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Anne Sophie Nicot

Researcher at University of Strasbourg

Publications -  5
Citations -  5464

Anne Sophie Nicot is an academic researcher from University of Strasbourg. The author has contributed to research in topics: Endosome & Actin. The author has an hindex of 4, co-authored 4 publications receiving 4959 citations. Previous affiliations of Anne Sophie Nicot include French Institute of Health and Medical Research.

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Journal ArticleDOI

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.
Journal ArticleDOI

A phosphoinositide conversion mechanism for exit from endosomes

TL;DR: It is reported that surface delivery of endosomal cargo requires hydrolysis of PI(3)P by the phosphatidylinositol 3-phosphatase MTM1, an enzyme whose loss of function leads to X-linked centronuclear myopathy (also called myotubular myopathy) in humans.
Journal ArticleDOI

Erratum to: Guidelines for the use and interpretation of assays for monitoring autophagy (3rd edition) (Autophagy, 12, 1, 1-222, 10.1080/15548627.2015.1100356

Daniel J. Klionsky, +2522 more
- 01 Jan 2016 - 
TL;DR: Author(s): Klionsky, DJ; Abdelmohsen, K; Abe, A; Abedin, MJ; Abeliovich, H; A Frozena, AA; Adachi, H, Adeli, K, Adhihetty, PJ; Adler, SG; Agam, G; Agarwal, R; Aghi, MK; Agnello, M; Agostinis, P; Aguilar, PV; Aguirre-Ghis
Posted ContentDOI

BIN1 regulates actin-membrane interactions during IRSp53-dependent filopodia formation

TL;DR: This paper showed that BIN1-mediated filopodia formation requires IRSp53, which allows its localization at negatively-curved membrane topologies and regulates the membrane-to-cortex architecture and functions as a molecular platform to recruit actin-binding proteins, dynamin and ezrin.