R
Ron R. Kopito
Researcher at Stanford University
Publications - 140
Citations - 25761
Ron R. Kopito is an academic researcher from Stanford University. The author has contributed to research in topics: Ubiquitin & Proteasome. The author has an hindex of 65, co-authored 134 publications receiving 24382 citations. Previous affiliations of Ron R. Kopito include Massachusetts Institute of Technology & University of California, Berkeley.
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Journal ArticleDOI
Aggresomes: A Cellular Response to Misfolded Proteins
TL;DR: The intracellular fate of cystic fibrosis transmembrane conductance regulator (CFTR) is investigated and it is demonstrated that undegraded CFTR molecules accumulate at a distinct pericentriolar structure which is termed the aggresome.
Book
Impairment of the ubiquitin proteasome system by protein aggregation
TL;DR: It is reported that protein aggregation directly impaired the function of the ubiquitin-proteasome system, suggesting a potential mechanism linking protein aggregation to cellular disregulation and cell death.
Journal ArticleDOI
Aggresomes, inclusion bodies and protein aggregation.
TL;DR: This work has suggested that, in animal cells, aggregated proteins are specifically delivered to inclusion bodies by dynein-dependent retrograde transport on microtubules and this microtubule-dependent inclusion body is called an aggresome.
Journal ArticleDOI
Degradation of CFTR by the ubiquitin-proteasome pathway
TL;DR: It is shown that the degradation of both wild-type and mutant CFTR is inhibited by two potent proteasome inhibitors that induce the accumulation of polyubiquitinated forms of immature CFTR, confirming that ubiquitination is required for rapid CFTR degradation.
Journal ArticleDOI
Misfolded proteins partition between two distinct quality control compartments
TL;DR: The formation of misfolded protein inclusions in the eukaryotic cytosol of yeast and mammalian cell culture models is examined to provide a framework for understanding the preferential accumulation of amyloidogenic proteins in inclusions linked to human disease.