The ring fragmentation product of thymidine C5-hydrate when present in DNA is repaired by the Escherichia coli Fpg and Nth proteins

Biochemistry

Volumn 37, Issue 21, 1998, Pages 7757-7763

  Jurado, Juan ^a   Saparbaev, Murat ^a   Matray, Tracy J ^b   Greenberg, Marc M ^b   Laval, Jacques ^a  

^a INSTITUT GUSTAVE ROUSSY   (France)

^b Department of Environmental and Radiological Health Sciences   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

ENDONUCLEASE;

ARTICLE; DNA DAMAGE; DNA REPAIR; ENZYME ACTIVITY; ESCHERICHIA COLI; NONHUMAN; OXIDATIVE STRESS; PRIORITY JOURNAL; RADIOLYSIS; ULTRAVIOLET RADIATION;

BACTERIAL PROTEINS; BASE COMPOSITION; CARCINOMA, HEPATOCELLULAR; CELL EXTRACTS; DEOXYRIBONUCLEASE (PYRIMIDINE DIMER); DNA; DNA DAMAGE; DNA FRAGMENTATION; DNA REPAIR; DNA-FORMAMIDOPYRIMIDINE GLYCOSYLASE; ENDODEOXYRIBONUCLEASES; ESCHERICHIA COLI; ESCHERICHIA COLI PROTEINS; HUMANS; KINETICS; MUTAGENS; N-GLYCOSYL HYDROLASES; OLIGODEOXYRIBONUCLEOTIDES; STRUCTURE-ACTIVITY RELATIONSHIP; THYMIDINE; TUMOR CELLS, CULTURED; UREA;

ESCHERICHIA COLI; NEGIBACTERIA;

EID: 0032568654     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi972982z     Document Type: Article

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