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Insights into the slow-onset tight-binding inhibition of Escherichia coli Dihydrofolate Reductase: detailed mechanistic characterization of Pyrrolo [3,2-f] quinazoline-1,3-diamine and its derivatives as novel tight-binding inhibitors
Dihydrofolate reductase, DHFR, is a pivotal enzyme involved in the de novo pathway for purine synthesis, and hence, represents an attractive target to disrupt systems that require rapid DNA turnover. The enzyme acquires resistance to available drugs by various molecular mechanisms, which necessitate...
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| Publicado en: | FEBS J |
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| Autores principales: | , |
| Formato: | Artigo |
| Lenguaje: | Inglês |
| Publicado: |
2015
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| Materias: | |
| Acceso en línea: | https://ncbi.nlm.nih.gov/pmc/articles/PMC4445455/ https://ncbi.nlm.nih.gov/pubmed/25703118 https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1111/febs.13244 |
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