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Reduced S-nitrosylation of TGFβ1 elevates its binding affinity toward the receptor and promotes fibrogenic signaling in the breast. [PDF]
J Biol ChemLetson J +5 more
europepmc +1 more source
Correction to "Wheel-Running Exercise Alleviates Anxiety-Like Behavior via Down-Regulating S-Nitrosylation of Gephyrin in the Basolateral Amygdala of Male Rats". [PDF]
Adv Sci (Weinh)europepmc +1 more source
S-Nitrosylation in Tumor Microenvironment [PDF]
International Journal of Molecular Sciences, 2021 S-nitrosylation is a selective and reversible post-translational modification of protein thiols by nitric oxide (NO), which is a bioactive signaling molecule, to exert a variety of effects. These effects include the modulation of protein conformation, activity, stability, and protein-protein interactions.
Vandana Sharma +2 more
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Protein S-nitrosylation: purview and parameters
Nature Reviews Molecular Cell Biology, 2005S-nitrosylation, the covalent attachment of a nitrogen monoxide group to the thiol side chain of cysteine, has emerged as an important mechanism for dynamic, post-translational regulation of most or all main classes of protein. S-nitrosylation thereby conveys a large part of the ubiquitous influence of nitric oxide (NO) on cellular signal transduction,
Akio Matsumoto +2 more
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S-Nitrosylation in Alzheimer's disease
Molecular Neurobiology, 2014S-Nitrosylation, a redox-mediated posttranslational modification, is a result of the covalent binding nitric oxide (NO)-related species to cysteine residues of target proteins with the formation of nitrosothiols (SNOs). Normally, protein S-nitrosylation could be a cellular signaling mechanism, as is often a reversible and selective process, akin to ...
Qing-Fei, Zhao, Jin-Tai, Yu, Lan, Tan
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S-nitrosylation regulates apoptosis
Nature, 1997Nitric oxide (NO) modulates the biological activity of proteins by direct interactions with their iron centres. It can also S-nitrosylate cysteines to form S-nitrosothiols. Such reactions affect the activity of membrane-bound, cytosolic and nuclear proteins including the NMDA receptor1, haemoglobin2 and transcription factors such as NF-κB3 and OxyR. NO
G, Melino +5 more
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Analysis of Protein S‐Nitrosylation
Current Protocols in Protein Science, 2011AbstractS‐Nitrosylation, the redox‐based modification of cysteine thiol side chains by nitric oxide, is a dynamic and reversible post‐translational modification of proteins that subserves many important cellular functions. Analysis of protein S‐nitrosylation is often challenging due to methodological limitations and the effects of various chemical and ...
Christopher M, Schonhoff, Moran, Benhar
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Cellular and Molecular Life Sciences, 1999
The transfer of a nitric oxide group to cysteine sulfhydryls on proteins, known as S-nitrosylation, is increasingly becoming recognized as a ubiquitous regulatory reaction comparable to phosphorylation. It represents a form of redox modulation in diverse tissues, including the brain.
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The transfer of a nitric oxide group to cysteine sulfhydryls on proteins, known as S-nitrosylation, is increasingly becoming recognized as a ubiquitous regulatory reaction comparable to phosphorylation. It represents a form of redox modulation in diverse tissues, including the brain.
exaly +4 more sources
Analysis of Protein S‐Nitrosylation
Current Protocols in Protein Science, 2004AbstractS‐nitrosylation is the binding of an NO group to a cysteine or other thiol. Like phosphorylation, S‐nitrosylation is a precisely targeted and rapidly reversible post‐translational modification that serves as an on/off switch for protein function during cell signaling.
Joan B, Mannick +1 more
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