Localizing matrix metalloproteinase activities in the pericellular environment.

Localizing matrix metalloproteinase activities in the pericellular environment.

Matrix metalloproteinases (MMPs) are a group of structurally related proteolytic enzymes containing a zinc ion in the active site. They are secreted from cells or bound to the plasma membrane and hydrolyze extracellular matrix (ECM) and cell surface-bound molecules. They therefore play key roles in...

Deskribapen osoa

Xehetasun bibliografikoak
Egile Nagusiak:	Murphy, G, Nagase, H
Formatua:	Journal article
Hizkuntza:	English
Argitaratua:	2011

Antzeko izenburuak

Progress in matrix metalloproteinase research.
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Matrix metalloproteinases and tissue inhibitors of metalloproteinases: structure, function, and biochemistry.
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A personal journey with matrix metalloproteinases
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Targeting mechanotransduction pathways in osteoarthritis: a focus on the pericellular matrix.
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Targeting mechanotransduction pathways in osteoarthritis: a focus on the pericellular matrix.
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Targeting mechanotransduction pathways in osteoarthritis: a focus on the pericellular matrix
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Complex Regulation of the Pericellular Proteolytic Microenvironment during Tumor Progression and Wound Repair: Functional Interactions between the Serine Protease and Matrix Metalloproteinase Cascades
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Measurement of matrix metalloproteinase activities in the medium of cultured synoviocytes using zymography.
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Development of a solid-phase assay for analysis of matrix metalloproteinase activity.
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In vivo imaging of matrix metalloproteinase 12 and matrix metalloproteinase 13 activities in the mouse model of collagen-induced arthritis.
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WARP interacts with collagen VI-containing microfibrils in the pericellular matrix of human chondrocytes.
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Pericellular matrix of articular cartilage. A novel mechanotransduction mechanism in articular chondrocytes?
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The expression and localization of membrane type-1 matrix metalloproteinase in human abdominal aortic aneurysms.
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Selectivity in glycosaminoglycan binding dictates the distribution and diffusion of fibroblast growth factors in the pericellular matrix
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Selective hydrolysis of triple-helical peptides by matrix metalloproteinases
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Matrix metalloproteinase triple-helical peptidase activities are differentially regulated by substrate stability.
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Kinetic analysis of matrix metalloproteinase triple-helicase activity using fluorogenic substrates
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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.
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Steps involved in activation of the pro-matrix metalloproteinase 9 (progelatinase B)-tissue inhibitor of metalloproteinases-1 complex by 4-aminophenylmercuric acetate and proteinases.
nork: Ogata, Y, et al.
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Kinetic analysis of matrix metalloproteinase activity using fluorogenic triple-helical substrates.
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Preferential inactivation of tissue inhibitor of metalloproteinases-1 that is bound to the precursor of matrix metalloproteinase 9 (progelatinase B) by human neutrophil elastase.
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Recognition and catabolism of synthetic heterotrimeric collagen peptides by matrix metalloproteinases.
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Inhibition of apoptosis of activated hepatic stellate cells by tissue inhibitor of metalloproteinase-1 is mediated via effects on matrix metalloproteinase inhibition: implications for reversibility of liver fibrosis.
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Reappraising metalloproteinases in rheumatoid arthritis and osteoarthritis: destruction or repair?
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Importance of matrix metalloproteinases in human trophoblast invasion.
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Coordination of two kinesin superfamily motor proteins, KIF3A and KIF13A, is essential for pericellular matrix degradation by membrane-type 1 matrix metalloproteinase (MT1-MMP) in cancer cells
nork: Gifford, V, et al.
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Loss of spatial organization and destruction of the pericellular matrix in early osteoarthritis in vivo and in a novel in vitro methodology
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