Dihydrofolate reductase protects endothelial nitric oxide synthase from uncoupling in tetrahydrobiopterin deficiency
Tetrahydrobiopterin (BH4) is a required cofactor for the synthesis of NO by endothelial nitric oxide synthase (eNOS), and endothelial BH4 bioavailability is a critical factor in regulating the balance between NO and superoxide production (eNOS coupling). Biosynthesis of BH4 is determined by the acti...
Glavni autori: | Crabtree, M, Hale, AB, Channon, K |
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Format: | Journal article |
Jezik: | English |
Izdano: |
2011
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Slični predmeti
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Dihydrofolate reductase protects endothelial nitric oxide synthase from uncoupling in tetrahydrobiopterin deficiency.
od: Crabtree, M, i dr.
Izdano: (2011) -
Integrated redox sensor and effector functions for tetrahydrobiopterin- and glutathionylation-dependent endothelial nitric-oxide synthase uncoupling.
od: Crabtree, M, i dr.
Izdano: (2013) -
Critical role for tetrahydrobiopterin recycling by dihydrofolate reductase in regulation of endothelial nitric-oxide synthase coupling: relative importance of the de novo biopterin synthesis versus salvage pathways.
od: Crabtree, M, i dr.
Izdano: (2009) -
Endothelial tetrahydrobiopterin deficiency accelerates atherosclerotic progression by nitric oxide synthase uncoupling
od: Khoo, J, i dr.
Izdano: (2005) -
Dihydrofolate reductase is required to maintain endothelial nitric oxide synthase coupling in vivo: Insights from methotrexate-treated BH4 deficient and GTPCH overexpressing mice
od: Crabtree, M, i dr.
Izdano: (2010)