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Richard M. Epand
Researcher at McMaster University
Publications - 521
Citations - 26937
Richard M. Epand is an academic researcher from McMaster University. The author has contributed to research in topics: Membrane & Peptide. The author has an hindex of 80, co-authored 515 publications receiving 25125 citations. Previous affiliations of Richard M. Epand include Brigham Young University & University of Edinburgh.
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Journal ArticleDOI
The Final Conformation of the Complete Ectodomain of the HA2 Subunit of Influenza Hemagglutinin Can by Itself Drive Low pH-dependent Fusion
TL;DR: Structural properties as well as the fusogenic activity of the full sized trimeric HA2(1–185) (here called HA2*) that presents the final conformation of the HA2 ectodomain are explored to substantiate the hypothesis that the final form of HA2 is more important for fusion than the conformational change that generates this form.
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The sticholysin family of pore-forming toxins induces the mixing of lipids in membrane domains.
Uris Ros,Michelle A. Edwards,Raquel F. Epand,María E. Lanio,Shirley Schreier,Christopher M. Yip,Carlos Alvarez,Richard M. Epand +7 more
TL;DR: It is hypothesized that expanding lipid disordered phases into lipid ordered phases decreases the lipid packing at the borders of the lipid raft, turning it into a more suitable environment for N-terminal insertion and pore formation.
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Role of Lipids in the Permeabilization of Membranes by Class L Amphipathic Helical Peptides
I. V. Polozov,A. I. Polozova,Ewan M. Tytler,Gattadahalli M. Anantharamaiah,Jere P. Segrest,G. A. Woolley,Richard M. Epand +6 more
TL;DR: The mechanism of membrane permeabilization by the 18L model peptide, which features the consensus class L sequence averaged from the number of naturally occurring lytic peptides, suggests the importance of nonbilayer phase propensity for certain functions of biological membranes.
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On the interaction between gp41 and membranes: the immunodominant loop stabilizes gp41 helical hairpin conformation.
TL;DR: The results suggest that the presence of the loop stabilizes the trimeric helical hairpin both when e-gp41 is in aqueous solution and when it is bound to the membrane surface.
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Cyclosporine A inhibits herpes simplex virus-induced cell fusion but not virus penetration into cells
TL;DR: HSV-1-induced cell fusion and penetration of virus into cells either proceed by mutually exclusive mechanisms or are differentially sensitive to cyclosporine.