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Wei-Ling Tsou

Researcher at Wayne State University

Publications -  20
Citations -  562

Wei-Ling Tsou is an academic researcher from Wayne State University. The author has contributed to research in topics: Spinocerebellar ataxia & Neurodegeneration. The author has an hindex of 11, co-authored 16 publications receiving 405 citations. Previous affiliations of Wei-Ling Tsou include National Yang-Ming University.

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An optimal ubiquitin-proteasome pathway in the nervous system: the role of deubiquitinating enzymes

TL;DR: The argument that understanding the UPP from the perspective of DUBs can yield new insight into diseases that result from anomalous intra- cellular processes or inter-cellular networks is made.
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Nanoplastics impact the zebrafish (Danio rerio) transcriptome: Associated developmental and neurobehavioral consequences.

TL;DR: Results of this study suggest that NPs can accumulate in the tissues of larval zebrafish, alter their transcriptome, and affect behavior and physiology, potentially decreasing organismal fitness in contaminated ecosystems.
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Systematic analysis of the physiological importance of deubiquitinating enzymes

TL;DR: The physiological significance of the DUB family of enzymes in intact animals is demonstrated, there is little functional redundancy among members of this family of proteases, and insight is provided for future investigations to understand DUB biology at the molecular, cellular and organismal levels.
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Ubiquitin-binding site 2 of ataxin-3 prevents its proteasomal degradation by interacting with Rad23

TL;DR: It is shown that, unlike most proteins, ataxin-3 turnover does not require its ubiquitination, but is regulated by Ubiquitin-Binding Site 2 (UbS2) on its N terminus, and that UbS2 is a potential target through which to enhance ataxIn-3 degradation for SCA3 therapy.
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Ubiquitination regulates the neuroprotective function of the deubiquitinase ataxin-3 in vivo.

TL;DR: It is reported that ubiquitination of the DUB ataxin-3 at lysine residue 117, which markedly enhances its protease activity in vitro, is critical for its ability to suppress toxic protein-dependent degeneration in Drosophila melanogaster.