Characterization of the full length uracil-DNA glycosylase in the extreme thermophile Thermotoga maritima

Mutation Research - DNA Repair

Volumn 485, Issue 3, 2001, Pages 187-195

  Sandigursky, M ^a   Faje, A ^a   Franklin, W A ^a  

^a ALBERT EINSTEIN COLLEGE OF MEDICINE   (United States)

Author keywords

Base excision repair; DNA glycosylase; Thermophile; Uracil

Indexed keywords

AMINO ACID; CIRCULAR DNA; URACIL DNA GLYCOSYLTRANSFERASE;

ARTICLE; ENZYME ACTIVITY; ENZYME PURIFICATION; ESCHERICHIA COLI; EXCISION REPAIR; GENE SEQUENCE; MOLECULAR CLONING; NONHUMAN; PRIORITY JOURNAL; PROTEIN CONTENT; PROTEIN EXPRESSION; PROTEIN FOLDING; TEMPERATURE DEPENDENCE; THERMOTOGA MARITIMA;

AMINO ACID SEQUENCE; ARTIFACTS; CIRCULAR DICHROISM; CLONING, MOLECULAR; DNA GLYCOSYLASES; DNA REPAIR; ENZYME STABILITY; ESCHERICHIA COLI; HEAT; MOLECULAR SEQUENCE DATA; N-GLYCOSYL HYDROLASES; PEPTIDE FRAGMENTS; PROTEIN DENATURATION; RECOMBINANT PROTEINS; SEQUENCE HOMOLOGY, AMINO ACID; THERMOTOGA MARITIMA; URACIL-DNA GLYCOSIDASE;

ESCHERICHIA COLI; THERMOTOGA MARITIMA;

EID: 0035804794     PISSN: 09218777     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0921-8777(00)00083-5     Document Type: Article

References (19)

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19. Using CLUSTAL for multiple sequence alignments