ArticleThe Journal of biological chemistry2014
An extended active-site motif controls the reactivity of the thioredoxin fold.
Article in The Journal of biological chemistry, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
5 citing papers in PubMed.
- Scaling the profile of life by function with SPIN.Bioinformatics advances · 2026Article
- Unlocking Protein Evolution Insights: Efficient and Interpretable Mutational Effect Predictions with GEMME.Methods in molecular biology (Clifton, N.J.) · 2026Article
- The role and mechanism of TXNDC5 in diseases.European journal of medical research · 2022Review
- Libertellenone H, a Natural Pimarane Diterpenoid, Inhibits Thioredoxin System and Induces ROS-Mediated Apoptosis in Human Pancreatic Cancer Cells.Molecules (Basel, Switzerland) · 2021Article
- Converting a Sulfenic Acid Reductase into a Disulfide Bond Isomerase.Antioxidants & redox signaling · 2015Article
Corrections and comments
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Authors and funding
6 authors.
Funding
Abstract
Proteins belonging to the thioredoxin (Trx) superfamily are abundant in all organisms. They share the same structural features, arranged in a seemingly simple fold, but they perform a multitude of functions in oxidative protein folding and electron transfer pathways. We use the C-terminal domain of the unique transmembrane reductant conductor DsbD as a model for an in-depth analysis of the factors controlling the reactivity of the Trx fold. We employ NMR spectroscopy, x-ray crystallography, mutagenesis, in vivo functional experiments applied to DsbD, and a comparative sequence analysis of Trx-fold proteins to determine the effect of residues in the vicinity of the active site on the ionization of the key nucleophilic cysteine of the -CXXC- motif. We show that the function and reactivity of Trx-fold proteins depend critically on the electrostatic features imposed by an extended active-site motif.
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Registered trials
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