Different splice variants of cartilage α1(XI) collagen chain undergo uniform amino-terminal processing
- 31 October 1998
- journal article
- research article
- Published by Elsevier in Matrix Biology
- Vol. 17 (5) , 393-396
- https://doi.org/10.1016/s0945-053x(98)90091-9
Abstract
No abstract availableKeywords
This publication has 7 references indexed in Scilit:
- Processing of Type XI CollagenPublished by Elsevier ,1996
- Ultrastructural localization of collagen types II, IX, and XI in the growth plate of human rib and fetal bovine epiphyseal cartilage: type XI collagen is restricted to thin fibrils.Journal of Histochemistry & Cytochemistry, 1995
- The Human COL11A2 Gene Structure Indicates that the Gene Has Not Evolved with the Genes for the Major Fibrillar CollagensJournal of Biological Chemistry, 1995
- Alternative mRNA Processing Occurs in the Variable Region of the Pro-α1(XI) and Pro-α2(XI) Collagen ChainsJournal of Biological Chemistry, 1995
- Diversity in the processing events at the N‐terminus of type‐V collagenEuropean Journal of Biochemistry, 1994
- Primary structure of the heparin-binding site of type V collagenBiochimica et Biophysica Acta (BBA) - General Subjects, 1990
- Inhibitors of procollagen N-protease. Synthetic peptides with sequences similar to the cleavage site in the pro.alpha.1 (I) chainBiochemistry, 1980