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Shengyun Fang

Researcher at University of Maryland, Baltimore

Publications -  100
Citations -  18957

Shengyun Fang is an academic researcher from University of Maryland, Baltimore. The author has contributed to research in topics: Ubiquitin ligase & Unfolded protein response. The author has an hindex of 41, co-authored 95 publications receiving 16939 citations. Previous affiliations of Shengyun Fang include United States Department of Veterans Affairs & National Institutes of Health.

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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

Guidelines for the use and interpretation of assays for monitoring autophagy

Daniel J. Klionsky, +1287 more
- 01 Apr 2012 - 
TL;DR: These guidelines are presented for the selection and interpretation of methods for use by investigators who aim to examine macroautophagy 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

RING fingers mediate ubiquitin-conjugating enzyme (E2)-dependent ubiquitination

Kevin L. Lorick, +5 more
- 28 Sep 1999 - 
TL;DR: It is suggested that a large number of RING finger-containing proteins, with otherwise diverse structures and functions, may play previously unappreciated roles in modulating protein levels via ubiquitination.
Journal ArticleDOI

Mdm2 Is a RING Finger-dependent Ubiquitin Protein Ligase for Itself and p53

Shengyun Fang, +4 more
- 24 Mar 2000 - 
TL;DR: Mdm2 is a ubiquitin protein ligase (E3) for p53 and that its activity is dependent on its RING finger, and it is shown that Mdm2 mediates its own ubiquitination in a Ringing finger-dependent manner, which requires no eukaryotic proteins other than ubiquitIn-activating enzyme (E1) and an ubiquit in-conjugating enzyme(E2).
Journal ArticleDOI

Ubiquitin protein ligase activity of IAPs and their degradation in proteasomes in response to apoptotic stimuli.

Yili Yang, +4 more
- 05 May 2000 - 
TL;DR: Whether proteasomes degrade anti-apoptotic molecules in cells induced to undergo apoptosis is examined, and autoubiquitination and degradation of IAPs may be a key event in the apoptotic program.