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Elmar J. Prenner
Researcher at University of Calgary
Publications - 100
Citations - 4562
Elmar J. Prenner is an academic researcher from University of Calgary. The author has contributed to research in topics: Lipid bilayer & Membrane. The author has an hindex of 31, co-authored 88 publications receiving 4085 citations. Previous affiliations of Elmar J. Prenner include University of Arizona & University of Alberta.
Papers
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Journal ArticleDOI
Tryptophan- and arginine-rich antimicrobial peptides: structures and mechanisms of action.
TL;DR: In this review, the structures of a number of different Trp- and Arg-rich antimicrobial peptides are examined and some of the major mechanistic studies are presented.
Journal ArticleDOI
Alum interaction with dendritic cell membrane lipids is essential for its adjuvanticity
Tracy L. Flach,Gilbert Ng,Aswin Hari,Melanie D. Desrosiers,Ping Zhang,Sandra Ward,Mark E. Seamone,Akosua Vilaysane,Ashley D. Mucsi,Yin Fong,Elmar J. Prenner,Chang-Chun Ling,Jürg Tschopp,Daniel A. Muruve,Matthias Amrein,Yan Shi +15 more
TL;DR: This study reports that, independent of inflammasome and membrane proteins, alum binds dendritic cell (DC) plasma membrane lipids with substantial force and proposes that alum triggers DC responses by altering membrane lipid structures.
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Differential scanning calorimetry: An invaluable tool for a detailed thermodynamic characterization of macromolecules and their interactions
Michael H. Chiu,Elmar J. Prenner +1 more
TL;DR: This review focuses on the use of DSC for biochemical and pharmaceutical applications.
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Differential scanning calorimetry and X-ray diffraction studies of the specificity of the interaction of antimicrobial peptides with membrane-mimetic systems.
Karl Lohner,Elmar J. Prenner +1 more
TL;DR: These studies clearly demonstrated that antimicrobial peptides show preferential interaction with specific phospholipid classes and revealed that in addition to charge-charge interactions, membrane curvature strain and hydrophobic mismatch between peptides and lipids are important parameters in determining the mechanism of membrane perturbation.
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The interaction of the antimicrobial peptide gramicidin S with lipid bilayer model and biological membranes.
TL;DR: The considerable lipid specificity of GS for binding to and destabilization of lipid bilayer model membranes indicates that the design of GS analogs with an improved antimicrobial potency and a markedly decreased toxicity for eukaryotic cell plasma membranes should be possible.