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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

Interaction of Phloretin with Lipid Monolayers: Relationship between Structural Changes and Dipole Potential Change

Richard Cseh, +1 more
- 01 Sep 1999 - 
TL;DR: This investigation studied the interaction of phloretin with monolayers formed of different lipids in the liquid-expanded and the condensed state and proposes a model that relates the area change to the dipole moment in a dynamic manner.
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Selective and specific internalization of clostridial C3 ADP-ribosyltransferases into macrophages and monocytes.

Jörg Fahrer, +7 more
- 01 Feb 2010 - 
TL;DR: It is demonstrated for the first time that low concentrations of both C3lim and C3bot are selectively internalized into macrophages/monocytes in less than 3 h, inducing the reorganization of the actin cytoskeleton by ADP‐ribosylation of Rho.
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Outer-membrane protein PhoE from Escherichia coli forms anion-selective pores in lipid-bilayer membranes.

Roland Benz, +2 more
- 16 Apr 1984 - 
TL;DR: In contrast to pores formed by the OmpF porin from E. coli the PhoE channel was found to be anion-selective at neutral pH, and this anionic selectivity is explained by the assumption that thePhoE pore contains an excess of fixed positive charges.
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Voltage-induced thickness changes of lipid bilayer membranes and the effect of an electric field on gramicidin A channel formation

Ernst Bamberg, +1 more
- 19 Mar 1976 - 
TL;DR: The time course of the current as a consequence of channel formation by gramicidin A did not correlate with the thickness change of the lipid membranes, suggesting a possible direct influence of the electric field.
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Characterization of Dominantly Negative Mutant ClyA Cytotoxin Proteins in Escherichia coli

Sun Nyunt Wai, +6 more
- 15 Sep 2003 - 
TL;DR: Study of the subcellular localization of the ClyA cytotoxic protein and of mutations causing defective translocation to the periplasm in Escherichia coli provided a molecular explanation for, the dominant negative feature of the mutant ClyA variants.