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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.
Papers
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Journal ArticleDOI
Mechanism of liposome destabilization by polycationic amino acids
Richard M. Epand,Wendy Lim +1 more
TL;DR: The promotion of leakage and fusion in anionic liposomes by polycationic amino acids is not a result of large changes in the physical properties or arrangements of the lipids but rather to a surface binding of the polyamino acids.
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Sendai virus N-terminal fusion peptide consists of two similar repeats, both of which contribute to membrane fusion.
TL;DR: It is postulate that replacement of Gly 7 and Gly12 by Ala increases the alpha helical content of the N-terminal region, with a concomitant increase in its fusogenic activity.
Journal Article
Prostaglandin E1: anomalous effects on glucose production in rat liver.
TL;DR: Inhibition of the synthesis of a reactive metabolic intermediate in prostaglandin biosynthesis may explain these apparently anomalous effects of prostaglandsin E 1 on glucose production.
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Irreversible unfolding of the neutral pH form of influenza hemagglutinin demonstrates that it is not in a metastable state.
Raquel F. Epand,Richard M. Epand +1 more
TL;DR: The results demonstrate that the compact folded structure of the influenza hemagglutinin protein is not a kinetically trapped metastable high-energy form and applies theories of irreversible thermodynamics to obtain the activation energy.
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Bilayer stabilizing peptides and the inhibition of viral infection: antimeasles activity of carbobenzoxy-Ser-Leu-amide.
TL;DR: One dipeptide, Z-Ser-Leu-NH2, reduces measles virus cytopathic effect (CPE) in Vero cells and a linear correlation was found between the respective HPLC retention time parameterk′ for the peptide and the slope of the bilayer stabilization curve determined with model membranes by differential scanning calorimetry.