ReviewCellular and molecular life sciences : CMLS2010
Multiple catalytically active thioredoxin folds: a winning strategy for many functions.
Review in Cellular and molecular life sciences : CMLS, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.
What it found
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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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Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
19 citing papers in PubMed, 32 citations in OpenAlex.
- Identification and characterization of TrxA: a novel bacterial thioredoxin-metallothionein chimera.Applied microbiology and biotechnology · 2026Article
- A universal cis-proline lock defines catalysis in thioredoxin-fold enzymes.Communications biology · 2026Article
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- Article
- Discovering Antioxidant Molecules in the Archaea Domain: Peroxiredoxin Bcp1 fromArchaea (Vancouver, B.C.) · 2016Article
- In Vivo Formation of the Protein Disulfide Bond That Enhances the Thermostability of Diphosphomevalonate Decarboxylase, an Intracellular Enzyme from the Hyperthermophilic Archaeon Sulfolobus solfataricus.Journal of bacteriology · 2015Article
- Loss of APD1 in yeast confers hydroxyurea sensitivity suppressed by Yap1p transcription factor.Scientific reports · 2015Article
- Crystal structure of mammalian selenocysteine-dependent iodothyronine deiodinase suggests a peroxiredoxin-like catalytic mechanism.Proceedings of the National Academy of Sciences of the United States of America · 2014Article
- Functional and structural characterization of protein disulfide oxidoreductase from Thermus thermophilus HB27.Extremophiles : life under extreme conditions · 2014Article
- Sulfolobus solfataricus thiol redox puzzle: characterization of an atypical protein disulfide oxidoreductase.Extremophiles : life under extreme conditions · 2014Article
- Lemon protein disulfide isomerase: cDNA cloning and biochemical characterization.Botanical studies · 2013Article
- Structural and biochemical characterization of the essential DsbA-like disulfide bond forming protein from Mycobacterium tuberculosis.BMC structural biology · 2013Article
- Thioredoxin and thioredoxin target proteins: from molecular mechanisms to functional significance.Antioxidants & redox signaling · 2013Review
- Peroxiredoxins in parasites.Antioxidants & redox signaling · 2012Review
- Proteomic analysis of Sulfolobus solfataricus during Sulfolobus Turreted Icosahedral Virus infection.Journal of proteome research · 2012Article
- Thiol/Disulfide system plays a crucial role in redox protection in the acidophilic iron-oxidizing bacterium Leptospirillum ferriphilum.PloS one · 2012Article
- Solution structure of the oncogenic MIEN1 protein reveals a thioredoxin-like fold with a redox-active motif.PloS one · 2012Article
- Atomic resolution insights into curli fiber biogenesis.Structure (London, England : 1993) · 2011Article
- Topological variation in the evolution of new reactions in functionally diverse enzyme superfamilies.Current opinion in structural biology · 2011Review
Corrections and comments
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Authors and funding
5 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The Thioredoxin (Trx) fold is a versatile protein scaffold consisting of a four-stranded β-sheet surrounded by three α-helices. Various insertions are possible on this structural theme originating different proteins, which show a variety of functions and specificities. During evolution, the assembly of different Trx fold domains has been used many times to build new multi-domain proteins able to perform a large number of catalytic functions. To clarify the interaction mode of the different Trx domains within a multi-domain structure and how their combination can affect catalytic performances, in this review, we report on a structural and functional analysis of the most representative proteins containing more than one catalytically active Trx domain: the eukaryotic protein disulfide isomerases (PDIs), the thermophilic protein disulfide oxidoreductases (PDOs) and the hybrid peroxiredoxins (Prxs).
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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.