Sort   by:  
 Page size 
MetabolomicsMetabolic response to point mutations reveals principles of modulation of in vivo enzyme activity and phenotype
The relationship between sequence variation and phenotype is poorly understood. Here, we use metabolomic analysis to elucidate the molecular mechanism underlying the filamentous phenotype of E. coli strains that carry destabilizing mutations in dihydrofolate reductase (DHFR). We find that partial lo...
2021-06-30 | MTBLS2795 | MetaboLights
ProteomicsHuman dihydrofolate reductase is a substrate of protein kinase CK2α
Dihydrofolate reductase (DHFR) is a prominent molecular target in antitumor, antibacterial and antiprotozoan chemotherapies. Our in silico amino acid sequence and 3D structure analyses revealed the presence of several putative CK2 phosphorylation sites. Indeed, CK2α subunit phosphorylated DHFR in v...
ORGANISM(S): Homo sapiens (Human) 
2019-04-15 | PXD011853 | Pride
Lc-ms/ms Ck2 : dihydrofolate reductase Protein phosphorylation Protein mutants Phosphoproteomics 
Genomics
Laboratory evolution of dihydrofolate reductase (DHFR)
PRJNA923701 | ENA
TranscriptomicsMicroarray Profiling of Messenger RNAs Associated with DHFR Knock-down and DHFR2 Knockout in HepG2 cell line
Dihydrofolate reductase activity is essential for the maintenance of One Carbon Metabolism, as it provides the pathway with tetrahydrofolate (the biologically active form of folate). Most of this cellular activity is due to DHFR. Its paralogue DHFR2 was thought to be responsible for mitochondrial di...
ORGANISM(S): Homo sapiens 
2024-02-01 | E-MTAB-12958 | biostudies-arrayexpress
UnknownSubstrate channeling between the human dihydrofolate reductase and thymidylate synthase.
Not available
S-EPMC4815301 | biostudies-literature
UnknownTales of Dihydrofolate Binding to R67 Dihydrofolate Reductase.
Not available
S-EPMC5147970 | biostudies-literature
UnknownCarbon-deuterium bonds as probes of dihydrofolate reductase.
Not available
S-EPMC2748670 | biostudies-literature
ProteomicsmHtt tobacco roots proteome, QEHFX
Samples were analyzed using a nanoACQUITY UPLC system (Waters) coupled to a Q-Exactive HF-X high resolution accurate mass tandem mass spectrometer (Thermo) via a nanoelectrospray ionization source. Briefly the sample was first trapped on a Symmetry C18 180 micron x 20 mm trapping column (5 microlite...
ORGANISM(S): Nicotiana Tabacum (ncbitaxon:4097) 
2019-11-07 | MSV000084557 | MassIVE
UnknownComputational Development of Inhibitors of Plasmid-Borne Bacterial Dihydrofolate Reductase.
Not available
S-EPMC9220120 | biostudies-literature
UnknownThe former annotated human pseudogene dihydrofolate reductase-like 1 (DHFRL1) is expressed and functional.
Not available
S-EPMC3174580 | biostudies-literature
Sort   by:  
 Page size