J
Jeffery W. Kelly
Researcher at Scripps Research Institute
Publications - 447
Citations - 45397
Jeffery W. Kelly is an academic researcher from Scripps Research Institute. The author has contributed to research in topics: Transthyretin & Amyloid disease. The author has an hindex of 108, co-authored 428 publications receiving 41240 citations. Previous affiliations of Jeffery W. Kelly include University of North Carolina at Chapel Hill & Texas A&M University.
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Adapting proteostasis for disease intervention.
TL;DR: The proteostasis network is described, a set of interacting activities that maintain the health of proteome and the organism that has the potential to ameliorate some of the most challenging diseases of this era.
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Biological and Chemical Approaches to Diseases of Proteostasis Deficiency
TL;DR: It is proposed that small molecules can enhance proteostasis by binding to and stabilizing specific proteins (pharmacologic chaperones) or by increasing the protestasis network capacity (proteostasis regulators) and that such therapeutic strategies, including combination therapies, represent a new approach for treating a range of diverse human maladies.
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The alternative conformations of amyloidogenic proteins and their multi-step assembly pathways
TL;DR: The conformational change hypothesis postulates that tertiary structural changes under partially denaturing conditions convert one of 17 normally soluble and functional human proteins into an alternative conformation that subsequently undergoes self-assembly into an amyloid fibril, the putative causative agent in amyloids disease.
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Functional amyloid--from bacteria to humans.
TL;DR: A greater understanding of the diverse physiological applications of this fold has the potential to provide a fresh perspective for the treatment of amyloid diseases.
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Opposing Activities Protect Against Age-Onset Proteotoxicity
TL;DR: Because the IIS pathway is central to the regulation of longevity and youthfulness in worms, flies, and mammals, these results suggest a mechanistic link between the aging process and aggregation-mediated proteotoxicity.