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1 ng membrane type I matrix metalloproteinase (MT1-MMP).
2 by membrane type 1-matrix metalloproteinase (MT1-MMP).
3 anterograde translocation and exocytosis of MT1-MMP.
4 M. tuberculosis-infected monocytes expressed MT1-MMP.
5 ctivity by recycling matrix metalloprotease, MT1-MMP.
6 proteolytic activity after targeting toward MT1-MMP.
7 27 and retromer could directly interact with MT1-MMP.
8 c cytoskeletal scaffold protein palladin and MT1-MMP.
9 oiety and proteolytic activity ligand toward MT1-MMP.
10 ction or the general proteolytic activity of MT1-MMP.
11 up-regulation of vimentin, fibronectin, and MT1-MMP.
12 small molecules targeting the PEX domain of MT1-MMP.
13 traction, which appears to be independent of MT1-MMP.
14 A sites that requires the targeted action of MT1-MMP.
15 localizes to invadopodia and interacts with MT1-MMP.
16 g of extracellular vesicles (EVs) containing MT1-MMP.
17 OP, a loop region in the catalytic domain of MT1-MMP ((163)PYAYIREG(170)), as an essential region for
19 nsible of Notch1 cleavage, here we show that MT1-MMP, a membrane-tethered matrix metalloproteinase in
20 MT1-MMP were engineered to express wild-type MT1-MMP, a phosphomimetic mutant (T567E), or a phosphode
23 However, the mechanisms of collagen-mediated MT1-MMP activation and its physiological relevance are n
25 formed mesenchymal cells as collagen-induced MT1-MMP activation in HT1080 fibrosarcoma cells and MT1-
28 us membrane type 1 matrix metalloproteinase (MT1-MMP) activity does not fully inhibit cell invasion.
30 by membrane type-1 matrix metalloproteinase (MT1-MMP), ADAMs (a disintegrin domain and metalloprotein
33 of membrane type-1 matrix metalloproteinase (MT1-MMP) anchored on invasive cancer cells and its prote
34 furin expression increases the activities of MT1-MMP and ADAM10 but not that of ADAM17, as demonstrat
35 ort a co-up-regulation and colocalization of MT1-MMP and atypical protein kinase C iota (aPKCiota) in
36 3-shRNA expression depletes shed vesicles of MT1-MMP and decreases cell invasiveness when embedded in
37 a regulator of Stx4-mediated trafficking of MT1-MMP and EGFR, advancing our understanding of the rol
38 The associations between the expression of MT1-MMP and EMT-associated proteins with clinicopatholog
39 ncreased gene and protein levels of MMP2 and MT1-MMP and induced matrix contraction in FHL-124 cells.
40 ormation is based on the cytoplasmic tail of MT1-MMP and its ability to bind the subcortical actin cy
45 a designer TIMP-1 with superb affinities for MT1-MMP and TACE, to the glycosyl-phosphatidyl inositol
46 will contribute to the laboratory studies of MT1-MMP and then, ultimately, to the design of novel, mo
47 dipitously more effective against MMP-8 than MT1-MMP and was utilized successfully in a mouse model o
48 of membrane type 1 matrix metalloproteinase (MT1-MMP) and EGF receptor (EGFR) to the cell surface dur
49 se membrane-type 1 matrix metalloproteinase (MT1-MMP) and membrane-mimicking environments interplay i
50 ne-anchored matrix metalloproteinases MMP14 (MT1-MMP) and MMP15 (MT2-MMP), which drive epithelial cel
51 Membrane type 1-matrix metalloproteinase (MT1-MMP) and tumor necrosis factor alpha (TNF-alpha)-con
52 es membrane-type 1 matrix metalloproteinase (MT1-MMP)- and ERK1/2-dependent scattering of pancreatic
54 gos (membrane-type 1 matrix metalloprotease [MT1-MMP] and beta3 integrin) required for invadosome for
59 ed membrane type 1-matrix metalloproteinase (MT1-MMP) as the key protease for collagen breakdown.
