about
Anticoagulant repertoire of the hookworm Ancylostoma caninumStructural basis of carbohydrate recognition by lectin II from Ulex europaeus, a protein with a promiscuous carbohydrate-binding siteArsenate reductase from S. aureus plasmid pI258 is a phosphatase drafted for redox dutyThe oxidase DsbA folds a protein with a nonconsecutive disulfideNonspecific base recognition mediated by water bridges and hydrophobic stacking in ribonuclease I fromEscherichia coliCoupling of domain swapping to kinetic stability in a thioredoxin mutantCorynebacterium glutamicum survives arsenic stress with arsenate reductases coupled to two distinct redox mechanismsNrdH-redoxin of Mycobacterium tuberculosis and Corynebacterium glutamicum Dimerizes at High Protein Concentration and Exclusively Receives Electrons from Thioredoxin ReductaseDissecting the Machinery That Introduces Disulfide Bonds in Pseudomonas aeruginosaMycoredoxin-1 is one of the missing links in the oxidative stress defence mechanism of MycobacteriaThe active site architecture in peroxiredoxins: a case study on Mycobacterium tuberculosis AhpEHow thioredoxin dissociates its mixed disulfideCysteines under ROS attack in plants: a proteomics view.Surface expression and ligand-based selection of cDNAs fused to filamentous phage gene VI.European contribution to the study of ROS: A summary of the findings and prospects for the future from the COST action BM1203 (EU-ROS).The essential catalytic redox couple in arsenate reductase from Staphylococcus aureus.Sulfenome mining in Arabidopsis thalianaA bacterial-two-hybrid selection system for one-step isolation of intracellularly functional Nanobodies.The quiescin sulfhydryl oxidase (hQSOX1b) tunes the expression of resistin-like molecule alpha (RELM-α or mFIZZ1) in a wheat germ cell-free extract.Arsenate reductase, mycothiol, and mycoredoxin concert thiol/disulfide exchangeProtein Methionine Sulfoxide Dynamics in Arabidopsis thaliana under Oxidative Stress.Pathways of disulfide bond formation in Escherichia coli.The disulphide isomerase DsbC cooperates with the oxidase DsbA in a DsbD-independent manner.Mycothiol/mycoredoxin 1-dependent reduction of the peroxiredoxin AhpE from Mycobacterium tuberculosis.Enzymatic catalysis: the emerging role of conceptual density functional theory.Structure, function, and mechanism of thioredoxin proteins.How proteins form disulfide bonds.Understanding the pK(a) of redox cysteines: the key role of hydrogen bonding.Low-molecular-weight thiols in thiol-disulfide exchange.Oxidative post-translational modifications of cysteine residues in plant signal transduction.DYn-2 Based Identification of Arabidopsis Sulfenomes.Redox Strategies for Crop Improvement.Diagonal chromatography to study plant protein modifications.Chemistry and Redox Biology of Mycothiol.Structural and biochemical analysis of Escherichia coli ObgE, a central regulator of bacterial persistence.A new role for Escherichia coli DsbC protein in protection against oxidative stressProtein S-mycothiolation functions as redox-switch and thiol protection mechanism in Corynebacterium glutamicum under hypochlorite stress.Corynebacterium diphtheriae methionine sulfoxide reductase a exploits a unique mycothiol redox relay mechanism.The glyceraldehyde-3-phosphate dehydrogenase GapDH of Corynebacterium diphtheriae is redox-controlled by protein S-mycothiolation under oxidative stress.The Corynebacterium glutamicum mycothiol peroxidase is a reactive oxygen species-scavenging enzyme that shows promiscuity in thiol redox control.
P50
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P50
description
researcher
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researcher
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wetenschapper
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հետազոտող
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name
J Messens
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J Messens
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J Messens
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J Messens
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J Messens
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J Messens
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J Messens
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J Messens
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J Messens
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J Messens
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J Messens
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J Messens
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J Messens
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J Messens
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J Messens
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J Messens
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J Messens
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J Messens
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P106
P1153
6603875334
P31
P496
0000-0002-2128-8264