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K. Matthew Scaglione

Researcher at Duke University

Publications -  33
Citations -  3568

K. Matthew Scaglione is an academic researcher from Duke University. The author has contributed to research in topics: Ubiquitin & Ubiquitin ligase. The author has an hindex of 18, co-authored 28 publications receiving 2386 citations. Previous affiliations of K. Matthew Scaglione include Medical College of Wisconsin & Saint Louis University.

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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.
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Certain pairs of ubiquitin-conjugating enzymes (E2s) and ubiquitin-protein ligases (E3s) synthesize nondegradable forked ubiquitin chains containing all possible isopeptide linkages.

Hyoung Tae Kim, +8 more
- 15 Jun 2007 - 
TL;DR: It is found that the U-box E3, CHIP, and Ring finger E3s, MuRF1 and Mdm2, with the E2, UbcH5, form a novel type of Ub chain that contains all seven possible linkages, but predominantly Lys48, Lys63, and Lys11 linkages.
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CGG Repeat-Associated Translation Mediates Neurodegeneration in Fragile X Tremor Ataxia Syndrome

Peter K. Todd, +17 more
- 08 May 2013 - 
TL;DR: It is demonstrated that CGG repeats trigger repeat-associated non-AUG-initiated (RAN) translation of a cryptic polyglycine-containing protein, FMRpolyG, which accumulates in ubiquitin-positive inclusions in Drosophila, cell culture, mouse disease models, and FXTAS patient brains.
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Accelerated neurodegeneration through chaperone-mediated oligomerization of tau

Laura J. Blair, +19 more
- 01 Oct 2013 - 
TL;DR: Overexpression of FKBP51 in a tau transgenic mouse model revealed that FK BP51 preserved the species of tau that have been linked to Alzheimer's disease (AD) pathogenesis, blocked amyloid formation, and decreased tangle load in the brain.
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The Deubiquitinating Enzyme Ataxin-3, a Polyglutamine Disease Protein, Edits Lys63 Linkages in Mixed Linkage Ubiquitin Chains

Brett J. Winborn, +8 more
- 26 Sep 2008 - 
TL;DR: Findings establish ataxin-3 as a novel DUB that edits topologically complex chains that binds and cleaves ubiquitin chains in a manner suggesting that it functions as a mixed linkage, chain-editing enzyme.