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J. Fred Dice

Researcher at Tufts University

Publications -  43
Citations -  8623

J. Fred Dice is an academic researcher from Tufts University. The author has contributed to research in topics: Chaperone-mediated autophagy & Protein degradation. The author has an hindex of 29, co-authored 43 publications receiving 8118 citations. Previous affiliations of J. Fred Dice include Harvard University & University of California, Santa Cruz.

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Journal ArticleDOI

Guidelines for the use and interpretation of assays for monitoring autophagy in higher eukaryotes

Daniel J. Klionsky, +235 more
- 16 Feb 2008 - 
TL;DR: A set of guidelines for the selection and interpretation of the methods that can be used by investigators who are attempting to examine macroautophagy and related processes, as well as by reviewers who need to provide realistic and reasonable critiques of papers that investigate these processes are presented.
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A role for a 70-kilodalton heat shock protein in lysosomal degradation of intracellular proteins

TL;DR: A 73-kilodalton protein was found to bind to peptide regions that target intracellular proteins for lysosomal degradation in response to serum withdrawal, and sequences of two internal peptides of the 73-kD protein confirm that it is a member of this family.
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A Receptor for the Selective Uptake and Degradation of Proteins by Lysosomes

TL;DR: Overexpression of human LGP96 in Chinese hamster ovary cells increased the activity of the selective lysosomal proteolytic pathway in vivo and in vitro.
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Age-related decline in chaperone-mediated autophagy.

TL;DR: A progressive age-related decrease in the levels of the lysosome-associated membrane protein type 2a that acts as a receptor for chaperone-mediated autophagy was responsible for decreased substrate binding in lysOSomes from old rats as well as from late passage human fibroblasts.
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Chaperone-Mediated Autophagy

TL;DR: Results show that CMA is also activated by oxidative stress, and in this case LAMP-2A is increased due to transcriptional regulation, and a rich complexity of mechanisms to control CMA activity is revealed.