A base-excision DNA-repair protein finds intrahelical lesion bases by fast sliding in contact with DNA

Proceedings of the National Academy of Sciences of the United States of America

Volumn 103, Issue 15, 2006, Pages 5752-5757

  Blainey, Paul C ^a   Van Oijen, Antoine M ^a,c   Banerjee, Anirban ^a   Verdine, Gregory L ^a,b   Xie, X Sunney ^a  

^a HARVARD UNIVERSITY   (United States)

^b HARVARD UNIVERSITY   (United States)

^c HARVARD MEDICAL SCHOOL   (United States)

Author keywords

DNA glycosylase mechanism; Hopping; Nonspecific binding; Shear flow stretching; Single molecule imaging

Indexed keywords

8 HYDROXYGUANINE; DNA; DNA BINDING PROTEIN; DNA GLYCOSYLTRANSFERASE; SODIUM CHLORIDE;

ARTICLE; CONCENTRATION RESPONSE; CRYSTAL STRUCTURE; DIFFUSION COEFFICIENT; EXCISION REPAIR; FLUORESCENCE; IMAGING; MUTATION; OXIDATIVE STRESS; PH; PRIORITY JOURNAL; PROTEIN DNA INTERACTION; SHEAR FLOW;

AMINO ACID SUBSTITUTION; BACTERIOPHAGE LAMBDA; BINDING SITES; DNA DAMAGE; DNA GLYCOSYLASES; DNA REPAIR; DNA, VIRAL; GUANINE; HUMANS; KINETICS; MICROSCOPY, FLUORESCENCE; MODELS, MOLECULAR; MUTAGENESIS, SITE-DIRECTED; NUCLEIC ACID CONFORMATION; PROTEIN CONFORMATION; RECOMBINANT PROTEINS; SUBSTRATE SPECIFICITY;

EID: 33645807371     PISSN: 00278424     EISSN: None     Source Type: Journal    
DOI: 10.1073/pnas.0509723103     Document Type: Article

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