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Identification of cysteine sulfenic acid in AhpC of alkyl hydroperoxide reductase.
Peroxiredoxin evolution and the regulation of hydrogen peroxide signaling.
Analysis of the link between enzymatic activity and oligomeric state in AhpC, a bacterial peroxiredoxin.
Conformational studies of the robust 2-Cys peroxiredoxin Salmonella typhimurium AhpC by solution phase hydrogen/deuterium (H/D) exchange monitored by electrospray ionization mass spectrometry.
Dimers to doughnuts: redox-sensitive oligomerization of 2-cysteine peroxiredoxins.
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.
Substrate specificity and redox potential of AhpC, a bacterial peroxiredoxin.
Cysteine pK(a) values for the bacterial peroxiredoxin AhpC.
Water-soluble triarylphosphines as biomarkers for protein S-nitrosation.
The sensitive balance between the fully folded and locally unfolded conformations of a model peroxiredoxin.
Dissecting peroxiredoxin catalysis: separating binding, peroxidation, and resolution for a bacterial AhpC.
Mechanistic Studies of Alkyl Hydroperoxide Reductase and Related Redox Proteins
Mechanisms and Regulation of Peroxiredoxins
Experimentally Dissecting the Origins of Peroxiredoxin Catalysis.
Differential Kinetics of Two-Cysteine Peroxiredoxin Disulfide Formation Reveal a Novel Model for Peroxide Sensing.