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1 inhibited by the serine protease inhibitor, phenylmethylsulfonyl fluoride.
2 ly inhibited by a serine protease inhibitor, phenylmethylsulfonyl fluoride.
3 Activity was inhibited by EDTA but not by phenylmethylsulfonyl fluoride.
4 oteasome inhibitors, but could be blocked by phenylmethylsulfonyl fluoride.
5 PSF is 210 times as potent as phenylmethylsulfonyl fluoride.
6 inositol-acyltransferase, it is inhibited by phenylmethylsulfonyl fluoride.
7 ocked by diisopropyl fluorophosphate (1 mm), phenylmethylsulfonyl fluoride (3 mm), leupeptin (100 mic
8 d mutant, and cells grown in the presence of phenylmethylsulfonyl fluoride (a serine protease inhibit
10 inhibit aggregate clearance, treatment with phenylmethylsulfonyl fluoride, an inhibitor of vacuolar
11 was inhibited by serine protease inhibitors phenylmethylsulfonyl fluoride and 4-(2-aminoethyl)-benze
12 and we observed that the protease inhibitors phenylmethylsulfonyl fluoride and alpha-macroglobulin co
14 lated GPI intermediates is inhibited by both phenylmethylsulfonyl fluoride and diisopropyl fluoride.
16 nyl phenylalanyl chloromethyl ketone), PMSF (phenylmethylsulfonyl fluoride), and dichloroisocoumarin,
17 nder cell-free conditions in the presence of phenylmethylsulfonyl fluoride, AR underwent Ca(2+)-depen
18 reversible by calpain inhibitors and not by phenylmethylsulfonyl fluoride, caspase inhibitors, or la
19 e activity by diisopropyl fluorophosphate or phenylmethylsulfonyl fluoride imply that protease IV is
21 yloliquefaciens determined by titration with phenylmethylsulfonyl fluoride is 25% higher than the con
23 the enzyme with 1 mM N-ethylmaleimide, 1 mM phenylmethylsulfonyl fluoride, or 3.1 microM bromoenol l
24 d leupeptin, but not for by pepstatin, EDTA, phenylmethylsulfonyl fluoride, or phenanthroline, consis
25 s potentially susceptible to inactivation by phenylmethylsulfonyl fluoride (PMSF) and benzenesulfonyl
26 e to commonly used serine-modifying reagents phenylmethylsulfonyl fluoride (PMSF) and diisopropylfluo
27 by inhibition of its enzymatic activity with phenylmethylsulfonyl fluoride (PMSF) or heat treatment.
28 i-PRCP, diisopropyl-fluorophosphonate (DFP), phenylmethylsulfonyl fluoride (PMSF), and Z-Pro-Proaldeh
29 d that the commonly used protease inhibitor, phenylmethylsulfonyl fluoride (PMSF), forms a covalent c
30 myeloperoxidase, lactoferrin, proteinase 3, phenylmethylsulfonyl fluoride (PMSF)-inactivated HLE, or
31 fact that the esteriflcation of retinol was phenylmethylsulfonyl fluoride resistant suggests that th
32 ed about 7-fold more palmityl-CoA-dependent, phenylmethylsulfonyl fluoride-resistant retinol esterifi
33 ncubation with the serine protease inhibitor phenylmethylsulfonyl fluoride resulted in complete abrog
34 was blocked by pretreating cathepsin G with phenylmethylsulfonyl fluoride, strongly implying that ox
36 his antiresorptive activity was abolished by phenylmethylsulfonyl fluoride, suggesting the importance
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