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1 aneously increasing tissue inhibitor of MMP (tissue inhibitor of metalloproteinase 2).
2 E cells, without affecting the expression of tissue inhibitor of metalloproteinase 2.
3 ilage degradation by augmenting induction of tissue inhibitor of metalloproteinase 2.
4 alloproteinase-2 and increased expression of tissue inhibitor of metalloproteinase-2.
5 proteinase, and significant up-regulation of tissue inhibitor of metalloproteinase-2.
6 ular matrix, an effect inhibitable by excess tissue inhibitor of metalloproteinase-2.
7 tor GM6001 or the specific MT1-MMP inhibitor tissue inhibitor of metalloproteinases 2.
8 ercellular adhesion molecule-1, eotaxin, and tissue inhibitor of metalloproteinases-2.
9 t activation of pro-MMP-2 in the presence of tissue inhibitor of metalloproteinases-2.
10 nd MMP19, and increased transcript levels of tissue inhibitors of metalloproteinase 2.
11 oMTb decreased expression of the inhibitors, tissue inhibitor of metalloproteinase-2, -3, and -4.
12 ling was associated with decreased levels of tissue inhibitors of metalloproteinase 2, -3, and -4 and
13 ne domain in the biosensor or treatment with tissue inhibitor of metalloproteinase-2, a cell-impermea
14 crossed with transgenic mice overexpressing tissue inhibitor of metalloproteinase-2-a natural MMP in
15 cient adenovirus carrying the cDNA for human tissue inhibitor of metalloproteinase-2 (AdCMV.hTIMP-2)
16 ulinlike growth factor-binding protein 7 and tissue inhibitor of metalloproteinases 2 after surgery (
17 issue inhibitor of metalloproteinases-1, and tissue inhibitor of metalloproteinases-2 all potently bl
19 r operating characteristic curve (95% CI) of tissue inhibitor of metalloproteinase-2 and insulin-like
20 the effect of nonrenal organ dysfunction on tissue inhibitor of metalloproteinase-2 and insulin-like
21 for each patient on enrollment and compared tissue inhibitor of metalloproteinase-2 and insulin-like
24 In multivariate analysis, the addition of tissue inhibitor of metalloproteinase-2 and insulin-like
25 he performance of the model with and without tissue inhibitor of metalloproteinase-2 and insulin-like
26 ating factor, stromal cell-derived factor-1, tissue inhibitor of metalloproteinase 2, and von Willebr
27 a membrane-associated factor, inhibited with tissue inhibitor of metalloproteinase-2, and abolished w
28 content, potentially through an increase in tissue inhibitor of metalloproteinase-2, and transmigrat
29 luble TSP2, with the MMP inhibitors BB94 and tissue inhibitor of metalloproteinase-2, and with a neut
30 tion in terms of facilitating (125)I-labeled tissue inhibitor of metalloproteinase 2 binding to trans
31 MMP-dependent, as it is blocked by BB-94 and tissue inhibitor of metalloproteinases-2 but not by inhi
32 urnover: matrix metalloproteinase 2 (MMP-2), tissue inhibitor of metalloproteinases 2, C-terminal typ
33 rofibrotic (transforming growth factor beta, tissue inhibitor of metalloproteinase 2, collagen type I
34 nfirmed the involvement of the MT1-MMP/MMP-2/tissue inhibitor of metalloproteinase-2 complex in this
36 itors, pigment epithelium-derived factor and tissue inhibitor of metalloproteinase-2, have been detec
39 adation by augmenting expression of mRNA for tissue inhibitor of metalloproteinases 2 that is inhibit
41 gative RCC cells expressed reduced levels of tissue inhibitor of metalloproteinase 2 (TIMP-2) relativ
43 -beta1-induced production of the profibrotic tissue inhibitor of metalloproteinase-2 (TIMP-2) and pla
44 sequencing of one such factor identified the tissue inhibitor of metalloproteinase-2 (TIMP-2) as a me
45 nase-2/-9 exhibited little change, the large tissue inhibitor of metalloproteinase-2 (TIMP-2) increas
46 a cell membrane-associated MMP (MT1-MMP) and tissue inhibitor of metalloproteinase-2 (TIMP-2) were hi
47 monstrated with three peptides homologous to tissue inhibitor of metalloproteinase-2 (TIMP-2), ie, CN
51 tion, gelatin substrate zymography, and 125I-tissue inhibitor of metalloproteinases 2 (TIMP-2) bindin
52 requires collagenase activity, is blocked by tissue inhibitor of metalloproteinases-2 (TIMP-2) and co
53 eport here the characterization of the human tissue inhibitor of metalloproteinases-2 (TIMP-2) gene.
54 dent increase in secretion of both MMP-2 and tissue inhibitor of metalloproteinases-2 (TIMP-2) in res
58 eby glycosylation affects the recruitment of tissue inhibitor of metalloproteinases-2 (TIMP-2) to the
59 an archetype member of the MMP family, binds tissue inhibitor of metalloproteinases-2 (TIMP-2), activ
60 monstrated previously that overexpression of tissue inhibitor of metalloproteinases-2 (TIMP-2), an in
61 itor of metalloproteinases family, including tissue inhibitor of metalloproteinases-2 (TIMP-2), regul
67 rocedure for the active N-terminal domain of tissue inhibitor of metalloproteinases-2 [TIMP-2-(1-127)
68 nogen activator inhibitor type 1 [PAI-1] and tissue inhibitor of metalloproteinases-2 [TIMP-2]) was m
69 zymography), and cellular contents of MMP2, tissue inhibitor of metalloproteinase-2 (TIMP2), and pho
70 proteinases (MT1-MMP) in the presence of the tissue inhibitor of metalloproteinases 2 (TIMP2) in a bu
73 her the MMP inhibitor GM-6001-X or exogenous tissue inhibitor of metalloproteinase-2 to concanavalin
77 n, as the expression of MMP-2, MMP-3, or the tissue inhibitor of metalloproteinase-2 was not changed.
78 fibronectin, matrix metalloproteinase-2, and tissue inhibitor of metalloproteinase-2 was studied with
79 these, matrix metalloproteinase-2 (MMP2) and tissue inhibitor of metalloproteinase-2 were down-regula
80 d expression of pro-MMP-2 and its inhibitor, tissue inhibitor of metalloproteinase-2, whereas soluble
81 inhibition of proMMP-2 cleavage; recombinant tissue inhibitor of metalloproteinase-2, which binds to
82 e addition of varying amounts of recombinant tissue inhibitor of metalloproteinase-2 with pro-MMP-2 t
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