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CoFactor brand of 5,10-methylenetetrahydrofolate

Known as: CoFactor 
National Institutes of Health

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5,10-methylenetetrahydrofolate

Papers overview

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Highly Cited
2013
Highly Cited
2013
General approach to reversing ketol-acid reductoisomerase cofactor dependence from NADPH to NADH
To date, efforts to switch the cofactor specificity of oxidoreductases from nicotinamide adenine dinucleotide phosphate (NADPH… 
Highly Cited
2011
Highly Cited
2011
A novel nonsense variant in Nav1.5 cofactor MOG1 eliminates its sodium current increasing effect and may increase the risk of arrhythmias.
Review
2006
Review
2006
PGC-1α: a potent transcriptional cofactor involved in the pathogenesis of type 2 diabetes
Data derived from several recent studies implicate peroxisome proliferator-activated receptor-γ coactivator-1α (PGC-1α) in the… 
Highly Cited
2002
Highly Cited
2002
Localization in the human retina of the X-linked retinitis pigmentosa protein RP2, its homologue cofactor C and the RP2 interacting protein Arl3.
Mutations in the retinitis pigmentosa 2 (RP2) gene cause a severe form of X-linked retinal degeneration. RP2 is a ubiquitous 350… 
2000
2000
Role of residue Phe225 in the cofactor-mediated, allosteric regulation of the serine protease coagulation factor VIIa.
Functional regulation by cofactors is fundamentally important for the highly ordered, consecutive activation of the coagulation… 
1995
1995
Human factor H and C4b-binding protein serve as factor I-cofactors both encompassing inactivation of C3b and C4b.
1995
1995
Sequence-specific binding of DNA by the EcoRV restriction and modification enzymes with nucleic acid and cofactor analogues.
The DNA-binding properties of the EcoRV restriction endonuclease and modification methyltransferase with their recognition… 
Highly Cited
1990
Highly Cited
1990
Mechanism of the reaction of ebselen with endogenous thiols: dihydrolipoate is a better cofactor than glutathione in the peroxidase activity of ebselen.
The therapeutic effect of ebselen has been linked to its peroxidase activity. In the present study, the peroxidase activity of… 
Highly Cited
1988
Highly Cited
1988
Reduced thioredoxin: a possible physiological cofactor for vitamin K epoxide reductase. Further support for an active site disulfide.
Highly Cited
1985
Highly Cited
1985
The formaldehyde dehydrogenase of Rhodococcus erythropolis, a trimeric enzyme requiring a cofactor and active with alcohols.
During growth on compounds containing methyl groups a formaldehyde dehydrogenase is induced in the gram-positive bacteria… 
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