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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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Factors determining pressure perturbation calorimetry measurements: evidence for the formation of metastable states at lipid phase transitions.

TL;DR: It is suggested that sequential cycles lead to a gradual loss in magnitude of the heat effect upon pressure perturbation and can be explained by the formation of a metastable glass-like state that converts to a stable phase at temperatures removed from the region of the phase transition.
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CDP-diacylglycerol, a critical intermediate in lipid metabolism.

TL;DR: A deeper understanding of the extensive synthetic and signaling networks stemming from this key lipid intermediate, CDP-DAG, is contributed to a deeperUnderstanding of lipid homeostasis and optimal biological functions.
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Caveolin-1 hydrophobic segment peptides insertion into membrane mimetic systems: role of proline residue.

TL;DR: The overall findings support the studies with the intact protein in cells and suggest that the peptide of WT caveolin-1 hydrophobic segment has an intrinsic preference not to maintain its conformation as a rigid transmembrane helix.
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Effect of magainin, class L, and class A amphipathic peptides on fatty acid spin labels in lipid bilayers.

TL;DR: Effects of these peptides on other lipids indicated that the mechanism by which they permeabilize lipid bilayers depends both on the peptide and on the lipid composition of the vesicles, which suggests that the perturbing effects of magainins on lipid chain order at permeabilizing concentrations are not directly responsible for the increased leakage of vesicle contents.
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Mitochondrial NM23-H4/NDPK-D: a bifunctional nanoswitch for bioenergetics and lipid signaling

TL;DR: A novel paradigm for the function of the mitochondrial nucleoside diphosphate kinase NM23-H4/NDPK-D is proposed: acting as a bifunctional nanoswitch in bioenergetics and cardiolipin (CL) trafficking and signaling, with potential for the development of interventions in various human pathologies.