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1 e 60-fold more toxic to mammalian cells than anthrax lethal factor.
2 structural similarities and differences with anthrax lethal factor.
3 ve been shown to act as potent inhibitors of anthrax lethal factor and may have potential application
4 y also inactivated the enzymatic activity of anthrax lethal factor and protected murine RAW-264.7 cel
5 holera toxin beta-subunit, diphtheria toxin, anthrax lethal factor and protective antigen, Staphyloco
6 fA is related to the catalytic domain of the anthrax lethal factor and the Mop protein involved in th
7 alogs to kill Staphylococcus aureus, inhibit anthrax lethal factor, and bind human immunodeficiency v
9 n that is conserved in anthrax edema factor, anthrax lethal factor, and botulinum neurotoxin serotype
10 hemical library against protease activity of anthrax lethal factor, and report a compound that inhibi
12 , treatment with the MEK inhibitors U0126 or anthrax lethal factor delayed GVBD and prevented spindle
13 Certhrax shares 31% sequence identity with anthrax lethal factor from Bacillus anthracis; however,
14 inum neurotoxin (BoNT) serotypes A and B and anthrax lethal factor in the picomolar range was demonst
16 an anti-cancer fusion protein consisting of anthrax lethal factor (LF) and the catalytic domain of P
18 -aa polypeptide that facilitates the exit of anthrax lethal factor (LF) from the endosome to the cyto
24 ensin RTD-1 is a noncompetitive inhibitor of anthrax lethal factor (LF) protease (IC50 = 390 +/- 20 n
25 ion of a cell-based fluorescent reporter for anthrax lethal factor (LF) protease activity using the p
26 s have also been evaluated for inhibition of anthrax lethal factor (LF), an unrelated metalloprotease
29 ly to its ability to kill S. aureus, inhibit anthrax lethal factor (LF), bind gp120 of HIV-1, dimeriz
31 98, George Vande Woude's lab discovered that anthrax lethal factor (LF), the principal virulence comp
34 ains the first of the two cleavage sites for anthrax lethal factor protease that have been found in t
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