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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.
4                                              Cathepsin V, a thymus and testis-specific human cysteine
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
7     In this study, a total of 11 chimeras of cathepsins V and L were generated to identify elastin-bi
8  1.6 A resolution crystal structure of human cathepsin V associated with an irreversible vinyl sulfon
9                            Gene silencing of cathepsin V by siRNA in human SK-N-MC cells results in r
10  to cathepsin L, but similar to cathepsin S, cathepsin V exhibited only a very weak collagenolytic ac
11                                Whereas human cathepsin V exhibits a potent elastolytic activity, the
12 than 80%, illustrating the prominent role of cathepsin V for neuropeptide production.
13 ndings indicate the unique function of human cathepsin V for producing enkephalin and NPY neuropeptid
14        Findings here show that expression of cathepsin V in neuroendocrine PC12 cells and human neuro
15 t could be exploited in identifying specific cathepsin V inhibitors or in identifying inhibitors of o
16                                              Cathepsin V is a highly effective elastase and has been
17                                              Cathepsin V is a human-specific cysteine protease gene.
18                                              Cathepsin V is a lysosomal cysteine protease that is exp
19 yet described among human proteases and that cathepsin V is present in atherosclerotic plaque specime
20                                              Cathepsin V is present in human brain cortex and hippoca
21 can be attributed to cysteine proteases with cathepsins V, K, and S contributing equally.
22            Degradative enzymes examined were cathepsin V/L2 and matrix metalloproteinase (MMP)-1, -2,
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
28      In vitro processing of proenkephalin by cathepsin V occurs at dibasic residue sites to generate
29 udy demonstrates the novel function of human cathepsin V protease for producing the neuropeptides enk
30                A homology structure model of cathepsin V revealed completely different electrostatic
31                              A comparison of cathepsin V's active site with the active sites of relat
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
34                                 Furthermore, cathepsin V was determined to be significantly more stab
35              The S2P2 subsite specificity of cathepsin V was found to be intermediate between those o
36                                              Cathepsin V was mapped to the chromosomal region 9q22.2,
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
39                            Colocalization of cathepsin V with enkephalin and NPY in secretory vesicle
40                   Furthermore, expression of cathepsin V with proNPY results in NPY production.

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