The post-translational modification S-sulfenylation functions as a key sensor of oxidative stress. Yet the dynamics of sulfenic acid in proteins remains largely elusive due to its fleeting nature. Here we use single-molecule force-clamp spectroscopy and
et al. S-glutathionylation of cryptic cysteines enhances titin elasticity by blocking protein folding. Cell 156, 1235–1246 (2014). Article CAS Google Scholar Beedle, A. E., Lynham, S. & Garcia-Manyes, S. Protein S-sulfenylation is a fleeting molecular switch that regulates non-enzymatic...
et al. S-glutathionylation of cryptic cysteines enhances titin elasticity by blocking protein folding. Cell 156, 1235–1246 (2014). Article CAS Google Scholar Beedle, A. E., Lynham, S. & Garcia-Manyes, S. Protein S-sulfenylation is a fleeting molecular switch that regulates non-enzymatic...
In this study, we proposed a new protein S-sulfenylation sites prediction method SulSite-GTB. First, fusion of amino acid composition, dipeptide composition, encoding based on grouped weight, K nearest neighbors, position-specific amino acid propensity, position-weighted amino...
Protein cysteine S-sulfenylation is an essential and reversible post-translational modification that plays a crucial role in transcriptional regulation, stress response, cell signaling and protein function. Studies have shown that S-sulfenylation is involved in many human diseases such as cancer, diabetes...
S., and Carroll, K. S. (2011) Redox-based probes for protein tyrosine phosphatases, Angew Chem Int Ed Engl 50, 4423-4427. Truong, T. H., and Carroll, K.S. (2012) Bioorthogonal Chemical Reporters for Analyzing Protein Sulfenylation in Cells, Curr Protoc Chem Biol 4, 101-122. If ...
Mitochondrial ROS regulate thermogenic energy expenditure and sulfenylation of UCP1 Article 30 March 2016 A critical assessment of the role of creatine in brown adipose tissue thermogenesis Article 09 January 2023 Endogenous FGF21-signaling controls paradoxical obesity resistance of UCP1-deficient mic...
Regulatory targets may include alterations in one or more of several different redox forms of cysteine including disulphide bonds, S-glutathionylation, S-nitrosylation, and S-sulfenylation [88]. On the nutritional side, bioavailability studies are required to ascertain the relative digestibility of the...
E. et al. Peroxide-dependent sulfenylation of the EGFR catalytic site enhances kinase activity. Nat. Chem. Biol. 8, 57–64 (2012). 4. Kulathu, Y. et al. Regulation of A20 and other OTU deubiquitinases by reversible oxidation. Nat. Commun. 4, 1569 (2013). 5. Leonard, S. E., ...
The study of S-sulfenylation commenced in 1976.157S-Sulfenylation is a process where hydrogen peroxide (H2O2) converts oxidized specific cysteine thiols to sulfenic acid (-SOH). Most interaction between cysteine thiol groups and H2O2is slow, which depends on the protein microenvironment, pH, pKa(-...