Molecular cloning and sequence analysis of the aggrecan interglobular domain from porcine, equine, bovine and ovine cartilage: Comparison of proteinase-susceptible regions and sites of keratan sulfate substitution
- 31 March 1998
- journal article
- research article
- Published by Elsevier in Matrix Biology
- Vol. 16 (8), 507-511
- https://doi.org/10.1016/s0945-053x(98)90021-x
Abstract
No abstract availableKeywords
This publication has 7 references indexed in Scilit:
- Complete Coding Sequence of Bovine Aggrecan: Comparative Structural AnalysisArchives of Biochemistry and Biophysics, 1997
- Aggrecan degradation in human intervertebral disc and articular cartilageBiochemical Journal, 1997
- Degradation of cartilage aggrecan by collagenase‐3 (MMP‐13)FEBS Letters, 1996
- N- and O-Linked Keratan Sulfate on the Hyaluronan Binding Region of Aggrecan from Mature and Immature Bovine CartilageJournal of Biological Chemistry, 1995
- Quantification of a matrix metalloproteinase-generated aggrecan G1 fragment using monospecific anti-peptide serumBiochemical Journal, 1995
- Monoclonal antibodies that specifically recognize neoepitope sequences generated by ‘aggrecanase’ and matrix metalloproteinase cleavage of aggrecan: application to catabolism in situ and in vitroBiochemical Journal, 1995
- Variability in the G3 domain content of bovine aggrecan from cartilage extracts and chondrocyte culturesArchives of Biochemistry and Biophysics, 1992