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Annie Sittler

Researcher at French Institute of Health and Medical Research

Publications -  28
Citations -  6319

Annie Sittler is an academic researcher from French Institute of Health and Medical Research. The author has contributed to research in topics: Ataxin 7 & Spinocerebellar ataxia. The author has an hindex of 15, co-authored 28 publications receiving 5801 citations. Previous affiliations of Annie Sittler include Collège de France & Pierre-and-Marie-Curie University.

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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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Alternative Splicing of Exon 14 Determines Nuclear or Cytoplasmic Localisation of FMR1 Protein Isoforms

Annie Sittler, +3 more
- 01 Jan 1996 - 
TL;DR: Analysis of various deletion mutants suggests the presence of a cytoplasmic retention domain encoded in exon 14 and of a nuclear association domain encoded within the first eight exons that appear however to lack a typical nuclear localisation signal.
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Novel Isoforms of the Fragile X Related Protein FXR1P are Expressed During Myogenesis

Edouard W. Khandjian, +10 more
- 01 Dec 1998 - 
TL;DR: The complex expression pattern ofFXR1P suggests tissue-specific expression for the various isoforms of FXR1 and the differential expression of FMRP and FXR 1Ps suggests that in certain types of cells and tissues, complementary functions may be fulfilled by the various F MRP family members.
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PML clastosomes prevent nuclear accumulation of mutant ataxin-7 and other polyglutamine proteins

Alexandre Janer, +14 more
- 03 Jul 2006 - 
TL;DR: It is shown that expression of PML isoform IV leads to the formation of distinct nuclear bodies enriched in components of the ubiquitin-proteasome system, which represent a potential therapeutic target for preventing polyQ disorders.
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SUMOylation attenuates the aggregation propensity and cellular toxicity of the polyglutamine expanded ataxin-7

Alexandre Janer, +9 more
- 01 Jan 2010 - 
TL;DR: Preventing the SUMOylation of expanded ATXN7 by mutating thesumO site increased both the amount of SDS-insoluble aggregates and of caspase-3 positive non-homogenous inclusions, which act toxic to the cells.