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1 target for the membrane-tethered collagenase membrane type 1-matrix metalloproteinase.
2 atinase A activation by binding to activated membrane type 1-matrix metalloproteinase 1 (MT1-MMP) on
3 ation) or pericellular collagen degradation (membrane type 1-matrix metalloproteinase ablation) were
4 EGF was involved in Cat.G signaling and that membrane type 1 matrix metalloproteinase activation may
5 ulation of the membrane-tethered collagenase membrane type 1 matrix metalloproteinase, and an inverse
6 utation caused an insertion of an additional membrane type 1 matrix metalloproteinase cleavage site i
7 roviral expression of a 5' 1.4 kb anti-sense membrane type 1 matrix metalloproteinase construct and a
8 uclear fragmentation after 1.4 kb anti-sense membrane type 1 matrix metalloproteinase construct expre
9 ase construct and a 3.4 kb full-length sense membrane type 1 matrix metalloproteinase construct in pr
10 h after transduction with 1.4 kb anti-sense membrane type 1 matrix metalloproteinase construct that
11 provide a novel molecular mechanism by which membrane type 1-matrix metalloproteinase controls tumor-
12 We show that knockdown of Galpha13 decreased membrane type 1 matrix metalloproteinase-driven proteoly
13 hed a novel method to track cell invasion by membrane type 1 matrix metalloproteinase-expressing canc
18 through direct coupling of endoglin and the membrane-type 1 matrix metalloproteinase (MMP)-14 at the
20 with that for HMB-45, but not with that for membrane type-1 matrix metalloproteinase (MT-1-MMP), whi
22 membrane called invadopodia, where the trans-membrane type 1 matrix metalloproteinase (MT1-MMP) accum
23 (MMP) inhibitor (GM6001) to block endogenous membrane type 1 matrix metalloproteinase (MT1-MMP) activ
24 al peptide exhibited impaired trafficking of membrane type 1 matrix metalloproteinase (MT1-MMP) and E
25 tant regulator of VM, specifically affecting membrane type 1 matrix metalloproteinase (MT1-MMP) and m
26 hereas protease inhibitor studies identified membrane type 1 matrix metalloproteinase (MT1-MMP) as th
28 cterized by high beta1-integrin activity and membrane type 1 matrix metalloproteinase (MT1-MMP) expre
29 he effects on cell viability, NF-kappaB, and membrane type 1 matrix metalloproteinase (MT1-MMP) expre
30 s at GenBank, we identified up-regulation of membrane type 1 matrix metalloproteinase (MT1-MMP) in hu
31 eptor (TLR)-2 and TLR-6 agonist as well as a membrane type 1 matrix metalloproteinase (MT1-MMP) induc
34 he functional activity of invasion-promoting membrane type 1 matrix metalloproteinase (MT1-MMP) is el
36 idence suggests that the cytoplasmic tail of membrane type 1 matrix metalloproteinase (MT1-MMP) is su
40 rane by proteases such as ADAM10 and -17 and membrane type 1 matrix metalloproteinase (MT1-MMP), the
46 I by matrix metalloproteinases 2 (MMP2) and membrane type 1 matrix metalloproteinases (MT1-MMP) in t
49 ed with up-regulated cellular levels of both membrane type 1-matrix metalloproteinase (MT1-MMP) and T
50 racellular matrix requires membrane-tethered membrane type 1-matrix metalloproteinase (MT1-MMP) as th
51 extracellular matrix degradation by inducing membrane type 1-matrix metalloproteinase (MT1-MMP) expre
52 imens showed increased fibrosis and enhanced membrane type 1-matrix metalloproteinase (MT1-MMP) expre
59 unction adhesion molecule (Jam)-B and Jam-C, membrane type 1-matrix metalloproteinase (MT1-MMP), and
62 of Snail in PDAC cells resulted in a robust membrane type 1-matrix metalloproteinase (MT1-MMP, MMP-1
63 et-7 in part through increased expression of membrane type 1-matrix metalloproteinase (MT1-MMP, MMP-1
65 peptide therapy depressed the expression of membrane type 1-matrix metalloproteinase (MT1-MMP/MMP-14
66 ion of breast carcinoma cells is mediated by membrane type 1-matrix metalloproteinase (MT1-MMP/MMP14)
67 at enabling recognition of the expression of membrane type-1 matrix metalloproteinase (MT1-MMP) ancho
69 an control the functional activity of T cell membrane type-1 matrix metalloproteinase (MT1-MMP) and t
70 n by an ADAM proteinase was coupled with the membrane type-1 matrix metalloproteinase (MT1-MMP) cleav
82 avage of the N-terminal propeptide domain of membrane type-1 matrix metalloproteinase (MT1-MMP) is re
86 ngiogenic role of corneal fibroblast-derived membrane type-1 matrix metalloproteinase (MT1-MMP) on ba
90 strate here that EphA2 and membrane-anchored membrane type-1 matrix metalloproteinase (MT1-MMP) were
91 that active Abl kinases form complexes with membrane type-1 matrix metalloproteinase (MT1-MMP), a cr
93 tory mechanisms that control the activity of membrane type-1 matrix metalloproteinase (MT1-MMP), a ke
94 een well established that invasion-promoting membrane type-1 matrix metalloproteinase (MT1-MMP), a mu
96 ionality of PTK7 is selectively regulated by membrane type-1 matrix metalloproteinase (MT1-MMP), ADAM
98 nduce an invasive phenotype characterized by membrane type-1 matrix metalloproteinase (MT1-MMP)-depen
99 in gene expression, which include defects in membrane type-1 matrix metalloproteinase (MT1-MMP)-depen
100 ized the substrate recognition properties of membrane type-1 matrix metalloproteinase (MT1-MMP; also
101 he rat cornea and localize the expression of membrane type-1 matrix metalloproteinase (MT1-MMP; MMP-1
103 nts, and the de novo expression of activated membrane type-1-matrix metalloproteinase (MT1-MMP).
104 icipates in this process is considered to be membrane-type 1 matrix metalloproteinase (MT1-MMP or MMP
105 as examined how the pericellular collagenase membrane-type 1 matrix metalloproteinase (MT1-MMP) and m
108 e collagenolysis are important activities of membrane-type 1 matrix metalloproteinase (MT1-MMP) to pr
110 recently showed that Snail (Snai1) promotes membrane-type 1 matrix metalloproteinase (MT1-MMP)- and
112 until activated specifically in the tumor by membrane-type 1 matrix metalloproteinase (MT1-MMP).
113 sion of the type I transmembrane proteinase, membrane-type 1 matrix metalloproteinase (MT1-MMP).
114 cytoskeletal reorganization and up-regulate membrane-type 1 matrix metalloproteinase (MT1-MMP; MMP14
116 blocking processing of the metastasis factor membrane-type 1 matrix metalloproteinase/MT1-MMP) at con
118 Similarly, MMP-7 (matrilysin) and MT1-MMP (membrane type 1 matrix metalloproteinase) solubilized XL
120 f crucial cancer-related substrates, such as membrane type 1 matrix metalloproteinase, transforming g
121 inverse relationship between dickkopf-1 and membrane type 1 matrix metalloproteinase was observed in
122 pro-matrix metalloproteinase 2 activation by membrane type 1 matrix metalloproteinase, we aimed at in
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