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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Promotion of plasmalogen biosynthesis reverse lipid changes in a Barth Syndrome cell model.
TL;DR: The results showed the efficacy of the promotion of plasmalogen biosynthesis on increasing the CL levels in a BTHS cell model and highlight the potential beneficial effect of a diet supplemented with plAsmalogen precursors to BTHs patients.
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Lipid concentration affects the kinetic stability of dielaidoylphosphatidylethanolamine bilayers.
TL;DR: The results demonstrate that the rate of conversion of the bilayer to the hexagonal phase is dependent on the concentration of the lipid suspension even under conditions of full hydration.
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The liver plasma membrane Ca2+ pump: Hormonal sensitivity
Sophie Lotersztajn,Sophie Lotersztajn,Richard M. Epand,Richard M. Epand,Ariane Mallat,Ariane Mallat,Catherine Pavoine,Catherine Pavoine,Françoise Pecker,Françoise Pecker +9 more
TL;DR: It is concluded that the inhibitory action of the Ca2+ mobilizing hormones and glucagon on the liver plasma membrane Ca2- pump might play a key role in the actions of these hormones by prolonging the elevation in cytosolic free Ca2+.
Journal Article
Mixing rates can markedly affect the kinetics of peptide-induced leakage from liposomes.
TL;DR: It is demonstrated that fast (millisecond range) peptide-membrane association creates a nonhomogeneous distribution which exists sufficiently long after peptide addition to markedly alter the course of leakage.
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Pyrazine derivatives affect membrane fluidity of vascular smooth muscle microsomes in relation to their biological activity
TL;DR: The results are consistent with the contention that these pyrazine derivatives not only interact with receptor protein molecules in the biological membranes, but also modulate these receptor properties via their interaction with the lipid bilayer altering the membrane microviscosity.