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Article

Functional analysis of paralogous thiol-disulfide oxidoreductases in Streptococcus gordonii.

The Journal of biological chemistry - 7 Jun 2013

Davey Lauren, Ng Crystal K W, Halperin Scott A, Lee Song F

Abstract excerpt

Disulfide bonds are important for the stability of many extracellular proteins, including bacterial virulence factors. Formation of these bonds is catalyzed by thiol-disulfide oxidoreductases (TDORs). Little is known about their formation in Gram-positive bacteria, particularly among facultative anaerobic Firmicutes, such as streptococci. To investigate disulfide bond formation in Streptococcus gordonii, we...

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Identifiers

PMID: 23615907
DOI: 10.1074/jbc.M113.464578
PMCID: PMC3675578

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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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