about
Purification and cloning of aggrecanase-1: a member of the ADAMTS family of proteinsCloning and characterization of ADAMTS11, an aggrecanase from the ADAMTS familyMembrane-type 6 matrix metalloproteinase (MT6-MMP, MMP-25) is the second glycosyl-phosphatidyl inositol (GPI)-anchored MMPMembrane-type 1 matrix metalloproteinase cytoplasmic tail-binding protein-1 is a new member of the Cupin superfamily. A possible multifunctional protein acting as an invasion suppressor down-regulated in tumorsThe Dimer Interface of the Membrane Type 1 Matrix Metalloproteinase Hemopexin Domain: CRYSTAL STRUCTURE AND BIOLOGICAL FUNCTIONSMembrane-type matrix metalloproteinases: Their functions and regulationsHomophilic complex formation of MT1-MMP facilitates proMMP-2 activation on the cell surface and promotes tumor cell invasion.The membrane-anchored MMP inhibitor RECK is a key regulator of extracellular matrix integrity and angiogenesisA compact, multidimensional spectrofluorometer exploiting supercontinuum generation.Discoidin domain receptor 2 mediates collagen-induced activation of membrane-type 1 matrix metalloproteinase in human fibroblasts.Human membrane type-4 matrix metalloproteinase (MT4-MMP) is encoded by a novel major transcript: isolation of complementary DNA clones for human and mouse mt4-mmp transcripts.Membrane type 4 matrix metalloproteinase (MT4-MMP, MMP-17) is a glycosylphosphatidylinositol-anchored proteinase.Metalloproteinase binding proteins: WO2009097397.Clusterin, an abundant serum factor, is a possible negative regulator of MT6-MMP/MMP-25 produced by neutrophils.Matrix metalloproteinases in cancer.ADAM10 controls collagen signaling and cell migration on collagen by shedding the ectodomain of discoidin domain receptor 1 (DDR1).Membrane-type 1 matrix metalloproteinase and cell migration.MT1-MMP: a potent modifier of pericellular microenvironment.Selective Inhibition of Membrane Type 1 Matrix Metalloproteinase Abrogates Progression of Experimental Inflammatory Arthritis: Synergy With Tumor Necrosis Factor BlockadeDevelopment of a specific affinity-matured exosite inhibitor to MT1-MMP that efficiently inhibits tumor cell invasion in vitro and metastasis in vivoMetalloproteinases: potential therapeutic targets for rheumatoid arthritis.Dimerization of MT1-MMP during cellular invasion detected by fluorescence resonance energy transfer.Detection of cartilage matrix degradation by autofluorescence lifetime.CD44 directs membrane-type 1 matrix metalloproteinase to lamellipodia by associating with its hemopexin-like domain.Analysis of MMP-dependent cell migration and invasion.Analyses of MT1-MMP activity in cells.Competitive disruption of the tumor-promoting function of membrane type 1 matrix metalloproteinase/matrix metalloproteinase-14 in vivo.CD44 binding through the hemopexin-like domain is critical for its shedding by membrane-type 1 matrix metalloproteinase.Altered proteolytic activities of ADAMTS-4 expressed by C-terminal processing.Involvement of tissue inhibitors of metalloproteinases (TIMPS) during matrix metalloproteinase activation.Relaxed specificity of matrix metalloproteinases (MMPS) and TIMP insensitivity of tumor necrosis factor-alpha (TNF-alpha) production suggest the major TNF-alpha converting enzyme is not an MMP.Degradation of interleukin 1beta by matrix metalloproteinases.Preferential inactivation of tissue inhibitor of metalloproteinases-1 that is bound to the precursor of matrix metalloproteinase 9 (progelatinase B) by human neutrophil elastase.Basal localization of MT1-MMP is essential for epithelial cell morphogenesis in 3D collagen matrix.Steps involved in activation of the complex of pro-matrix metalloproteinase 2 (progelatinase A) and tissue inhibitor of metalloproteinases (TIMP)-2 by 4-aminophenylmercuric acetateCharacterization of the interface between normal and transformed epithelial cells.Matrix metalloproteinase expression and function during fin regeneration in zebrafish: analysis of MT1-MMP, MMP2 and TIMP2.MT-LOOP-dependent localization of membrane type I matrix metalloproteinase (MT1-MMP) to the cell adhesion complexes promotes cancer cell invasion.Inhibition of Shedding of Low-Density Lipoprotein Receptor-Related Protein 1 Reverses Cartilage Matrix Degradation in Osteoarthritis.Cytoplasmic tail-dependent internalization of membrane-type 1 matrix metalloproteinase is important for its invasion-promoting activity.
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P50
description
researcher ORCID ID = 0000-0002-2128-2823
@en
wetenschapper
@nl
name
Yoshifumi Itoh
@ast
Yoshifumi Itoh
@en
Yoshifumi Itoh
@es
Yoshifumi Itoh
@nl
type
label
Yoshifumi Itoh
@ast
Yoshifumi Itoh
@en
Yoshifumi Itoh
@es
Yoshifumi Itoh
@nl
prefLabel
Yoshifumi Itoh
@ast
Yoshifumi Itoh
@en
Yoshifumi Itoh
@es
Yoshifumi Itoh
@nl
P106
P31
P496
0000-0002-2128-2823