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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Journal ArticleDOI
DipA, a Pore-Forming Protein in the Outer Membrane of Lyme Disease Spirochetes Exhibits Specificity for the Permeation of Dicarboxylates
Marcus Thein,Mari Bonde,Ignas Bunikis,Katrin Denker,Albert Sickmann,Albert Sickmann,Sven Bergström,Roland Benz,Roland Benz +8 more
TL;DR: The results imply that DipA forms a porin specific for dicarboxylates which may play an important role for the uptake of specific nutrients in different Borrelia species.
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Use of irreversible electrical breakdown of lipid bilayers for the study of interaction of membranes with surface active molecules.
TL;DR: It is observed that macromolecules having a strong binding affinity to the membrane alter the time course of pore formation significantly, and this method is proposed as a simple test for adsorption of macromolescules to membranes.
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Characterization of SH groups in porin of bovine heart mitochondria. Porin cysteines are localized in the channel walls.
TL;DR: Porin from bovine heart mitochondria contains probably two cysteines, Cys126 is the most sensitive to N-ethylmaleimide binding, and at least one of the cysteine is localized between 0.51 nm and 1.75 nm deep in the protein micelle.
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Discovery of a novel channel-forming protein in the cell wall of the non-pathogenic Nocardia corynebacteroides.
Franziska G Riess,Roland Benz +1 more
TL;DR: Detergent extracts of whole cells of the Gram-positive, non-pathogenic, strictly aerobic bacterium Nocardia corynebacteroides contain channel-forming activity and asymmetric addition of the 134 kDa protein to lipid bilayer membranes resulted in an asymmetric voltage-dependence.
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Single-channel analysis of the conductance fluctuations induced in lipid bilayer membranes by complement proteins C5b-9.
TL;DR: Single-channel analysis of electrical fluctuations induced in planar bilayer membranes by the purified human complement proteins C5b6, C7, C8, and C9 has been analyzed and indicated that the ions move inside the complement pore in a manner similar to the way they move in the aqueous phase.