60 e accumulation of the MMP16 substrate MMP14 (MT1-MMP) as well as L1CAM cell adhesion molecule, identi
61 ading to the decreased surface expression of MT1-MMP, as observed previously in transformed fibroblas
62 -MMP, we identify the membrane-anchored MMP, MT1-MMP, as the dominant collagenase that is operative w
64 ted by phospholipase D2 drives deposition of MT1-MMP at the site of invadopodia formation and is crit
65 TIMP-2 by alpha1(IV)NC1 led to saturation of MT1-MMP binding sites, which in turn led to inhibition o
67 not due to loss of the catalytic function of MT1-MMP but due to inefficient localization of the enzym
69 osteosarcoma display a strong expression of MT1-MMP, but the role of MT1-MMP in osteosarcoma progres
71 mbrane type-1 matrix metalloprotease (MMP14, MT1-MMP) by heterotrimeric G proteins, and in turn, the
72 Using this antibody, we have shown that the MT1-MMP-catalyzed activation of proMMP-2 is involved in
73 oxia regulates the function of DCs via KIF2A/MT1-MMP/CD44 axis, providing critical information to und
74 its L622D mutant with the single inactivated MT1-MMP cleavage site differentially regulate cell motil
75 , its Chuzhoi mutant with the two functional MT1-MMP cleavage sites, and its L622D mutant with the si
76 he membrane type-1 matrix metalloproteinase (MT1-MMP) cleavage of the PKP(621) downward arrowLI site
77 interaction in same cell-surface complexes, MT1-MMP cleaved EphA2 at its Fibronectin type-III domain
78 evidence that aPKCiota, in association with MT1-MMP-containing endosomes, phosphorylates cortactin,
79 syndrome protein and Scar homolog (WASH) on MT1-MMP-containing late endosomes in invasive breast car
80 catalytic function of the metalloproteinase MT1-MMP controls ECM structure, cell shape, and an integ
81 al. describe an unexpected function for the MT1-MMP cytoplasmic domain in imprinting spatial memory
83 Here, we provide mechanistic insight into MT1-MMP cytoplasmic tail binding protein 1 (MTCBP-1) wit
84 nslational regulation of the Thr(567) in the MT1-MMP cytoplasmic tail may function as a regulatory me
85 e basis of a yeast two-hybrid screen for the MT1-MMP cytoplasmic tail-binding proteins, we identify h
86 mors and lung metastases, but, surprisingly, MT1-MMP deficiency did not affect primary tumor growth,
87 at membrane type-1 matrix metalloproteinase (MT1-MMP) deficient mice have reduced complexity of the n
88 cally to the glomerular layer was reduced in MT1-MMP-deficient mice in contrast to controls while num
89 rge parts of the RMS were fully preserved in MT1-MMP-deficient mice, but we detected an increase in c
91 esin motors to drive endosome tubulation and MT1-MMP delivery to the surface of cancer cells, identif
94 ves membrane type 1 matrix metallopatrinase (MT1-MMP)-dependent proteolysis as well as Pak, Raf, and
95 age mechanism of MT1-MMP on Notch1, and that MT1-MMP-dependent activation of Notch1 sustains melanoma
96 ng integrins, inhibited the collagen-induced MT1-MMP-dependent activation of pro-MMP-2 and up-regulat
97 ogical inhibition of DDR2 also inhibited the MT1-MMP-dependent cellular degradation of collagen film,
98 etion of RAB7, FYCO1, or Protrudin inhibited MT1-MMP-dependent extracellular matrix degradation and c
99 ted monocytes degraded collagen matrix in an MT1-MMP-dependent manner, and MT1-MMP neutralization dec
100 In turn, LIMK1 and LIMK2 are required for MT1-MMP-dependent matrix degradation and cell invasion i
103 s have revealed a novel mechanism regulating MT1-MMP during cellular invasion and have identified the
104 In this study, we investigated the role of MT1-MMP during various stages of osteosarcoma developmen
105 These data identify a critical ARF6-JIP-MT1-MMP-dynein-dynactin-kinesin-1 axis promoting an inva
106 r JIP3/JIP4 in breast tumor cells results in MT1-MMP endosome mispositioning and reduces MT1-MMP exoc
108 yndrome protein and scar homologue (WASH) on MT1-MMP endosomes on which they recruit dynein-dynactin
110 expressed, fully functional, active cellular MT1-MMP enzyme are roughly equal to 1 x 10(5) molecules/
111 mounts of the cell surface-associated active MT1-MMP enzyme in multiple cancer cell types, including
117 e an inverse correlation between MTCBP-1 and MT1-MMP expression both in cultured cell lines and human
120 anoma cells affects Notch1 cleavage, whereas MT1-MMP expression in ADAM10/17 double knock-out fibrobl
124 in RGC axons and Muller glia, mimicking the MT1-MMP expression pattern seen in rabbits and neonatal
125 he acquisition of either wild-type or mutant MT1-MMP expression results in altered cohesion of epithe
131 We find that this interaction displaces MT1-MMP from invadopodia, thereby attenuating their numb
132 st-tumor cell lines impaired the delivery of MT1-MMP from late endocytic storage compartments to the
133 dynamin-2, which control the trafficking of MT1-MMP from late endosome to the plasma membrane and pl
134 activation in HT1080 fibrosarcoma cells and MT1-MMP function in MDA-MB231 breast cancer cells were n
136 MT-LOOP region of MT1-MMP (LOOPAb) inhibited MT1-MMP functions, fully mimicking the phenotype of the
143 Membrane type 1-matrix metalloproteinase (MT1-MMP) has an essential role in matrix degradation and
146 how the requirement of the metalloproteinase MT1-MMP in endothelial cells and fibroblasts, but not ca
149 trong expression of MT1-MMP, but the role of MT1-MMP in osteosarcoma progression is currently unknown
150 unctional importance of the interaction with MT1-MMP in pericellular matrix degradation and mesenchym
152 etect endogenous and overexpressed exogenous MT1-MMP in the Eca109 and Eca9706 cell lines, respective
154 and MaCSCs as well as surface expression of MT1-MMP in tumor cells harboring the P878A/P881A mutatio
161 a membrane type 1 matrix metalloproteinase (MT1-MMP) inducer, which increased granulocyte macrophage
163 e for the development of novel and selective MT1-MMP inhibitors that specifically target the PEX doma
167 vading cells, N-WASP promoted trafficking of MT1-MMP into invasive pseudopodia, primarily from late e
169 ssociation of KIF5B, surface localization of MT1-MMP, invadopodia, and invasion in cancer cells.
