MHhal binds tightly to substrates containing mismatches at the target base

Nucleic Acids Research

Volumn 23, Issue 8, 1995, Pages 1388-1395

  Klimašauskas, Saulius ^a   Roberts, Richard J ^a,b  

^a Howard Hughes Medical Institute Cold Spring Harbor Laboratory Cold Spring Harbor   (United States)

^b NEW ENGLAND BIOLABS   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

ADENINE; BINDING PROTEIN; CYTOSINE; DNA METHYLTRANSFERASE; GUANINE; METHYL GROUP; S ADENOSYLHOMOCYSTEINE; THYMINE; URACIL;

ARTICLE; BASE MISPAIRING; BINDING AFFINITY; CONTROLLED STUDY; DNA BINDING; DNA HELIX; ENZYME BINDING; PRIORITY JOURNAL; PROTEIN DNA INTERACTION;

BASE SEQUENCE; CYTOSINE; DINUCLEOSIDE PHOSPHATES; DNA; KINETICS; METHYLATION; MOLECULAR SEQUENCE DATA; NUCLEIC ACID HETERODUPLEXES; S-ADENOSYLHOMOCYSTEINE; S-ADENOSYLMETHIONINE; SITE-SPECIFIC DNA METHYLTRANSFERASE (CYTOSINE-SPECIFIC); SUBSTRATE SPECIFICITY; SUPPORT, U.S. GOV'T, P.H.S.; URACIL;

EID: 0028990179     PISSN: 03051048     EISSN: None     Source Type: Journal    
DOI: 10.1093/nar/23.8.1388     Document Type: Article

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