ArticleThe Journal of biological chemistry2015
Mechanism-based proteomic screening identifies targets of thioredoxin-like proteins.
Article in The Journal of biological chemistry, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.
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Who cites it
17 citing papers in PubMed, 36 citations in OpenAlex.
- Thioredoxin System in Insects: Uncovering the Roles of Thioredoxins and Thioredoxin Reductase beyond the Antioxidant Defences.Insects · 2024Review
- Thioredoxin regulates the redox state and the activity of the human tRNA ligase complex.RNA (New York, N.Y.) · 2023Article
- TXNL1 has dual functions as a redox active thioredoxin-like protein as well as an ATP- and redox-independent chaperone.Redox biology · 2023Article
- Biological and Catalytic Properties of Selenoproteins.International journal of molecular sciences · 2023Review
- Compensatory Protection of Thioredoxin-Deficient Cells from Etoposide-Induced Cell Death by Selenoprotein W via Interaction with 14-3-3.International journal of molecular sciences · 2021Article
- The Mia40/CHCHD4 Oxidative Folding System: Redox Regulation and Signaling in the Mitochondrial Intermembrane Space.Antioxidants (Basel, Switzerland) · 2021Review
- The role of TXNL1 in disease: treatment strategies for cancer and diseases with oxidative stress.Molecular biology reports · 2021Review
- The Mysterious Multitude: Structural Perspective on the Accessory Subunits of Respiratory Complex I.Frontiers in molecular biosciences · 2021Review
- Redox Systems Biology: Harnessing the Sentinels of the Cysteine Redoxome.Antioxidants & redox signaling · 2020Review
- A disease-associated Aifm1 variant induces severe myopathy in knockin mice.Molecular metabolism · 2018Article
- Apoptosis-Inducing Factor (AIF) in Physiology and Disease: The Tale of a Repented Natural Born Killer.EBioMedicine · 2018Review
- Thioredoxin Profiling of Multiple Thioredoxin-Like Proteins inFrontiers in microbiology · 2018Article
- Differences in Reperfusion-Induced Mitochondrial Oxidative Stress and Cell Death Between Hippocampal CA1 and CA3 Subfields Are Due to the Mitochondrial Thioredoxin System.Antioxidants & redox signaling · 2017Article
- Defining NADH-Driven Allostery Regulating Apoptosis-Inducing Factor.Structure (London, England : 1993) · 2016Article
- Trapping redox partnerships in oxidant-sensitive proteins with a small, thiol-reactive cross-linker.Free radical biology & medicine · 2016Article
- Multifunctional Thioredoxin-Like Protein from the Gastrointestinal Parasitic NematodesJournal of parasitology research · 2016Article
- MIEN1 promotes oral cancer progression and implicates poor overall survival.Cancer biology & therapy · 2015Article
Corrections and comments
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Authors and funding
7 authors at 3 institutions in 2 countries.
Funding
Abstract
Thioredoxin (Trx)-fold proteins are protagonists of numerous cellular pathways that are subject to thiol-based redox control. The best characterized regulator of thiols in proteins is Trx1 itself, which together with thioredoxin reductase 1 (TR1) and peroxiredoxins (Prxs) comprises a key redox regulatory system in mammalian cells. However, there are numerous other Trx-like proteins, whose functions and redox interactors are unknown. It is also unclear if the principles of Trx1-based redox control apply to these proteins. Here, we employed a proteomic strategy to four Trx-like proteins containing CXXC motifs, namely Trx1, Rdx12, Trx-like protein 1 (Txnl1) and nucleoredoxin 1 (Nrx1), whose cellular targets were trapped in vivo using mutant Trx-like proteins, under conditions of low endogenous expression of these proteins. Prxs were detected as key redox targets of Trx1, but this approach also supported the detection of TR1, which is the Trx1 reductant, as well as mitochondrial intermembrane proteins AIF and Mia40. In addition, glutathione peroxidase 4 was found to be a Rdx12 redox target. In contrast, no redox targets of Txnl1 and Nrx1 could be detected, suggesting that their CXXC motifs do not engage in mixed disulfides with cellular proteins. For some Trx-like proteins, the method allowed distinguishing redox and non-redox interactions. Parallel, comparative analyses of multiple thiol oxidoreductases revealed differences in the functions of their CXXC motifs, providing important insights into thiol-based redox control of cellular processes.
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