Base-excision repair activity of uracil-DNA glycosylase monitored using the latch zone of α-hemolysin

Journal of the American Chemical Society

Volumn 135, Issue 51, 2013, Pages 19347-19353

  Jin, Qian ^a   Fleming, Aaron M ^a   Johnson, Robert P ^a   Ding, Yun ^a   Burrows, Cynthia J ^a   White, Henry S ^a  

^a UNIVERSITY OF UTAH   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

ACTIVITY-BASED; DEOXYURIDINE; DNA NUCLEOTIDES; DNA-REPAIR ENZYMES; HIGH RESOLUTION; N-GLYCOSIDIC BONDS; REACTION SUBSTRATES; URACIL-DNA GLYCOSYLASE;

AROMATIC COMPOUNDS; BLOOD; NANOPORES; NUCLEOTIDES; TOOLS;

DNA;

ALPHA HEMOLYSIN; BOVINE SERUM ALBUMIN; DEOXYURIDINE; DNA BASE; DOUBLE STRANDED DNA; ION CHANNEL; POLYDEOXYRIBONUCLEOTIDE SYNTHASE; POTASSIUM CHLORIDE; SINGLE STRANDED DNA; URACIL DNA GLYCOSIDASE;

ARTICLE; DNA DETERMINATION; DNA STRUCTURE; ENZYME ACTIVITY; ENZYME SUBSTRATE; EXCISION REPAIR; GEL ELECTROPHORESIS; HIGH PERFORMANCE LIQUID CHROMATOGRAPHY; HYDROLYSIS; MOLECULAR RECOGNITION; NANOPORE; REACTION TIME; STATIC ELECTRICITY;

BASE SEQUENCE; DNA REPAIR; HEMOLYSIN PROTEINS; POROSITY; URACIL-DNA GLYCOSIDASE;

EID: 84891317517     PISSN: 00027863     EISSN: 15205126     Source Type: Journal    
DOI: 10.1021/ja410615d     Document Type: Article

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