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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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Regulation of CTP: phosphocholine cytidylyltransferase activity by the physical properties of lipid membranes: an important role for stored curvature strain energy.
TL;DR: Stored curvature strain energy is an important determinant of CT activation and may reflect an increased surface hydrophobicity of class II lipid membranes, implying a role for surface dehydration in CT's interactions with membranes containing class II lipids.
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Lipopeptaibols, a novel family of membrane active, antimicrobial peptides.
Claudio Toniolo,Marco Crisma,Fernando Formaggio,Cristina Peggion,Raquel F. Epand,Richard M. Epand +5 more
TL;DR: Using solution methodologies, a series of analogues of trichogin GA IV was synthesized which allowed determination of the minimal lipid chain and peptide main-chain lengths for the onset of membrane activity and exploitation of a number of spectroscopic techniques aimed at determining its preferred conformation under a variety of conditions.
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Effect of end group blockage on the properties of a class A amphipathic helical peptide
Y. V. Venkatachalapathi,Michael C. Phillips,Richard M. Epand,Raquel F. Epand,Ewan M. Tytler,Jere P. Segrest,Gattadahalli M. Anantharamaiah +6 more
TL;DR: The activation of the plasma enzyme lecithin: cholesterol acyltransferase by the Ac‐18A‐NH2 peptide is greater than the 18A analog and comparable to that observed with the apo A‐I, which is the major protein component of high‐density lipoprotein and a potent inhibitor of lipid hexagonal phase formation.
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Amphipathic helix and its relationship to the interaction of calcitonin with phospholipids
TL;DR: The ability of human calcitonin to solubilize dimyristoylphosphatidylglycerol and to alter the phase transition properties of this phospholipid while maintaining a low content of helix indicates that the presence of an amphipathic helix is not a requirement for these effects.
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Membrane-Active Peptides and the Clustering of Anionic Lipids
Parvesh Wadhwani,Raquel F. Epand,Nico Heidenreich,Jochen Bürck,Anne S. Ulrich,Richard M. Epand +5 more
TL;DR: A remarkable correlation was found between the net positive charge of the peptides and their capacity to induce anionic lipid clustering, which was independent of their secondary structure and likely contributes to the mechanism of antibacterial action of highly cationic CPPs.