Regulatory inter-domain interactions influence Hsp70 recruitment to the DnaJB8 chaperone
The Hsp70/Hsp40 system plays an important role in maintaining cellular proteostasis but so far it is not well understood how Hsp70 proteins are recruited to specific Hsp40 co-chaperones. Here, the authors combine biochemical and biophysical approaches to characterise the oligomeric mammalian Hsp40 D...
Guardado en:
Autores principales: | Bryan D. Ryder, Irina Matlahov, Sofia Bali, Jaime Vaquer-Alicea, Patrick C. A. van der Wel, Lukasz A. Joachimiak |
---|---|
Formato: | article |
Lenguaje: | EN |
Publicado: |
Nature Portfolio
2021
|
Materias: | |
Acceso en línea: | https://doaj.org/article/60d78f39be754f40b8a931a46a1f1dfb |
Etiquetas: |
Agregar Etiqueta
Sin Etiquetas, Sea el primero en etiquetar este registro!
|
Ejemplares similares
-
The molecular chaperones DNAJB6 and Hsp70 cooperate to suppress α-synuclein aggregation
por: Francesco A. Aprile, et al.
Publicado: (2017) -
The chaperone HSPB1 prepares protein aggregates for resolubilization by HSP70
por: Conrado C. Gonçalves, et al.
Publicado: (2021) -
HSP70 and FLT3-ITD: Targeting chaperone system to overcome drug resistance
por: Jing Yang, et al.
Publicado: (2021) -
Chaperone-Based Therapeutic Target Innovation: Heat Shock Protein 70 (HSP70) for Type 2 Diabetes Mellitus
por: Mulyani WRW, et al.
Publicado: (2020) -
The Hsp70-Hsp90 co-chaperone Hop/Stip1 shifts the proteostatic balance from folding towards degradation
por: Kaushik Bhattacharya, et al.
Publicado: (2020)