Proline hydroxylation in collagen supports integrin binding by two distinct mechanisms

Collagens are the most abundant extracellular matrix proteins in vertebrates and have a characteristic triple-helix structure. Hydroxylation of proline residues is critical for helix stability, and diminished prolyl hydroxylase activity causes wide-spread defects in connective tissues. Still, the ro...

Полное описание

Сохранить в:
Библиографические подробности
Опубликовано в: :J Biol Chem
Главные авторы: Sipilä, Kalle H., Drushinin, Kati, Rappu, Pekka, Jokinen, Johanna, Salminen, Tiina A., Salo, Antti M., Käpylä, Jarmo, Myllyharju, Johanna, Heino, Jyrki
Формат: Artigo
Язык:Inglês
Опубликовано: American Society for Biochemistry and Molecular Biology 2018
Предметы:
Glycobiology and Extracellular Matrices
Online-ссылка:https://ncbi.nlm.nih.gov/pmc/articles/PMC5961056/
https://ncbi.nlm.nih.gov/pubmed/29615493
https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1074/jbc.RA118.002200
Метки: Добавить метку
Нет меток, Требуется 1-ая метка записи!

Схожие документы