Adenine removal activity and bacterial complementation with the human MutY homologue (MUTYH) and Y165C, G382D, P391L and Q324R variants associated with colorectal cancer

DNA Repair

Volumn 8, Issue 12, 2009, Pages 1400-1410

  Kundu, Sucharita ^a   Brinkmeyer, Megan K ^a   Livingston, Alison L ^a   David, Sheila S ^a  

^a UNIVERSITY OF CALIFORNIA   (United States)

Author keywords

8 Oxoguanine; Adenine glycosylase; MAP; MUTYH; Oxidative stress; P391L MUTYH; Q324R MUTYH

Indexed keywords

8 HYDROXYGUANINE; ADENINE; ADENINE GLYCOSYLASE; DNA GLYCOSYLASE MUTY; DNA GLYCOSYLTRANSFERASE; PLASMID DNA; UNCLASSIFIED DRUG;

ARTICLE; COLON POLYPOSIS; COLORECTAL CANCER; DNA REPLICATION; ENZYME ACTIVE SITE; ENZYME ACTIVITY; ENZYME ASSAY; ESCHERICHIA COLI; EXCISION REPAIR; GENE MUTATION; GENE OVEREXPRESSION; NUCLEOTIDE SEQUENCE; OXIDATIVE STRESS; POLYMERASE CHAIN REACTION; PRIORITY JOURNAL; SITE DIRECTED MUTAGENESIS;

ADENINE; CATALYTIC DOMAIN; COLONIC NEOPLASMS; CRYSTALLOGRAPHY, X-RAY; DNA GLYCOSYLASES; ENZYME STABILITY; ESCHERICHIA COLI; HUMANS; MODELS, MOLECULAR; MUTATION; PROTEIN STRUCTURE, TERTIARY; SUBSTRATE SPECIFICITY;

BACTERIA (MICROORGANISMS); ESCHERICHIA COLI;

EID: 70450224248     PISSN: 15687864     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.dnarep.2009.09.009     Document Type: Article

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