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1 intracellularly with the latter credited to cathepsin V.
2 ne proteases that would be selective against cathepsin V.
3 rated to identify elastin-binding domains in cathepsin V.
5 d in atherosclerotic plaques, an increase of cathepsins V and K activities may accelerate the destruc
6 ically inhibit the elastolytic activities of cathepsins V and K via the formation of specific catheps
8 1.6 A resolution crystal structure of human cathepsin V associated with an irreversible vinyl sulfon
10 to cathepsin L, but similar to cathepsin S, cathepsin V exhibited only a very weak collagenolytic ac
13 ndings indicate the unique function of human cathepsin V for producing enkephalin and NPY neuropeptid
15 t could be exploited in identifying specific cathepsin V inhibitors or in identifying inhibitors of o
19 yet described among human proteases and that cathepsin V is present in atherosclerotic plaque specime
23 In addition, decreased TIMP-1 and increased cathepsin V/L2 levels may play a role in the matrix degr
24 activity (P < 0.03); a 1.5-fold increase of cathepsin V/L2 mRNA (P < 0.03) and abnormal protein dist
25 ioxidant enzymes, matrix metalloproteinases, cathepsin V/L2, and tissue inhibitor of matrix metallopr
26 Keratoconus corneas have elevated levels of cathepsins V/L2, -B, and -G, which can stimulate hydroge
27 ly, the electrostatic potential of the human cathepsin V model structure resembled that of the model
29 udy demonstrates the novel function of human cathepsin V protease for producing the neuropeptides enk
32 k for understanding the structural basis for cathepsin V's activity and will aid in the design of inh
33 contributing to the elastolytic activity of cathepsin V that are distant from the active cleft of th
37 model-based electrostatic potential of human cathepsin V was neutral to weakly positive at and in the
38 press a third elastolytic cysteine protease, cathepsin V, which exhibits the most potent elastase act
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