Disulfide Linkage

Known as: Disulfide Bond 
A disulfide linkage is a covalent bond between 2 sulfide atoms from the thiol group of 2 cysteine residues (S-S). They occur both interstrand and… (More)
National Institutes of Health

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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
2003
Highly Cited
2003
Adiponectin is an adipocyte-derived hormone, which has been shown to play important roles in the regulation of glucose and lipid… (More)
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Highly Cited
2001
Highly Cited
2001
Yap1p, a crucial transcription factor in the oxidative stress response of Saccharomyces cerevisiae, is transported in and out of… (More)
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Highly Cited
2000
Highly Cited
2000
A new class of glutathione transferases has been discovered by analysis of the expressed sequence tag data base and sequence… (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
1998
Highly Cited
1998
The OxyR transcription factor is sensitive to oxidation and activates the expression of antioxidant genes in response to hydrogen… (More)
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Highly Cited
1997
Highly Cited
1997
Glutaredoxins belong to the thioredoxin superfamily of structurally similar thiol-disulfide oxidoreductases catalyzing thiol… (More)
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Highly Cited
1993
Highly Cited
1993
A novel hypotensive peptide was discovered in human pheochromocytoma by monitoring the elevating activity of platelet cAMP. Since… (More)
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Highly Cited
1992
Highly Cited
1992
Methods have been developed to assess the stereochemical quality of any protein structure both globally and locally using various… (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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