About: Degradation of type IX collagen by matrix metalloproteinase 3 (stromelysin) from human rheumatoid synovial cells

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About: Degradation of type IX collagen by matrix metalloproteinase 3 (stromelysin) from human rheumatoid synovial cells Goto Sponge NotDistinct Permalink

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scientific article published on 01 February 1989

Attributes	Values
rdf:type	Item
description	wetenschappelijk artikel (nl) наукова стаття, опублікована в лютому 1989 (uk) im Februar 1989 veröffentlichter wissenschaftlicher Artikel (de) artículu científicu espublizáu en febreru de 1989 (ast) artikull shkencor i botuar më 01 shkurt 1989 (sq) scientific article published on 01 February 1989 (en)
publication date	wds:Q69953408-7F02372C-D40F-4A7E-B97D-F4ADBDE5DE49
publication date	1989-02-01 00:00:00Z (xsd:dateTime)
language of work or name	wds:Q69953408-A12EE2DE-1CFD-4636-B5E4-5DBF84919912
language of work or name	English
cites work	wds:Q69953408-099A5803-A5DE-43FA-A5FD-B57872B649A1 wds:Q69953408-155B4028-EAE8-47B2-9010-356875C35A2B wds:Q69953408-31E8DB14-5868-46F3-BCFE-6754272DB6C9 wds:Q69953408-40351E87-731E-4C0C-8115-C9112EAA3522 wds:Q69953408-5C5C1B3C-80C6-4706-A6D3-03F7AEA5A1CF wds:Q69953408-7AD79A54-DE10-4F05-BAAF-3F3BBE804011 wds:Q69953408-7BAE0CA6-09E0-4ACC-ACD4-D04AADB8F044 wds:Q69953408-835AF4DD-10F3-4C1A-85F9-60658441690F wds:Q69953408-D2AAF05A-99B8-439F-BDF5-1BD6FCDC3ACC wds:Q69953408-DBA0F0A5-6D6A-4BCC-82AA-C247AD27CBE8 wds:Q69953408-F3DD2E90-7EF5-41D3-9A06-6775506F52EC
cites work	D-periodic distribution of collagen type IX along cartilage fibrils Synthesis and characterization of cDNA encoding a cartilage-specific short collagen Stromelysin is an activator of procollagenase. A study with natural and recombinant enzymes Construction and characterization of cDNA encoding the alpha 2 chain of chicken type IX collagen Collagen type IX: evidence for covalent linkages to type II collagen in cartilage Neutral proteases capable of proteoglycan digesting activity in osteoarthritic and normal human articular cartilage An endopeptidase from rheumatoid synovial tissue culture. Cartilage type IX collagen is cross-linked by hydroxypyridinium residues A rapid and reproducible assay for collagenase using [1-14C]acetylated collagen On the role of type IX collagen in the extracellular matrix of cartilage: type IX collagen is localized to intersections of collagen fibrils Susceptibility of cartilage collagens type II, IX, X, and XI to human synovial collagenase and neutrophil elastase.
author name string	wds:Q69953408-7A8BA9A8-B080-40C5-A7F6-F2E0AB9006CC wds:Q69953408-99308797-A895-4297-AB8C-0BC5B4C21A24 wds:Q69953408-9DD2EDAA-30EF-43C7-A3E6-BD6EA14D579E wds:Q69953408-C282F888-7506-4CB4-B230-1211A5597BE9
author name string	Kimata K Nagase H Konomi H Yada T
rdfs:label	Degradation of type IX collagen by matrix metalloproteinase 3 (nl) Degradation of type IX collagen by matrix metalloproteinase 3 (stromelysin) from human rheumatoid synovial cells (en) Degradation of type IX collagen by matrix metalloproteinase 3 (stromelysin) from human rheumatoid synovial cells (sq)
skos:prefLabel	Degradation of type IX collagen by matrix metalloproteinase 3 (nl) Degradation of type IX collagen by matrix metalloproteinase 3 (stromelysin) from human rheumatoid synovial cells (en) Degradation of type IX collagen by matrix metalloproteinase 3 (stromelysin) from human rheumatoid synovial cells (sq)
name	Degradation of type IX collagen by matrix metalloproteinase 3 (nl) Degradation of type IX collagen by matrix metalloproteinase 3 (stromelysin) from human rheumatoid synovial cells (en) Degradation of type IX collagen by matrix metalloproteinase 3 (stromelysin) from human rheumatoid synovial cells (sq)
author	wds:Q69953408-080D586F-7F7E-46BF-8A80-EC36F1135CAE
author	Yasunori Okada
title	wds:Q69953408-78218A93-BCAA-4606-BDA6-029063603373
title	Degradation of type IX collagen by matrix metalloproteinase 3 (stromelysin) from human rheumatoid synovial cells (en)
page(s)	wds:Q69953408-F811EF5F-38D7-4373-B0D9-4BB80B952B8A
page(s)	473-476
instance of	wds:Q69953408-CDD9ABB2-E289-4937-94D2-DA15E9D8B93F
instance of	scholarly article
