R
Reshma Shringarpure
Researcher at University of Southern California
Publications - 9
Citations - 1516
Reshma Shringarpure is an academic researcher from University of Southern California. The author has contributed to research in topics: Proteasome & Proteolysis. The author has an hindex of 9, co-authored 9 publications receiving 1467 citations.
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Ubiquitin Conjugation Is Not Required for the Degradation of Oxidized Proteins by Proteasome
TL;DR: Contrary to earlier popular belief that most proteasomal degradation is conducted by the 26 S proteasome with ubiquitinylated substrates, this work suggests that oxidized proteins are degraded without ubiquitin conjugation (or ATP hydrolysis) possibly by the 20 S protease, or the immunoproteasome, or both.
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Protein turnover by the proteasome in aging and disease.
TL;DR: Considerable evidence now indicates that proteasome activity declines during aging, as the protease is progressively inhibited by binding to ever increasing levels of oxidized and cross-linked protein aggregates.
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Protein oxidation and 20S proteasome-dependent proteolysis in mammalian cells.
TL;DR: Interestingly, it appears that the 20S 'core' proteasome conducts the recognition and elimination of oxidized proteins in an ATP-independent and ubiquitin-independent pathway.
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Age-related changes in protein oxidation and proteolysis in mammalian cells.
TL;DR: Evidence indicates that proteasome activity does, indeed, decline during aging as the enzyme complex is progressively inhibited by oxidized and cross-linked protein aggregates, and it is proposed that cellular aging involves both an increase in (mitochondrial) oxidant production and a progressive decline in proteAsome activity.
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4-Hydroxynonenal-modified amyloid-beta peptide inhibits the proteasome: possible importance in Alzheimer's disease.
TL;DR: This work investigated the proteasome inhibitory action of Aβ1–40 (a peptide comprising the first 40 residues of A β) modified by the intracellular oxidant hydrogen peroxide, and by the lipid peroxidation product 4-hydroxynonenal.