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Simone Engelender

Researcher at Technion – Israel Institute of Technology

Publications -  72
Citations -  15173

Simone Engelender is an academic researcher from Technion – Israel Institute of Technology. The author has contributed to research in topics: Parkin & Parkinson's disease. The author has an hindex of 36, co-authored 69 publications receiving 13370 citations. Previous affiliations of Simone Engelender include Johns Hopkins University School of Medicine & Johns Hopkins 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.
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

Inducible expression of mutant α-synuclein decreases proteasome activity and increases sensitivity to mitochondria-dependent apoptosis

TL;DR: In this article, the authors showed that expression of mutant alpha-synuclein results in sensitivity to impairment of proteasome activity, leading to mitochondrial abnormalities and neuronal cell death in Parkinson's disease.
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Synphilin-1 associates with alpha-synuclein and promotes the formation of cytosolic inclusions.

TL;DR: It is found that α-synuclein interacts in vivo with synphilin-1 in neurons, and co-transfection of both proteins (but not control proteins) in HEK 293 cells yields cytoplasmic eosinophilic inclusions.