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Article

Quantitation of changes in protein phosphorylation: a simple method based on stable isotope labeling and mass spectrometry.

Proceedings of the National Academy of Sciences of the United States of America - 4 Feb 2003

Bonenfant Debora, Schmelzle Tobias, Jacinto Estela, Crespo Jose L, Mini Thierry, Hall Michael N, Jenoe Paul

Abstract excerpt

Reversible protein phosphorylation plays an important role in many cellular processes. However, a simple and reliable method to measure changes in the extent of phosphorylation is lacking. Here, we present a method to quantitate the changes in phosphorylation occurring in a protein in response to a stimulus. The method consists of three steps: (i) enzymatic digestion in H(2)16O or isotopically enriched H(2)18O to...

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Identifiers

PMID: 12540831
DOI: 10.1073/pnas.232735599
PMCID: PMC298695

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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