J O Stracke

Summary

Affiliation: University of East Anglia
Country: UK

Publications

  1. ncbi request reprint Biochemical characterization of the catalytic domain of human matrix metalloproteinase 19. Evidence for a role as a potent basement membrane degrading enzyme
    J O Stracke
    School of Biological Sciences, University of East Anglia, Norwich, NR4 7TJ, United Kingdom
    J Biol Chem 275:14809-16. 2000
  2. ncbi request reprint Matrix metalloproteinases 19 and 20 cleave aggrecan and cartilage oligomeric matrix protein (COMP)
    J O Stracke
    School of Biological Sciences, University of East Anglia, Norwich NR4 7TJ, UK
    FEBS Lett 478:52-6. 2000
  3. ncbi request reprint Catalytic activities of membrane-type 6 matrix metalloproteinase (MMP25)
    W R English
    School of Biological Sciences, University of East Anglia, Norwich NR4 7TJ, UK
    FEBS Lett 491:137-42. 2001

Detail Information

Publications3

  1. ncbi request reprint Biochemical characterization of the catalytic domain of human matrix metalloproteinase 19. Evidence for a role as a potent basement membrane degrading enzyme
    J O Stracke
    School of Biological Sciences, University of East Anglia, Norwich, NR4 7TJ, United Kingdom
    J Biol Chem 275:14809-16. 2000
    ..Finally, and in contrast to studies with other MMPs, MMP-19 catalytic domain was not able to activate any of the latent MMPs tested in vitro...
  2. ncbi request reprint Matrix metalloproteinases 19 and 20 cleave aggrecan and cartilage oligomeric matrix protein (COMP)
    J O Stracke
    School of Biological Sciences, University of East Anglia, Norwich NR4 7TJ, UK
    FEBS Lett 478:52-6. 2000
    ....
  3. ncbi request reprint Catalytic activities of membrane-type 6 matrix metalloproteinase (MMP25)
    W R English
    School of Biological Sciences, University of East Anglia, Norwich NR4 7TJ, UK
    FEBS Lett 491:137-42. 2001
    ..Our findings suggest that MT6-MMP could play a role in cellular migration and invasion of the extracellular matrix and basement membranes and its activity may be tightly regulated by all members of the TIMP family...