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Structure, Function, and Evolution of the Crimean-Congo Hemorrhagic Fever Virus Nucleocapsid Protein
DOI:
10.1128/JVI.01555-12
PMID:
22875964
Authors:
Stephen
Carter
(University of Leeds)
,
Rebecca
Surtees
(University of Leeds)
,
Cheryl T
Walter
(University of Leeds, U.K.)
,
Antonio
Ariza
(University of Leeds)
,
Eric
Bergeron
(Centers for Disease Control and Prevention, Atlanta, USA)
,
Stuart T
Nichol
(Centers for Disease Control and Prevention, Atlanta, USA)
,
Julian A
Hiscox
(University of Leeds, U.K.)
,
Thomas A
Edwards
(University of Leeds, U.K.)
,
John N
Barr
(University of Leeds, U.K.)
Co-authored by industrial partner:
No
Type:
Journal Paper
Journal:
Journal Of Virology
, VOL 86 (20)
, PAGES 10914-10923
State:
Published (Approved)
Published:
October 2012
Diamond Proposal Number(s):
6386
Abstract: Crimean-Congo hemorrhagic fever virus (CCHFV) is an emerging tick-borne virus of the Bunyaviridae family responsible for fatal human disease for which preventative or therapeutic measures do not exist. We solved the crystal structure of the Baghdad-12 strain CCHFV nucleocapsid protein (N), a potential therapeutic target, at a resolution of 2.1 angstroms.
Journal Keywords: Caspase; Crystallography ; X-Ray ; Evolution ; Molecular ; Hemorrhagic; Crimean-Congo ; Hemorrhagic; Crimean ; Nucleocapsid ; Nucleocapsid; Phylogeny ; Protein; Tertiary ; RNA ; Viral ; RNA-Binding; Sequence Alignment
Subject Areas:
Biology and Bio-materials
Instruments:
I02-Macromolecular Crystallography
,
I03-Macromolecular Crystallography
,
I04-1-Macromolecular Crystallography (fixed wavelength)
,
I04-Macromolecular Crystallography
,
I24-Microfocus Macromolecular Crystallography
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