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Éva Margittai

Researcher at Semmelweis University

Publications -  37
Citations -  7128

Éva Margittai is an academic researcher from Semmelweis University. The author has contributed to research in topics: Endoplasmic reticulum & Unfolded protein response. The author has an hindex of 20, co-authored 37 publications receiving 6459 citations. Previous affiliations of Éva Margittai include Hungarian Academy of Sciences & Vita-Salute San Raffaele University.

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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.
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Endoplasmic reticulum stress.

Gábor Bánhegyi, +15 more
- 01 Oct 2007 - 
TL;DR: The emerging role of ER stress in diverse human pathophysiological conditions such as carcinogenesis and tumor progression, cerebral ischemia, plasma cell maturation and apoptosis, obesity, insulin resistance, and type 2 diabetes is summarized.
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On the role of 4-hydroxynonenal in health and disease.

Miklós Csala, +9 more
- 01 May 2015 - 
TL;DR: HNE-mediated signaling can largely influence the fate of the cell through modulating major cellular processes, such as autophagy, proliferation and apoptosis, and the role of HNE in the pathophysiology of cancer, cardiovascular and neurodegenerative diseases is discussed.
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Ero1α regulates Ca(2+) fluxes at the endoplasmic reticulum-mitochondria interface (MAM).

Tiziana Anelli, +9 more
- 15 May 2012 - 
TL;DR: The results indicate that the levels, subcellular localization, and activity of Ero1α coordinately regulate Ca(2+) and redox homeostasis and signaling in the early secretory compartment.
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Uncoupled redox systems in the lumen of the endoplasmic reticulum. Pyridine nucleotides stay reduced in an oxidative environment.

Simona Piccirella, +15 more
- 24 Feb 2006 - 
TL;DR: The results demonstrated the separate existence of two redox systems in the endoplasmic reticulum lumen, which explains the contemporary functioning of oxidative folding and of powerful reductive reactions.