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Orsolya Kapuy

Researcher at Semmelweis University

Publications -  46
Citations -  7615

Orsolya Kapuy is an academic researcher from Semmelweis University. The author has contributed to research in topics: Autophagy & Unfolded protein response. The author has an hindex of 20, co-authored 38 publications receiving 6072 citations. Previous affiliations of Orsolya Kapuy include University of Oxford & Budapest University of Technology and Economics.

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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.
Journal ArticleDOI

Switches and latches: a biochemical tug-of-war between the kinases and phosphatases that control mitosis

TL;DR: It is proposed that phosphatase regulation creates coherent feed-forward loops and adds extra amplification loops to the Cdk1:CycB regulatory network, thus forming an integral part of the mitotic switch, which is based on the antagonistic interaction of two groups of proteins.
Journal ArticleDOI

Irreversibility of mitotic exit is the consequence of systems-level feedback

TL;DR: It is shown that forced cyclin destruction in mitotic budding yeast cells efficiently drives mitotic exit events, and these remain reversible after termination of cyclin proteolysis, with recovery of the mitotic state and cyclin levels.
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Bistability by multiple phosphorylation of regulatory proteins.

TL;DR: The properties of a particular bistable reaction network motivated by the antagonistic relationship between cyclin-dependent kinase and its multiply phosphorylated target, Cdh1, which is involved in the degradation of cyclin molecules are studied.