Cargando…
Collagen’s primary structure determines collagen:HSP47 complex stoichiometry
Collagens play important roles in development and homeostasis in most higher organisms. In order to function, collagens require the specific chaperone HSP47 for proper folding and secretion. HSP47 is known to bind to the collagen triple helix, but the exact positions and numbers of binding sites are...
Autores principales: | Abraham, Elena T., Oecal, Sinan, Mörgelin, Matthias, Schmid, Philipp W.N., Buchner, Johannes, Baumann, Ulrich, Gebauer, Jan M. |
---|---|
Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
American Society for Biochemistry and Molecular Biology
2021
|
Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8626583/ https://www.ncbi.nlm.nih.gov/pubmed/34487762 http://dx.doi.org/10.1016/j.jbc.2021.101169 |
Ejemplares similares
-
Aberrant binding of mutant HSP47 affects posttranslational modification of type I collagen and leads to osteogenesis imperfecta
por: Syx, Delfien, et al.
Publicado: (2021) -
Identification of HSP47 Binding Site on Native Collagen and Its Implications for the Development of HSP47 Inhibitors
por: Cai, Haiyan, et al.
Publicado: (2021) -
NMR and Mutational Identification of the Collagen-Binding Site of the Chaperone Hsp47
por: Yagi-Utsumi, Maho, et al.
Publicado: (2012) -
Photoactivatable Hsp47: A Tool to Regulate Collagen Secretion and Assembly
por: Khan, Essak S., et al.
Publicado: (2019) -
Retraction: Photoactivatable Hsp47: A Tool to Regulate Collagen Secretion and Assembly
por: Khan, Essak S., et al.
Publicado: (2023)