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Byung-Hoon Lee

Researcher at Daegu Gyeongbuk Institute of Science and Technology

Publications -  133
Citations -  11677

Byung-Hoon Lee is an academic researcher from Daegu Gyeongbuk Institute of Science and Technology. The author has contributed to research in topics: Proteasome & Deubiquitinating enzyme. The author has an hindex of 39, co-authored 126 publications receiving 10414 citations. Previous affiliations of Byung-Hoon Lee include Harvard University & Hanyang University.

Papers
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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

Enhancement of proteasome activity by a small-molecule inhibitor of USP14

Byung-Hoon Lee, +15 more
- 09 Sep 2010 - 
TL;DR: It is shown that USP14, a proteasome-associated deubiquitinating enzyme, can inhibit the degradation of ubiquitin–protein conjugates both in vitro and in cells.
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Deregulation of HDAC1 by p25/Cdk5 in Neurotoxicity

Dohoon Kim, +18 more
- 10 Dec 2008 - 
TL;DR: This work shows that deregulation of histone deacetylase 1 (HDAC1) activity by p25/Cdk5 induces aberrant cell-cycle activity and double-strand DNA breaks leading to neurotoxicity, and outlines a pathological signaling pathway illustrating the importance of maintaining HDAC1 activity in the adult neuron.
Journal ArticleDOI

Trimming of ubiquitin chains by proteasome-associated deubiquitinating enzymes

Min Jae Lee, +4 more
- 01 May 2011 - 
TL;DR: Emerging evidence suggests that small molecule USP14 inhibitors can enhance proteasome function in cells, which is consistent with this model, and the responsiveness of substrates to inhibition of proteasomal deubiquitinating enzymes may vary substantially.
Journal ArticleDOI

Rpn1 provides adjacent receptor sites for substrate binding and deubiquitination by the proteasome

Yuan Shi, +15 more
- 19 Feb 2016 - 
TL;DR: The results indicate that proteasome subunit Rpn1 can recognize both ubiquitin and UBL domains of substrate shuttling factors that themselves bind ubiquit in and function as reversibly associated proteasomal Ubiquitin receptors.