K
Kenny K.K. Chung
Researcher at Hong Kong University of Science and Technology
Publications - 35
Citations - 5118
Kenny K.K. Chung is an academic researcher from Hong Kong University of Science and Technology. The author has contributed to research in topics: Parkin & Ubiquitin ligase. The author has an hindex of 23, co-authored 35 publications receiving 4890 citations. Previous affiliations of Kenny K.K. Chung include Johns Hopkins University School of Medicine & Johns Hopkins University.
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Journal ArticleDOI
Parkin functions as an E2-dependent ubiquitin– protein ligase and promotes the degradation of the synaptic vesicle-associated protein, CDCrel-1
TL;DR: It is suggested that Parkin functions as an E3 ubiquitin-protein ligase through its ring domains and that it may control protein levels via ubiquitination.
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Parkin ubiquitinates the α-synuclein–interacting protein, synphilin-1: implications for Lewy-body formation in Parkinson disease
Kenny K.K. Chung,Yi Zhang,Kah-Leong Lim,Yuji Tanaka,Hui Huang,Jun Gao,Christopher A. Ross,Valina L. Dawson,Ted M. Dawson +8 more
TL;DR: It is shown that parkin interacts with and ubiquitinates the α-synuclein–interacting protein, synphilin-1, which provides a molecular basis for the ubiquitination of Lewy-body–associated proteins and links parkin and α- synuclein in a common pathogenic mechanism through their interaction with synphil in-1.
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S-Nitrosylation of Parkin Regulates Ubiquitination and Compromises Parkin's Protective Function
Kenny K.K. Chung,Bobby Thomas,Xiaojie Li,Olga Pletnikova,Juan C. Troncoso,Laura Marsh,Valina L. Dawson,Ted M. Dawson +7 more
TL;DR: It is shown that parkin is S-nitrosylated in vitro, as well as in vivo in a mouse model of PD and in brains of patients with PD and diffuse Lewy body disease, which could contribute to the degenerative process in these disorders by impairing the ubiquitination of parkin substrates.
Journal ArticleDOI
Parkin mediates nonclassical, proteasomal-independent ubiquitination of synphilin-1 : implications for Lewy body formation
Kah-Leong Lim,Katherine C. M. Chew,Jeanne M.M. Tan,Cheng Wang,Kenny K.K. Chung,Yi Zhang,Yuji Tanaka,Yuji Tanaka,Wanli W. Smith,Simone Engelender,Christopher A. Ross,Valina L. Dawson,Ted M. Dawson +12 more
TL;DR: The results suggest that parkin is a dual-function ubiquitin ligase and that K63-linked ubiquitination of synphilin-1 by parkin may be involved in the formation of Lewy body inclusions associated with PD.
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Oxidative and nitrosative stress in Parkinson's disease
TL;DR: Thorough understanding of how oxidative stress can contribute to the pathogenesis of PD will help formulate potential therapy for the treatment of this neurodegenerative disorder in the future.