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1 ld better therapeutic index than the natural tyrocidine.
3 eptide thioester with the native sequence of tyrocidine A and can additionally cyclize peptide analog
6 nking glycans directly to the Asn residue of tyrocidine A diminished its antibacterial activity, but
7 yclic beta-hairpin antimicrobial decapeptide tyrocidine A, (Tyrc A) was substituted with the d-Phe-2-
8 decapeptide-thioester to form the antibiotic tyrocidine A, and can catalyse pentapeptide-thioester di
9 rting from the cyclic decapeptide antibiotic tyrocidine A, this chemoenzymatic approach allows us to
10 for the production of the cyclic decapeptide tyrocidine A, TycC TE, retains autonomous ability to cat
13 irectly against bacterial cells identified a tyrocidine analogue of improved antibacterial activity.
14 ocidine synthetase, 13 head-to-tail cyclized tyrocidine derivatives were obtained with one to three p
16 osomal peptides (NRP) such as the antibiotic tyrocidine have D-amino acids, introduced by epimerase (
18 hioesterase (TE) domain from the multidomain tyrocidine nonribosomal peptide synthetase (NRPS) was re
19 we show that the excised TE domain from the tyrocidine NRPS can be used to generate an array of size
20 ults demonstrate that the TE domain from the tyrocidine NRPS can catalyze cyclization of depsipeptide
21 The excised thioesterase domain from the tyrocidine NRPS has been shown to catalyze the cyclizati
22 re we report that the excised TE domain from tyrocidine synthetase efficiently catalyses cyclization
23 iction and establish that the C(5) domain of tyrocidine synthetase is indeed (D)C(L), the apoT (thiol
24 strate that the first condensation domain of tyrocidine synthetase shows low selectivity at the donor
25 This specificity profile indicates that the tyrocidine synthetase TE, and by analogy many other TE d
26 g a thioesterase domain from the decapeptide tyrocidine synthetase, 13 head-to-tail cyclized tyrocidi
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