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Steven P. Gygi

Researcher at Harvard University

Publications -  778
Citations -  147003

Steven P. Gygi is an academic researcher from Harvard University. The author has contributed to research in topics: Proteome & Phosphorylation. The author has an hindex of 172, co-authored 704 publications receiving 129173 citations. Previous affiliations of Steven P. Gygi include University of Rochester Medical Center & Cell Signaling Technology.

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Changes in cell morphology are coordinated with cell growth through the TORC1 pathway.

TL;DR: In this article, the authors demonstrate that the actin cytoskeleton polarization of yeast inhibits the highly conserved Target of Rapamycin Complex 1 (TORC1) pathway, and that this mechanism serves to coordinate the ability of cells to increase in size with their biosynthetic capacity.
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Reconstitution of the Mycobacterium tuberculosis pupylation pathway in Escherichia coli

TL;DR: Surprisingly, Pup and PafA were sufficient to pupylate at least 51 E. coli proteins in addition to the mycobacterial proteins, suggesting that pupylation signals are intrinsic to targeted proteins and might not require Mycobacterium‐specific cofactors for substrate recognition by PAFA in vivo.
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Cogenerating Synthetic Parts toward a Self-Replicating System.

TL;DR: It is shown that using stable isotope labeling with amino acids, mass spectrometry based quantitative proteomics could detect 26 of the 33 50S and 20 of the 21 30S subunit r-proteins when coexpressed in batch format PURE system and points to what is still needed to obtain self-replicating synthetic ribosomes in situ in the PURES system.
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Nicotine-induced protein expression profiling reveals mutually altered proteins across four human cell lines.

TL;DR: Perturbations in protein levels resulting from nicotine treatment in four cell lines are measured using tandem mass tags (TMT10‐plex) and high‐resolution mass spectrometry to highlight proteins, including APP, APLP2, LAPTM4B, and NCOA4, which were dysregulated by nicotine in all cell lines investigated and may have implications in downstream signaling pathways, particularly autophagy.
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Generation of multiple reporter ions from a single isobaric reagent increases multiplexing capacity for quantitative proteomics

TL;DR: This work presents Combinatorial Isobaric Mass Tags (CMTs), an isobaric labeling architecture with the unique ability to generate multiple series of reporter ions simultaneously, and demonstrates that utilization of multiple reporter ion series improves multiplexing capacity of CMT.