The molecular basis of chaperone-mediated interleukin 23 assembly control
It is unclear how unassembled secretory pathway proteins are discriminated from misfolded ones. Here the authors combine biophysical and cellular experiments to study the folding of heterodimeric interleukin 23 and describe how ER chaperones recognize unassembled proteins and aid their assembly into...
Guardado en:
Autores principales: | Susanne Meier, Sina Bohnacker, Carolin J. Klose, Abraham Lopez, Christian A. Choe, Philipp W. N. Schmid, Nicolas Bloemeke, Florian Rührnößl, Martin Haslbeck, Julia Esser-von Bieren, Michael Sattler, Po-Ssu Huang, Matthias J. Feige |
---|---|
Formato: | article |
Lenguaje: | EN |
Publicado: |
Nature Portfolio
2019
|
Materias: | |
Acceso en línea: | https://doaj.org/article/7a8999f450d04116918a03d1d6abd258 |
Etiquetas: |
Agregar Etiqueta
Sin Etiquetas, Sea el primero en etiquetar este registro!
|
Ejemplares similares
-
A network of chaperones prevents and detects failures in membrane protein lipid bilayer integration
por: João P. L. Coelho, et al.
Publicado: (2019) -
Publisher Correction: A network of chaperones prevents and detects failures in membrane protein lipid bilayer integration
por: João P. L. Coelho, et al.
Publicado: (2019) -
Interleukin 22 disrupts pancreatic function in newborn mice expressing IL-23
por: Lili Chen, et al.
Publicado: (2019) -
Conformational dynamics modulate the catalytic activity of the molecular chaperone Hsp90
por: Sophie L. Mader, et al.
Publicado: (2020) -
Structural basis underlying viral hijacking of a histone chaperone complex
por: Hongda Huang, et al.
Publicado: (2016)