R
Roland Benz
Researcher at Jacobs University Bremen
Publications - 406
Citations - 20726
Roland Benz is an academic researcher from Jacobs University Bremen. The author has contributed to research in topics: Membrane & Lipid bilayer. The author has an hindex of 75, co-authored 399 publications receiving 19923 citations. Previous affiliations of Roland Benz include Tokai University & University of Bari.
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Cloning of the mspa gene encoding a porin from mycobacterium smegmatis
Michael Niederweis,Sabine Ehrt,Christian Heinz,Uta Klöcker,Stefanie Karosi,Kristine M. Swiderek,Lee W. Riley,Roland Benz +7 more
TL;DR: The results demonstrate that the mspA gene encodes a protein of M. smegmatis, which assembles to an extremely stable oligomer with high channel‐forming activity, and suggest that MspA is the prototype of a new class of channel-forming proteins.
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Outer membrane protein P of Pseudomonas aeruginosa: regulation by phosphate deficiency and formation of small anion-specific channels in lipid bilayer membranes.
TL;DR: A new major outer membrane protein, P, was induced in Pseudomonas aeruginosa PAO1 upon growth in medium containing 0.2 mM or less inorganic phosphate and was found to be highly specific for anions.
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Transport of oppositely charged lipophilic probe ions in lipid bilayer membranes having various structures
Arnold D. Pickar,Roland Benz +1 more
TL;DR: In this paper, a comparative study of the charge transport kinetics of oppositely charged lipophilic probe ions in lipid bilayer membranes of varying composition was carried out by using the charge pulse technique.
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Relaxation studies of ion transport systems in lipid bilayer membranes.
TL;DR: Different relaxation techniques which have been developed for this purpose during the last years are described, as well as applications to a number of ion transport systems.
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Low pH-induced formation of ion channels by clostridium difficile toxin B in target cells.
TL;DR: The results suggest that large clostridial cytotoxins including C. difficile toxin B and C. sordellii lethal toxin undergo structural changes at low pH of endosomes that are accompanied by membrane insertion and channel formation.