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Open AccessJournal ArticleDOI

Biochemistry of arsenic detoxification

Barry P. Rosen
- 02 Oct 2002 - 
- Vol. 529, Iss: 1, pp 86-92
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.

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Citations
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Journal ArticleDOI

High-throughput identification of catalytic redox-active cysteine residues.

TL;DR: In this paper, a procedure for high-throughput identification of catalytic redox-active Cys in proteins by searching for sporadic selenocysteine-Cys pairs in sequence databases was developed.
Journal ArticleDOI

Arsenic metabolism by microbes in nature and the impact on arsenic remediation

TL;DR: This review highlights the current understanding of the biochemistry and molecular biology involved in these natural arsenic metabolisms, and some successful examples of engineered microbes by harnessing these natural mechanisms for effective remediation.
Book ChapterDOI

Arsenic Metabolism in Prokaryotic and Eukaryotic Microbes

TL;DR: An understanding of the molecular details of metalloid transport systems and detoxification enzymes is essential for the rational design of new drugs, and for treating drug-resistant microorganisms and tumor cells.
Journal ArticleDOI

The microbial genomics of arsenic.

TL;DR: The increasing number of genomes available and the development of descriptive and comparative approaches have made it possible not only to identify several genetic determinants of the arsenic metabolism, but also to elucidate their phylogenetic distribution and their modes of regulation.
Journal ArticleDOI

Arsenic Methylation, Urinary Arsenic Metabolites and Human Diseases: Current Perspective

TL;DR: A review of the current literature suggests that reduced methylation capacity with increased MMAV percentage, decreased DMAV Percentage, or decreased D MAV/MMAV is associated with skin lesions, skin cancer, bladder cancer, peripheral vascular disease, muscle cramps and structural chromosome aberrations in peripheral lymphocytes obtained from exposed subjects.
References
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Journal ArticleDOI

Distantly related sequences in the alpha- and beta-subunits of ATP synthase, myosin, kinases and other ATP-requiring enzymes and a common nucleotide binding fold.

TL;DR: Related sequences in both alpha and beta and in other enzymes that bind ATP or ADP in catalysis help to identify regions contributing to an adenine nucleotide binding fold in both ATP synthase subunits.
Journal ArticleDOI

CLUSTAL: A package for performing multiple sequence alignment on a microcomputer

TL;DR: An approach for performing multiple alignments of large numbers of amino acid or nucleotide sequences is described, based on first deriving a phylogenetic tree from a matrix of all pairwise sequence similarity scores obtained using a fast pairwise alignment algorithm.
Journal ArticleDOI

Classification and evolution of P-loop GTPases and related ATPases.

TL;DR: In this article, the authors compared sequences and available structures for all the widely distributed representatives of the P-loop GTPases and GTPase-related proteins with the aim of constructing an evolutionary classification for this superclass of proteins and reconstructing the principal events in their evolution.
Journal ArticleDOI

Comparative toxicity of trivalent and pentavalent inorganic and methylated arsenicals in rat and human cells.

TL;DR: It is suggested that trivalent methylated arsenicals, intermediary products of arsenic methylation, may significantly contribute to the adverse effects associated with exposure to iAs, and high methylation capacity does not protect cells from the acute toxicity of triavalent arsenicals.
Journal ArticleDOI

The MRP gene encodes an ATP-dependent export pump for leukotriene C4 and structurally related conjugates.

TL;DR: It is concluded that the biosynthetic release of LTC4 from cells is mediated by the 190-kDa product of the MRP gene, a primary-active ATP-dependent export pump for conjugates of lipophilic compounds with glutathione and several other anionic residues.
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