The oligomeric conformation of peroxiredoxins links redox state to function.
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Circadian clocks in human red blood cellsPeroxiredoxins are conserved markers of circadian rhythmsMicrobial 2-Cys Peroxiredoxins: Insights into Their Complex Physiological RolesUtilizing Natural and Engineered Peroxiredoxins As Intracellular Peroxide ReportersPlastid thioredoxins: a "one-for-all" redox-signaling system in plantsThe thioredoxin/peroxiredoxin/sulfiredoxin system: current overview on its redox function in plants and regulation by reactive oxygen and nitrogen speciesCrystal Structure of Reduced and of Oxidized Peroxiredoxin IV Enzyme Reveals a Stable Oxidized Decamer and a Non-disulfide-bonded Intermediate in the Catalytic CycleMoonlighting by Different Stressors: Crystal Structure of the Chaperone Species of a 2-Cys PeroxiredoxinStructural Snapshots of Yeast Alkyl Hydroperoxide Reductase Ahp1 Peroxiredoxin Reveal a Novel Two-cysteine Mechanism of Electron Transfer to Eliminate Reactive Oxygen SpeciesPeroxiredoxin chaperone activity is critical for protein homeostasis in zinc-deficient yeast.Thioredoxins, glutaredoxins, and peroxiredoxins--molecular mechanisms and health significance: from cofactors to antioxidants to redox signalingObserved octameric assembly of a Plasmodium yoelii peroxiredoxin can be explained by the replacement of native "ball-and-socket" interacting residues by an affinity tag.Comparative proteome analysis of high and low cadmium accumulating soybeans under cadmium stress.Crystallization and preliminary crystallographic analysis of mouse peroxiredoxin II with significant pseudosymmetry.Free radicals and antioxidants: updating a personal view.A novel protein kinase-like domain in a selenoprotein, widespread in the tree of life.Mechanism of oxidative inactivation of human presequence protease by hydrogen peroxidePeroxiredoxin-1 protects estrogen receptor α from oxidative stress-induced suppression and is a protein biomarker of favorable prognosis in breast cancerThe N-terminal β-sheet of peroxiredoxin 4 in the large yellow croaker Pseudosciaena crocea is involved in its biological functions.Tuning of peroxiredoxin catalysis for various physiological rolesConformational studies of the robust 2-Cys peroxiredoxin Salmonella typhimurium AhpC by solution phase hydrogen/deuterium (H/D) exchange monitored by electrospray ionization mass spectrometry.Oxidation-reduction cycles of peroxiredoxin proteins and nontranscriptional aspects of timekeepingReduction of cysteine sulfinic acid in eukaryotic, typical 2-Cys peroxiredoxins by sulfiredoxin.Structure-based insights into the catalytic power and conformational dexterity of peroxiredoxins.Peroxiredoxins in plants and cyanobacteria.Mitochondrial peroxiredoxin functions as crucial chaperone reservoir in Leishmania infantum.How pH modulates the dimer-decamer interconversion of 2-Cys peroxiredoxins from the Prx1 subfamily.Redox regulation of mammalian sperm capacitation.Peroxiredoxins in parasites.Site-directed mutagenesis substituting cysteine for serine in 2-Cys peroxiredoxin (2-Cys Prx A) of Arabidopsis thaliana effectively improves its peroxidase and chaperone functions.Application of iTRAQ Reagents to Relatively Quantify the Reversible Redox State of Cysteine ResiduesContribution of proteomic studies towards understanding plant heavy metal stress response.Analysis of the redox oscillations in the circadian clockworkMultilevel regulation of 2-Cys peroxiredoxin reaction cycle by S-nitrosylationKinetic analysis of structural influences on the susceptibility of peroxiredoxins 2 and 3 to hyperoxidationPeroxiredoxin 1 is a tumor-associated antigen in esophageal squamous cell carcinomaDestroy and exploit: catalyzed removal of hydroperoxides from the endoplasmic reticulumDissecting the integrative antioxidant and redox systems in plant mitochondria. Effect of stress and S-nitrosylationTransition steps in peroxide reduction and a molecular switch for peroxide robustness of prokaryotic peroxiredoxins.Resolution of oxidative stress by thioredoxin reductase: Cysteine versus selenocysteine.
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The oligomeric conformation of peroxiredoxins links redox state to function.
description
article científic
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article scientifique
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articolo scientifico
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artigo científico
@pt
bilimsel makale
@tr
scientific article published on 22 May 2009
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vedecký článok
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vetenskaplig artikel
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videnskabelig artikel
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vědecký článek
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name
The oligomeric conformation of peroxiredoxins links redox state to function.
@en
The oligomeric conformation of peroxiredoxins links redox state to function.
@nl
type
label
The oligomeric conformation of peroxiredoxins links redox state to function.
@en
The oligomeric conformation of peroxiredoxins links redox state to function.
@nl
prefLabel
The oligomeric conformation of peroxiredoxins links redox state to function.
@en
The oligomeric conformation of peroxiredoxins links redox state to function.
@nl
P2860
P1433
P1476
The oligomeric conformation of peroxiredoxins links redox state to function
@en
P2093
Juan-José Lázaro
Sergio Barranco-Medina
P2860
P304
P356
10.1016/J.FEBSLET.2009.05.029
P407
P577
2009-05-22T00:00:00Z