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The arsenic hyperaccumulating Pteris vittata expresses two arsenate reductases

https://doi.org/10.1038/srep14525
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Outgoing claims: the papers this work cites, builds on, or argues with.

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Proteome analysis and identification of symbiosis-related proteins from Medicago truncatula Gaertn. by two-dimensional electrophoresis and mass spectrometry
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Blue silver: A very sensitive colloidal Coomassie G‐250 staining for proteome analysis
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Proteomic analysis of Pteris vittata fronds: Two arbuscular mycorrhizal fungi differentially modulate protein expression under arsenic contamination
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A Rapid and Sensitive Method for the Quantitation of Microgram Quantities of Protein Utilizing the Principle of Protein-Dye Binding
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A model of Cdc25 phosphatase catalytic domain and Cdk-interaction surface based on the presence of a rhodanese homology domain
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Arsenic resistance in Pteris vittata L.: identification of a cytosolic triosephosphate isomerase based on cDNA expression cloning in Escherichia coli
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Deviations from michaelis-menten behaviour of plant glutamate dehydrogenase with ammonium as variable substrate
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Characterization of the Arabidopsis thaliana Arath;CDC25 dual-specificity tyrosine phosphatase
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Arsenic transformation in the growth media and biomass of hyperaccumulator Pteris vittata L.
inferredcites →https://doi.org/10.1016/j.chemosphere.2006.02.048openalex-snapshot
Arbuscular mycorrhizae increase the arsenic translocation factor in the As hyperaccumulating fern Pteris vittata L.
inferredcites →https://doi.org/10.1016/j.envint.2008.07.012openalex-snapshot
The role of arsenate reductase and superoxide dismutase in As accumulation in four Pteris species
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Proteomic analysis as a tool for investigating arsenic stress in Pteris vittata roots colonized or not by arbuscular mycorrhizal symbiosis
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Absorption of foliar-applied arsenic by the arsenic hyperaccumulating fern (Pteris vittata L.)
inferredcites →https://doi.org/10.1016/j.tibtech.2007.02.003openalex-snapshot
Arsenic hazards: strategies for tolerance and remediation by plants
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A global health problem caused by arsenic from natural sources
inferredcites →https://doi.org/10.1016/s0098-8472(03)00040-6openalex-snapshot
Interactive effects of pH, arsenic and phosphorus on uptake of As and P and growth of the arsenic hyperaccumulator Pteris vittata L. under hydroponic conditions
inferredcites →https://doi.org/10.1016/s0378-1097(98)00430-3openalex-snapshot
Saccharomyces cerevisiae ACR2 gene encodes an arsenate reductase
inferredcites →https://doi.org/10.1021/es052559aopenalex-snapshot
Localizing the Biochemical Transformations of Arsenate in a Hyperaccumulating Fern
inferredcites →https://doi.org/10.1038/35054664openalex-snapshot
A fern that hyperaccumulates arsenic
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Engineering tolerance and hyperaccumulation of arsenic in plants by combining arsenate reductase and γ-glutamylcysteine synthetase expression
inferredcites →https://doi.org/10.1038/ncomms5617openalex-snapshot
Natural variation in arsenate tolerance identifies an arsenate reductase in Arabidopsis thaliana
inferredcites →https://doi.org/10.1039/b512792kopenalex-snapshot
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inferredcites →https://doi.org/10.1046/j.1469-8137.2002.00512.xopenalex-snapshot
Arsenic distribution and speciation in the fronds of the hyperaccumulator Pteris vittata
inferredcites →https://doi.org/10.1046/j.1469-8137.2003.00542.xopenalex-snapshot
Mechanisms of arsenate tolerance in Cytisus striatus
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High‐affinity phosphate/arsenate transport in white lupin (Lupinus albus) is relatively insensitive to phosphate status
inferredcites →https://doi.org/10.1073/pnas.0509770102openalex-snapshot
Hyperaccumulation of arsenic in the shoots of Arabidopsis silenced for arsenate reductase (ACR2)
inferredcites →https://doi.org/10.1074/jbc.m103354200openalex-snapshot
The Phosphatase C(X)5R Motif Is Required for Catalytic Activity of the Saccharomyces cerevisiae Acr2p Arsenate Reductase
inferredcites →https://doi.org/10.1074/jbc.m302610200openalex-snapshot
Directed Evolution of a Yeast Arsenate Reductase into a Protein-tyrosine Phosphatase
inferredcites →https://doi.org/10.1074/jbc.m910401199openalex-snapshot
Purification and Characterization of Acr2p, theSaccharomyces cerevisiae Arsenate Reductase
inferredcites →https://doi.org/10.1080/15226514.2013.798613openalex-snapshot
A Critical Review of the Arsenic Uptake Mechanisms and Phytoremediation Potential ofPteris vittata
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Mechanisms of Arsenic Hyperaccumulation in Pteris vittata . Uptake Kinetics, Interactions with Phosphate, and Arsenic Speciation
inferredcites →https://doi.org/10.1104/pp.010733openalex-snapshot
Uptake Kinetics of Arsenic Species in Rice Plants
inferredcites →https://doi.org/10.1104/pp.104.044073openalex-snapshot
Arsenic Hyperaccumulation in Gametophytes ofPteris vittata. A New Model System for Analysis of Arsenic Hyperaccumulation
inferredcites →https://doi.org/10.1104/pp.104.057422openalex-snapshot
Characterization of Arsenate Reductase in the Extract of Roots and Fronds of Chinese Brake Fern, an Arsenic Hyperaccumulator
inferredcites →https://doi.org/10.1104/pp.106.084079openalex-snapshot
A Novel Arsenate Reductase from the Arsenic Hyperaccumulating Fern Pteris vittata
inferredcites →https://doi.org/10.1104/pp.122.3.793openalex-snapshot
Detoxification of Arsenic by Phytochelatins in Plants
inferredcites →https://doi.org/10.1104/pp.122.4.1171openalex-snapshot
Reduction and Coordination of Arsenic in Indian Mustard
inferredcites →https://doi.org/10.1105/tpc.109.069773openalex-snapshot
A Vacuolar Arsenite Transporter Necessary for Arsenic Tolerance in the Arsenic Hyperaccumulating Fern Pteris vittata Is Missing in Flowering Plants
inferredcites →https://doi.org/10.1111/j.1399-3054.1962.tb08052.xopenalex-snapshot
A Revised Medium for Rapid Growth and Bio Assays with Tobacco Tissue Cultures
inferredcites →https://doi.org/10.1111/j.1469-8137.2007.02009.xopenalex-snapshot
A CDC25 homologue from rice functions as an arsenate reductase
inferredcites →https://doi.org/10.1111/j.1469-8137.2007.02195.xopenalex-snapshot
Rapid reduction of arsenate in the medium mediated by plant roots
inferredcites →https://doi.org/10.1111/j.1469-8137.2008.02716.xopenalex-snapshot
Arsenic uptake and metabolism in plants
inferredcites →https://doi.org/10.1126/science.1081903openalex-snapshot
The Ecology of Arsenic
inferredcites →https://doi.org/10.1371/journal.pbio.1002009openalex-snapshot
Genome-wide Association Mapping Identifies a New Arsenate Reductase Enzyme Critical for Limiting Arsenic Accumulation in Plants
inferredcites →https://doi.org/10.1371/journal.pone.0042408openalex-snapshot
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inferredcites →https://doi.org/10.2166/wst.2010.223openalex-snapshot
Arsenic hyperaccumulation by Pteris vittata and Pityrogramma calomelanos: a comparative study of uptake efficiency in arsenic-treated soils and waters
inferredcites →https://doi.org/10.3389/fphys.2012.00182openalex-snapshot
Arsenic Toxicity: The Effects on Plant Metabolism

