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.
Papers
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Journal ArticleDOI
ApoA-I Mimetic Peptides with Differing Ability to Inhibit Atherosclerosis Also Exhibit Differences in Their Interactions with Membrane Bilayers
Shaila P. Handattu,David W. Garber,Dawn Horn,Donald W. Hughes,Bob Berno,Alex D. Bain,Vinod K. Mishra,Mayakonda N. Palgunachari,Geeta Datta,Gattadahalli M. Anantharamaiah,Richard M. Epand +10 more
TL;DR: It is demonstrated that the peptide 3F-2, which has more potent anti-inflammatory activity in vitro when administered intraperitoneally to female apoE null mice for 6 weeks, inhibits atherosclerosis, whereas 3F14 does not, which supports the proposal that the molecular basis for the difference in the biological activities of the two peptides lies with their different interactions with membranes.
Journal ArticleDOI
Biologically potent analogues of salmon calcitonin which do not contain an N-terminal disulfide-bridged ring structure.
TL;DR: In vitro activation of adenylate cyclase by human calcitonin analogues is not always correlated with in vivo hypocalcemic potency.
Journal ArticleDOI
Conformational stability and membrane interaction of the full-length ectodomain of HIV-1 gp41: implication for mode of action.
Naama Lev,Yael Fridmann-Sirkis,Lior Blank,Arkady Bitler,Raquel F. Epand,Richard M. Epand,Yechiel Shai +6 more
TL;DR: The results support the emerging model in which one of the roles of gp41 folding into the SHB conformation is to slow down membrane disruption effects induced by early exposed gp41, however, it can further affect membrane morphology once exposed to negatively charged membranes during late stages.
Journal ArticleDOI
The role of the ganglioside GD1a as a receptor for Sendai virus
TL;DR: The ganglioside GD1a, which serves as a receptor for Sendai virus, also affects lipid polymorphism as determined by 31P nuclear magnetic resonance, and enhances virus binding to liposomes of all the compositions studied, but leakage rates and fusion rate constants are either unaffected or reduced.
Book ChapterDOI
Membrane Lipid Polymorphism
TL;DR: The property of lipid polymorphism can be applied to understand how fundamental intrinsic curvature properties of a membrane alter the physical properties of the membrane bilayer, which will affect the functional characteristics of membrane proteins.