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Article

Evolution of a mass spectrometry-grade protease with PTM-directed specificity.

Proceedings of the National Academy of Sciences of the United States of America - 20 Dec 2016

Tran Duc T, Cavett Valerie J, Dang Vuong Q, Torres Héctor L, Paegel Brian M

Abstract excerpt

Mapping posttranslational modifications (PTMs), which diversely modulate biological functions, represents a significant analytical challenge. The centerpiece technology for PTM site identification, mass spectrometry (MS), requires proteolytic cleavage in the vicinity of a PTM to yield peptides for sequencing. This requirement catalyzed our efforts to evolve MS-grade mutant PTM-directed proteases. Citrulline, a...

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Identifiers

PMID: 27940920
DOI: 10.1073/pnas.1609925113
PMCID: PMC5187733

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 5 Sept 2026. Manifest publication-graph-cohort-2026-09-05.1.

Source receipt: pubmed, retrieved 5 Sept 2026.

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