ArticleBiometals : an international journal on the role of metal ions in biology, biochemistry, and medicine2011
The ArsD As(III) metallochaperone.
Article in Biometals : an international journal on the role of metal ions in biology, biochemistry, and medicine, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
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.
The trial behind it
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.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
16 citing papers in PubMed, 40 citations in OpenAlex.
- Synergistic function of ars genes in arsenic detoxification and biosynthesis of organoarsenicals.Biometals : an international journal on the role of metal ions in biology, biochemistry, and medicine · 2026Review
- Mechanisms of Arsenic Interaction inInternational journal of molecular sciences · 2025Review
- Biosensor-aided isolation of anaerobic arsenic-methylating bacteria from soil.ISME communications · 2025Article
- Bacterial approaches to sensing and responding to respiration and respiration metabolites.Molecular microbiology · 2021Review
- Comamonas testosteroni antA encodes an antimonite-translocating P-type ATPase.The Science of the total environment · 2021Article
- Microbes involved in arsenic mobilization and respiration: a review on isolation, identification, isolates and implications.Environmental geochemistry and health · 2020Review
- The Human Gut Microbiome's Influence on Arsenic Toxicity.Current pharmacology reports · 2019Article
- A global survey of arsenic-related genes in soil microbiomes.BMC biology · 2019Article
- Heavy Metal Susceptibility of Escherichia coli Isolated from Urine Samples from Sweden, Germany, and Spain.Antimicrobial agents and chemotherapy · 2018Article
- Transcriptomic Analysis Reveals Adaptive Responses of an Enterobacteriaceae Strain LSJC7 to Arsenic Exposure.Frontiers in microbiology · 2016Article
- An ArsR/SmtB family member is involved in the regulation by arsenic of the arsenite oxidase operon in Thiomonas arsenitoxydans.Applied and environmental microbiology · 2014Article
- YCF1-mediated cadmium resistance in yeast is dependent on copper metabolism and antioxidant enzymes.Antioxidants & redox signaling · 2014Article
- Identification of a novel membrane transporter mediating resistance to organic arsenic in Campylobacter jejuni.Antimicrobial agents and chemotherapy · 2014Article
- Article
- The complex process of GETting tail-anchored membrane proteins to the ER.Current opinion in structural biology · 2012Review
- Metallo-GTPase HypB from Helicobacter pylori and its interaction with nickel chaperone protein HypA.The Journal of biological chemistry · 2012Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
3 authors at 2 institutions in 1 country.
Funding
Abstract
Arsenic, a toxic metalloid widely existing in the environment, causes a variety of health problems. The ars operon encoded by Escherichia coli plasmid R773 has arsD and arsA genes, where ArsA is an ATPase that is the catalytic subunit of the ArsAB As(III) extrusion pump, and ArsD is an arsenic chaperone for ArsA. ArsD transfers As(III) to ArsA and increases the affinity of ArsA for As(III), allowing resistance to environmental concentrations of arsenic. Cys12, Cys13 and Cys18 in ArsD form a three sulfur-coordinated As(III) binding site that is essential for metallochaperone activity. ATP hydrolysis by ArsA is required for transfer of As(III) from ArsD to ArsA, suggesting that transfer occurs with a conformation of ArsA that transiently forms during the catalytic cycle. The 1.4 Å x-ray crystal structure of ArsD shows a core of four β-strands flanked by four α-helices in a thioredoxin fold. Docking of ArsD with ArsA was modeled in silico. Independently ArsD mutants exhibiting either weaker or stronger interaction with ArsA were selected. The locations of the mutations mapped on the surface of ArsD are consistent with the docking model. The results suggest that the interface with ArsA involves one surface of α1 helix and metalloid binding site of ArsD.
Indexed as
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.