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Bacterial protein disulfide isomerase: efficient catalysis of oxidative protein folding at acidic pH
(1993)BiochemistryJournal Article -
A bacterial thioredoxin-like protein that is exposed to the periplasm has redox properties comparable with those of cytoplasmic thioredoxins
(1995)Journal of Biological ChemistryJournal Article -
Efficient catalysis of disulfide formation during protein folding with a single active-site cysteine
(1995)Journal of Molecular BiologyJournal Article -
In vivo control of redox potential during protein folding catalyzed by bacterial protein disulfide-isomerase (DsbA)
(1993)Journal of Biological ChemistryJournal Article -
Competition between DsbA-mediated oxidation and conformational folding of RTEM1 beta-lactamase
(1996)BiochemistryJournal Article -
The redox properties of protein disulfide isomerase (DsbA) of Escherichia coli result from a tense conformation of its oxidized form
(1993)Journal of Molecular BiologyJournal Article -
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Determination of the three-dimensional structure of the bifunctional alpha-amylase/trypsin inhibitor from ragi seeds by NMR spectroscopy
(1995)BiochemistryJournal Article -
Redox properties of protein disulfide isomerase (DsbA) from Escherichia coli
(1993)Protein ScienceJournal Article