The redox state of SECIS binding protein 2 controls its localization and selenocysteine incorporation function - Test2 - elhamkhani - TriplyDB

The redox state of SECIS binding protein 2 controls its localization and selenocysteine incorporation function

The redox state of SECIS binding protein 2 controls its localization and selenocysteine incorporation function

http://www.wikidata.org/entity/Q24548981

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Cellular and molecular basis of deiodinase-regulated thyroid hormone signaling Thyroid Hormones, Oxidative Stress, and Inflammation Inherited defects in thyroid hormone cell-membrane transport and metabolism Selenium cytotoxicity in cancer The molecular biology of selenocysteine The syndromes of reduced sensitivity to thyroid hormone The cysteine proteome Selective up-regulation of human selenoproteins in response to oxidative stress Hydrogen peroxide probes directed to different cellular compartments.The syndrome of inherited partial SBP2 deficiency in humans.Threading the needle: getting selenocysteine into proteins Selenoproteins: molecular pathways and physiological roles.Hypermethylated-capped selenoprotein mRNAs in mammals.Regulation and function of selenoproteins in human disease Redox control systems in the nucleus: mechanisms and functions.IL-6 promotes nonthyroidal illness syndrome by blocking thyroxine activation while promoting thyroid hormone inactivation in human cells Insulin-like growth factor-1 regulates glutathione peroxidase expression and activity in vascular endothelial cells: Implications for atheroprotective actions of insulin-like growth factor-1.Mutations in the selenocysteine insertion sequence-binding protein 2 gene lead to a multisystem selenoprotein deficiency disorder in humans.Inherited defects of thyroid hormone metabolism Glutathione peroxidase-1 in health and disease: from molecular mechanisms to therapeutic opportunities A recoding element that stimulates decoding of UGA codons by Sec tRNA[Ser]Sec Understanding selenoprotein function and regulation through the use of rodent models.The L7Ae RNA binding motif is a multifunctional domain required for the ribosome-dependent Sec incorporation activity of Sec insertion sequence binding protein 2.The Selenocysteine-Specific Elongation Factor Contains Unique Sequences That Are Required for Both Nuclear Export and Selenocysteine Incorporation.Prominent role of exopeptidase DPP III in estrogen-mediated protection against hyperoxia in vivo Arsenic trioxide and auranofin inhibit selenoprotein synthesis: implications for chemotherapy for acute promyelocytic leukaemia.Functional characterization of alternatively spliced human SECISBP2 transcript variants.Clinical and molecular characterization of a novel selenocysteine insertion sequence-binding protein 2 (SBP2) gene mutation (R128X).Novel structural determinants in human SECIS elements modulate the translational recoding of UGA as selenocysteine.Interplay between selenium levels, selenoprotein expression, and replicative senescence in WI-38 human fibroblasts.Interacting effects of early dietary conditions and reproductive effort on the oxidative costs of reproduction.Characterization of the UGA-recoding and SECIS-binding activities of SECIS-binding protein 2 SBP2 binding affinity is a major determinant in differential selenoprotein mRNA translation and sensitivity to nonsense-mediated decay.Roles of selenoprotein antioxidant protection in zebrafish, Danio rerio, subjected to dietary oxidative stress.New Insights toward the Acute Non-Thyroidal Illness Syndrome.A novel insight into the mechanism of mammalian selenoprotein synthesis.A short motif in Drosophila SECIS Binding Protein 2 provides differential binding affinity to SECIS RNA hairpins Evolutionary history of selenocysteine incorporation from the perspective of SECIS binding proteins Disruption of the mitochondrial thioredoxin system as a cell death mechanism of cationic triphenylmethanes.Interplay between Selenium Levels and Replicative Senescence in WI-38 Human Fibroblasts: A Proteomic Approach.

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The redox state of SECIS binding protein 2 controls its localization and selenocysteine incorporation function

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2006 nî lūn-bûn

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2006年の論文

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The redox state of SECIS bindi ...... ysteine incorporation function

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The redox state of SECIS bindi ...... ysteine incorporation function

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The redox state of SECIS bindi ...... ysteine incorporation function

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The redox state of SECIS bindi ...... ysteine incorporation function

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The redox state of SECIS bindi ...... ysteine incorporation function

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The redox state of SECIS bindi ...... ysteine incorporation function

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Molecular and Cellular Biology

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The redox state of SECIS bindi ...... ysteine incorporation function

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Arne Holmgren

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Frank Striebel

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Kum Kum Khanna

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Laura V Papp

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P2860

Exp5 exports eEF1A via tRNA from nuclei and synergizes with other transport pathways to confine translation to the cytoplasm

How selenium has altered our understanding of the genetic code

The SBP2 and 15.5 kD/Snu13p proteins share the same RNA binding domain: identification of SBP2 amino acids important to SECIS RNA binding.

Functional characterization of the eukaryotic SECIS elements which direct selenocysteine insertion at UGA codons

SECIS-SBP2 interactions dictate selenocysteine incorporation efficiency and selenoprotein hierarchy

A novel RNA binding protein, SBP2, is required for the translation of mammalian selenoprotein mRNAs

Structure and mechanism of mammalian thioredoxin reductase: the active site is a redox-active selenolthiol/selenenylsulfide formed from the conserved cysteine-selenocysteine sequence

Characterization of the SECIS binding protein 2 complex required for the co-translational insertion of selenocysteine in mammals

CRM1 is an export receptor for leucine-rich nuclear export signals

Regulation of yAP-1 nuclear localization in response to oxidative stress.

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4895-4910

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2719729

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10.1128/MCB.02284-05

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13

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26

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Hendrick Kennedy

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2006-07-01T00:00:00Z

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7000797

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16782878

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L-selenocysteine

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1489162

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