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Stéphane Duvezin-Caubet

Researcher at University of Bordeaux

Publications -  31
Citations -  7435

Stéphane Duvezin-Caubet is an academic researcher from University of Bordeaux. The author has contributed to research in topics: Mitochondrion & ATP synthase. The author has an hindex of 19, co-authored 29 publications receiving 6797 citations. Previous affiliations of Stéphane Duvezin-Caubet include Ludwig Maximilian University of Munich & Centre national de la recherche scientifique.

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Guidelines for the use and interpretation of assays for monitoring autophagy (3rd edition)

Daniel J. Klionsky, +2522 more
- 21 Jan 2016 - 
TL;DR: In this paper, the authors present a set of guidelines for the selection and interpretation of methods for use by investigators who aim to examine macro-autophagy and related processes, as well as for reviewers who need to provide realistic and reasonable critiques of papers that are focused on these processes.
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Mitophagy is triggered by mild oxidative stress in a mitochondrial fission dependent manner.

TL;DR: It is demonstrated that in mammalian cells under mild oxidative stress a DRP1-dependent type of mitophagy is triggered while a concomitant induction of non-selective autophagy was not observed, and proposed that these mild oxidative conditions resembling well physiological situations are thus very helpful for studying the molecular pathways governing the selective removal of dysfunctional mitochondria.
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Amyloid aggregates of the HET-s prion protein are infectious.

TL;DR: It is shown that biolistic introduction of aggregated recombinant HET-s protein into fungal cells induces emergence of the [Het-s] prion with a high frequency, demonstrating that prion infectivity can be created de novo, in vitro from recombinant protein in this system.
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OPA1 Processing Reconstituted in Yeast Depends on the Subunit Composition of the m-AAA Protease in Mitochondria

TL;DR: These results provide evidence for different substrate specificities of m-AAA proteases composed of different subunits and reveal a striking evolutionary switch of proteases involved in the proteolytic processing of dynamin-like GTPases in mitochondria.