ArticleFrontiers in molecular neuroscience2020
The Molecular Simulation Study of nNOS Activation Induced by the Interaction Between Its Calmodulin-Binding Domain and SUMO1.
Article in Frontiers in molecular neuroscience, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.
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Who cites it
4 citing papers in PubMed, 5 citations in OpenAlex.
- FNR-like unit interacts with C-terminal related residues trigger nNOS reductase domain conformational flexibility change.Frontiers in neuroscience · 2026Article
- K739 is preferentially targeted over K725 in the deSUMOylation process of neuronal nitric oxide synthase.Frontiers in chemistry · 2025Article
- Polarized benzene rings can promote the interaction between CaM and the CaMBD region of nNOS.Frontiers in molecular neuroscience · 2024Article
- N-Lobe of TXNIP Is Critical in the Allosteric Regulation of NLRP3Frontiers in aging neuroscience · 2022Article
Corrections and comments
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Authors and funding
2 authors at 2 institutions in 1 country.
Funding
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Abstract
Neuronal nitric oxide synthase (nNOS), an enzyme required for learning and memory, catalyzes L-arginine decomposition during nitric oxide production in mammalian neurons. Over-activation of nNOS leads to oxidative/nitrosative stress, which is part of the pathophysiological process of various neuropsychiatric disorders. Previous experimental studies suggest that nNOS is a target for small ubiquitin-like modifier 1 (SUMO1), and that SUMO1-ylation upregulates nNOS catalytic activity in hippocampal neurons. To date, a comprehensive structural model has not been proposed for nNOS SUMO1-ylation. In this study, our aim was to build
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