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Article

Multiple oxidative post-translational modifications of human glutamine synthetase mediate peroxynitrite-dependent enzyme inactivation and aggregation.

The Journal of biological chemistry - 1 Mar 2023

Campolo Nicolás, Mastrogiovanni Mauricio, Mariotti Michele, Issoglio Federico M, Estrin Darío, Hägglund Per, Grune Tilman, Davies Michael J, Bartesaghi Silvina, Radi Rafael

Abstract excerpt

Glutamine synthetase (GS), which catalyzes the ATP-dependent synthesis of L-glutamine from L-glutamate and ammonia, is a ubiquitous and conserved enzyme that plays a pivotal role in nitrogen metabolism across all life domains. In vertebrates, GS is highly expressed in astrocytes, where its activity sustains the glutamate-glutamine cycle at glutamatergic synapses and is thus essential for maintaining brain...

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Methodology Data sources Editorial policy Privacy Delete account & data About Contact Helena Bioinformatics

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Identifiers

PMID: 36702251
DOI: 10.1016/j.jbc.2023.102941
PMCID: PMC10011836

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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