2013
DOI: 10.1007/s10973-013-2944-3
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Calorimetric investigation of normal and pathological human meniscus

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Cited by 2 publications
(2 citation statements)
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“…Similar values of denaturation temperatures are reported for samples from other collagenbased tissues [8,10,22,23]. Thermal stability of collagen molecules reflects the overall condition of the structure, cross-links in the collagen network, and its interactions with the surrounding molecules [4,21,[24][25][26]. Parameters of thermal transition of collagen in tissues were shown to be sensitive to the number of cross-links as well as to the level of hydration of collagen molecules [21-24, 27, 28].…”
Section: Discussionmentioning
confidence: 58%
“…Similar values of denaturation temperatures are reported for samples from other collagenbased tissues [8,10,22,23]. Thermal stability of collagen molecules reflects the overall condition of the structure, cross-links in the collagen network, and its interactions with the surrounding molecules [4,21,[24][25][26]. Parameters of thermal transition of collagen in tissues were shown to be sensitive to the number of cross-links as well as to the level of hydration of collagen molecules [21-24, 27, 28].…”
Section: Discussionmentioning
confidence: 58%
“…The ability to analyze the volatile products during a mass loss is also a valuable possibility, when available [7][8][9][10]. Previously differential scanning calorimetry (DSC) was used for the investigation of normal and degenerative human meniscus cartilage, and water content has not been measured [11][12][13][14]. A significant paper from this field was the study of Than et al [15], further studies measured the difference between primary osteoarthritis and septic arthritis [16].…”
Section: Introductionmentioning
confidence: 99%