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Limor Avrahami

Researcher at Tel Aviv University

Publications -  11
Citations -  5747

Limor Avrahami is an academic researcher from Tel Aviv University. The author has contributed to research in topics: GSK-3 & Autophagy. The author has an hindex of 9, co-authored 11 publications receiving 5248 citations.

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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

Inhibition of Glycogen Synthase Kinase-3 Ameliorates β-Amyloid Pathology and Restores Lysosomal Acidification and Mammalian Target of Rapamycin Activity in the Alzheimer Disease Mouse Model IN VIVO AND IN VITRO STUDIES

TL;DR: Inhibition of GSK-3 restores lysosomal acidification that in turn enables clearance of Aβ burdens and reactivation of mTOR, which facilitates amelioration in cognitive function and provides evidence that mTOR is a target activated by G SKS-3 but inhibited by impaired lysOSomal Acidification and elevation in amyloid precursor protein/Aβ loads.
Journal ArticleDOI

Combined regulation of mTORC1 and lysosomal acidification by GSK-3 suppresses autophagy and contributes to cancer cell growth

TL;DR: This study shows that overexpression of GSK-3 isoforms activated mTORC1 and suppressed autophagy in MCF-7 human breast cancer cells as indicated by reduced beclin-1 levels and upregulation of sequestosome 1 (p62/SQSTM1).
Journal Article

Guidelines for the use and interpretation of assays for monitoring autophagy (3rd edition)

Daniel J. Klionsky, +2459 more
- 01 Jan 2016 - 
Journal ArticleDOI

A unique type of GSK-3 inhibitor brings new opportunities to the clinic

TL;DR: A new type of GSK-3 inhibitor, L807mts, is described that acts through a substrate-to-inhibitor conversion mechanism that occurs within the catalytic site of the enzyme.