R
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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Fusion peptides and the mechanism of viral fusion
TL;DR: There are several mechanisms by which viral fusion peptides accelerate the process of membrane fusion, including the promotion of negative curvature, lowering the rupture tension of the lipid monolayer, acting as an anchor to join the fusion membranes, transmitting a force to the membrane or imparting energy to the system by other means.
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Effects of increasing hydrophobicity on the physical-chemical and biological properties of a class A amphipathic helical peptide.
Geeta Datta,Manjula Chaddha,Susan Hama,Mohamad Navab,Alan M. Fogelman,David W. Garber,Vinod K. Mishra,Richard M. Epand,Raquel F. Epand,Sissel Lund-Katz,Michael C. Phillips,Jere P. Segrest,Gattadahalli M. Anantharamaiah +12 more
TL;DR: The effects of increasing the hydrophobicity of a series of homologous class A amphipathic peptides, including 5F, on physical and functional properties related to atherosclerosis inhibition by systematically replacing existing nonpolar amino acids with phenylalanine suggest that an appropriate balance between peptide-peptide and peptides-lipid interactions is required for optimal biological activity of amphipaths.
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Diacylglycerols, lysolecithin, or hydrocarbons markedly alter the bilayer to hexagonal phase transition temperature of phosphatidylethanolamines.
TL;DR: The sensitivity of the bilayer to hexagonal phase transition temperature to the presence of additives is at least as great as that which has been observed for any other lipid phase transition.
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Interaction with a Membrane Surface Triggers a Reversible Conformational Change in Bax Normally Associated with Induction of Apoptosis
TL;DR: It is reported that purified Bax undergoes a reversible conformational change upon incubation with lipid vesicles in the absence of other proteins, providing evidence that Bax activation proceeds in a stepwise fashion, with multiple triggers and potential levels of regulation.
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Ceragenins: cholic acid-based mimics of antimicrobial peptides.
Xin Zhong Lai,Yanshu Feng,Jacob Pollard,Judy N. Chin,Michael J. Rybak,Robert Bucki,Raquel F. Epand,Richard M. Epand,Paul B. Savage +8 more
TL;DR: Nonpeptide mimics of antimicrobial peptides may provide the best of both worlds: a means of using the same mechanism chosen by Nature to control bacterial growth without the problems associated with peptide therapeutics.