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Chad A. Dickey

Researcher at University of South Florida

Publications -  145
Citations -  19491

Chad A. Dickey is an academic researcher from University of South Florida. The author has contributed to research in topics: Tau protein & Tauopathy. The author has an hindex of 55, co-authored 142 publications receiving 16240 citations. Previous affiliations of Chad A. Dickey include University of Michigan & Sewanee: The University of the South.

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Journal ArticleDOI

Guidelines for the use and interpretation of assays for monitoring autophagy (3rd edition)

Daniel J. Klionsky, +2522 more
- 21 Jan 2016 - 
TL;DR: In this paper, the authors present a set of guidelines for the selection and interpretation of methods for use by investigators who aim to examine macro-autophagy and related processes, as well as for reviewers who need to provide realistic and reasonable critiques of papers that are focused on these processes.
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Mutations in progranulin cause tau-negative frontotemporal dementia linked to chromosome 17

Matt Baker, +26 more
- 24 Aug 2006 - 
TL;DR: It is demonstrated that in multiple FTD families with significant evidence for linkage to the same region on chromosome 17q21, FTD is caused by mutations in progranulin (PGRN) that are likely to create null alleles and identified mutations in PGRN as a cause of neurodegenerative disease.
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A beta peptide vaccination prevents memory loss in an animal model of Alzheimer's disease.

Dave Morgan, +14 more
- 21 Dec 2000 - 
TL;DR: It is shown that vaccination with Aβ protects transgenic mice from the learning and age-related memory deficits that normally occur in this mouse model for Alzheimer's disease and may prevent and, possibly, treat Alzheimer's dementia.
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Amyloid Oligomers Exacerbate Tau Pathology in a Mouse Model of Tauopathy

Maj Linda B. Selenica, +7 more
- 11 Apr 2013 - 
TL;DR: The data suggest that even brief elevations in Aβ production, may have enduring impact on the risk for tauopathy, and Soluble Aβ1-42 oligomers have long-lasting effects on tau phosphorylation in the rTg4510 model.
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The high-affinity HSP90-CHIP complex recognizes and selectively degrades phosphorylated tau client proteins

Chad A. Dickey, +16 more
- 01 Mar 2007 - 
TL;DR: It is reported that inhibition of Hsp90 led to decreases in p-tau levels independent of heat shock factor 1 (HSF1) activation, and this is the first demonstration to the authors' knowledge that blockade of the refolding pathway promotes p-Tau turnover through degradation.