Dissecting peroxiredoxin catalysis: separating binding, peroxidation, and resolution for a bacterial AhpC - Wikidata - awgldk - TriplyDB

Dissecting peroxiredoxin catalysis: separating binding, peroxidation, and resolution for a bacterial AhpC

Dissecting peroxiredoxin catalysis: separating binding, peroxidation, and resolution for a bacterial AhpC

http://www.wikidata.org/entity/Q35811190

about

An unexplored role for Peroxiredoxin in exercise-induced redox signalling?Overview on Peroxiredoxin Kinetic Approaches to Measuring Peroxiredoxin Reactivity Peroxiredoxins: guardians against oxidative stress and modulators of peroxide signaling Essential role of the flexible linker on the conformational equilibrium of bacterial peroxiredoxin reductase for effective regeneration of peroxiredoxin.Experimentally Dissecting the Origins of Peroxiredoxin Catalysis.Kinetic analysis of structural influences on the susceptibility of peroxiredoxins 2 and 3 to hyperoxidation Transition steps in peroxide reduction and a molecular switch for peroxide robustness of prokaryotic peroxiredoxins.One- and two-electron oxidation of thiols: mechanisms, kinetics and biological fates.Urate hydroperoxide oxidizes human peroxiredoxin 1 and peroxiredoxin 2.Catalytic Thr or Ser Residue Modulates Structural Switches in 2-Cys Peroxiredoxin by Distinct Mechanisms.Redox-sensitive GFP fusions for monitoring the catalytic mechanism and inactivation of peroxiredoxins in living cells.NMR studies reveal a novel grab and release mechanism for efficient catalysis of the bacterial 2-Cys peroxiredoxin machinery.Endogenous, regulatory cysteine sulfenylation of ERK kinases in response to proliferative signals.

P2860

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P2860

Dissecting peroxiredoxin catalysis: separating binding, peroxidation, and resolution for a bacterial AhpC

http://www.wikidata.org/entity/Q35811190

description

2015 nî lūn-bûn

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2015年の論文

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2015年論文

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2015年論文

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2015年論文

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2015年論文

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2015年論文

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2015年论文

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2015年论文

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2015年论文

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name

Dissecting peroxiredoxin catal ...... esolution for a bacterial AhpC

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Dissecting peroxiredoxin catal ...... esolution for a bacterial AhpC

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type

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Dissecting peroxiredoxin catal ...... esolution for a bacterial AhpC

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Dissecting peroxiredoxin catal ...... esolution for a bacterial AhpC

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Dissecting peroxiredoxin catal ...... esolution for a bacterial AhpC

@en

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Cristina M Furdui

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Derek Parsonage

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Kimberly J Nelson

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P Andrew Karplus

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Samantha Alley

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P2860

Construction of Escherichia coli K-12 in-frame, single-gene knockout mutants: the Keio collection

Cloning and sequencing of thiol-specific antioxidant from mammalian brain: alkyl hydroperoxide reductase and thiol-specific antioxidant define a large family of antioxidant enzymes

Analysis of the link between enzymatic activity and oligomeric state in AhpC, a bacterial peroxiredoxin

Structure of intact AhpF reveals a mirrored thioredoxin-like active site and implies large domain rotations during catalysis

Peroxiredoxin evolution and the regulation of hydrogen peroxide signaling

Cysteine p K a Values for the Bacterial Peroxiredoxin AhpC † ‡

Structural Evidence that Peroxiredoxin Catalytic Power Is Based on Transition-State Stabilization

The Sensitive Balance between the Fully Folded and Locally Unfolded Conformations of a Model Peroxiredoxin

Protein production by auto-induction in high density shaking cultures

Model for the exceptional reactivity of peroxiredoxins 2 and 3 with hydrogen peroxide: a kinetic and computational study

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1567-1575

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10.1021/BI501515W

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7

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54

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Gerardo Ferrer-Sueta

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271530148

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4489686

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