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1 re sensitive to KAS inhibitors cerulenin and thiolactomycin.
2 , S. pneumoniae FabH was weakly inhibited by thiolactomycin.
3 from acetyl-CoA increases in the presence of thiolactomycin.
4 rom butyryl-CoA decreases in the presence of thiolactomycin.
6 extracts were both effectively inhibited by thiolactomycin, a known type II fatty acid synthase inhi
7 vivo, although it was much less potent than thiolactomycin, a validated fatty acid synthesis inhibit
8 olved, we enzymatically interrogated diverse thiolactomycin analogues and prepared an unnatural thiot
9 n addition, purified mtFabH was sensitive to thiolactomycin and resistant to cerulenin in an in vitro
12 nthesis from acetyl-CoA is less sensitive to thiolactomycin, and it is suggested that the basis for t
14 mycobacterial phospholipid and with several thiolactomycin derivatives that were designed as substra
17 that mtFabH may not be the primary target of thiolactomycin inhibition in vivo and led to several cha
20 additional set of in vivo experiments using thiolactomycin provides support for the role of FabH and
21 eriments demonstrated that concentrations of thiolactomycin ranging from 0.1 to 0.2 mg/ml produced bo
22 on in Mycobacterium bovis BCG did not confer thiolactomycin resistance, suggesting that mtFabH may no
23 is and characterization of optically pure 5R-thiolactomycin (TLM) analogues that show improved whole
30 ors have previously been reported, including thiolactomycin (TLM), which is produced by Nocardia spp.
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