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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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Vegetative insecticidal protein (Vip1Ac) of Bacillus thuringiensis HD201: evidence for oligomer and channel formation.

TL;DR: The binding component (Vip1Ac) of the ADP-ribosylating vegetative insecticidal protein of Bacillus thuringiensis HD201 was isolated from the supernatant of cell cultures and Mass spectroscopic analysis of this high molecular mass band identified it as Vip1 Ac.
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Identification of channel-forming activity in the cell wall of Corynebacterium glutamicum.

TL;DR: The cell wall of the gram-positive Corynebacterium glutamicum was prepared and an ion-permeable channel with a single-channel conductance of about 6 nS in 1 M KCl was prepared, indicating that it is a water-filled channel wide enough to allow unhindered diffusion of ions.
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Phloretin-Induced Changes of Lipophilic Ion Transport across the Plasma Membrane of Mammalian Cells

TL;DR: The adsorption of [W(CO)(5)CN](-) was significantly reduced by phloretin, which is in reasonable agreement with the known phlrotin-induced effects on artificial and biological membranes, and is consistent with the assumption that the binding of phLoretin reduces the intrinsic dipole potential of the plasma membrane.
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The low-molecular-mass subunit of the cell wall channel of the Gram-positive Corynebacterium glutamicum. Immunological localization, cloning and sequencing of its gene porA.

TL;DR: Southern blots demonstrated that only the chromosomes of corynebacteria contain homologous sequences to porA; no hybridization could be detected with DNA from other mycolata.
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Use of Nonelectrolytes Reveals the Channel Size and Oligomeric Constitution of the Borrelia burgdorferi P66 Porin

TL;DR: The organization of P66 as a possible octamer was confirmed by Blue Native PAGE and immunoblot analysis, which both demonstrated that P66 forms a complex with a mass of approximately 460 kDa, and two dimension SDS PAGE revealed that P 66 is the only polypeptide in the complex.