Titlebook: Collagen; Primer in Structure, Jürgen Brinckmann,Holger Notbohm,P. K. Müller Book 2005 Springer-Verlag Berlin Heidelberg 2005 biochemistry.

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The Collagen Superfamily,genous domains found in collagens. We also discuss data on collagen-related diseases with particular emphasis on gene therapy and on the involvement of collagens in neurodegenerative diseases, which emerge as a major threat for public health in aging populations.

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Collagen Biosynthesis,e helical conformation. The formation of the triple helix is a slow process compared to the folding of globular proteins, including . isomerization of the many prolyl and hydroxyprolyl peptide bonds. Recent advances have indicated that these processes are assisted by a set of the ER-resident molecul

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Collagen Cross-Links,als in the osteoporosis field. This review summarizes recent research directions with examples of advances in understanding complex interactions in cartilage collagen and the role of lysyl hydroxylase isoforms in regulating the pathway of cross-linking chemistry.

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Margot Weijnen,Zofia Lukszo,Samira Farahaniduring folding. Therefore, oligomerization domains flank triple helical domains in natural collagens. The mechanism by which these domains influence stability and kinetics was elucidated with model peptides using different types of trimerization domains. Finally, the review briefly describes mutatio

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Shaping an Inclusive Energy Transitiongenous domains found in collagens. We also discuss data on collagen-related diseases with particular emphasis on gene therapy and on the involvement of collagens in neurodegenerative diseases, which emerge as a major threat for public health in aging populations.

Perennial長(zhǎng)期的

https://doi.org/10.1007/978-3-030-74586-8e helical conformation. The formation of the triple helix is a slow process compared to the folding of globular proteins, including . isomerization of the many prolyl and hydroxyprolyl peptide bonds. Recent advances have indicated that these processes are assisted by a set of the ER-resident molecul

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