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
O-Mycoloylated Proteins from Corynebacterium AN UNPRECEDENTED POST-TRANSLATIONAL MODIFICATION IN BACTERIA
Emilie Huc,Emilie Huc,Xavier Meniche,Xavier Meniche,Xavier Meniche,Roland Benz,Nicolas Bayan,Alexandre Ghazi,Marielle Tropis,Marielle Tropis,Mamadou Daffé,Mamadou Daffé +11 more
TL;DR: It is shown that the post-translational mycoloylation of PorA occurs at Ser-15 and is necessary for the pore-forming activity of C. glutamicum.
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Reversible electrical breakdown of squid giant axon membrane
Roland Benz,Franco Conti +1 more
TL;DR: Because of the high conductance of the membrane during breakdown it seems very likely that this results in pore formation, and it is probable that the reversible electrical breakdown is mainly caused by mechanical instability produced by electrostriction of the membranes, but the decrease in the Born energy for ion injection into the membrane, accompanying the decreases in membrane thickness, may play also an important role.
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Channel formation by salmon and human calcitonin in black lipid membranes.
TL;DR: It is discussed that the superior therapeutic effect of salmon Ct as a tool to treat bone disorders, including Paget disease, osteoporosis, and hypercalcemia of malignancy, rather than human Ct is related to the lack of the fibrillating property of salmonCt.
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Both α-haemolysin determinants contribute to full virulence of uropathogenic Escherichia coli strain 536
Gábor Nagy,Artur Altenhoefer,Oliver Knapp,Elke Maier,Ulrich Dobrindt,Gabriele Blum-Oehler,Roland Benz,Levente Emödy,Jörg Hacker +8 more
TL;DR: The data suggest that the two hly paralogues encode identical toxin functions; however, due to different regulation of expression, they participate at distinct stages of the infectious process.
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The Fusobacterium nucleatum Major Outer-Membrane Protein (FomA) Forms Trimeric, Water-Filled Channels in Lipid Bilayer Membranes
TL;DR: The pore-forming activity of the major outer-membrane protein FomA of the anaerobic Fusobacterium nucleatum was studied in artificial lipid bilayer membranes and strongly suggests that the trimer is the functional unit of the porin.