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Hyun Kyu Song

Researcher at Korea University

Publications -  178
Citations -  13347

Hyun Kyu Song is an academic researcher from Korea University. The author has contributed to research in topics: Autophagy & Ubiquitin ligase. The author has an hindex of 44, co-authored 167 publications receiving 11174 citations. Previous affiliations of Hyun Kyu Song include Max Planck Society & Harvard 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 (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

The structures of HsIU and the ATP-dependent protease HsIU-HsIV.

TL;DR: The crystal structures of free HslU and an 820,000 relative molecular mass complex of HSlU and HslV are reported–the first structure of a complete set of components of an ATP-dependent protease.
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Endoribonucleolytic Cleavage of m6A-Containing RNAs by RNase P/MRP Complex.

TL;DR: In this paper, the authors show that m6A-containing RNAs are subject to endoribonucleolytic cleavage via YTHDF2 (m6A reader protein), HRSP12 (adaptor protein), and RNase P/MRP (endoribon nucleases) via endore-ibonuclear cleavage.
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The crystal structure of a triacylglycerol lipase from Pseudomonas cepacia reveals a highly open conformation in the absence of a bound inhibitor.

TL;DR: The crystal structure of a triacylglycerol lipase from Pseudomonas cepacia (PcL) in the absence of a bound inhibitor using X-ray crystallography suggests that this enzyme shares the same mechanisms of catalysis and interfacial activation as other lipases.