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1 roteasome inhibitors NLVS, MG132, and clasto-lactacystin beta-lactone.
2 ) to the active proteasome inhibitor, clasto-lactacystin beta-lactone.
3 acy of the active lactacystin analog, clasto-lactacystin beta-lactone.
4 y lactacystin, MG132, epoxomicin, and clasto-lactacystin beta-lactone.
5 -L-leucyl-L-leucyl-L-norvalinal), and clasto-lactacystin-beta-lactone].
6 show that proteasome inhibition with clasto-lactacystin beta-lactone (4 microM, 1 h) stabilizes the
7 he degradation of apoB was reduced by clasto-lactacystin beta-lactone, a potent proteasome inhibitor,
8 n was inhibited to a lesser extent by clasto-lactacystin beta-lactone, ALLN, and Nalpha-tosyl-L-pheny
9 rentiation, the proteasome inhibitors clasto-lactacystin beta-lactone and carbobenzoxy-leucinyl-leuci
10 t lactacystin acts as a precursor for clasto-lactacystin beta-lactone and that the latter is the sole
11 retase cleavage was not observed with clasto-lactacystin beta-lactone and thus, cannot be attributed
12 However, proteasome-specific inhibitors, lactacystin-beta-lactone and epoxomicin, could not stabi
13 roteasome inhibitors (lactacystin and clasto-lactacystin beta-lactone) and was associated with elevat
14 en with another proteasome inhibitor, clasto-lactacystin beta-lactone, but not with an inhibitor of v
15 on of the 26S proteasome by MG115 and clasto-lactacystin-beta-lactone enhanced the accumulation of hi
18 -Phe-chloromethylketone (AAF-cmk) and clasto-lactacystin beta-lactone (lactacystin), an inhibitor of
20 Treatment at 48 h with LLL but not clasto-lactacystin beta-lactone resulted in partial uncoupling
21 as inactivated by the ester inhibitor clasto-lactacystin-beta-lactone severalfold faster than the wt,
22 presence of the proteosome inhibitor clasto-lactacystin beta-lactone, suggesting that p12(DOC-1) may
24 oteasome inhibitors (NLVS, MG132, and clasto-lactacystin beta-lactone) were tested for their ability
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