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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.

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A General Mass Spectrometry-Based Assay for the Quantitation of Protein−Ligand Binding Interactions in Solution [J. Am. Chem. Soc. 2002, 124, 10256−10257].

TL;DR: A new method that utilizes matrix-assisted laser desorption/ionization (MALDI) mass spectrometry and exploits the hydrogen/deuterium (H/D) exchange properties of proteins was developed for measuring the thermodynamic properties of protein-ligand complexes in solution.
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Interspecies Differences in Proteome Turnover Kinetics Are Correlated With Life Spans and Energetic Demands

TL;DR: It is shown that organismal lifespan is negatively correlated with turnover rates of highly abundant proteins and suggested that in lieu of rapid constitutive turnover, long-lived species may have evolved more energetically efficient mechanisms for selective detection and clearance of damaged proteins.
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Convergent Replication of Mouse Synthetic Prion Strains

TL;DR: Results indicate that synthetic prions can assume multiple intermediate conformations before converging into one conformation optimized for in vivo propagation.
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Developmentally regulated H2Av buffering via dynamic sequestration to lipid droplets in Drosophila embryos.

TL;DR: The buffering mechanism is elucidated and it is demonstrated that it is developmentally controlled, providing a mechanistic basis for the emerging role of LDs as regulators of protein homeostasis and demonstrating that LDs can control developmental progression.
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Quantitative Analysis of in Vivo Methionine Oxidation of the Human Proteome.

TL;DR: This work identifies and quantifies a number of novel sites of in vivo methionine oxidation in an unstressed human cell line by isotopically labeling unoxidized methionines with 18O labeled hydrogen peroxide and quantifying the relative ratios of 18O and 16O oxidized methamphetamineionines.