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1 ed that all four cell lines expressed latent progelatinase A (M(r) 66,000).
2                                              Progelatinase A (proGLA) activation is thought to be ini
3                                              Progelatinase A (ProMMP-2) was present in all the vitreo
4 concentrations, serves as an intermediate in progelatinase A activation by binding to activated membr
5                                              Progelatinase A activation requires its binding to a com
6 enzyme at Tyr112, but also directly mediated progelatinase A activation via a two-step proteolytic ca
7 ribed to MT-MMP-1 is its ability to act as a progelatinase A activator, purified transmembrane deleti
8 an activator of the matrix metalloproteinase progelatinase A at cell surfaces.
9                We conclude that HSCs produce progelatinase A during activation in vitro and activate
10 -2 matrix metalloproteinase can also process progelatinase A in a comparable fashion to the type-1 at
11                      Its ability to activate progelatinase A is dependent on its proteolytic activity
12  results suggest that cellular activation of progelatinase A may be initiated by different members of
13                                              Progelatinase A occurred in all vitrectomy samples.
14          Here we show that the activation of progelatinase A occurs within the cell and that the acti
15 urfaces as active species, ready to activate progelatinase A or degrade ECM molecules.
16 nse oligonucleotide inhibition of endogenous progelatinase A production, or the MMP inhibitor 1,10-ph
17 , MT4-MMPCD was also able to activate 72-kDa progelatinase A to its 68-kDa form.
18 ther MT-MMPs, MT5-MMP specifically activates progelatinase A when co-expressed in Madin-Darby canine
19 t cells with the ability to not only process progelatinase A, but also directly degrade extracellular
20        Legumain was demonstrated to activate progelatinase A.
21 es, independent of its downstream substrate, progelatinase A.
22 if HE255LGH renders MT5-MMP inactive against progelatinase A.
23 ability to both degrade gelatin and activate progelatinase A.
24 ly or indirectly mediating the activation of progelatinase A.
25 ansfected cells and subsequent activation of progelatinase A.
26 ysis or via activating other enzymes such as progelatinase A.
27 , which inhibit mast cell chymase, prevented progelatinase activation.
28 l 13 amino acids of the purified mastocytoma progelatinase are 50-67% identical to those of human, mo
29 of plasminogen resulted in activation of the progelatinases associated with the vesicles, indicating
30 tifies the protease as a canine homologue of progelatinase B (92-kDa gelatinase, MMP-9), determines t
31 ast cell alpha-chymase cleaves and activates progelatinase B (progel B).
32                                              Progelatinase B (ProMMP-9) was found in approximately 80
33  collagenase-3 and our results indicate that progelatinase B activation proceeds via bimolecular clea
34 nt on C-terminal domain interactions between progelatinase B and collagenase-3, as assessed using wil
35  reactive stroma, whereas MCP-4 can activate progelatinase B and induce hyperplastic skin to become a
36                                  Cleavage of progelatinase B by purified dog alpha-chymase yielded an
37                                              Progelatinase B can be activated in vitro by organomercu
38 stimuli may regulate the amount of mast cell progelatinase B expressed by mast cells.
39                                 Induction of progelatinase B is blocked by U-73122, Ro31-8220, and th
40                                              Progelatinase B mRNA and enzyme expression are strongly
41 cells secrete a metalloproteinase related to progelatinase B that is directly activated outside of th
42 anules by degranulating mast cells, converts progelatinase B to an enzymatically active form.
43                                        Human progelatinase B was activated by collagenase-3 in a time
44 dog mastocytoma cells constitutively secrete progelatinase B which is activated by alpha-chymase.
45 elastolytic matrix metalloproteinases (MMPs) progelatinase B, prometalloelastase, and promatrilysin.
46 04-amino acid protein 80% identical to human progelatinase B.
47 l to those of human, mouse, and rabbit 92-kD progelatinase (gelatinase B; matrix metalloproteinase-9)
48 es, mastocytoma cell chymase activated 92-kD progelatinase in the absence of other enzymes or cofacto
49  phenotype alongside increased expression of progelatinase MMP-3 in WT mice.
50 present in secretory granules hydrolyzed the progelatinase to active fragments.
51  gelatinase B, a 2.3-kilobase clone encoding progelatinase was isolated from a BR mastocytoma library
52                          Replacing Asp432 in progelatinase with either Glu, Asn, Gly, or Lys resulted

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