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Article

1H, 15N and 13C backbone and side-chain assignments of reduced and S-nitrosated C62only mutant of human thioredoxin.

Biomolecular NMR assignments - 1 Oct 2021

Almeida Vitor S, Iqbal Anwar, Almeida Fabio C L

Abstract excerpt

Thioredoxins are ubiquitous and conserved small proteins. The redox-active site is composed of highly conserved Cys32 and Cys35. In higher eukaryotes, thioredoxin evolved to a gain of function in nitrosative control, with 3 extra cysteines, Cys62, Cys69, and Cys73. Human thioredoxin 1 (hTrx) is directly involved in cellular signal transduction through S-nitrosation. The understanding of the mechanism of...

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Identifiers

PMID: 33751377
DOI: 10.1007/s12104-021-10015-w

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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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