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Serena Carra

Researcher at University of Modena and Reggio Emilia

Publications -  92
Citations -  16097

Serena Carra is an academic researcher from University of Modena and Reggio Emilia. The author has contributed to research in topics: Heat shock protein & Protein degradation. The author has an hindex of 41, co-authored 78 publications receiving 12887 citations. Previous affiliations of Serena Carra include University of Groningen & University Medical Center Groningen.

Papers
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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.
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.
Journal ArticleDOI

Guidelines for the use and interpretation of assays for monitoring autophagy (4th edition)

Daniel J. Klionsky, +2983 more
- 08 Feb 2021 - 
TL;DR: In this article, the authors present a set of guidelines for investigators to select and interpret methods to examine autophagy and related processes, and for reviewers to provide realistic and reasonable critiques of reports that are focused on these processes.
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Structural and functional diversities between members of the human HSPB, HSPH, HSPA, and DNAJ chaperone families

Michel J. Vos, +3 more
- 08 Jul 2008 - 
TL;DR: Heat shock proteins (HSPs) were originally identified as stress-responsive proteins required to deal with proteotoxic stresses but now several diversities between members and families can be found that not only point to differences in client specificity but also seem to serve differential client handling and processing.
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An aberrant phase transition of stress granules triggered by misfolded protein and prevented by chaperone function

Daniel Mateju, +9 more
- 14 Jun 2017 - 
TL;DR: It is found that misfolded proteins, such as ALS‐linked variants of SOD1, specifically accumulate and aggregate within SGs in human cells, which decreases the dynamics of SGs, changes SG composition, and triggers an aberrant liquid‐to‐solid transition of in vitro reconstituted compartments.