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Valeria Crippa

Researcher at University of Milan

Publications -  64
Citations -  9483

Valeria Crippa is an academic researcher from University of Milan. The author has contributed to research in topics: Proteasome & Autophagy. The author has an hindex of 33, co-authored 56 publications receiving 7457 citations. Previous affiliations of Valeria Crippa include University of Florence.

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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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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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The small heat shock protein B8 (HspB8) promotes autophagic removal of misfolded proteins involved in amyotrophic lateral sclerosis (ALS)

TL;DR: Using motor neuronal fALS models, it is demonstrated that HspB8 decreases aggregation and increases mutant SOD1 solubility and clearance, without affecting wild-type S OD1 turnover, and the pharmacological modulation of HSpB8 expression in motor neurons may have important implications to unravel the molecular mechanisms involved both in fALS and in sALS.
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Trehalose induces autophagy via lysosomal-mediated TFEB activation in models of motoneuron degeneration

TL;DR: It is demonstrated that trehalose regulates autophagy by inducing rapid and transient lysosomal enlargement and membrane permeabilization (LMP) by correlated with the calcium-dependent phosphatase PPP3/calcineurin activation, TFEB dephosphorylation and nuclear translocation.
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Mutation of SOD1 in ALS: a gain of a loss of function

TL;DR: The toxicity of mutant SOD1 might, therefore, arise from an initial misfolding reducing nuclear protection from the active enzyme (loss of function in the nuclei), a process that may be involved in ALS pathogenesis.