Cargando…
Mechanism of Hsp70 specialized interactions in protein translocation and the unfolded protein response
Hsp70 chaperones interact with substrate proteins in a coordinated fashion that is regulated by nucleotides and enhanced by assisting cochaperones. There are numerous homologues and isoforms of Hsp70 that participate in a wide variety of cellular functions. This diversity can facilitate adaption or...
Autores principales: | Larburu, Natacha, Adams, Christopher J., Chen, Chao-Sheng, Nowak, Piotr R., Ali, Maruf M. U. |
---|---|
Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
The Royal Society
2020
|
Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7479934/ https://www.ncbi.nlm.nih.gov/pubmed/32810420 http://dx.doi.org/10.1098/rsob.200089 |
Ejemplares similares
-
Structure and Molecular Mechanism of ER Stress Signaling by the Unfolded Protein Response Signal Activator IRE1
por: Adams, Christopher J., et al.
Publicado: (2019) -
Sulfatide-Hsp70 Interaction Promotes Hsp70 Clustering and Stabilizes Binding to Unfolded Protein
por: Harada, Yoichiro, et al.
Publicado: (2015) -
Alternative ATPase domain interactions in eukaryotic Hsp70 chaperones
por: Ben-Khoud, Yassin, et al.
Publicado: (2023) -
Hsp70 at the membrane: driving protein translocation
por: Craig, Elizabeth A.
Publicado: (2018) -
Structural determinants for protein unfolding and translocation by the Hsp104 protein disaggregase
por: Lee, Jungsoon, et al.
Publicado: (2017)