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1 with differences in the cellular contents of muramidase-1 or muramidase-2, with the levels of PBP 5 p
2 in the cellular contents of muramidase-1 or muramidase-2, with the levels of PBP 5 produced, or with
3 idoglycan O-acetylation modulates endogenous muramidase activity affecting the cell-surface propertie
5 ectly involved in rod formation and that the muramidase activity of FlgJ, though needed for formation
7 the hypothesis that the catalytic activity (muramidase activity) of lysozyme is not required for bac
11 d sensitivity of mutant cell walls to the M1 muramidase and decreased sensitivity to lysostaphin, whi
18 s: (i) an N-terminal domain with homology to muramidases from several gram-positive bacterial species
20 the two catalytic domains and found that the muramidase is essential, whereas the peptidase is partia
21 ed accumulation of SecA2 substrate, N-acetyl muramidase (NamA) in the cell wall, providing evidence f
22 Surprisingly, FlgJ functions as neither a muramidase nor a lytic transglycosylases but rather as a
25 tants were more sensitive than the parent to muramidases such as hen egg white lysozyme and to the Cw
28 s present on mucosal surfaces is lysozyme, a muramidase that hydrolyzes the peptidoglycan backbone of
29 ted with bacterial resistance to lysozyme, a muramidase that serves as a central component of innate
32 en suggested that it is a flagellum-specific muramidase which locally digests the peptidoglycan layer
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