PubMed ID	wds:Q69953408-27C34CD7-4FFD-44FC-BC83-96C7D795E524
PubMed ID	http://rdf.ncbi.nlm.nih.gov/pubchem/reference/2920840
PubMed ID	2920840
published in	wds:Q69953408-8599CC5A-AB9B-4A9C-B07F-2686D0ABEB89
published in	FEBS Letters
issue	wds:Q69953408-230D3496-764C-4222-972C-80729ADFB143
volume	wds:Q69953408-47F26855-304B-497D-A5B1-0B11786872EE
issue	2
volume	244
DOI	wds:Q69953408-B82C1B6B-6272-467D-8565-4B461ABF09EB
DOI	http://dx.doi.org/10.1016/0014-5793(89)80586-1
DOI	10.1016/0014-5793(89)80586-1
is about of	https://www.wikidata.org/wiki/Special:EntityData/Q69953408
is cites work of	Synthetic inhibitors of bacterial and mammalian interstitial collagenases Stromelysin-1: three-dimensional structure of the inhibited catalytic domain and of the C-truncated proenzyme The NC2 domain of collagen IX provides chain selection and heterotrimerization The pathobiology of osteoarthritis and the rationale for the use of pentosan polysulfate for its treatment Synovial procollagenase activation by human mast cell tryptase dependence upon matrix metalloproteinase 3 activation The role of the C-terminal domain of human collagenase-3 (MMP-13) in the activation of procollagenase-3, substrate specificity, and tissue inhibitor of metalloproteinase interaction Preferential mRNA expression of prostromelysin relative to procollagenase and in situ localization in human articular cartilage Discoordinate expression of stromelysin, collagenase, and tissue inhibitor of metalloproteinases-1 in rheumatoid human synovial fibroblasts. Synergistic effects of interleukin-1 and tumor necrosis factor-alpha on stromelysin expression Proteinase-mediated cartilage degradation in osteoarthritis Activation of precursors for matrix metalloproteinases 1 (interstitial collagenase) and 3 (stromelysin) by rat mast-cell proteinases I and II Effects of three avocado/soybean unsaponifiable mixtures on metalloproteinases, cytokines and prostaglandin E2 production by human articular chondrocytes The collagens of articular cartilage Detection of stromelysin in synovial fluid and serum from patients with rheumatoid arthritis and osteoarthritis Biochemistry of articular cartilage in health and disease Increased gene expression of matrix metalloproteinase-3 (stromelysin) in skin fibroblasts from patients with severe recessive dystrophic epidermolysis bullosa Susceptibility of the cartilage collagens types II, IX and XI to degradation by the cysteine proteinases, cathepsins B and L Tissue inhibitor of metalloproteinases from human bone marrow stromal cell line KM 102 has erythroid-potentiating activity, suggesting its possibly bifunctional role in the hematopoietic microenvironment Computational sequence analysis of matrix metalloproteinases. Histamine-stimulated production of matrix metalloproteinase 1 by human rheumatoid synovial fibroblasts is mediated by histamine H1-receptors Involvement of MMP-1 and MMP-3 in collagen degradation induced by IL-1 in rabbit cartilage explant culture. Coordinate synthesis of stromelysin, interleukin-1, and oncogene proteins in experimental osteoarthritis. An immunohistochemical study. Cyclooxygenase inhibitors augment the production of pro-matrix metalloproteinase 9 (progelatinase B) in rabbit articular chondrocytes Rheological Properties and Age-Related Changes of the Human Vitreous Humor Hox10-regulated endodermal cell migration is essential for development of the ascidian intestine. Analysis of mass spectrometry data from the secretome of an explant model of articular cartilage exposed to pro-inflammatory and anti-inflammatory stimuli using machine learning. Degradation of cartilage collagens type II, IX, X and XI by enzymes derived from human articular chondrocytes. Expression of stromelysin and urokinase type plasminogen activator protein in resection specimens and biopsies at different stages of osteoarthritis of the knee Matrix metalloproteinase (stromelysin-1) increases the albumin permeability of isolated rat glomeruli Dissociation of collagenase-tissue inhibitor of metalloproteinases-1 (TIMP-1) complex - its application for the independent measurements of TIMP-1 and collagenase activity in crude culture media and body fluids

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