Triple Helicase Activity and the Structural Basis of Collagenolysis
Biology of Extracellular Matrix, ISSN: 2191-1959, Vol: 2, Page: 95-122
2011
- 15Citations
- 16Captures
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Example: if you select the 1-year option for an article published in 2019 and a metric category shows 90%, that means that the article or review is performing better than 90% of the other articles/reviews published in that journal in 2019. If you select the 3-year option for the same article published in 2019 and the metric category shows 90%, that means that the article or review is performing better than 90% of the other articles/reviews published in that journal in 2019, 2018 and 2017.
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Book Chapter Description
The degradation of interstitial collagens I, II and III is an integral part of many biological events such as embryonic development, organ morphogenesis, tissue remodelling and repair, and in diseases such as arthritis, cancer, atherosclerosis, aneurysm and fibrosis, but these collagens are resistant to most proteolytic enzymes due to their triple helical structures. In vertebrates, the enzymes that degrade interstitial collagens are collagenases that are members of the matrix metalloproteinase (MMP) family, and cathepsin K, a lysosomal cysteine proteinase. Non-vertebrate collagenases include collagenolytic serine proteinases in crustacea and Clostridium histolyticum collagenases, also called “bacterial collagenases.” This chapter describes the unique properties of these collagenolytic proteinases and the current proposal as to how they recognize triple helical structures and cleave them. Potential enzymatic pathways that may be involved in the degradation of collagen fibrils are also discussed.
Bibliographic Details
http://www.scopus.com/inward/record.url?partnerID=HzOxMe3b&scp=84864506555&origin=inward; http://dx.doi.org/10.1007/978-3-642-16861-1_5; https://link.springer.com/10.1007/978-3-642-16861-1_5; https://dx.doi.org/10.1007/978-3-642-16861-1_5; https://link.springer.com/chapter/10.1007/978-3-642-16861-1_5; http://www.springerlink.com/index/10.1007/978-3-642-16861-1_5; http://www.springerlink.com/index/pdf/10.1007/978-3-642-16861-1_5
Springer Science and Business Media LLC
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