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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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Bioremediation potential of three acclimated bacteria with reference to heavy metal removal from waste

TL;DR: Three bacterial species Staphylococcus sp, Streptomyces sp and Flavobacterium sp were acclimatized for heavy metal removal and were concluded to be very potent to remove chromium and lead heavy metals form the waste.
Journal ArticleDOI

Characterisation of hyper tolerant Bacillus firmus L-148 for arsenic oxidation

TL;DR: Robust, hyper-tolerant, fast As(III) oxidizing, least nutrient requiring and multi-metal resistance qualities of the strain were used in microcosm studies for bioremediation.
Journal ArticleDOI

Relative efficacies of insulin and poly (lactic-co-glycolic) acid encapsulated nano-insulin in modulating certain significant biomarkers in arsenic intoxicated L6 cells.

TL;DR: Overall results suggested that both insulin and NIn improved mitochondrial functioning in arsenite-intoxicated L6 cells, NIn showing better effects at a much lower dose than that produced by insulin, therefore, has potential for therapeutic use in the management of arsenic induced diabetes.
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Diversity of Arsenate Reductase Genes ( arsC Genes) from Arsenic-Resistant Environmental Isolates of E. coli

TL;DR: A significant divergence in the DNA sequence was found in the arsC genes among As-resistant environmental E. coli strains from this study, and arsenic resistance, a genetic character, arose from a common ancestral background.
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Electrochemically driven catalysis of Rhizobium sp. NT-26 arsenite oxidase with its native electron acceptor cytochrome c552.

TL;DR: The obtained kinetic constants from digital simulation provide new insight into the kinetics of the NT-26 Aio catalytic mechanism, which oxidizes arsenite to arsenate.
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.
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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.
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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.
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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.
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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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