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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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Molecular properties of diacylglycerol kinase-epsilon in relation to function.
TL;DR: The nature of the acyl chain specificity of the enzyme indicates that DGKϵ is associated with the synthesis of phosphatidylinositol, and an important property of DGK ϵ is that it is specific for diacylglycerol species containing an arachidonoyl group.
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Quaternary structure of the neuronal protein NAP-22 in aqueous solution.
TL;DR: It is demonstrated, using fluorescence resonance energy transfer, that at low concentrations, NAP-22 labeled with Texas Red binds equally well to liposomes of phosphatidylcholine either with or without the addition of 40 mol% cholesterol.
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Effects of lipid structure on peptide-lipid interactions. Complexes of salmon calcitonin with phosphatidylglycerol and with phosphatidic acid.
TL;DR: There was a much greater increase in carboxyfluorescein leakage from phosphatidylglycerol-containing vesicles induced by salmon calcitonin demonstrating the greater ability of the peptide to rupture bilayers containing this phospholipid.
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Aliphatic aldehydes promote myelin basic protein-induced fusion of phospholipid vesicles
TL;DR: The ability of aliphatic aldehydes to promote myelin basic protein-induced membrane fusion may be of relevance to myelin structure and function and, particularly, to the pathology of demyelinating diseases such as multiple sclerosis.
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Association of phosphatidic acid with the bovine mitochondrial ADP/ATP carrier.
TL;DR: It is shown for the first time that phosphatidic acid, although a minor component, is one of the lipids bound to Anc, and the short spin-lattice relaxation time found by (31)P magic angle spinning nuclear magnetic resonance (MAS/NMR) for phosphatids indicates that it is tightly bound to the protein.