What points at this work

Incoming claims: where this work appears in other papers’ reference lists and arguments.

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New Evidence of the Timing of Arsenic Accumulation, Expression of Arsenic-Response Genes and Phytoextraction Efficiency in Field-Grown Pteris Vittata Plants
inferred← citeshttps://doi.org/10.1007/978-3-319-75103-0_17openalex-snapshot
Novel Genes of Hyperaccumulator Ferns in Arsenic Tolerance, Uptake, and Metabolism: Implications for Crop Improvement
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Scope of Ferns in Horticulture and Economic Development
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New evidence of the timing of arsenic accumulation and expression of arsenic-response genes in field-grown Pteris vittata plants under different arsenic concentrations
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Efficient arsenate reduction in As-hyperaccumulator Pteris vittata are mediated by novel arsenate reductases PvHAC1 and PvHAC2
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Selenium Increased Arsenic Accumulation by Upregulating the Expression of Genes Responsible for Arsenic Reduction, Translocation, and Sequestration in Arsenic Hyperaccumulator Pteris vittata
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An Endophytic Bacterial Consortium modulates multiple strategies to improve Arsenic Phytoremediation Efficacy in Solanum nigrum
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The first complete chloroplast genome of Pteris vittata (Pteridaceae), an arsenic hyperaccumulating fern
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