2.7.7.60	analysis	CTP:phosphocholine cytidylyltransferase enzyme assay that employs separation of non-radioactive 4-(cytidine 5'-diphospho)-2-C-methyl-D-erythritol from CTP. The assay can be applied to glycerol 3-phosphate cytidylyltransferase and CTP:2-C-methyl-D-erythritol-4-phosphate cytidylyltransferase synthetase (CMS), members of the cytidylyltransferase family that produce CDP-glycerol and CDP-methylerythritol, respectively	737438	
2.7.7.60	biotechnology	high-throughput methods for the screening of 2C-methyl-D-erythritol synthase IspC protein, 4-diphosphocytidyl-2C-methyl-D-erythritol synthase IspD protein, 4-diphosphocytidyl-2Cmethyl-D-erythritol kinase IspE protein, and 2C-methyl-D-erythritol 2,4-cyclodiphosphate synthase IspF protein, against large compound libraries. Assays use up to three auxiliary enzymes monitored at 340 and all robust	675583	
2.7.7.60	drug development	2-C-methyl-D-erythritol 4-phosphate cytidyltransferase, enzyme IspD, is a potential therapeutic drug target in Plasmodium vivax	-, 761199	
2.7.7.60	drug development	due to the absence of the pathway in mammals enzyme provides a potential target for new antibiotics	660578, 660697	
2.7.7.60	drug development	insights in structure and function of MtIspD	-, 692926	
2.7.7.60	drug development	IspD is a druggable target for the development of additional antimalarial agents. 1R,3S-MMV008138 shows promise as a potential scaffold for target-based antimalarial drug development	760261	
2.7.7.60	drug development	PfIspD enzyme inhibitor MMV008138 does not target the human IspD, reinforcing MMV008138 as a prototype of a distinct class of species-selective IspD-targeting antimalarial agents	760263	
2.7.7.60	drug development	the methyl erythritol phosphate (MEP) pathway, including enzyme MEP cytidylyltransferase (IspD), represents an attractive series of targets for antibiotic design, considering each enzyme of the pathway is both essential and has no human homologues	-, 760333	
2.7.7.60	medicine	the structure of CMS of Mycobacterium tuberculosis could be a starting point for structure-based design of new antituberculosis drugs	-, 705229