Disulfides

Known as: Disulfides [Chemical/Ingredient], disulfide 
Chemical groups containing the covalent disulfide bonds -S-S-. The sulfur atoms can be bound to inorganic or organic moieties.

Topic mentions per year

Topic mentions per year

1936-2017
01000200019362016

Papers overview

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Review
2016
Review
2016
Members of the lymphocyte antigen-6 (Ly6)/urokinase-type plasminogen activator receptor (uPAR) superfamily of proteins are… (More)
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Highly Cited
2010
Highly Cited
2010
The electronic properties of ultrathin crystals of molybdenum disulfide consisting of N=1,2,…,6 S-Mo-S monolayers have been… (More)
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Highly Cited
2006
Highly Cited
2006
The spectrophotometric/microplate reader assay method for glutathione (GSH) involves oxidation of GSH by the sulfhydryl reagent 5… (More)
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Highly Cited
2004
Highly Cited
2004
The majority of disulfide-linked cytosolic proteins are thought to be enzymes that transiently form disulfide bonds while… (More)
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Highly Cited
2000
Highly Cited
2000
We report the isolation and characterization of a novel human peptide with antimicrobial activity, termed LEAP-1 (liver-expressed… (More)
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Highly Cited
2000
Highly Cited
2000
We explored genomic expression patterns in the yeast Saccharomyces cerevisiae responding to diverse environmental transitions… (More)
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Highly Cited
1999
Highly Cited
1999
Under physiological conditions, the Escherichia coli cytoplasm is maintained in a reduced state that strongly disfavors the… (More)
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Highly Cited
1991
Highly Cited
1991
We describe a mutation (dsbA) that renders Escherichia coli severely defective in disulfide bond formation. In dsbA mutant cells… (More)
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Highly Cited
1979
Highly Cited
1979
Intact ribonucleic acid (RNA) has been prepared from tissues rich in ribonuclease such as the rat pancreas by efficient… (More)
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Highly Cited
1979
Highly Cited
1979
Thioredoxin from Escherichia coli was shown to catalyze the reduction of insulin disulfides by dithiothreitol. A quantitative… (More)
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