Toremifene interacts with and destabilizes the Ebola virus glycoprotein

Yuguang Zhao, Jingshan Ren, Karl Harlos, Daniel M. Jones, Antra Zeltina, Thomas A. Bowden, Sergi Padilla-Parra, Elizabeth E. Fry and David I. Stuart ()
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Yuguang Zhao: University of Oxford, Wellcome Trust Centre for Human Genetics
Jingshan Ren: University of Oxford, Wellcome Trust Centre for Human Genetics
Karl Harlos: University of Oxford, Wellcome Trust Centre for Human Genetics
Daniel M. Jones: University of Oxford, Wellcome Trust Centre for Human Genetics
Antra Zeltina: University of Oxford, Wellcome Trust Centre for Human Genetics
Thomas A. Bowden: University of Oxford, Wellcome Trust Centre for Human Genetics
Sergi Padilla-Parra: University of Oxford, Wellcome Trust Centre for Human Genetics
Elizabeth E. Fry: University of Oxford, Wellcome Trust Centre for Human Genetics
David I. Stuart: University of Oxford, Wellcome Trust Centre for Human Genetics

Nature, 2016, vol. 535, issue 7610, 169-172

Abstract: High-resolution structures of the unliganded Ebola virus glycoprotein (GP) and of GP bound to the drugs toremifene and ibuprofen are presented, providing insights into how the drugs inhibit viral fusion with the endosomal membrane.

Date: 2016
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DOI: 10.1038/nature18615

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