Single collagen fibrils isolated from high stress and low stress tendons show differing susceptibility to enzymatic degradation by the interstitial collagenase matrix metalloproteinase-1 (MMP-1)
Author:
Funder
Natural Sciences and Engineering Research Council of Canada
Publisher
Elsevier BV
Subject
Cell Biology,Genetics,Molecular Biology,Histology,Biochemistry,Biophysics
Reference52 articles.
1. Collagen;Avery,2008
2. Different Crimp Patterns in Collagen Fibrils Relate to the Subfibrillar Arrangement;Franchi;Connect. Tissue Res.,2008
3. Tendon matrix composition and turnover in relation to functional requirements;Birch;Int. J. Exp. Pathol.,2007
4. Collagen fibrils in functionally distinct tendons have differing structural responses to tendon rupture and fatigue loading;Herod;Acta Biomater.,2016
5. Lower strength of the human posterior patellar tendon seems unrelated to mature collagen cross-linking and fibril morphology;Hansen;J. Appl. Physiol.,2010
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