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.
Journal ArticleDOI
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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Arsenate reductase II. Purine nucleoside phosphorylase in the presence of dihydrolipoic acid is a route for reduction of arsenate to arsenite in mammalian systems.
TL;DR: The experimental results indicate PNP is an important route for the reduction of arsenate to arsenite in mammalian systems.
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Metalloid Resistance Mechanisms in Prokaryotes
TL;DR: This review focuses on the biochemistry of the proteins of the ars operon of R-factor R773, which is novel in several respects and provides a high affinity digital switch to turn the regulated protein on with rapidity.
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Inorganic arsenic: a need and an opportunity to improve risk assessment.
Willard R. Chappell,Barbara D. Beck,K G Brown,R Chaney,R Cothern,C R Cothern,K J Irgolic,D W North,I Thornton,T A Tsongas +9 more
TL;DR: The central premise and recommendations are straightforward: the risk of adverse health effects associated with arsenic in drinking water is unknown for low arsenic concentrations found in the United States, such as at the current interim maximum contaminant level of 50 microg/l and below.
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Arsenate reductase from S. aureus plasmid pI258 is a phosphatase drafted for redox duty
TL;DR: Results provide evidence that ArsC from pI258 evolved from LMW PTPase by the grafting of a redox function onto a pre-existing catalytic site and that its evolutionary origin is different from those of arsenate reductases from Escherichia coli plasmid R773 and from Saccharomyces cerevisiae.
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A model of Cdc25 phosphatase catalytic domain and Cdk-interaction surface based on the presence of a rhodanese homology domain.
TL;DR: Recent determination of the crystal structure of the Cdc25a catalytic domain supports the validity of the model and demonstrates the power of the generalized sequence profile technique in homology-based modeling of the three-dimensional structure of a protein having a weak but significant sequence similarity with a structurally characterized protein.