ArticleAntioxidants & redox signaling2016
Cysteine Mutational Studies Provide Insight into a Thiol-Based Redox Switch Mechanism of Metal and DNA Binding in FurA from Anabaena sp. PCC 7120.
Article in Antioxidants & redox signaling, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
What it found
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Who cites it
9 citing papers in PubMed, 18 citations in OpenAlex.
- From photosynthetic electron flow to gene regulation: redox signal transduction in cyanobacteria.FEMS microbiology reviews · 2026Review
- Reverse Thiol Trapping Approach to Assess the Thiol Status of Metal-Binding Mitochondrial Proteins.Methods in molecular biology (Clifton, N.J.) · 2024Article
- Meddling with Metal Sensors: Fur-Family Proteins as Signaling Hubs.Journal of bacteriology · 2023Review
- Glutaredoxins regulate maize inflorescence meristem development via redox control of TGA transcriptional activity.Nature plants · 2021Article
- Thioredoxin Dependent Changes in the Redox States of FurA fromAntioxidants (Basel, Switzerland) · 2021Article
- The Central Role of Redox-Regulated Switch Proteins in Bacteria.Frontiers in molecular biosciences · 2021Review
- Mechanistic insights into heme-mediated transcriptional regulation via a bacterial manganese-binding iron regulator, iron response regulator (Irr).The Journal of biological chemistry · 2020Article
- Protein S-Bacillithiolation Functions in Thiol Protection and Redox Regulation of the Glyceraldehyde-3-Phosphate Dehydrogenase Gap in Staphylococcus aureus Under Hypochlorite Stress.Antioxidants & redox signaling · 2018Article
- Proper Sterol Distribution Is Required forG3 (Bethesda, Md.) · 2016Article
Corrections and comments
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Authors and funding
10 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
aimsThe ferric uptake regulator (Fur) is the main transcriptional regulator of genes involved in iron homeostasis in most prokaryotes. FurA from Anabaena sp. PCC 7120 contains five cysteine residues, four of them arranged in two redox-active CXXC motifs. The protein needs not only metal but also reducing conditions to remain fully active in vitro. Through a mutational study of the cysteine residues present in FurA, we have investigated their involvement in metal and DNA binding.
resultsResidue C INNOVATION: We propose that C
conclusionThis mechanism supports a novel feature of a Fur protein that emerges as a regulator, which connects the response to changes in the intracellular redox state and iron management in cyanobacteria. Antioxid. Redox Signal. 00, 000-000.
Identifiers
What OpenQuestion holds
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.