Results 11 to 20 of about 48,162 (258)
Affinity chromatography of dihydrofolate reductase [PDF]
1. Dihydrofolate reductase was purified from Lactobacillus casei MTX/R, and studied on affinity columns containing folic acid and methotrexate. Two forms of the enzyme were interconverted by incubation with substrates. 2. Affinity columns were prepared from agarose activated with cyanogen bromide and coupled with 1,6-diaminohexane.
N. G. L. Harding, P. C. H. Newbold
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Adaptations for Pressure and Temperature in Dihydrofolate Reductases [PDF]
Enzymes from extremophilic microbes that live in extreme conditions are generally adapted so that they function under those conditions, although adaptations for extreme temperatures and pressures can be difficult to unravel. Previous studies have shown mutation of Asp27 in Escherichia coli dihydrofolate reductase (DHFR) to Glu27 in Moritella profunda ...
Ryan W. Penhallurick+3 more
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Tales of Dihydrofolate Binding to R67 Dihydrofolate Reductase
Homotetrameric R67 dihydrofolate reductase possesses 222 symmetry and a single active site pore. This situation results in a promiscuous binding site that accommodates either the substrate, dihydrofolate (DHF), or the cofactor, NADPH. NADPH interacts more directly with the protein as it is larger than the substrate.
Michael R. Duff+5 more
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DHFR (dihydrofolate reductase) [PDF]
Dihydrofolate reductase (DHFR) is a member of the reductase enzyme family, which is ubiquitously expressed in all organisms. Levels of this enzyme peak at the G1/S cell cycle boundary. Autoregulation, through DHFR-RNA interactions, has also been reported.
Krajinovic, Maja+2 more
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Objectives/Background: Dihydrofolate reductase (DHFR) is one of the validated drug targets in Mycobacterium tuberculosis (Mtb) infection. DHFR inhibitors have been used to treat various life-threatening diseases such as cancer, malaria, and several ...
Mymoona Akhter
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Mining electron density for functionally relevant protein polysterism in crystal structures. [PDF]
This review focuses on conceptual and methodological advances in our understanding and characterization of the conformational heterogeneity of proteins.
Fraser, James S, Jackson, Colin J
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A novel bicyclic 2,4-diaminopyrimidine inhibitor of Streptococcus suis dihydrofolate reductase [PDF]
Streptococcus suis is a Gram-positive bacterial pathogen of pigs and an emerging zoonotic pathogen. It has become increasingly resistant to multiple classes of antibiotics.
Warangkhana Songsungthong+5 more
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A designed phenylalanyl-tRNA synthetase variant allows efficient in vivo incorporation of aryl ketone functionality into proteins [PDF]
Incorporation of non-natural amino acids into proteins in vivo expands the scope of protein synthesis and design. p-Acetylphenylalanine was incorporated into recombinant dihydrofolate reductase (DHFR) in Escherichia coli via a computationally designed ...
Carrico, Isaac S.+4 more
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A trimethoprim derivative impedes antibiotic resistance evolution
The efficacy of the antibiotic trimethoprim, which inhibits bacterial dihydrofolate reductase (DHFR), is limited by the rapid emergence of resistant bacteria. Here, Manna et al.
Madhu Sudan Manna+15 more
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Tissue-specific expression from a compound TATA-dependent and TATA-independent promoter [PDF]
We have found that the mouse metallothionein-I (MT-I) gene promoter functions in an unusual, compound manner. It directs both TATA-dependent and TATA-independent modes of transcription in vivo.
Garrity, Paul A., Wold, Barbara J.
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