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Etienne Maisonneuve

Researcher at Aix-Marseille University

Publications -  21
Citations -  3381

Etienne Maisonneuve is an academic researcher from Aix-Marseille University. The author has contributed to research in topics: Stringent response & Protein aggregation. The author has an hindex of 16, co-authored 21 publications receiving 3027 citations. Previous affiliations of Etienne Maisonneuve include Newcastle University & Free University of Berlin.

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Existence of Abnormal Protein Aggregates in Healthy Escherichia coli Cells

TL;DR: The results led us to speculate that protein aggregates may function as a temporary "trash organelle" for cellular detoxification, and it was shown that the levels of reactive oxygen species and unfolded or misfolded proteins determine the Levels of Protein aggregates.
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The role of thiol oxidative stress response in heat-induced protein aggregate formation during thermotolerance in Bacillus subtilis.

TL;DR: It is demonstrated that the transcription factor Spx, a regulatory substrate of ClpXP, is critical for the prevention of protein aggregate formation because its regulon encodes redox chaperones, such as thioredoxin, required for protection against thiol‐specific oxidative stress.
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A microscope automated fluidic system to study bacterial processes in real time.

TL;DR: A novel hybrid micro fluidic device that combines a thin agar pad and a custom flow chamber that allows real time analysis of a broad array of biological processes such as growth, development and motility is designed.
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Remarkable Functional Convergence: Alarmone ppGpp Mediates Persistence by Activating Type I and II Toxin-Antitoxins.

TL;DR: It is demonstrated that the conserved GTPase Obg and the second messenger ppGpp mediate persistence by activation of a type I toxin-antitoxin module (hokB/sokB) in E. coli.
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YtfK activates the stringent response by triggering the alarmone synthetase SpoT in Escherichia coli.

TL;DR: The protein YtfK promotes SpoT-dependent accumulation of (p)ppGpp and is required for activation of the stringent response during phosphate and fatty acid starvation, and the results indicate that YTFK can interact with SpoT.