MassIVE MSV000090778

Partial Public

Direct mapping of ligandable tyrosines and lysines in cells with chiral sulfonyl fluoride probes

Description

Advances in chemoproteomic technology have revealed covalent interactions between small molecules and protein nucleophiles, primarily cysteine, on a proteome-wide scale. Most chemoproteomic screening approaches are indirect, relying on competition between electrophilic fragments and a minimalist electrophilic probe with inherently limited proteome coverage. Here, we develop a chemoproteomic platform for direct electrophile-site identification based on enantiomeric pairs of clickable arylsulfonyl fluoride probes. Using stereoselective site modification as a proxy for ligandability in intact cells, we identified 634 tyrosines and lysines within functionally diverse protein sites, liganded by structurally diverse probes. [doi:10.25345/C5C24QS42] [dataset license: CC0 1.0 Universal (CC0 1.0)]

Keywords: TMT quantification

Contact

Principal Investigators:
(in alphabetical order)
Jack Taunton, University of California, San Francisco, United States
Submitting User: yingchen_jacktauntonlab
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Identification Results
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Originally identified proteins that were automatically remapped by MassIVE to proteins in the SwissProt human reference database.

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Number of distinct proteins found to be differentially abundant in at least one comparison across all analyses (original submission and reanalyses) associated with this dataset.

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Distinct protein accessions are counted across all files submitted in the "Statistical Analysis of Quantified Analytes" category having a "Protein" column in this dataset.

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