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Eun-Kyoung Choi

Researcher at Hallym University

Publications -  105
Citations -  8087

Eun-Kyoung Choi is an academic researcher from Hallym University. The author has contributed to research in topics: Scrapie & Calsenilin. The author has an hindex of 33, co-authored 101 publications receiving 7376 citations. Previous affiliations of Eun-Kyoung Choi include Korean Academy of Science and Technology & Tohoku 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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Calsenilin: a calcium-binding protein that interacts with the presenilins and regulates the levels of a presenilin fragment.

TL;DR: Calsenilin interacts with both PS1 and PS2 in cultured cells, and can regulate the levels of a proteolytic product of PS2, which may mediate the effects of wild-type and mutant presenilins on apoptosis and on Aß formation.
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Mitochondrial dysfunction induced by oxidative stress in the brains of hamsters infected with the 263 K scrapie agent.

TL;DR: It is suggested that mitochondrial dysfunction caused by oxidative stress gives rise to neurodegeneration in prion disease.
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Expression of cytokine genes and increased nuclear factor-kappa B activity in the brains of scrapie-infected mice.

TL;DR: The results suggest that prion accumulation in astrocytes might activate NF-kappaB through the increase of ROS generation, and thus alterations in NF- kappaB-directed gene expression may contribute to both the neurodegeneration and proinflammatory responses which occur in scrapie.
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The cellular prion protein (PrPC) prevents apoptotic neuronal cell death and mitochondrial dysfunction induced by serum deprivation.

TL;DR: The results strongly suggest that PrP(C) may play a central role as an effective anti-apoptotic protein through caspase-dependent apoptotic pathways in mitochondria, supporting the concept that disruption of PrP (C) and consequent reduction of anti-APoptotic capacity ofPrP( C) may be one of the pathogenic mechanisms of prion diseases.