171 The membrane-anchored matrix metalloprotease MT1-MMP is a potent collagenolytic enzyme with a well-es
175 s reported in other cancers, tumor-expressed MT1-MMP is dispensable for all stages of osteosarcoma pr
176 ow that the membrane-bound metalloproteinase MT1-MMP is enriched not only at podosomes but also at di
182 evidence shows that the cytoplasmic tail of MT1-MMP is subjected to phosphorylation, and this post-t
183 es the processing of Notch1, indicating that MT1-MMP is sufficient to promote Notch1 activation indep
185 Membrane-type 1 matrix metalloproteinase (MT1-MMP) is a membrane-bound MMP that is highly expresse
187 Membrane type 1-matrix metalloproteinase (MT1-MMP) is associated with enhanced tumorigenicity in m
192 ng function by Y315F endophilin A2 mutant or MT1-MMP knockdown reduced markers for EMT and MaCSC acti
193 ll invasion by facilitating translocation of MT1-MMP-laden endosomes to the plasma membrane, enabling
194 magnitude of LV myocardial growth, altering MT1-MMP levels caused specific matrix-dependent changes
197 pecifically recognizes the MT-LOOP region of MT1-MMP (LOOPAb) inhibited MT1-MMP functions, fully mimi
199 certain MMP types, such as membrane type-1 (MT1) MMP, may also be involved in profibrotic cascades t
202 th concentric remodeling), a 60% increase in MT1-MMP-mediated LTBP-1 hydrolysis and a 190% increase i
203 PO, significant differences in LV function, MT1-MMP-mediated LTBP-1 hydrolysis, and collagen content
204 ene expression, and this process required an MT1-MMP-mediated sequential activation of the Src and JA
205 ed membrane type 1-matrix metalloproteinase (MT1-MMP) mediates proteolysis-based invasive tumor growt
206 -peptide substitution (p.Thr17Arg) decreases MT1-MMP membrane localization with consequent impairment
207 Membrane type 1 matrix metalloproteinase (MT1-MMP, MMP-14) is a transmembrane collagenase highly e
208 antagonist SB203580, downregulated MMP-9 and MT1-MMP/MMP-14 expressions by FN-stimulated macrophages,
210 n of the membrane-anchored metalloproteinase MT1-MMP (Mmp14) in mesenchymal progenitors, but not in c
211 Membrane type 1 matrix metalloproteinase (MT1-MMP/MMP14) is a zinc-dependent type I transmembrane
212 by membrane type 1-matrix metalloproteinase (MT1-MMP/MMP14), the main invadopodial matrix degradative
213 te membrane-type 1 matrix metalloproteinase (MT1-MMP; MMP14), which functions in actin-based pseudopo
218 reas overexpression of a nonphosphorylatable MT1-MMP mutant (Y573F) abrogated CSF-2 and CSF-3 transcr
219 mesenchymal tumor cell invasion, whereas in MT1-MMP-negative cells, palladin overexpression was insu
220 n matrix in an MT1-MMP-dependent manner, and MT1-MMP neutralization decreased collagen degradation by
221 an in vivo setting, mice heterozygous for an MT1-MMP-null allele display a distinct survival advantag
222 ing a potential direct cleavage mechanism of MT1-MMP on Notch1, and that MT1-MMP-dependent activation
223 e MT-LOOP effectively inhibited functions of MT1-MMP on the cell surface, including proMMP-2 activati
224 he membrane type 1 matrix metalloproteinase (MT1-MMP or MMP-14) is a collagenase that is key in leuko
225 Membrane type 1-matrix metalloproteinase (MT1-MMP or MMP-14) is a zinc-transmembrane metalloprotea
229 and transgenic mice with cardiac-restricted MT1-MMP overexpression or MT1-MMP reduced expression und
231 that the previously described Src-dependent MT1-MMP phosphorylation is a prerequisite for ubiquitina
232 The present study tested the hypothesis that MT1-MMP plays a direct role in the matrix remodeling res
233 tion of F-actin binding protein cortactin to MT1-MMP-positive endosomes and invadopodia formation and
234 , which is present in F-actin-rich puncta on MT1-MMP-positive endosomes and regulates cortactin assoc
236 hat LIMK1 regulates cortactin association to MT1-MMP-positive endosomes, while LIMK2 controls invadop
237 sm that involves tubular connections between MT1-MMP-positive late endosomes and the plasma membrane
241 centas, levels of MT1-MMP mRNA and of active MT1-MMP protein were reduced (-34.2%, P < 0.05, and -21.
