Cargando…
A conserved strategy for structure change and energy transduction in Hsp104 and other AAA+ protein motors
The superfamily of massively large AAA+ protein molecular machines functions to convert the chemical energy of cytosolic ATP into physicomechanical form and use it to perform an extraordinary number of physical operations on proteins, nucleic acids, and membrane systems. Cryo-EM studies now reveal s...
Autores principales: | Ye, Xiang, Mayne, Leland, Englander, S. Walter |
---|---|
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/PMC8449053/ https://www.ncbi.nlm.nih.gov/pubmed/34384781 http://dx.doi.org/10.1016/j.jbc.2021.101066 |
Ejemplares similares
-
Correction: A conserved strategy for structure change and energy transduction in Hsp104 and other AAA+ protein motors
por: Ye, Xiang, et al.
Publicado: (2021) -
Recent structural insights into the mechanism of ClpP protease regulation by AAA+ chaperones and small molecules
por: Mabanglo, Mark F., et al.
Publicado: (2022) -
Structure, function, and substrates of Clp AAA+ protease systems in cyanobacteria, plastids, and apicoplasts: A comparative analysis
por: Bouchnak, Imen, et al.
Publicado: (2021) -
Structural insights of the p97/VCP AAA+ ATPase: How adapter interactions coordinate diverse cellular functionality
por: Braxton, Julian R., et al.
Publicado: (2023) -
Folding or holding?—Hsp70 and Hsp90 chaperoning of misfolded proteins in neurodegenerative disease
por: Rutledge, Benjamin S., et al.
Publicado: (2022)