EC Number   |
Title |
Organism |
|---|
   1.16.1.8 | Distinct conformational behaviors of four mammalian dual-flavin reductases (cytochrome P450 reductase, methionine synthase reductase, neuronal nitric oxide synthase, endothelial nitric oxide synthase) determine their unique catalytic profiles |
Homo sapiens |
| 1.16.1.8 | Functional variant in methionine synthase reductase intron-1 is associated with pleiotropic congenital malformations |
Homo sapiens |
| 1.16.1.8 | Proximal FAD histidine residue influences interflavin electron transfer in cytochrome P450 reductase and methionine synthase reductase |
Homo sapiens |
| 1.16.1.8 | Riboflavin status modifies the effects of methylenetetrahydrofolate reductase (MTHFR) and methionine synthase reductase (MTRR) polymorphisms on homocysteine |
Homo sapiens |
| 1.16.1.8 | A common variant in methionine synthase reductase combined with low cobalamin (vitamin B12) increases risk for spina bifida |
Homo sapiens |
| 1.16.1.8 | A functional variant in MTRR intron-1 significantly increases the risk of congenital heart disease in han Chinese population |
Homo sapiens |
| 1.16.1.8 | Aromatic substitution of the FAD-shielding tryptophan reveals its differential role in regulating electron flux in methionine synthase reductase and cytochrome P450 reductase |
Homo sapiens |
| 1.16.1.8 | Cloning and mapping of a cDNA for methionine synthase reductase, a flavoprotein defective in patients with homocystinuria |
Homo sapiens |
| 1.16.1.8 | Differences in the efficiency of reductive activation of methionine synthase and exogenous electron acceptors between the common polymorphic variants of human methionine synthase reductase |
Homo sapiens |
| 1.16.1.8 | ELDOR spectroscopy reveals that energy landscapes in human methionine synthase reductase are extensively remodelled following ligand and partner protein binding |
Homo sapiens |