243 nvadopodia formation and the polarization of MT1-MMP recycling compartments, required for invadopodia
244 imilar among WT, MT1-MMP overexpression, and MT1-MMP reduced expression after PO, significant differe
246 cardiac-restricted MT1-MMP overexpression or MT1-MMP reduced expression underwent PO for 4 weeks.
249 the putative membrane interaction region of MT1-MMP (Ser466Pro) resulted in lower enzyme activation
251 melanoma cells and identify Notch1 as a new MT1-MMP substrate that plays important biological roles
252 fection of primary human monocytes increased MT1-MMP surface expression 31.7-fold and gene expression
253 cyte networks caused a 17.5-fold increase in MT1-MMP surface expression dependent on p38 MAPK and G p
254 inkage through the LINC complex and triggers MT1-MMP surface-exposure to facilitate nucleus movement.
260 arative work with an equipotent radiolabeled MT1-MMP targeting antibody demonstrated starkly differen
261 cycle and identify a structural function of MT1-MMP that is independent of its proteolytic activity.
262 nd membrane type 1 matrix metalloproteinase (MT1-MMP), the latter of which we recently identified as
263 sed not only to visualize the trafficking of MT1-MMP through the cell compartment, but also to quanti
264 tant role for SNARE-regulated trafficking of MT1-MMP to invadopodia during cellular invasion of ECM.
266 irected recruitment of the metalloproteinase MT1-MMP to invadopodia plays a critical role in this inv
269 of the transmembrane matrix metalloprotease, MT1-MMP to promote invasive behaviour leading to basemen
270 te membrane type-1 matrix metalloproteinase (MT1-MMP) to podosomes or invadosomes to break extracellu
272 of membrane type I matrix metalloproteinase (MT1-MMP) to the leading edge is thought to be a crucial
273 eases, such as the transmembrane collagenase MT1-MMP, together with actin-based protrusions, to break
274 synthesizes a pool of PI(4)P that maintains MT1-MMP traffic in the degradative pathway and suppresse
276 st-translational modification is involved in MT1-MMP trafficking as well as in modulating cellular in
278 extension of invasive pseudopods into which MT1-MMP traffics and for providing the correct cytoskele
280 NMR derived structural models indicate that MT1-MMP transiently associates with bicelles and cells t
282 a membrane in pseudopodia, N-WASP stabilized MT1-MMP via direct tethering of its cytoplasmic tail to
283 ted delivery of the matrix metalloproteinase MT1-MMP via endosomal transport by mechanisms that are n
285 pression of membrane type 1 metalloprotease (MT1-MMP) via down-regulating the kinesin-like protein KI
290 c peptide with subnanomolar affinity towards MT1-MMP was identified, and its radioconjugate showed se
291 tial expression pattern of MMP-2, -3, -9 and MT1-MMP was studied in the healthy mouse retina via immu
292 s, including MMP-13, MMP-8, MMP-2, MMP-9, or MT1-MMP, we identify the membrane-anchored MMP, MT1-MMP,
293 cells that express low endogenous levels of MT1-MMP were engineered to express wild-type MT1-MMP, a
294 ed membrane type-1 matrix metalloproteinase (MT1-MMP) were selectively up-regulated and coexpressed i
295 t cancer HCC1806 cells is partly mediated by MT1-MMP, which also regulates collagen-induced receptor
296 A tempting target is the membrane-associated MT1-MMP, which has well-documented importance in matrix
297 ed expression of mesenchymal genes including MT1-MMP, which was required for collagen-stimulated inva
299 was accompanied by reduced colocalization of MT1-MMP with membranes containing the endosomal markers