to edit your profile (add a photo, awards, links to other websites, etc.)
Edit My Profile
My Person List (
Return to Top
Search Result Details
Back to Search Results
This page shows the details of why an item matched the keywords from your search.
One or more keywords matched the following items that are connected to
Peroxiredoxin evolution and the regulation of hydrogen peroxide signaling.
Structure-based insights into the catalytic power and conformational dexterity of peroxiredoxins.
Catalytic mechanism of thiol peroxidase from Escherichia coli. Sulfenic acid formation and overoxidation of essential CYS61.
Bacterial defenses against oxidants: mechanistic features of cysteine-based peroxidases and their flavoprotein reductases.
Oxidized and synchrotron cleaved structures of the disulfide redox center in the N-terminal domain of Salmonella typhimurium AhpF.
Cysteine reactivity and thiol-disulfide interchange pathways in AhpF and AhpC of the bacterial alkyl hydroperoxide reductase system.
Mutant AhpC peroxiredoxins suppress thiol-disulfide redox deficiencies and acquire deglutathionylating activity.
Introduction: What we do and do not know regarding redox processes of thiols in signaling pathways.
The basics of thiols and cysteines in redox biology and chemistry.
X-ray structures of thioredoxin and thioredoxin reductase from Entamoeba histolytica and prevailing hypothesis of the mechanism of Auranofin action.
Backbone chemical shift assignments for Xanthomonas campestris peroxiredoxin Q in the reduced and oxidized states: a dramatic change in backbone dynamics.
Structural changes upon peroxynitrite-mediated nitration of peroxiredoxin 2; nitrated Prx2 resembles its disulfide-oxidized form.
Differential Kinetics of Two-Cysteine Peroxiredoxin Disulfide Formation Reveal a Novel Model for Peroxide Sensing.
Unraveling the effects of peroxiredoxin 2 nitration; role of C-terminal tyrosine 193.