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.
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Journal ArticleDOI
Global analysis of protein expression in yeast
Sina Ghaemmaghami,Won-Ki Huh,Kiowa Bower,Russell W. Howson,Archana Belle,Noah Dephoure,Erin K. O'Shea,Jonathan S. Weissman +7 more
TL;DR: A Saccharomyces cerevisiae fusion library is created where each open reading frame is tagged with a high-affinity epitope and expressed from its natural chromosomal location, and it is found that about 80% of the proteome is expressed during normal growth conditions.
Journal ArticleDOI
Genome-Wide Analysis in Vivo of Translation with Nucleotide Resolution Using Ribosome Profiling
TL;DR: A ribosomesome-profiling strategy based on the deep sequencing of ribosome-protected mRNA fragments is presented and enables genome-wide investigation of translation with subcodon resolution and is used to monitor translation in budding yeast under both rich and starvation conditions.
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Single-cell proteomic analysis of S. cerevisiae reveals the architecture of biological noise
John R. S. Newman,Sina Ghaemmaghami,Sina Ghaemmaghami,Jan Ihmels,David K. Breslow,Matthew Noble,Joseph L. DeRisi,Joseph L. DeRisi,Jonathan S. Weissman +8 more
TL;DR: A strategy that pairs high-throughput flow cytometry and a library of GFP-tagged yeast strains to monitor rapidly and precisely protein levels at single-cell resolution is presented, revealing a remarkable structure to biological noise.
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Analysis of proteome dynamics in the mouse brain
TL;DR: The developed methodology can be adapted to assess in vivo proteome homeostasis in any model organism that will tolerate a labeled diet and may be particularly useful in the analysis of neurodegenerative diseases in vivo.
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Quantitative protein stability measurement in vivo.
TL;DR: The results indicate that the thermodynamic stability of monomeric λ repressor within the cell is the same as its stability measured in a simple buffer in vitro, but when the E. coli are placed in a hyperosmotic environment, the in vivo stability is greatly enhanced.