17 articles for thisTarget
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Synthesis and bioactivity of฿-substituted fosmidomycin analogues targeting 1-deoxy-D-xylulose-5-phosphate reductoisomerase.
Universiteit Gent
Catechol-rhodanine derivatives: Specific and promiscuous inhibitors of Escherichia coli deoxyxylulose phosphate reductoisomerase (DXR).
University of Strasburg
Binding modes of reverse fosmidomycin analogs toward the antimalarial target IspC.
Heinrich Heine Universit£T
Development of inhibitors of the 2C-methyl-D-erythritol 4-phosphate (MEP) pathway enzymes as potential anti-infective agents.
University of Groningen
AFMoC enhances predictivity of 3D QSAR: a case study with DOXP-reductoisomerase.
Philipps University
Growth inhibition of Mycobacterium smegmatis by prodrugs of deoxyxylulose phosphate reducto-isomerase inhibitors, promising anti-mycobacterial agents.
University of Strasburg
Structures of 1-Deoxy-D-Xylulose-5-Phosphate Reductoisomerase/Lipophilic Phosphonate Complexes.
Baylor College of Medicine
Substrate analogs for the investigation of deoxyxylulose 5-phosphate reductoisomerase inhibition: synthesis and evaluation.
Oregon State University
Synthesis and biological evaluation of cyclopropyl analogues of fosmidomycin as potent Plasmodium falciparum growth inhibitors.
Ghent University
Synthesis of alpha-substituted fosmidomycin analogues as highly potent Plasmodium falciparum growth inhibitors.
Ghent University
Novel reverse thia-analogs of fosmidomycin: Synthesis and antiplasmodial activity.
Heinrich Heine University D£Sseldorf
Isoprenoid biosynthesis as a drug target: bisphosphonate inhibition of Escherichia coli K12 growth and synergistic effects of fosmidomycin.
University of Illinois At Urbana - Champaign
Flavonoids: true or promiscuous inhibitors of enzyme? The case of deoxyxylulose phosphate reductoisomerase.
University of Strasburg
Hydroxybenzaldoximes Are D-GAP-Competitive Inhibitors of E. coli 1-Deoxy-D-Xylulose-5-Phosphate Synthase.
The Johns Hopkins University School of Medicine
A fragment-based approach to understanding inhibition of 1-deoxy-D-xylulose-5-phosphate reductoisomerase.
University of Bristol