The DOI matches its Crossref record; 78 of the 78 references it cites were found in a registry or an index.
Regulation by S-Nitrosylation of Protein Post-translational Modification
Open accessAbstract
Protein post-translational modification by S-nitrosylation conveys a ubiquitous influence of nitric oxide on signal transduction in eukaryotic cells. The wide functional purview of S-nitrosylation reflects in part the regulation by S-nitrosylation of the principal protein post-translational modifications that play a role in cell signaling, including phosphorylation, acetylation, ubiquitylation and related modifications, palmitoylation, and alternative Cys-based redox modifications. In this minireview, we discuss the mechanisms through which S-nitrosylation exerts its broad pleiotropic influence on protein post-translational modification.
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Cites
Phosphorylation meets ubiquitination: the control of NF-κB activity
Karin, M., & Ben-Neriah, Y. (2000) · Annual Review of Immunology · doi:10.1146/annurev.immunol.18.1.621 · Cited by 4,766
Lysine acetylation targets protein complexes and co-regulates major cellular functions
Choudhary, C., Kumar, C., Gnad, F., Nielsen, M. L., Rehman, M., Walther, T. C., Olsen, J. V., & Mann, M. (2009) · Science · doi:10.1126/science.1175371 · Cited by 4,040
Signal transduction by reactive oxygen species
Finkel, T. (2011) · Journal of Cell Biology · doi:10.1083/jcb.201102095 · Cited by 2,322 · cited 1×
“In addition to S-nitrosylation, Cys residues in proteins may undergo a variety of redox-based modifications and electrophilic substitutions (68, 69).”
BackgroundProtein S-nitrosylation: Purview and parameters
Hess, D. T., Matsumoto, A., Kim, S.-O., Marshall, H. E., & Stamler, J. S. (2005) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm1569 · Cited by 2,153
Self-citationUbiquitin ligases: cell-cycle control and cancer
Nakayama, K. I., & Nakayama, K. (2006) · Nature Reviews Cancer · doi:10.1038/nrc1881 · Cited by 1,433
ATM Activation by Oxidative Stress
Guo, Z., Kozlov, S., Lavin, M. F., Person, M. D., & Paull, T. T. (2010) · Science · doi:10.1126/science.1192912 · Cited by 1,079
S-nitrosylated GAPDH initiates apoptotic cell death by nuclear translocation following Siah1 binding
Hara, M. R., Agrawal, N., Kim, S. F., Cascio, M. B., Fujimuro, M., Ozeki, Y., Takahashi, M., Cheah, J. H., Tankou, S. K., Hester, L. D., et al. (2005) · Nature Cell Biology · doi:10.1038/ncb1268 · Cited by 1,070
Redox-based regulation of signal transduction: principles, pitfalls, and promises
Janssen-Heininger, Y. M. W., Mossman, B. T., Heintz, N. H., Forman, H. J., Kalyanaraman, B., Finkel, T., Stamler, J. S., Rhee, S. G., & van der Vliet, A. (2008) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2008.03.011 · Cited by 784
Self-citationS -Nitrosylation of Parkin Regulates Ubiquitination and Compromises Parkin's Protective Function
Chung, K. K. K., Thomas, B., Li, X., Pletnikova, O., Troncoso, J. C., Marsh, L., Dawson, V. L., & Dawson, T. M. (2004) · Science · doi:10.1126/science.1093891 · Cited by 769
Fas-Induced Caspase Denitrosylation
Mannick, J. B., Hausladen, A., Liu, L., Hess, D. T., Zeng, M., Miao, Q. X., Kane, L. S., Gow, A. J., & Stamler, J. S. (1999) · Science · doi:10.1126/science.284.5414.651 · Cited by 742
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Cited by
Chemical Biology of H2S Signaling through Persulfidation
Filipovic, M. R., Zivanovic, J., Alvarez, B., & Banerjee, R. (2018) · Chemical Reviews · doi:10.1021/acs.chemrev.7b00205 · Cited by 1,046
Role of Glutathione in Cancer: From Mechanisms to Therapies
Kennedy, L., Sandhu, J. K., Harper, M.-E., & Cuperlovic-Culf, M. (2020) · Biomolecules · doi:10.3390/biom10101429 · Cited by 880
Kalogeris, T., Baines, C. P., Krenz, M., & Korthuis, R. J. (2016) · Comprehensive Physiology · doi:10.1002/cphy.c160006 · Cited by 718
Nitric oxide function in plant abiotic stress
Fancy, N. N., Bahlmann, A., & Loake, G. J. (2017) · Plant, Cell & Environment · doi:10.1111/pce.12707 · Cited by 481
Redox regulation of the Calvin–Benson cycle: something old, something new
Michelet, L., Zaffagnini, M., Morisse, S., Sparla, F., Pérez-Pérez, M. E., Francia, F., Danon, A., Marchand, C. H., Fermani, S., Trost, P., et al. (2013) · Frontiers in Plant Science · doi:10.3389/fpls.2013.00470 · Cited by 443
Metadata
- Authors
- Hess, D. T., & Stamler, J. S.
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 2012-02
- Volume
- 287
- Issue
- 7
- Pages
- 4411-4418
- ISSN
- 0021-9258 (ISSN-L)
- OpenAlex
- W2031615792
- Cited by
- 385
- References
- 78
- FWCI
- 9.64
- Type
- journal article
- Language
- en
- Open access
- hybrid
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- Hess, D. T., & Stamler, J. S. (2012). Regulation by S-Nitrosylation of Protein Post-translational Modification. Journal of Biological Chemistry. https://doi.org/10.1074/jbc.r111.285742
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