Biochemistry of arsenic detoxification
TLDR
While the overall schemes for arsenic resistance are similar in prokaryotes and eukaryotes, some of the specific proteins are the products of separate evolutionary pathways.About:
This article is published in FEBS Letters.The article was published on 2002-10-02 and is currently open access. It has received 726 citations till now. The article focuses on the topics: Arsenate reductase activity & Arsenate reductase.read more
Citations
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Journal ArticleDOI
The Ecology of Arsenic
Ronald S. Oremland,John F. Stolz +1 more
TL;DR: This work reviews what is known about arsenic-metabolizing bacteria and their potential impact on speciation and mobilization of arsenic in nature and investigates their role in aquifers.
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Wound healing - A literature review.
Ana Cristina Gonzalez,Tila Fortuna Costa,Zilton A. Andrade,Alena Ribeiro Alves Peixoto Medrado +3 more
TL;DR: The purpose of this review is to describe the various cellular and molecular aspects involved in the skin healing process.
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Arsenic hazards: strategies for tolerance and remediation by plants
Rudra Deo Tripathi,Sudhakar Srivastava,Seema Mishra,Nandita Singh,Rakesh Tuli,Dharmendra K. Gupta,Frans J. M. Maathuis +6 more
TL;DR: Recent advances in arsenic tolerance are discussed and their potential applications, particularly in the context of multigenic engineering approaches, are discussed.
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Arsenic binding to proteins.
TL;DR: Although the adverse health effects arising from exposure to arsenic have been well-recognized, the mechanism(s) of action responsible for the diverse range of health effects are complicated and poorly understood.
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Occurrence of arsenic contamination in Canada: sources, behavior and distribution.
TL;DR: An analysis of the currently available information on recognized problem areas, and an overview of current knowledge of the principal hydrogeochemical processes of arsenic transportation and transformation are provided, however, a more detailed understanding of local sources of arsenic and mechanisms of arsenic release is required.
References
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Membrane topology of the ArsB protein, the membrane subunit of an anion-translocating ATPase.
TL;DR: To localize individual segments of the ArsB protein, a ternary fusion method was developed, where portions of the arsB gene were inserted in-frame between the coding regions for two heterologous proteins, in this case a portion of a newly identified arsD gene and the blaM sequence encoding the mature beta-lactamase.
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Arsenate reduction mediated by the plasmid‐encoded ArsC protein is coupled to glutathione
TL;DR: Since ArsC‐catalysed reduction of arsenate provides high level resistance, physical coupling of the ArsC reaction to efflux of the resulting arsenite is hypothesised.
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Two new genes, PHO86 and PHO87, involved in inorganic phosphate uptake in Saccharomyces cerevisiae
TL;DR: In this article, the PHO84 gene in Saccharomyces cerevisiae encodes a Pi transporter, mutation of which confers constitutive synthesis of repressible acid phosphatase (rAPase), in medium containing repressibly amounts of Pi, and an arsenate-resistant phenotype.
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Enzymatic Reduction of Arsenic Compounds in Mammalian Systems: Reduction of Arsenate to Arsenite by Human Liver Arsenate Reductase
TL;DR: The isolation and characterization of this enzyme demonstrates that in humans, the reduction of arsenate to arsenite is enzymatically catalyzed and is not solely the result of chemical reduction by glutathione as has been proposed in the past.
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Saccharomyces cerevisiae ACR2 gene encodes an arsenate reductase
Rita Mukhopadhyay,Barry P. Rosen +1 more
TL;DR: The ACR2 gene of Saccharomyces cerevisiae was disrupted by insertion of a HIS3 gene and cells with the disruption were sensitive to arsenate, and the combination of chimeric MBP-Acr2-6H protein and yeast cytosol from an ACR1-disrupted strain exhibited arsenate reductase activity.