scispace - formally typeset
S

Sina Ghaemmaghami

Researcher at University of Rochester

Publications -  62
Citations -  11237

Sina Ghaemmaghami is an academic researcher from University of Rochester. The author has contributed to research in topics: Proteome & Protein turnover. The author has an hindex of 24, co-authored 55 publications receiving 10170 citations. Previous affiliations of Sina Ghaemmaghami include California Institute for Quantitative Biosciences & University of California, San Francisco.

Papers
More filters
Journal ArticleDOI

Redox-mediated regulation of an evolutionarily conserved cross-β structure formed by the TDP43 low complexity domain.

TL;DR: Evidence is presented that the low complexity domain of TDP43 self-associates into a specific structural conformation that may be important to its normal biological function, including facilitating synapse-localized translation as well as aberrant aggregation of the protein in neurodegenerative diseases.
Journal ArticleDOI

Proteome-wide modulation of degradation dynamics in response to growth arrest

TL;DR: It is demonstrated that fibroblasts selectively increase degradation rates of long-lived proteins as they transition from a proliferating to a quiescent state, by the concurrent activation of lysosomal biogenesis and up-regulation of macroautophagy.
Journal ArticleDOI

A survey of antiprion compounds reveals the prevalence of non-PrP molecular targets.

TL;DR: It is suggested that in comparison to PrP conformers themselves, proteins that play auxiliary roles in prion propagation may be more effective targets for future drug discovery efforts.
Journal ArticleDOI

Pharmacokinetics of quinacrine efflux from mouse brain via the P-glycoprotein efflux transporter.

TL;DR: It is argued that the inhibition of the P-gp efflux transporter should improve the poor pharmacokinetic properties of quinacrine in the CNS.
Journal ArticleDOI

Global analysis of cellular protein flux quantifies the selectivity of basal autophagy.

TL;DR: The methodology outlined in the study provides a global strategy for quantifying the selectivity of basal macroautophagy and indicates that in quiescent fibroblasts, macroautophile contributes to the basal turnover of a substantial fraction of the proteome.