Cargando…
Structural mechanisms of chaperone mediated protein disaggregation
The ClpB/Hsp104 and Hsp70 classes of molecular chaperones use ATP hydrolysis to dissociate protein aggregates and complexes, and to move proteins through membranes. ClpB/Hsp104 are members of the AAA+ family of proteins which form ring-shaped hexamers. Loops lining the pore in the ring engage substr...
Autor principal: | Sousa, Rui |
---|---|
Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Frontiers Media S.A.
2014
|
Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4428496/ https://www.ncbi.nlm.nih.gov/pubmed/25988153 http://dx.doi.org/10.3389/fmolb.2014.00012 |
Ejemplares similares
-
Cooperation of Hsp70 and Hsp100 chaperone machines in protein disaggregation
por: Mogk, Axel, et al.
Publicado: (2015) -
Multi-layered molecular mechanisms of polypeptide holding, unfolding and disaggregation by HSP70/HSP110 chaperones
por: Finka, Andrija, et al.
Publicado: (2015) -
The role of molecular chaperones in clathrin mediated vesicular trafficking
por: Sousa, Rui, et al.
Publicado: (2015) -
Cryo-EM structure of the diapause chaperone artemin
por: Parvate, Amar D., et al.
Publicado: (2022) -
The Impact of Hidden Structure on Aggregate Disassembly by Molecular Chaperones
por: Shoup, Daniel, et al.
Publicado: (2022)