2019
DOI: 10.1016/j.bone.2018.09.024
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Alterations in non-type I collagen biomarkers in osteogenesis imperfecta

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Cited by 15 publications
(3 citation statements)
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“…Collagen types I, II, III, V, and XI are able to form fibrils that are necessary for structural support and resistance to mechanical stress in connective tissues [16,17]. Type I collagen is the most abundant form and is mainly present in the tendons and skin [18][19][20].…”
Section: Introductionmentioning
confidence: 99%
“…Collagen types I, II, III, V, and XI are able to form fibrils that are necessary for structural support and resistance to mechanical stress in connective tissues [16,17]. Type I collagen is the most abundant form and is mainly present in the tendons and skin [18][19][20].…”
Section: Introductionmentioning
confidence: 99%
“…Degradation biomarkers are further divided into Col-I neoepitope (C1M), C-terminal telopeptide of Col-I (CTX-I), and Col-I-derived crosslinked carboxy-terminal telopeptide (ICTP). Furthermore, synthesis biomarkers are broken down into carboxy-terminal propeptides of pro Col-I (PICP) and amino-terminal propeptides of pro Col-I (PINP) [ 98 ].…”
Section: Biomarkers For Col-imentioning
confidence: 99%
“…Although there are differences between collagen and collagen peptides, they are closely related. Collagen is the parent protein of collagen peptides, while collagen peptides are low molecular weight fragments produced after collagen is biologically processed [6][7][8]. Fish collagen and terrestrial animal collagen amino acid structure is similar, with good water solubility, biosafety, biodegradability, etc, and its living environment is relatively clean, in the control of viruses, cross-infection and other risks than the terrestrial animals have obvious advantages and is considered to be an important source of medical collagen replacement [9,10].…”
Section: Introductionmentioning
confidence: 99%