Phosphorylation Controls Endothelial Nitric-oxide Synthase by Regulating Its Conformational Dynamics
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phosphorylation regulates eNOS and provides a foundation to compare its regulation by other phosphorylation events.
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Ser1177 is located in the C-terminal portion of eNOS in a helical C-terminal tail element that blocks flavin reduction and regulates the conformational equilibrium of the reductase domain.
“Ser1177 is located in the C-terminal portion of eNOS in a helical C-terminal tail element that blocks flavin reduction and regulates the conformational equilibrium of the reductase domain”
From Sources of Vascular Nitric Oxide and Reactive Oxygen Species and Their Regulation (2019) · cites this paper as [404]
Ser1177 phosphorylation activates electron flow through the reductase domain and increases NO synthesis in functional eNOS.
“Ser1177 phosphorylation activates electron flow through the reductase domain and, hence, increases NO synthesis in functional eNOS.”
From Sources of Vascular Nitric Oxide and Reactive Oxygen Species and Their Regulation (2019) · cites this paper as [404]
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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
- Haque, M. M., Ray, S. S., & Stuehr, D. J.
- Affiliations
- Cleveland Clinic (US)
- Corresponding author
- Haque, Mohammad Mahfuzul
- Stuehr, Dennis J.
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 2016-10
- Volume
- 291
- Issue
- 44
- Pages
- 23047-23057
- ISSN
- 0021-9258 (ISSN-L)
- PMC
- PMC5087725
- OpenAlex
- W2513555323
- Cited by
- 24
- References
- 58
- Citations by year
- 2026: 1 · 2025: 2 · 2024: 2 · 2023: 3 · 2022: 1 · 2021: 1 · 2020: 2 · 2019: 3 · 2018: 6 · 2017: 3
- FWCI
- 3.22
- Type
- journal article
- Language
- en
- Open access
- hybrid
- doi.org
- Licence
- Locations
- Journal of Biological Chemistry (publishedVersion, cc-by)
- Europe PMC (PubMed Central) (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- Funders
- National Institutes of Health (GM051491, HL076491)
- Topics
- Health Sciences › Medicine › Physiology › Nitric Oxide and Endothelin Effects
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Kinase Regulation and GTPase Signaling
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Receptor Mechanisms and Signaling
- Keywords
- endothelial nitric oxide synthase, phosphorylation, protein conformational dynamics, enzyme regulation, post-translational modification
- MeSH terms
- Animals, Cattle, Flavins, Kinetics, Nitric Oxide, Phosphorylation, Protein Conformation, Amino Acid Substitution, Amino Acid Motifs, Cytochromes c, Nitric Oxide Synthase Type III
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