About: Yoshifumi Itoh

Facets (new session)
Description
Metadata
Settings
- owl:sameAs
- Inference Rule:

About: Yoshifumi Itoh Goto Sponge NotDistinct Permalink

An Entity of Type : wikibase:Item, within Data Space : wikidata.demo.openlinksw.com associated with source document(s)

rheumatology researcher ORCID ID = 0000-0002-2128-2823

Attributes	Values
rdf:type	Item
description	연구원 (ko) wetenschapper (nl) дослідник (uk) эрдэмтэн (mn) 研究者 (zh) rheumatology researcher ORCID ID = 0000-0002-2128-2823 (en)
rdfs:label	Yoshifumi Itoh (en) Yoshifumi Itoh (es) Yoshifumi Itoh (nl) Yoshifumi Itoh (ast)
skos:prefLabel	Yoshifumi Itoh (en) Yoshifumi Itoh (es) Yoshifumi Itoh (nl) Yoshifumi Itoh (ast)
name	Yoshifumi Itoh (en) Yoshifumi Itoh (es) Yoshifumi Itoh (nl) Yoshifumi Itoh (ast)
instance of	wds:Q58809398-14A48D21-BFE2-4EB1-96A1-1D042BF91022
instance of	Homo sapiens
occupation	wds:Q58809398-1057F34C-D708-405E-A67D-FBB22C4C09C0
employer	wds:Q58809398-0cd552a2-4dbc-c118-32d4-8e549756c00d wds:Q58809398-24F78702-79A7-4374-83E1-A858DC062CE8 wds:Q58809398-F2C2AE14-4F7C-48A8-A294-0624A53B23A5 wds:Q58809398-ee6d26c6-42a0-d594-f57c-891117c63b03
official website	wds:Q58809398-C4D39A1D-1B02-4F3E-AB8B-03F1EF644875
occupation	researcher
employer	University of Kansas Medical Center University of Oxford University of Tokyo The Kennedy Institute of Rheumatology
official website	https://www.kennedy.ox.ac.uk/team/yoshi-itoh
ORCID iD	wds:Q58809398-1969819D-9C4B-4F50-988B-08B9B8FE4045
ORCID iD	https://orcid.org/0000-0002-2128-2823
ORCID iD	0000-0002-2128-2823
is about of	https://www.wikidata.org/wiki/Special:EntityData/Q58809398
is author of	Membrane-type 6 matrix metalloproteinase (MT6-MMP, MMP-25) is the second glycosyl-phosphatidyl inositol (GPI)-anchored MMP Dimerization of MT1-MMP during cellular invasion detected by fluorescence resonance energy transfer MT1-MMP: an enzyme with multidimensional regulation Steps involved in activation of the complex of pro-matrix metalloproteinase 2 (progelatinase A) and tissue inhibitor of metalloproteinases (TIMP)-2 by 4-aminophenylmercuric acetate Membrane-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 tumors Intact vitronectin induces matrix metalloproteinase-2 and tissue inhibitor of metalloproteinases-2 expression and enhanced cellular invasion by melanoma cells Cloning and characterization of ADAMTS11, an aggrecanase from the ADAMTS family The membrane-anchored MMP inhibitor RECK is a key regulator of extracellular matrix integrity and angiogenesis Altered proteolytic activities of ADAMTS-4 expressed by C-terminal processing Importance of matrix metalloproteinases in human trophoblast invasion 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. Front-cell-specific expression of membrane-type 1 matrix metalloproteinase and gelatinase A during cohort migration of colon carcinoma cells induced by hepatocyte growth factor/scatter factor Membrane type 4 matrix metalloproteinase (MT4-MMP, MMP-17) is a glycosylphosphatidylinositol-anchored proteinase. Plasma membrane-bound tissue inhibitor of metalloproteinases (TIMP)-2 specifically inhibits matrix metalloproteinase 2 (gelatinase A) activated on the cell surface Homophilic complex formation of MT1-MMP facilitates proMMP-2 activation on the cell surface and promotes tumor cell invasion. MT1-MMP: a potent modifier of pericellular microenvironment. Characterization of the interface between normal and transformed epithelial cells Purification and cloning of aggrecanase-1: a member of the ADAMTS family of proteins Degradation of interleukin 1beta by matrix metalloproteinases. Ageladine A: an antiangiogenic matrixmetalloproteinase inhibitor from the marine sponge Agelas nakamurai Steps involved in activation of the pro-matrix metalloproteinase 9 (progelatinase B)-tissue inhibitor of metalloproteinases-1 complex by 4-aminophenylmercuric acetate and proteinases Membrane-type matrix metalloproteinases: Their functions and regulations The Dimer Interface of the Membrane Type 1 Matrix Metalloproteinase Hemopexin Domain: CRYSTAL STRUCTURE AND BIOLOGICAL FUNCTIONS Matrix metalloproteinase-2 production and its binding to the matrix are increased in abdominal aortic aneurysms 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. CD44 directs membrane-type 1 matrix metalloproteinase to lamellipodia by associating with its