EC Number |
Application |
Reference |
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1.5.1.3 | analysis |
development of a survival protein-fragment complementation assay based on dihydrofolate reductase. Proteins of interest are fused to complementary fragments of dihydrofolate reductase. If the proteins of interst interact physically, the dihydrofolate complementary fragments are brought together and fold into the native structure, reconstituting its activity |
689136 |
1.5.1.3 | analysis |
development of a yeast protein fragment complementation assay system using dihydrofolate reductase and application for investigating eukaryotic protein-protein interaction in vivo. Fusion of human oncoprotein Ras and Ras-binding domain of Raf-1 to dihydrofolate reductase as a model and evaluation of interaction between these proteins |
684654 |
1.5.1.3 | analysis |
heteroduplex tracking assay to detect dihydrofolate redctase L164-mutations in variants representing 1% of the parasites in an individual host |
684381 |
1.5.1.3 | analysis |
selectable and amplifiable gene marker for e.g. somatic cell hybridization studies |
392209 |
1.5.1.3 | analysis |
study of protein dynamics, using a pump-probe method that employs pulsed-laser photothermal heating of a gold nanoparticle (AuNP) to directly excite a local region of the protein structure and transient absorbance to probe the effect on enzyme activity. Activity is accelerated by pulsed-laser excitation when the AuNP is attached close to a network of coupled motions in DHFR. No rate acceleration is observed when the AuNP is attached away from the network with pulsed excitation, or for any attachment site with continuous wave excitation |
765687 |
1.5.1.3 | analysis |
use of multiple protein structure technique for structure-based drug discovery. Construction of receptor-based pharmacophores using multiple X-ray crystallographic structures. Models incorporate a fair degree of protein flexibility and are highly selective for known inhibitors over drug-like non-inhibitors |
687287 |
1.5.1.3 | biotechnology |
in vivo screening system to select for functionally active proteins with increased solubility. Fusion of enzyme to green fluorescent protein as reporter for solubility |
676933 |
1.5.1.3 | biotechnology |
method for screening combinatorial or other libraries of enzyme based on affinities of the inhibitors with the enzyme |
671315 |
1.5.1.3 | biotechnology |
method for screening combinatorial or other libraries of Plasmodium falciparum enzyme based on affinities of the inhibitors with the enzyme |
671315 |
1.5.1.3 | drug development |
comparison of Danio rerio and human enzyme to evaluate the suitability of the fish enzyme as an assay system for antifolate drug discovery. Structural and kinetic proterties of both enzymes are similar and susceptibilites to known inhibitors are also comparable |
686360 |