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Eric Chevet

Researcher at University of Rennes

Publications -  123
Citations -  15197

Eric Chevet is an academic researcher from University of Rennes. The author has contributed to research in topics: Endoplasmic reticulum & Unfolded protein response. The author has an hindex of 41, co-authored 101 publications receiving 12675 citations. Previous affiliations of Eric Chevet include University of Paris & Université Bordeaux Segalen.

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Journal ArticleDOI

Guidelines for the use and interpretation of assays for monitoring autophagy

Daniel J. Klionsky, +1287 more
- 01 Apr 2012 - 
TL;DR: These guidelines are presented for the selection and interpretation of methods for use by investigators who aim to examine macroautophagy 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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Integrated analysis of somatic mutations and focal copy-number changes identifies key genes and pathways in hepatocellular carcinoma

TL;DR: Functional analyses showed tumor suppressor properties for IRF2, whose inactivation, exclusively found in hepatitis B virus-related tumors, led to impaired TP53 function, and association of mutations in specific genes suggested that Wnt/β-catenin signaling might cooperate in liver carcinogenesis with both oxidative stress metabolism and Ras/mitogen-activated protein kinase (MAPK) pathways.
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Targeting the unfolded protein response in disease

TL;DR: Recent advances in the design of novel compounds and therapeutic strategies to manipulate levels of ER stress in disease are discussed.
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Endoplasmic reticulum-mediated phagocytosis is a mechanism of entry into macrophages.

TL;DR: This study has found that fusion of the endoplasmic reticulum (ER) with the macrophage plasmalemma, underneath phagocytic cups, is a source of membrane for phagosome formation in macrophages.
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Proteostasis control by the unfolded protein response.

TL;DR: An overview of recent insights into the mechanisms that cells employ to maintain proteostasis and how the unfolded protein response determines cell fate under endoplasmic reticulum stress is provided.