Jeffery W. Kelly
Scripps Research Institute
447 Papers
4.7K Citations
Jeffery W. Kelly is an academic researcher from Scripps Research Institute. The author has contributed to research in topics: Transthyretin & Chemistry. The author has an hindex of 108, co-authored 428 publications. Previous affiliations of Jeffery W. Kelly include University of North Carolina at Chapel Hill & Texas A&M University.
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Papers
Mechanisms of amyloidogenesis
TL;DR: A fourth model — nucleated conformational conversion — that invokes oligomeric intermediates for initiation and assembly of amyloid fibril assembly is introduced.
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The oxidative stress metabolite 4-hydroxynonenal promotes Alzheimer protofibril formation.
TL;DR: 4-HNE accelerates the formation of Abeta protofibrils while inhibiting the production of straight, mature fibrils, providing further incentive to understand the role of oxidative stress and small-molecule Abeta modifications in sporadic AD.
Pharmacologic ATF6 activation confers global protection in widespread disease models by reprograming cellular proteostasis
Erik A Blackwood,Khalid Azizi,Donna J. Thuerauf,Ryan J Paxman,Lars Plate,Jeffery W. Kelly,R. Luke Wiseman,Christopher C. Glembotski +7 more
TL;DR: It is shown that the ATF6 arm of the unfolded protein response can be pharmacologically activated with a small molecule in vivo, providing protection from ischemia/reperfusion injury in the heart, the brain, and the kidney.
The V122I cardiomyopathy variant of transthyretin increases the velocity of rate-limiting tetramer dissociation, resulting in accelerated amyloidosis
TL;DR: The increase in the velocity of rate-limiting tetramer dissociation coupled with the lowered tetramer stability may explain why V122I confers an apparent absolute anatomic risk for cardiac amyloid deposition.
172
An Adaptable Standard for Protein Export from the Endoplasmic Reticulum
R. Luke Wiseman,R. Luke Wiseman,Evan T. Powers,Evan T. Powers,Joel N. Buxbaum,Jeffery W. Kelly,Jeffery W. Kelly,William E. Balch,William E. Balch +8 more
TL;DR: A model of folding for export (FoldEx) establishes that no single feature dictates folding and transport efficiency, and a network view provides insight into the basis for cellular diversity, disease origins, and proteinHomeostasis, and predicts strategies for restoring protein homeostasis in protein-misfolding diseases.
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