Collagen cross-links as a determinant of bone quality: a possible explanation for bone fragility in aging, osteoporosis, and diabetes mellitus
By M. Saito, K. Marumo. Osteoporosis International, 2010
869 citations recorded by the source corpus.
Subfields: Genetics, Oncology, Orthopedics and Sports Medicine
View Paper: https://www.semanticscholar.org/paper/17defb01c7ce5974abdadec51bcdad4364588963
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In Genetics
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In Orthopedics and Sports Medicine
Citations in the corpus
- The collagen family. (2011, background): “Pyridinoline and deoxypyridinoline are used as urinary markers of bone resorption in patients with bone diseases such as osteoporosis (Saito and Marumo 2010).”
- Characterization of Bone and Bone-Based Graft Materials Using FTIR Spectroscopy (2012, background): “Besides the usual bone mass loss associated with age, the accumulation of glycation cross-links and of mature enzymatic cross-links in collagen is also thought to contribute to the fragility and brittleness of bone (Saito & Marumo, 2009; Viguet-Carrin et al., 2010).”
- Advanced Glycation End-Products (AGEs): Formation, Chemistry, Classification, Receptors, and Diseases Related to AGEs (2022, background): “The accumulation and crosslinking of AGEs caused by oxidation stiffen the collagen structure and collagen-rich tissues such as tendons, bones [215], or the keratoconus.”
- Collagen for bone tissue regeneration. (2012, background): “In fact, collagen cross-links are divided into two types: enzymatic cross-links, mediated by lysine hydroxylase and lysyl oxidase; and non-enzymatic cross-links, commonly called glycation or oxidation induced Advanced glycation end products (AGE) cross-links [19].”