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- W1994296952 abstract "Species differences among dihydrofolate reductases were first detected and most strikingly illustrated by the selective binding of small molecule inhibitors. This led on the one hand to practical applications in the chemotherapy of microbial infections, and on the other hand to stimuli for sequence and conformation studies of representative enzymes. The recent availability of the requisite tools has amply confirmed the existence of large differences in sequence among bacterial enzymes and between bacterial and mammalian enzymes. The latter, although more homogeneous than bacterial enzymes, still exhibit many sequence differences. Current work has provided x-ray conformations of two bacterial enzyme complexes, but similar studies of a mammalian enzyme are not yet available. Consequently, the site and mode of binding of the selective inhibitors are still speculative sequence and conformation studies are potentially valuable for the design of selective inhibitors, but their employment in this fashion awaits further developments." @default.
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- W1994296952 title "Dihydrofolate reductases as targets for inhibitors" @default.
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- W1994296952 doi "https://doi.org/10.1016/0065-2571(80)90025-4" @default.
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