Spring-loaded mechanism of DNA unwinding by hepatitis C virus NS3 helicase

Science

Volumn 317, Issue 5837, 2007, Pages 513-516

  Myong, Sua ^a,b   Bruno, Michael M ^c,d   Pyle, Anna M ^c,d   Ha, Taekjip ^a,b,d  

^a University of Illinois at Urbana Champaign   (United States)

^b UNIVERSITY OF ILLINOIS AT URBANA CHAMPAIGN   (United States)

^c YALE UNIVERSITY   (United States)

^d HOWARD HUGHES MEDICAL INSTITUTE   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

ADENOSINE TRIPHOSPHATE; DNA BASE; NONSTRUCTURAL PROTEIN 3; NUCLEOTIDE; VIRUS DNA;

DNA; GENOME; HEPATITIS; VIRUS;

ARTICLE; BASE PAIRING; DNA DENATURATION; DNA PROTEIN COMPLEX; ENZYME ACTIVITY; FLUORESCENCE; HEPATITIS C VIRUS; NONHUMAN; PRIORITY JOURNAL; PROTEIN FUNCTION; PROTEIN SECONDARY STRUCTURE; TENSION; VIRUS GENOME; VIRUS REPLICATION;

ADENOSINE TRIPHOSPHATE; BASE PAIRING; DNA; DNA HELICASES; FLUORESCENCE RESONANCE ENERGY TRANSFER; HEPACIVIRUS; MODELS, BIOLOGICAL; MODELS, MOLECULAR; NUCLEIC ACID CONFORMATION; TEMPERATURE; VIRAL NONSTRUCTURAL PROTEINS;

HEPATITIS C VIRUS;

EID: 34547595373     PISSN: 00368075     EISSN: 10959203     Source Type: Journal    
DOI: 10.1126/science.1144130     Document Type: Article

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26. We thank C. Joo for help in manuscript preparation. Supported by NIH grants R01-GM060620 and R01-GM065367. T.H. and A.M.P. are investigators with the Howard Hughes Medical Institute.