The DOI matches its Crossref record; 8 of the 8 references it cites were found in a registry or an index.
eNOS activation and NO function: Structural motifs responsible for the posttranslational control of endothelial nitric oxide synthase activity
Open accessAbstract
Rather than being a constitutive enzyme as was first suggested, endothelial nitric oxide synthase (eNOS) is dynamically regulated at the transcriptional, posttranscriptional, and posttranslational levels. This review will focus on how changes in eNOS function are conferred by various posttranslational modifications. The latest knowledge regarding eNOS targeting to the plasma membrane will be discussed as the role of protein phosphorylation as a modulator of catalytic activity. Furthermore, new data are presented that provide novel insights into how disruption of the eNOS dimer prevents eNOS uncoupling and the production of superoxide under conditions of elevated oxidative stress and identifies a novel regulatory region we have termed the ‘flexible arm’.
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Citations
Cites
Activation of nitric oxide synthase in endothelial cells by Akt-dependent phosphorylation
Dimmeler, S., Fleming, I., Fisslthaler, B., Hermann, C., Busse, R., & Zeiher, A. M. (1999) · Nature · doi:10.1038/21224 · Cited by 3,591
Dissecting the Interaction between Nitric Oxide Synthase (NOS) and Caveolin
Garcı́a-Cardeña, G., Martasek, P., Masters, B. S. S., Skidd, P. M., Couet, J., Li, S., Lisanti, M. P., & Sessa, W. C. (1997) · Journal of Biological Chemistry · doi:10.1074/jbc.272.41.25437 · Cited by 821
Fleming, I., Fisslthaler, B., Dimmeler, S., Kemp, B. E., & Busse, R. (2001) · Circulation Research · doi:10.1161/hh1101.092677 · Cited by 770 · cited 14×
“Increases in intracellular calcium levels activate CaM that in turn activates CaM kinase II, which also phosphor- ylates S1177 (Fleming et al. 2001).”
BackgroundInfluentialDrummond, G. R., Cai, H., Davis, M. E., Ramasamy, S., & Harrison, D. G. (2000) · Circulation Research · doi:10.1161/01.res.86.3.347 · Cited by 430
McCabe, T. J., Fulton, D., Roman, L. J., & Sessa, W. C. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.275.9.6123 · Cited by 387 · cited 4×
“Although the AKT1-mediated activation of eNOS by FSS has been reported to be independent of changes in intracellular calcium (Dimmeler et al. 1999), it is more likely that the phosphorylation of S1177 renders the enzyme more responsive to much lower levels of calcium (McCabe et al. 2000).”
BackgroundResultInfluentialSelf-citationThomas, S. R., Chen, K., & Keaney, J. F. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m109107200 · Cited by 381
Harris, M. B., Ju, H., Venema, V. J., Liang, H., Zou, R., Michell, B. J., Chen, Z.-P., Kemp, B. E., & Venema, R. C. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m100229200 · Cited by 363
Shinozaki, K., Kashiwagi, A., Nishio, Y., Okamura, T., Yoshida, Y., Masada, M., Toda, N., & Kikkawa, R. (1999) · Diabetes · doi:10.2337/diabetes.48.12.2437 · Cited by 329
Cited by
Janaszak-Jasiecka, A., Płoska, A., Wierońska, J. M., Dobrucki, L. W., & Kalinowski, L. (2023) · Cellular & Molecular Biology Letters · doi:10.1186/s11658-023-00423-2 · Cited by 358
Raber, P. L., Thevenot, P., Sierra, R., Wyczechowska, D., Halle, D., Ramirez, M. E., Ochoa, A. C., Fletcher, M., Velasco, C., Wilk, A., et al. (2014) · International Journal of Cancer · doi:10.1002/ijc.28622 · Cited by 297
Regulation of obesity and insulin resistance by nitric oxide
Sansbury, B. E., & Hill, B. G. (2014) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2014.05.016 · Cited by 274
“posttranslational modifications [94,157,158].”
Arginine and Endothelial Function
Gambardella, J., Khondkar, W., Morelli, M. B., Wang, X., Santulli, G., & Trimarco, V. (2020) · Biomedicines · doi:10.3390/biomedicines8080277 · Cited by 253
Hydrogen Sulfide and Endothelial Dysfunction: Relationship with Nitric Oxide
Altaany, Z., Moccia, F., Munaron, L., Mancardi, D., & Wang, R. (2014) · Current Medicinal Chemistry · doi:10.2174/0929867321666140706142930 · Cited by 86
Metadata
- Authors
- Rafikov, R., Fonseca, F. V., Kumar, S., Pardo, D., Darragh, C., Elms, S., Fulton, D., & Black, S. M.
- Venue
- Journal of Endocrinology
- Publisher
- Bioscientifica
- Published
- 2011-06-03
- Volume
- 210
- Issue
- 3
- Pages
- 271-284
- ISSN
- 0022-0795 (ISSN-L)
- 1479-6805
- OpenAlex
- W2171689984
- Cited by
- 235
- References
- 8
- FWCI
- 13.68
- Type
- journal article
- Language
- en
- Open access
- bronze
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- Rafikov, R., Fonseca, F. V., Kumar, S., Pardo, D., Darragh, C., Elms, S., Fulton, D., & Black, S. M. (2011). eNOS activation and NO function: Structural motifs responsible for the posttranslational control of endothelial nitric oxide synthase activity. Journal of Endocrinology. https://doi.org/10.1530/joe-11-0083
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Bibliographic data: Semantic Scholar, OpenAlex, Crossref.
Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.
