Control of Electron Transfer in Neuronal Nitric Oxide Synthase by Calmodulin, Substrate, Substrate Analogs, and Nitric Oxide
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Effects of folic acid on eNOS uncoupling seem related to antioxidant properties of folic acid metabolites.
“The effects on eNOS uncoupling seem related to the antioxidant properties of the folic acid metabolites (900).”
From Sources of Vascular Nitric Oxide and Reactive Oxygen Species and Their Regulation (2019) · cites this paper as [900]
Supplementation of folic acid (5-methyltetrahydrofolate) shows positive effects on eNOS function.
“Supplementation of folic acid (5-methyltetrahydrofolate) shows positive effects on eNOS function (900, 978) and has been shown to prevent nitroglycerin tolerance in short-term human studies (375).”
From Sources of Vascular Nitric Oxide and Reactive Oxygen Species and Their Regulation (2019) · cites this paper as [900]
Cites
Nitric oxide synthase structure and mechanism
Marletta, M. A. (1993) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)31375-9 · Cited by 1,341 · see citing works
Nitric Oxide Synthases: Properties and Catalytic Mechanism
Griffith, O. W., & Stuehr, D. J. (1995) · Annual Review of Physiology · doi:10.1146/annurev.ph.57.030195.003423 · Cited by 1,311 · see citing works
Self-citation(1986) · Springer eBooks · doi:10.1007/978-1-4757-9939-2 · Cited by 727 · see citing works
N omega-hydroxy-L-arginine is an intermediate in the biosynthesis of nitric oxide from L-arginine.
Stuehr, D. J., Kwon, N. S., Nathan, C. F., Griffith, O. W., Feldman, P. L., & Wiseman, J. S. (1991) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)38112-2 · Cited by 575 · see citing works
Self-citationCa2+/calmodulin-dependent formation of hydrogen peroxide by brain nitric oxide synthase
Heinzel, B., John, M., Klatt, P., Böhme, E., & Mayer, B. (1992) · Biochemical Journal · doi:10.1042/bj2810627 · Cited by 530 · see citing works
Nitric oxide synthases reveal a role for calmodulin in controlling electron transfer.
Abu‐Soud, H. M., & Stuehr, D. J. (1993) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.90.22.10769 · Cited by 410 · see citing works
Self-citationKlatt, P., Schmidt, K., Uray, G., & Mayer, B. (1993) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)82401-2 · Cited by 256 · see citing works
Rogers, N. E., & Ignarro, L. J. (1992) · Biochemical and Biophysical Research Communications · doi:10.1016/0006-291x(92)91550-a · Cited by 252 · see citing works
Abu‐Soud, H. M., Yoho, L. L., & Stuehr, D. J. (1994) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)31597-7 · Cited by 249 · see citing works
Self-citationAbu‐Soud, H. M., Wang, J., Rousseau, D. L., Fukuto, J. M., Ignarro, L. J., & Stuehr, D. J. (1995) · Journal of Biological Chemistry · doi:10.1074/jbc.270.39.22997 · Cited by 193 · see citing works
Self-citationAbu‐Soud, H. M., Feldman, P. L., Clark, P., & Stuehr, D. J. (1994) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)31638-7 · Cited by 127 · see citing works
Self-citationHeme coordination of NO in NO synthase.
Wang, J., Rousseau, D. L., Abu‐Soud, H. M., & Stuehr, D. J. (1994) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.91.22.10512 · Cited by 109 · see citing works
Self-citationL-arginine and calmodulin regulation of the heme iron reactivity in neuronal nitric oxide synthase.
Matsuoka, A., Stuehr, D. J., Olson, J. S., Clark, P., & Ikeda‐Saito, M. (1994) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)31996-8 · Cited by 99 · see citing works
Self-citationWolff, D. J., Datto, G. A., Samatovicz, R. A., et al. (1993) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)98368-7 · Cited by 89 · see citing works
NITRIC OXIDE SYNTHASES: WHY SO COMPLEX?
Masters, B. S. S. (1994) · Annual Review of Nutrition · doi:10.1146/annurev.nu.14.070194.001023 · Cited by 83 · see citing works
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Wink, D. A., & Mitchell, J. B. (1998) · Free Radical Biology and Medicine · doi:10.1016/s0891-5849(98)00092-6 · Cited by 1,606 · see citing works
Sources of Vascular Nitric Oxide and Reactive Oxygen Species and Their Regulation
Tejero, J., Shiva, S., & Gladwin, M. T. (2019) · Physiological Reviews · doi:10.1152/physrev.00036.2017 · Cited by 541 · see citing works
- Authors
- Stuehr, D. J., Abu-Soud, H. M., Rousseau, D. L., Feldman, P. L., & Wang, J.
- Affiliations
- Cleveland Clinic (US)
- AT&T (United States) (US)
- Venue
- Advances in Pharmacology
- Publisher
- Elsevier
- Published
- 1995
- Volume
- 34
- Pages
- 207-213
- ISSN
- 1054-3589 (ISSN-L)
- OpenAlex
- W1525692152
- Cited by
- 16
- References
- 15
- Citations by year
- 2019: 1 · 2018: 2
- FWCI
- 2.91
- Type
- book chapter
- Language
- en
- Open access
- closed
- Locations
- Advances in pharmacology (publishedVersion)
- PubMed (publishedVersion)
- Topics
- Health Sciences › Medicine › Physiology › Nitric Oxide and Endothelin Effects
- Physical Sciences › Chemistry › Inorganic Chemistry › Metal-Catalyzed Oxygenation Mechanisms
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Hemoglobin structure and function
- Keywords
- neuronal nitric oxide synthase, calmodulin, electron transfer, heme iron reduction, NADPH oxidation, L-arginine, substrate analogues, nitric oxide production, calcium-binding proteins
- MeSH terms
- Animals, Calmodulin, Electron Transport, Humans, Neurons, Nitric Oxide, Nitric Oxide Synthase
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