‘Gelatinase-like’ activity from articular chondrocytes in monolayer culture-Reference-Cited by-同舟云学术

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‘Gelatinase-like’ activity from articular chondrocytes in monolayer culture

Published:1983-04 Issue:2 Volume:762 Page:227-231
ISSN:0167-4889
Container-title:Biochimica et Biophysica Acta (BBA) - Molecular Cell Research
language:en
Short-container-title:Biochimica et Biophysica Acta (BBA) - Molecular Cell Research

Author:

Sapolsky Asher I.,Sheff Michael F.,Matsuta Kunio,Howell David S.,Moskowitz Roland W.,Goldberg Victor M.,Norby David P.,Malemud Charles J.

Publisher

Elsevier BV

Subject

Cell Biology,Molecular Biology

Reference17 articles.

1. Neutral proteinases from articular chondrocytes in culture. 2. Metal-dependent latent neutral proteoglycanase, and inhibitory activity

2. Neutral proteinases from articular chondrocytes in culture. I. A latent collagenase that degrades human cartilage type II collagen

3. Sulfate incorporation by articular chondrocytes in monolayer culture

4. Identification of three genetically distinct collagens by cyanogen bromide cleavage of insoluble human skin and cartilage collagen

Cited by 10 articles. 订阅此论文施引文献订阅此论文施引文献，注册后可以免费订阅5篇论文的施引文献，订阅后可以查看论文全部施引文献

1. Expression of 92-kD type IV collagenase/gelatinase (gelatinase B) in osteoarthritic cartilage and its induction in normal human articular cartilage by interleukin 1.;Journal of Clinical Investigation;1993-07-01

2. In vivo effects of naproxen on composition, proteoglycan metabolism, and matrix metalloproteinase activities in canine articular cartilage;Journal of Orthopaedic Research;1993-03

3. Proteolytic enzymes as mediators of glomerular injury;Kidney International;1991-08

4. Production of gelatin-degrading matrix metalloproteinases (‘type IV collagenases’) and inhibitors by articular chondrocytes during their dedifferentiation by serial subcultures and under stimulation by interleukin-1 and tumor necrosis factor α;Biochimica et Biophysica Acta (BBA) - Molecular Cell Research;1991-08

5. Purification and Characterisation of Human 72-kDa Gelatinase (Type IV Collagenase). Use of Immunolocalisation to Demonstrate the Non-coordinate Regulation of the 72-kDa and 95-kDa Gelatinases by Human Fibroblasts;Biological Chemistry Hoppe-Seyler;1991-01

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