITY; ARTICLE; B LYMPHOCYTE; CATALYSIS; DEAMINATION; DNA CONFORMATION; EXCISION REPAIR; GENE LOCUS; GENOME; HUMAN; IONIC STRENGTH; MOUSE; NONHUMAN; PRIORITY JOURNAL; SOMATIC HYPERMUTATION;

ANIMALS; BASE SEQUENCE; BIOCATALYSIS; CELL LINE, TUMOR; CYTIDINE DEAMINASE; DNA; DNA GLYCOSYLASES; DNA REPAIR; DNA, SINGLE-STRANDED; DNA-(APURINIC OR APYRIMIDINIC SITE) LYASE; GENOME; HUMANS; MAGNESIUM; MICE; RECOMBINANT PROTEINS; SUBSTRATE SPECIFICITY; URACIL; URACIL-DNA GLYCOSIDASE;

EID: 84861479923     PISSN: 15687864     EISSN: 15687856     Source Type: Journal    
DOI: 10.1016/j.dnarep.2012.03.003     Document Type: Article

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