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Journal article

Toremifene interacts with and destabilizes the Ebola virus glycoprotein.

Abstract:

Ebola viruses (EBOVs) are responsible for repeated outbreaks of fatal infections, including the recent deadly epidemic in West Africa. There are currently no approved therapeutic drugs or vaccines for the disease. EBOV has a membrane envelope decorated by trimers of a glycoprotein (GP, cleaved by furin to form GP1 and GP2 subunits) which is solely responsible for host cell attachment, endosomal entry and membrane fusion. GP is thus a primary target for the development of antiviral drugs. Here...

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Publication status:
Published
Peer review status:
Peer reviewed

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Publisher copy:
10.1038/nature18615

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Institution:
University of Oxford
Division:
MSD
Department:
NDM
Sub department:
Structural Biology
Role:
Author
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Institution:
University of Oxford
Division:
MSD
Department:
NDM
Sub department:
Human Genetics Wt Centre
Role:
Author
More by this author
Institution:
University of Oxford
Division:
MSD
Department:
NDM
Sub department:
Structural Biology
Role:
Author
More by this author
Institution:
University of Oxford
Division:
MSD
Department:
NDM
Sub department:
Human Genetics Wt Centre
Role:
Author
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Funding agency for:
Zhao, Y
Grant:
283570
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Funding agency for:
Ren, J
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Funding agency for:
Ren, J
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Funding agency for:
Bowden, T
Grant:
MR/L009528/1
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Funding agency for:
Harlos, K
Grant:
MR/N00065X/1
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Publisher:
Nature Publishing Group Publisher's website
Journal:
Nature Journal website
Volume:
535
Pages:
169-172
Publication date:
2016-06-01
Acceptance date:
2016-05-26
DOI:
EISSN:
1476-4687
ISSN:
0028-0836
Source identifiers:
631690
Language:
English
Pubs id:
pubs:631690
UUID:
uuid:bf711b30-68b8-49b9-a6a8-7236cf6de661
Local pid:
pubs:631690
Deposit date:
2016-07-07

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