ArticleProceedings of the National Academy of Sciences of the United States of America2002
Functional interaction of endothelial nitric oxide synthase with a voltage-dependent anion channel.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2002. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 29 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
29 citing papers in PubMed, 72 citations in OpenAlex.
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- Subcellular Localization Guides eNOS Function.International journal of molecular sciences · 2024Review
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- Endothelial Contribution to Warfarin-Induced Arterial Media Calcification in Mice.International journal of molecular sciences · 2021Article
- VDAC1 at the Intersection of Cell Metabolism, Apoptosis, and Diseases.Biomolecules · 2020Review
- Label-free quantitative proteomics analysis reveals distinct molecular characteristics in endocardial endothelium.Molecular and cellular biochemistry · 2019Article
- VDAC1 at the crossroads of cell metabolism, apoptosis and cell stress.Cell stress · 2017Article
- Voltage-Dependent Anion Channel 1 As an Emerging Drug Target for Novel Anti-Cancer Therapeutics.Frontiers in oncology · 2017Review
- The Mitochondrial Voltage-Dependent Anion Channel 1, CaFrontiers in oncology · 2017Review
- Nitrotyrosine impairs mitochondrial function in fetal lamb pulmonary artery endothelial cells.American journal of physiology. Cell physiology · 2016Article
- Pim1 kinase promotes angiogenesis through phosphorylation of endothelial nitric oxide synthase at Ser-633.Cardiovascular research · 2016Article
- Interaction of endothelial nitric oxide synthase with mitochondria regulates oxidative stress and function in fetal pulmonary artery endothelial cells.American journal of physiology. Lung cellular and molecular physiology · 2015Article
- Orphan Nuclear Receptor Nur77 Inhibits Cardiac Hypertrophic Response to Beta-Adrenergic Stimulation.Molecular and cellular biology · 2015Article
- β3-adrenergic receptor activity modulates melanoma cell proliferation and survival through nitric oxide signaling.Naunyn-Schmiedeberg's archives of pharmacology · 2014Article
- Regulation of endothelial nitric oxide synthase activity by protein-protein interaction.Current pharmaceutical design · 2014Review
- Post-translational regulation of endothelial nitric oxide synthase in vascular endothelium.Frontiers in physiology · 2013Review
- Protein-L-isoaspartate (D-aspartate) O-methyltransferase protects cardiomyocytes against hypoxia induced apoptosis through inhibiting proapoptotic kinase Mst1.International journal of cardiology · 2013Article
- Role of TRPM7 channels in hyperglycemia-mediated injury of vascular endothelial cells.PloS one · 2013Article
- Voltage-dependent anion channel-2 interaction with nitric oxide synthase enhances pulmonary artery endothelial cell nitric oxide production.American journal of respiratory cell and molecular biology · 2012Article
Corrections and comments
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Authors and funding
2 authors at 2 institutions in 1 country.
Funding
Abstract
Endothelium-derived nitric oxide (NO) is an important regulator of vascular function. NO is produced by endothelial NO synthase (eNOS) whose function is modulated, in part, by specific protein interactions. By coimmunoprecipitation experiments followed by MS analyses, we identified a human voltage-dependent anion/cation channel or porin as a binding partner of eNOS. The interaction between porin and eNOS was demonstrated by coimmunoprecipitation studies in nontransfected human endothelial cells and Cos-7 cells transiently transfected with eNOS and porin cDNAs. In vitro binding studies with glutathione S-transferase-porin indicated that porin binds directly to eNOS and that this interaction augmented eNOS activity. The calcium ionophore, and bradykinin, which are known to activate eNOS, markedly increased porin-eNOS interaction, suggesting a potential role of intracellular Ca(2+) in mediating this interaction. Theses results indicate that the interaction between a voltage-dependent membrane channel and eNOS may be important for regulating eNOS activity.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.