27 Article(s)Download |
PMID | Title | Pub. Year | #Total Relationships |
1 | 30724552 | Crowders Steal Dihydrofolate Reductase Ligands through Quinary Interactions. | 2019 Mar 5 | 3 |
2 | 30979096 | Studies on the Interaction between Poly-Phosphane Gold(I) Complexes and Dihydrofolate Reductase: An Interplay with Nicotinamide Adenine Dinucleotide Cofactor. | 2019 Apr 11 | 2 |
3 | 30040418 | Effect of Asp122 Mutation on the Hydride Transfer in E. coli DHFR Demonstrates the Goldilocks of Enzyme Flexibility. | 2018 Aug 23 | 3 |
4 | 30564747 | The crystal structure of a tetrahydrofolate-bound dihydrofolate reductase reveals the origin of slow product release. | 2018 | 2 |
5 | 28422217 | Increased substrate affinity in the Escherichia coli L28R dihydrofolate reductase mutant causes trimethoprim resistance. | 2017 May 10 | 1 |
6 | 24517487 | Investigation of osmolyte effects on FolM: comparison with other dihydrofolate reductases. | 2014 Mar 4 | 4 |
7 | 25453083 | Toward resolving the catalytic mechanism of dihydrofolate reductase using neutron and ultrahigh-resolution X-ray crystallography. | 2014 Dec 23 | 3 |
8 | 23420416 | Multiple intermediates, diverse conformations, and cooperative conformational changes underlie the catalytic hydride transfer reaction of dihydrofolate reductase. | 2013 | 1 |
9 | 18724364 | A domino effect in antifolate drug action in Escherichia coli. | 2008 Oct | 1 |
10 | 17916364 | Allosteric communication in dihydrofolate reductase: signaling network and pathways for closed to occluded transition and back. | 2007 Nov 16 | 1 |
11 | 16241906 | Coupling of protein motions and hydrogen transfer during catalysis by Escherichia coli dihydrofolate reductase. | 2006 Feb 15 | 1 |
12 | 15726569 | Computational methods for the study of enzymic reaction mechanisms III: a perturbation plus QM/MM approach for calculating relative free energies of protonation. | 2005 Apr 30 | 2 |
13 | 15213241 | Mass spectrometry on hydrogen/deuterium exchange of dihydrofolate reductase: effects of ligand binding. | 2004 Jun | 1 |
14 | 15609999 | Conformational changes in the active site loops of dihydrofolate reductase during the catalytic cycle. | 2004 Dec 28 | 1 |
15 | 12756296 | Correlated motion and the effect of distal mutations in dihydrofolate reductase. | 2003 Jun 10 | 2 |
16 | 12765545 | Hydride transfer during catalysis by dihydrofolate reductase from Thermotoga maritima. | 2003 Sep 1 | 2 |
17 | 12852950 | High throughput screening identifies novel inhibitors of Escherichia coli dihydrofolate reductase that are competitive with dihydrofolate. | 2003 Aug 4 | 1 |
18 | 12862454 | How dihydrofolate reductase facilitates protonation of dihydrofolate. | 2003 Jul 23 | 2 |
19 | 12021443 | Role of water in the catalytic cycle of E. coli dihydrofolate reductase. | 2002 Jun | 2 |
20 | 11472112 | Energetically most likely substrate and active-site protonation sites and pathways in the catalytic mechanism of dihydrofolate reductase. | 2001 Apr 18 | 6 |
21 | 8003467 | Determination by Raman spectroscopy of the pKa of N5 of dihydrofolate bound to dihydrofolate reductase: mechanistic implications. | 1994 Jun 14 | 4 |
22 | 8461309 | How do mutations at phenylalanine-153 and isoleucine-155 partially suppress the effects of the aspartate-27-->serine mutation in Escherichia coli dihydrofolate reductase? | 1993 Apr 6 | 1 |
23 | 1961697 | The electrostatic potential of Escherichia coli dihydrofolate reductase. | 1991 | 1 |
24 | 2502633 | 2,4-Diamino-5-benzylpyrimidines and analogues as antibacterial agents. 11. Quinolylmethyl analogues with basic substituents conveying specificity. | 1989 Aug | 1 |
25 | 3052577 | Dihydrofolate reductase from Escherichia coli: the kinetic mechanism with NADPH and reduced acetylpyridine adenine dinucleotide phosphate as substrates. | 1988 Jul 26 | 1 |
26 | 3275776 | Evaluation of the importance of hydrophobic interactions in drug binding to dihydrofolate reductase. | 1988 Jan | 1 |
27 | 7011378 | Kinetics of substrate, coenzyme, and inhibitor binding to Escherichia coli dihydrofolate reductase. | 1981 Feb 17 | 1 |