FAQ

dihydrofolic acid binding

Known as: DHF binding, dihydrofolate binding 
Interacting selectively and non-covalently with dihydrofolic acid, a folic acid in which the bicyclic pteridine structure is in the dihydro… (More)
National Institutes of Health

Topic mentions per year

Topic mentions per year

1994-2013
01219942013

Papers overview

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2013
2013
Insight into the molecular mechanism about lowered dihydrofolate binding affinity to dihydrofolate reductase-like 1 (DHFRL1).
Human dihydrofolate reductase-like 1 (DHFRL1) has been identified as a second human dihydrofolate reductase (DHFR) enzyme… (More)
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2011
2011
Thermodynamics and solvent effects on substrate and cofactor binding in Escherichia coli chromosomal dihydrofolate reductase.
Chromosomal dihydrofolate reductase from Escherichia coli catalyzes the reduction of dihydrofolate to tetrahydrofolate using… (More)
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2008
2008
A balancing act between net uptake of water during dihydrofolate binding and net release of water upon NADPH binding in R67 dihydrofolate reductase.
R67 dihydrofolate reductase (DHFR) catalyzes the reduction of dihydrofolate (DHF) to tetrahydrofolate using NADPH as a cofactor… (More)
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2008
2008
R67, the other dihydrofolate reductase: rational design of an alternate active site configuration.
R67 dihydrofolate reductase (DHFR) bears no sequence or structural homologies with chromosomal DHFRs. The gene for this enzyme… (More)
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2006
2006
Effects of temperature and viscosity on R67 dihydrofolate reductase catalysis.
R67 dihydrofolate reductase (DHFR) is a novel homotetrameric protein that possesses 222 symmetry and a single, voluminous active… (More)
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1997
1997
A glutamine 67--> histidine mutation in homotetrameric R67 dihydrofolate reductase results in four mutations per single active site pore and causes substantial substrate and cofactor inhibition.
R67 dihydrofolate reductase (DHFR) is a type II DHFR produced by bacteria as a resistance mechanism to increasing clinical use of… (More)
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1994
1994
Nonadditivity of mutational effects at the folate binding site of Escherichia coli dihydrofolate reductase.
The function of the hydrophobic residues Leu28, Phe31, Ile50, and Leu54 at the folate binding site in Escherichia coli… (More)
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