Gene Ontology annotation through association of InterPro records with GO terms
Annotation inferences using phylogenetic trees
Electronic Gene Ontology annotations created by ARBA machine learning models
Combined Automated Annotation using Multiple IEA Methods
Crystallization and preliminary X-ray analysis of the catalytic core of the alkylhydroperoxide reductase component AhpF from Escherichia coli.
Localization, annotation, and comparison of the Escherichia coli K-12 proteome under two states of growth.
A complexomic study of Escherichia coli using two-dimensional blue native/SDS polyacrylamide gel electrophoresis.
Comparison of SDS- and methanol-assisted protein solubilization and digestion methods for Escherichia coli membrane proteome analysis by 2-D LC-MS/MS.
Protein abundance profiling of the Escherichia coli cytosol.
Structure, mechanism and ensemble formation of the alkylhydroperoxide reductase subunits AhpC and AhpF from Escherichia coli.
Essential role of the flexible linker on the conformational equilibrium of bacterial peroxiredoxin reductase for effective regeneration of peroxiredoxin.
Alkyl hydroperoxide reductase is the primary scavenger of endogenous hydrogen peroxide in Escherichia coli.
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Ahp (AhpCF) provides the H2O2-scavenging activity that persists in catalase-null mutants; Ahp catalase triple mutants cannot scavenge H2O2.
"Thus, Ahp provides the scavenging activity that persists in catalase null mutants."
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Ahp turnover depends on NADH supply, so catalase dominates at high H2O2 concentrations.
"This arrangement is reasonable because the cell cannot provide enough NADH for Ahp to rapidly degrade large amounts of H 2 O 2 ."
An alkyl hydroperoxide reductase induced by oxidative stress in Salmonella typhimurium and Escherichia coli: genetic characterization and cloning of ahp.
AhpF can be dissected into two functional units: tandem repeats of two thioredoxin-like folds in the N-terminus mediate electron transfer from the thioredoxin reductase-like C-terminus to AhpC.