The DOI matches its Crossref record; 9 of the 9 references it cites were found in a registry or an index.
S-Nitrosylation Signaling in Cell Biology
Abstract
S-Nitrosylated proteins form when a cysteine thiol reacts with nitric oxide (NO) in the presence of an electron acceptor to form an S-NO bond. Under physiological conditions, this posttranslational modification affects the function a wide array of cell proteins, ranging from ion channels to nuclear regulatory proteins. Recent evidence suggests that 1) S-nitrosylated proteins can be synthesized by exposure of specific redox-active motifs to NO, through transnitrosation/transfer reactions, or through metalloprotein-catalyzed reactions; 2) S-nitrosothiols can be sequestered in membranes, lipophilic protein folds, or in vesicles to preserve their activity; and 3) S-nitrosothiols can be degraded by a number of enzymes systems. These recent insights regarding the bioactivities, molecular signaling pathways, and metabolism of endogenous S-nitrosothiols have suggested several new therapies for disease ranging from cystic fibrosis to pulmonary hypertension.
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Cites
HIFα Targeted for VHL-Mediated Destruction by Proline Hydroxylation: Implications for O 2 Sensing
Ivan, M., Kondo, K., Yang, H., Kim, W., Valiando, J., Ohh, M., Salic, A., Asara, J. M., Lane, W. S., & Kaelin Jr., W. G. (2001) · Science · doi:10.1126/science.1059817 · Cited by 4,735
Lipton, S. A., Choi, Y.-B., Pan, Z.-H., Lei, S. Z., Chen, H.-S. V., Sucher, N. J., Loscalzo, J., Singel, D. J., & Stamler, J. S. (1993) · Nature · doi:10.1038/364626a0 · Cited by 2,433
The biology of nitrogen oxides in the airways
Gaston, B., Drazen, J. M., Loscalzo, J., & Stamler, J. S. (1994) · American Journal of Respiratory and Critical Care Medicine · doi:10.1164/ajrccm.149.2.7508323 · Cited by 918
Self-citationA metabolic enzyme for S-nitrosothiol conserved from bacteria to humans
Liu, L., Hausladen, A., Zeng, M., Que, L., Heitman, J., & Stamler, J. S. (2001) · Nature · doi:10.1038/35068596 · Cited by 913
Arnelle, D. R., & Stamler, J. S. (1995) · Archives of Biochemistry and Biophysics · doi:10.1006/abbi.1995.1231 · Cited by 604 · cited 2×
“Under certain circumstances, SNOs could also serve as “NO donors” in the sense that they are activated by homolytic cleavage to form NO radicals which, in turn, diffuse to a site of bioactivity (2).”
BackgroundLiu, X., Miller, M. J. S., Joshi, M. S., Thomas, D. D., & Lancaster, J. R. (1998) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.95.5.2175 · Cited by 602
Export by red blood cells of nitric oxide bioactivity
Pawloski, J. R., Hess, D. T., & Stamler, J. S. (2001) · Nature · doi:10.1038/35054560 · Cited by 579
Metal ion catalysis in nitrosothiol (RSNO) decomposition
McAninly, J., Williams, D. L. H., Askew, S. C., Butler, A. R., & Russell, C. (1993) · Journal of the Chemical Society, Chemical Communications · doi:10.1039/c39930001758 · Cited by 150 · cited 1×
“Several inorganic processes can lead to cleavage of the SNO bond (1, 38).”
BackgroundEffect of Superoxide Dismutase on the Stability ofS-Nitrosothiols
Jourd'heuil, D., Laroux, F. S., Miles, A. M., Wink, D. A., & Grisham, M. B. (1999) · Archives of Biochemistry and Biophysics · doi:10.1006/abbi.1998.1010 · Cited by 123
Cited by
NADPH Oxidases in Cardiovascular Health and Disease
Cave, A. C., Brewer, A. C., Narayanapanicker, A., Ray, R., Grieve, D. J., Walker, S., & Shah, A. M. (2006) · Antioxidants & Redox Signaling · doi:10.1089/ars.2006.8.691 · Cited by 630
Regulation of HIF-1α Stability through S-Nitrosylation
Li, F., Sonveaux, P., Rabbani, Z. N., Liu, S., Yan, B., Huang, Q., Vujaskovic, Z., Dewhirst, M. W., & Li, C.-Y. (2007) · Molecular Cell · doi:10.1016/j.molcel.2007.02.024 · Cited by 437
Savidge, T. C., Newman, P., Pothoulakis, C., Ruhl, A., Neunlist, M., Bourreille, A., Hurst, R., & Sofroniew, M. V. (2007) · Gastroenterology · doi:10.1053/j.gastro.2007.01.051 · Cited by 428
Redox Regulation of the NPR1-TGA1 System of Arabidopsis thaliana by Nitric Oxide
Lindermayr, C., Sell, S., Müller, B., Leister, D., & Durner, J. (2010) · The Plant Cell · doi:10.1105/tpc.109.066464 · Cited by 425
Maia, L. B., & Moura, J. J. G. (2014) · Chemical Reviews · doi:10.1021/cr400518y · Cited by 401
Metadata
- Authors
- Gaston, B. M.
- Venue
- Molecular Interventions
- Publisher
- CLOCKSS Archive
- Published
- 2003-08-01
- Volume
- 3
- Issue
- 5
- Pages
- 253-263
- ISSN
- 1534-0384 (ISSN-L)
- OpenAlex
- W2055147450
- Cited by
- 192
- References
- 9
- FWCI
- 2.57
- Type
- journal article
- Language
- en
- Open access
- closed
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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
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