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Erhard Bremer

Researcher at University of Marburg

Publications -  170
Citations -  12681

Erhard Bremer is an academic researcher from University of Marburg. The author has contributed to research in topics: Bacillus subtilis & Ectoine. The author has an hindex of 61, co-authored 164 publications receiving 11488 citations. Previous affiliations of Erhard Bremer include Max Planck Society & University of Konstanz.

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Protection of Bacillus subtilis against Cold Stress via Compatible-Solute Acquisition

TL;DR: Glycine betaine strongly stimulated growth at 15°C and permitted cell proliferation at the growth-inhibiting temperature of 13°C, which highlights an underappreciated facet of the acclimatization of B. subtilis to cold environments and allows a comparison of the characteristics of compatible solutes with respect to their osmotic, heat, and cold stress-protective properties.
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Osmotic regulation of porin expression: a role for DNA supercoiling

TL;DR: It is suggested that environmentally induced changes in DNA supercoiling may play a role in determining the level of porin expression, and these findings have implications for current models of Porin regulation.
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The osmz(bgly) gene encodes the dna-binding protein h-ns (h1a), a component of the escherichia coli k12 nucleoid

TL;DR: The results suggest that the nucleoid-associated DNA-binding protein H-NS (H1a) plays a critical role in gene expression and in determining the structure of the genetic material.
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Crystal Structures of the Choline/Acetylcholine Substrate-binding Protein ChoX from Sinorhizobium meliloti in the Liganded and Unliganded-Closed States

TL;DR: Fluorescence-based ligand binding assays used to quantitate substrate binding by the periplasmic ligand-binding protein ChoX confirmed that ChoX recognizes choline and acetylcholine with high and medium affinity, respectively, and solved the crystal structures of ChoX in a closed, substrate-free conformation.
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The nucleoid-associated DNA-binding protein H-NS is required for the efficient adaptation of Escherichia coli K-12 to a cold environment.

TL;DR: It is shown that the ability to cope efficiently with a cold environment is strongly impaired in E. coli strains carrying hns mutations, and synthesis of a truncated H-NS protein with only 75 amino-terminal amino acids was insufficient to restore growth at low temperature.