S-Nitrosylation

Known as: SNO, peptidyl-cysteine S-nitrosylation, protein S-nitrosylation 
The covalent addition of a nitric oxide (NO) group to the sulphur (S) atom of a cysteine residue in a protein, to form peptidyl-S-nitrosyl-L-cysteine… (More)
National Institutes of Health

Papers overview

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Highly Cited
2009
Highly Cited
2009
Mitochondria continuously undergo two opposing processes, fission and fusion. The disruption of this dynamic equilibrium may… (More)
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Highly Cited
2008
Highly Cited
2008
Changes in redox status have been observed during immune responses in different organisms, but the associated signaling… (More)
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Highly Cited
2006
Highly Cited
2006
Stress proteins located in the cytosol or endoplasmic reticulum (ER) maintain cell homeostasis and afford tolerance to severe… (More)
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Review
2005
Review
2005
S-nitrosylation, the covalent attachment of a nitrogen monoxide group to the thiol side chain of cysteine, has emerged as an… (More)
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Highly Cited
2004
Highly Cited
2004
Parkin is an E3 ubiquitin ligase involved in the ubiquitination of proteins that are important in the survival of dopamine… (More)
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Highly Cited
2002
Highly Cited
2002
Matrix metalloproteinases (MMPs) are implicated in the pathogenesis of neurodegenerative diseases and stroke. However, the… (More)
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Highly Cited
2001
Highly Cited
2001
Nitric oxide (NO) has been linked to numerous physiological and pathophysiological events that are not readily explained by the… (More)
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Review
2001
Review
2001
posttranslational modifications of proteins operate by of Medicine and Biochemistry shifting a dynamic equilibrium between… (More)
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Highly Cited
1998
Highly Cited
1998
Several ion channels are reportedly redox responsive, but the molecular basis for the changes in activity is not known. The… (More)
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Highly Cited
1992
Highly Cited
1992
Endothelium-derived relaxing factor (EDRF) activity has been attributed to the highly labile nitric oxide radical (NO). In view… (More)
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