ArticleProceedings of the National Academy of Sciences of the United States of America2015
A universal entropy-driven mechanism for thioredoxin-target recognition.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 33 papers.
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Who cites it
33 citing papers in PubMed, 62 citations in OpenAlex.
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- Homeostatic regulation of NAD(H) and NADP(H) in cells.Genes & diseases · 2024Review
- Citrus Flavanone Effects on the Nrf2-Keap1/GSK3/NF-κB/NLRP3 Regulation and Corticotroph-Stress Hormone Loop in the Old Pituitary.International journal of molecular sciences · 2024Article
- Disulfidptosis, A Novel Cell Death Pathway: Molecular Landscape and Therapeutic Implications.Aging and disease · 2024Review
- Protein Tyrosine Phosphatase regulation by Reactive Oxygen Species.Advances in cancer research · 2024Review
- Oxidative Stress in Healthy and Pathological Red Blood Cells.Biomolecules · 2023Review
- Emerging Chemical Biology of Protein Persulfidation.Antioxidants & redox signaling · 2023Review
- Article
- Glutamine metabolism in cancers: Targeting the oxidative homeostasis.Frontiers in oncology · 2022Review
- Prdx1 Interacts with ASK1 upon Exposure to HAntioxidants (Basel, Switzerland) · 2021Article
- Selective redox signaling shapes plant-pathogen interactions.Plant physiology · 2021Review
- Fighting Oxidative Stress with Sulfur: Hydrogen Sulfide in the Renal and Cardiovascular Systems.Antioxidants (Basel, Switzerland) · 2021Review
- Molecular Basis for the Interactions of Human Thioredoxins with Their Respective Reductases.Oxidative medicine and cellular longevity · 2021Article
- NADPH homeostasis in cancer: functions, mechanisms and therapeutic implications.Signal transduction and targeted therapy · 2020Review
- The mammalian cytosolic thioredoxin reductase pathway acts via a membrane protein to reduce ER-localised proteins.Journal of cell science · 2020Article
- Persulfidation-based Modification of Cysteine Desulfhydrase and the NADPH Oxidase RBOHD Controls Guard Cell Abscisic Acid Signaling.The Plant cell · 2020Article
- Selective Persulfide Detection Reveals Evolutionarily Conserved Antiaging Effects of S-Sulfhydration.Cell metabolism · 2019Article
- Substrate specificity of thioredoxins and glutaredoxins - towards a functional classification.Heliyon · 2019Article
- An interplay of structure and intrinsic disorder in the functionality of peptidylarginine deiminases, a family of key autoimmunity-related enzymes.Cellular and molecular life sciences : CMLS · 2019Review
Corrections and comments
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
Cysteine residues in cytosolic proteins are maintained in their reduced state, but can undergo oxidation owing to posttranslational modification during redox signaling or under conditions of oxidative stress. In large part, the reduction of oxidized protein cysteines is mediated by a small 12-kDa thiol oxidoreductase, thioredoxin (Trx). Trx provides reducing equivalents for central metabolic enzymes and is implicated in redox regulation of a wide number of target proteins, including transcription factors. Despite its importance in cellular redox homeostasis, the precise mechanism by which Trx recognizes target proteins, especially in the absence of any apparent signature binding sequence or motif, remains unknown. Knowledge of the forces associated with the molecular recognition that governs Trx-protein interactions is fundamental to our understanding of target specificity. To gain insight into Trx-target recognition, we have thermodynamically characterized the noncovalent interactions between Trx and target proteins before S-S reduction using isothermal titration calorimetry (ITC). Our findings indicate that Trx recognizes the oxidized form of its target proteins with exquisite selectivity, compared with their reduced counterparts. Furthermore, we show that recognition is dependent on the conformational restriction inherent to oxidized targets. Significantly, the thermodynamic signatures for multiple Trx targets reveal favorable entropic contributions as the major recognition force dictating these protein-protein interactions. Taken together, our data afford significant new insight into the molecular forces responsible for Trx-target recognition and should aid the design of new strategies for thiol oxidoreductase inhibition.
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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.