Kinetic mechanism of DNA unwinding by the BLM helicase core and molecular basis for its low processivity

Biochemistry

Volumn 49, Issue 4, 2010, Pages 656-668

  Yang, Ye ^a   Dou, Shuo Xing ^a   Xu, Ya Nan ^a,b   Bazeille, Nicolas ^c   Wang, Peng Ye ^a   Rigolet, Pascal ^c   Xu, Hou Qiang ^c   Xi, Xu Guang ^c  

^a INSTITUTE OF PHYSICS   (China)

^b RENMIN UNIVERSITY OF CHINA   (China)

^c CNRS   (France)

Author keywords

[No Author keywords available]

Indexed keywords

ATP HYDROLYSIS; DNA SUBSTRATES; DNA UNWINDING; DUPLEX DNA; EFFECTIVE THERAPY; GENERAL POPULATION; HELICASES; KINETIC MECHANISM; MOLECULAR BASIS; PROCESSIVITY; RECESSIVE DISORDER; STEP SIZE; STOPPED FLOW;

DNA; OLIGOMERIZATION; PROTEINS;

GENES;

ADENOSINE TRIPHOSPHATE; BLOOM SYNDROME HELICASE; DNA; DOUBLE STRANDED DNA;

AMINO ACID SEQUENCE; ARTICLE; CONTROLLED STUDY; DNA BINDING; ENZYME INHIBITION; ENZYME MECHANISM; HYDROLYSIS; OLIGOMERIZATION; PRIORITY JOURNAL; PROTEIN STRUCTURE;

ADENOSINE DIPHOSPHATE; ADENOSINE TRIPHOSPHATE; BINDING SITES; BLOOM SYNDROME; DIMERIZATION; DNA; HUMANS; HYDROLYSIS; KINETICS; RECQ HELICASES;

EID: 75149165723     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi901459c     Document Type: Article

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