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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Journal ArticleDOI
Arginine-lysine positional swap of the LL-37 peptides reveals evolutional advantages of the native sequence and leads to bacterial probes
Xiuqing Wang,José Carlos Bozelli Junior,Biswajit Mishra,Tamara Lushnikova,Richard M. Epand,Guangshun Wang +5 more
TL;DR: The original peptide is more efficient in bacterial killing, but less toxic to human cells, than the K-R swapped peptides, revealing the evolutionary significance of the native sequence for host defense.
Journal ArticleDOI
Protein kinase C: An example of a calcium-regulated protein binding to membranes (Review)
Marian Mosior,Richard M. Epand +1 more
TL;DR: Conformational studies, together with classical thermodynamic studies, can provide a more detailed understanding of the functional, as well as, the structural, properties of amphitropic proteins.
Journal ArticleDOI
Flanking Residues Help Determine Whether a Hydrophobic Segment Adopts a Monotopic or Bitopic Topology in the Endoplasmic Reticulum Membrane
Morten H. H. Nørholm,Yulia V. Shulga,Satoko Aoki,Richard M. Epand,Gunnar von Heijne,Gunnar von Heijne +5 more
TL;DR: This work probes the topology of a membrane-attached enzyme, the ϵ isoform of human diacylglycerol kinase (DGKϵ), when inserted into rough microsomes and finds that charged flanking residues as well as proline residues embedded in the hydrophobic segment are important determinants of monotopic versus bitopic topology.
Book ChapterDOI
Chapter 6 Modulation of Lipid Polymorphism by Peptides
TL;DR: This suggestion that the fusogenic segments of viral fusion proteins may initiate membrane fusion by destabilizing the bilayer of target membranes is supported by the findings that many bilayerstabilizing peptides and proteins are found to be inhibitors of viral infectivity and syncytia formation.
Journal ArticleDOI
Biologically active calcitonin analogs which have minimal interactions with phospholipids.
TL;DR: It is demonstrated that two calcitonin analogs, [Gly8,Ala16]-des-Leu19 salmon calcitonIn and des-1-amino-[Ala1,7,Gly 8]-des -Leu 19 salmon calcitein have minimal interactions with phospholipids, and the presence of a phospholipsid-induced amphipathic helical sequence is not required for activity.