hemopexin-like domain. Matrix metalloproteinases in cancer. Palmitoylation at Cys574 is essential for MT1-MMP to promote cell migration. Invasive potential of human rheumatoid tenosynovial cells is in part MT1-MMP dependent. Effects of interleukin-6 on the metabolism of connective tissue components in rheumatoid synovial fibroblasts Cytoplasmic tail-dependent internalization of membrane-type 1 matrix metalloproteinase is important for its invasion-promoting activity. CD44 binding through the hemopexin-like domain is critical for its shedding by membrane-type 1 matrix metalloproteinase. Preferential inactivation of tissue inhibitor of metalloproteinases-1 that is bound to the precursor of matrix metalloproteinase 9 (progelatinase B) by human neutrophil elastase. Degradation of cross-linked fibrin by matrix metalloproteinase 3 (stromelysin 1): hydrolysis of the gamma Gly 404-Ala 405 peptide bond Callysponginol sulfate A, an MT1-MMP inhibitor isolated from the marine sponge Callyspongia truncata Membrane-type 1 matrix metalloproteinase and cell migration. Matrix metalloproteinases and TIMPS in cultured C57BL/6J-cpk kidney tubules Competitive disruption of the tumor-promoting function of membrane type 1 matrix metalloproteinase/matrix metalloproteinase-14 in vivo. Matrix metalloproteinase expression and function during fin regeneration in zebrafish: analysis of MT1-MMP, MMP2 and TIMP2. A compact, multidimensional spectrofluorometer exploiting supercontinuum generation. Development of a specific affinity-matured exosite inhibitor to MT1-MMP that efficiently inhibits tumor cell invasion in vitro and metastasis in vivo MT-LOOP-dependent localization of membrane type I matrix metalloproteinase (MT1-MMP) to the cell adhesion complexes promotes cancer cell invasion Selective Inhibition of Membrane Type 1 Matrix Metalloproteinase Abrogates Progression of Experimental Inflammatory Arthritis: Synergy With Tumor Necrosis Factor Blockade Involvement of tissue inhibitors of metalloproteinases (TIMPS) during matrix metalloproteinase activation. Matrix metalloproteinases and their inhibitors in human vitreous. Discoidin domain receptors: Microenvironment sensors that promote cellular migration and invasion Fluorescence quenching studies of matrix metalloproteinases (MMPs): evidence for structural rearrangement of the proMMP-2/TIMP-2 complex upon mercurial activation Metalloproteinases: potential therapeutic targets for rheumatoid arthritis. Basal localization of MT1-MMP is essential for epithelial cell morphogenesis in 3D collagen matrix Inhibition of Shedding of Low-Density Lipoprotein Receptor-Related Protein 1 Reverses Cartilage Matrix Degradation in Osteoarthritis. Hypergravity and microgravity exhibited reversal effects on the bone and muscle mass in mice ADAM10 controls collagen signaling and cell migration on collagen by shedding the ectodomain of discoidin domain receptor 1 (DDR1). Matrix metalloproteinase-2 in a murine model of infantile-type polycystic kidney disease Detection of cartilage matrix degradation by autofluorescence lifetime. Clusterin, an abundant serum factor, is a possible negative regulator of MT6-MMP/MMP-25 produced by neutrophils. Analysis of MMP-dependent cell migration and invasion. Analyses of MT1-MMP activity in cells. Metalloproteinases in Rheumatoid Arthritis: Potential Therapeutic Targets to Improve Current Therapies. Identification of rabbit uterine cervical procollagenase activator as rabbit matrix metalloproteinase 3 (stromelysin) Discoidin domain receptor 2 mediates collagen-induced activation of membrane-type 1 matrix metalloproteinase in human fibroblasts. Epithelial polarization in 3D matrix requires DDR1 signaling to regulate actomyosin contractility MT1-MMP-dependent cell migration: proteolytic and non-proteolytic mechanisms Progesterone increases the production of tissue inhibitor of metalloproteinases-2 in rabbit uterine cervical fibroblasts

Faceted Search & Find service v1.16.117 as of May 05 2024

Alternative Linked Data Documents: ODE Content Formats:

RDF

ODATA

Microdata

About

OpenLink Virtuoso version 07.20.3239 as of May 5 2024, on Linux (x86_64-centos_6-linux-gnu), Single-Server Edition (378 GB total memory, 188 GB memory in use)
Data on this page belongs to its respective rights holders.
Virtuoso Faceted Browser Copyright © 2009-2024 OpenLink Software