ArticlePLoS computational biology2009
An atlas of the thioredoxin fold class reveals the complexity of function-enabling adaptations.
Article in PLoS computational biology, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 72 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
72 citing papers in PubMed, 140 citations in OpenAlex.
- The emerging role of calsequestrin 2: from calcium sensor and modulator to arrhythmia driver.Journal of physiology and biochemistry · 2026Review
- SH3BGRL proteins are thioredoxin fold-containing actin filament pointed end capping proteins (TPECs).Scientific reports · 2026Article
- TXNL1 in redox and protein quality control: mechanisms and disease relevance.Frontiers in cell and developmental biology · 2026Review
- Copper Activates a Redox Switch to Reversibly Inhibit Glyceraldehyde-3-Phosphate Dehydrogenase.Biochemistry · 2025Article
- Comparative Quantitative Proteomic Analysis of High and Low Toxin-ProducingMarine drugs · 2025Article
- Unveiling the versatility of the thioredoxin framework: Insights from the structural examination ofComputational and structural biotechnology journal · 2024Article
- Resistance to freezing conditions of endemic Antarctic polychaetes is enhanced by cryoprotective proteins produced by their microbiome.Science advances · 2024Article
- The Structural Biology of Catalase Evolution.Sub-cellular biochemistry · 2024Review
- TXNL1 has dual functions as a redox active thioredoxin-like protein as well as an ATP- and redox-independent chaperone.Redox biology · 2023Article
- Two disulfide-reducing pathways are required for the maturation of plastid c-type cytochromes in Chlamydomonas reinhardtii.Genetics · 2023Article
- The Importance of Thioredoxin-1 in Health and Disease.Antioxidants (Basel, Switzerland) · 2023Review
- Article
- AC81 Is a Putative Disulfide Isomerase Involved in Baculoviral Disulfide Bond Formation.Journal of virology · 2022Article
- DciA Helicase Operators Exhibit Diversity across Bacterial Phyla.Journal of bacteriology · 2022Article
- A glance at post-translational modifications of human thyroglobulin: potential impact on function and pathogenesis.European thyroid journal · 2022Review
- Bioinformatic Analyses of Peroxiredoxins and RF-Prx: A Random Forest-Based Predictor and Classifier for Prxs.Methods in molecular biology (Clifton, N.J.) · 2022Article
- Crystal structure of plasmoredoxin, a redox-active protein unique for malaria parasites.Current research in structural biology · 2022Article
- Redox interactome in malaria parasite Plasmodium falciparum.Parasitology research · 2021Review
- Visualizing the superfamily of metallo-β-lactamases through sequence similarity network neighborhood connectivity analysis.Heliyon · 2021Article
- The bacterial copper resistance protein CopG contains a cysteine-bridged tetranuclear copper cluster.The Journal of biological chemistry · 2020Article
12 more citing papers are in PubMed but not listed here.
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
The group of proteins that contain a thioredoxin (Trx) fold is huge and diverse. Assessment of the variation in catalytic machinery of Trx fold proteins is essential in providing a foundation for understanding their functional diversity and predicting the function of the many uncharacterized members of the class. The proteins of the Trx fold class retain common features-including variations on a dithiol CxxC active site motif-that lead to delivery of function. We use protein similarity networks to guide an analysis of how structural and sequence motifs track with catalytic function and taxonomic categories for 4,082 representative sequences spanning the known superfamilies of the Trx fold. Domain structure in the fold class is varied and modular, with 2.8% of sequences containing more than one Trx fold domain. Most member proteins are bacterial. The fold class exhibits many modifications to the CxxC active site motif-only 56.8% of proteins have both cysteines, and no functional groupings have absolute conservation of the expected catalytic motif. Only a small fraction of Trx fold sequences have been functionally characterized. This work provides a global view of the complex distribution of domains and catalytic machinery throughout the fold class, showing that each superfamily contains remnants of the CxxC active site. The unifying context provided by this work can guide the comparison of members of different Trx fold superfamilies to gain insight about their structure-function relationships, illustrated here with the thioredoxins and peroxiredoxins.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.