Protein S-nitrosylation: purview and parameters

By D. Hess, Akio Matsumoto, Sung-Oog Kim, H. E. Marshall, J. Stamler. Nature reviews. Molecular cell biology, 2005

2,131 citations recorded by the source corpus.

Subfields: Molecular Biology, Physiology

View Paper: https://www.semanticscholar.org/paper/75c4bf86bb0e65c90ec47097c7bf61aa74b52c6f

How researchers see this paper

The researchers whose trusted networks rank it highest, strongest advocate first. Every researcher gets a different order.

In Molecular Biology

1. B. Kalyanaraman
2. H. Forman
3. D. Trachootham
4. Peng Huang
5. Wangang Zhang
6. D. Ahn
7. S. Rhee
8. Marcia A. Ogasawara

In Physiology

1. H. Forman
2. S. Snyder
3. S. Rhee
4. Toren Finkel
5. B. Kalyanaraman

Citations in the corpus

• S-nitrosylated GAPDH initiates apoptotic cell death by nuclear translocation following Siah1 binding (2005, background): “Sulphonation of cysteine can arise following S -nitrosylation (-SNO) via hydrolysis to sulphenic acid (-SOH) and sequential oxidation to sulphinic acid (-SO 2 H), and then sulphonic acid (-SO 3 H”
• Principles for characterizing the potential human health effects from exposure to nanomaterials: elements of a screening strategy (2005, methodology): “These can be monitored by measuring oxidative stress using dichlorofluorescein [98] or oxidized glutathione as endpoints [99] and nitrosated proteins as a measure of active nitrogen species [100].”
• Protein Oxidation: Basic Principles and Implications for Meat Quality (2013, background): “S-nitrosylation is the covalent attachment of a nitrogen monoxide group to the thiol side chain of cysteine (Hess et al., 2005).”
• Hydrogen sulfide: a versatile regulator of environmental stress in plants (2015, background): “Several studies demonstrated that the functions of proteins in NO signaling pathways were regulated through S-nitrosylation by numerous mechanisms (Hess et al. 2005; Wang et al. 2006; Astier et al. 2011; Gupta 2011; Hess and Stamler 2012).”
• Hydrogen sulfide-linked sulfhydration of NF-κB mediates its anti-apoptotic actions (2012, background): “S-Nitrosylation of p65 Is Followed by Sulfhydration Proteins are typically sulfhydrated at reactive cysteines, which are also the sites of physiologic S-nitrosylation (Hess et al., 2005; Jaffrey et al., 2001).”
• Zinc-Binding Cysteines: Diverse Functions and Structural Motifs (2014, background): “Cysteine residues are susceptible to a myriad of post-translational modifications including oxidation, nitrosylation, and disulfide formation [59–61].”