A novel human DNA glycosylase that removes oxidative DNA damage and is homologous to Escherichia coli endonuclease VIII

DNA Repair

Volumn 1, Issue 7, 2002, Pages 517-529

  Bandaru, Viswanath ^a   Sunkara, Sirisha ^a   Wallace, Susan S ^a   Bond, Jeffrey P ^a  

^a UNIVERSITY OF VERMONT COLLEGE OF MEDICINE   (United States)

Author keywords

Base excision repair; DNA glycosylases; Fpg Nei family; Human endonuclease VIII; Nei proteins; Oxidative DNA damage; Phylogeny

Indexed keywords

DEOXYRIBONUCLEASE; DEOXYRIBONUCLEASE (PYRIMIDINE DIMER); DNA FORMAMIDOPYRIMIDINE GLYCOSYLASE; DNA FORMAMIDOPYRIMIDINE GLYCOSYLASE, E COLI; DNA-FORMAMIDOPYRIMIDINE GLYCOSYLASE, E COLI; ESCHERICHIA COLI PROTEIN; GLYCOSIDASE; SODIUM CHLORIDE; DNA GLYCOSYLTRANSFERASE; ENDONUCLEASE; GENE PRODUCT; ISOENZYME; LYASE; PYRIMIDINE DERIVATIVE; SCHIFF BASE;

AMINO ACID SEQUENCE; ANIMAL; ARTICLE; DNA REPAIR; ESCHERICHIA COLI; GENETICS; HUMAN; METABOLISM; MOLECULAR CLONING; MOLECULAR EVOLUTION; MOLECULAR GENETICS; MOUSE; NEOPLASM; PH; SEQUENCE ALIGNMENT; SEQUENCE HOMOLOGY; CATALYSIS; CHROMOSOME 15; DNA DAMAGE; ENZYME ACTIVE SITE; ENZYME ANALYSIS; ENZYME INACTIVATION; ENZYME SUBSTRATE; GENE DELETION; GENE IDENTIFICATION; GENE LOCATION; GENE MAPPING; GENE STRUCTURE; NONHUMAN; NUCLEOTIDE SEQUENCE; OXIDATIVE STRESS; PHYLOGENY; PRIORITY JOURNAL; PROTEIN FAMILY; PROTEIN MOTIF; PROTEIN PURIFICATION;

AMINO ACID SEQUENCE; ANIMALS; CLONING, MOLECULAR; DEOXYRIBONUCLEASE (PYRIMIDINE DIMER); DNA REPAIR; DNA-FORMAMIDOPYRIMIDINE GLYCOSYLASE; ENDODEOXYRIBONUCLEASES; ESCHERICHIA COLI; ESCHERICHIA COLI PROTEINS; EVOLUTION, MOLECULAR; HUMANS; HYDROGEN-ION CONCENTRATION; MICE; MOLECULAR SEQUENCE DATA; N-GLYCOSYL HYDROLASES; NEOPLASMS; SEQUENCE ALIGNMENT; SEQUENCE HOMOLOGY, AMINO ACID; SODIUM CHLORIDE; ANIMAL; HUMAN; SUPPORT, NON-U.S. GOV'T; SUPPORT, U.S. GOV'T, P.H.S.;

BACTERIA (MICROORGANISMS); ESCHERICHIA COLI; EUKARYOTA; PROKARYOTA;

EID: 0037125133     PISSN: 15687864     EISSN: None     Source Type: Journal    
DOI: 10.1016/S1568-7864(02)00036-8     Document Type: Article

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