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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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In vivo and in vitro studies of major surface loop deletion mutants of the Escherichia coli K‐12 maltoporin: contribution to maltose and maltooligosaccharide transport and binding

TL;DR: In vivo and in vitro results suggest that maltooligosaccharides enter the LamB channel from the cell surface side with the non‐reducing end in advance, which results in a considerable difference in the on‐rate of carbohydrate binding from the extracellular side compared with that from the periplasmic side.
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Pores from mitochondrial outer membranes of yeast and a porin-deficient yeast mutant: a comparison.

TL;DR: In this article, the porin-free mitochondrial outer membrane of a yeast mutant was reconstituted with a single-channel conductance of 2.0 nS in 1 M KCl and the characteristics of general diffusion pores with an estimated effective diameter of 1.2 nm.
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Formation of small transmembrane pores: An intermediate stage on the way to Bacillus cereus non-hemolytic enterotoxin (Nhe) full pores in the absence of NheA.

TL;DR: The NheBC complex itself has a tendency to increase the membrane permeability prior to the emergence of full pores containing also NheA, so the benefit of these complexes is a more stable cell binding as well as stronger and earlier cytotoxic effect.
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CymA of Klebsiella oxytoca Outer Membrane: Binding of Cyclodextrins and Study of the Current Noise of the Open Channel

TL;DR: CymA, the outer membrane component of the cyclodextrin (CD) uptake and metabolism system of Klebsiella oxytoca, was reconstituted into lipid bilayer membranes, and the channel properties of this unusual porin were studied in detail.
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The BBA01 protein, a member of paralog family 48 from Borrelia burgdorferi, is potentially interchangeable with the channel-forming protein P13.

TL;DR: It is demonstrated that BBA01 is a channel-forming protein with properties surprisingly similar to those of P13, which together with the high degree of sequence similarity suggests that the two proteins may have similar and interchangeable functions.