ATP-induced helicase slippage reveals highly coordinated subunits

Nature

Volumn 478, Issue 7367, 2011, Pages 132-135

  Sun, Bo ^a,b   Johnson, Daniel S ^a,b,d   Patel, Gayatri ^c   Smith, Benjamin Y ^a,b   Pandey, Manjula ^c   Patel, Smita S ^c   Wang, Michelle D ^a,b  

^a Cornell University   (United States)

^b Department of Obstetrics Gynecology   (United States)

^c RUTGERS ROBERT WOOD JOHNSON MEDICAL SCHOOL   (United States)

^d ROCKEFELLER UNIVERSITY   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

ADENOSINE TRIPHOSPHATE; DOUBLE STRANDED DNA; HELICASE; THYMIDINE TRIPHOSPHATE;

BACTERIOPHAGE; CONCENTRATION (COMPOSITION); ENZYME ACTIVITY; GENE EXPRESSION; GENETIC ANALYSIS; HYDROLYSIS; MOLECULAR ANALYSIS; NUCLEIC ACID; OBSERVATIONAL METHOD; RECOMBINATION; TRANSLOCATION;

ARTICLE; BACTERIOPHAGE T7; DNA BINDING; DNA DENATURATION; DNA REPLICATION; ENZYME BINDING; ENZYME KINETICS; HYDROLYSIS; MICHAELIS CONSTANT; MOLECULAR DYNAMICS; PRIORITY JOURNAL; PROTEIN DNA INTERACTION;

ADENOSINE TRIPHOSPHATE; BACTERIOPHAGE T7; BASE PAIRING; BINDING, COMPETITIVE; BIOCATALYSIS; DNA; DNA HELICASES; DNA PRIMASE; DNA REPLICATION; DNA, SINGLE-STRANDED; HYDROLYSIS; KINETICS; MODELS, BIOLOGICAL; NUCLEIC ACID DENATURATION; PROTEIN SUBUNITS; THERMODYNAMICS; THYMINE NUCLEOTIDES;

EID: 80053897431     PISSN: 00280836     EISSN: 14764687     Source Type: Journal    
DOI: 10.1038/nature10409     Document Type: Article

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