Cargando…
Overlapping and Specific Functions of the Hsp104 N Domain Define Its Role in Protein Disaggregation
Hsp104 is a ring-forming protein disaggregase that rescues stress-damaged proteins from an aggregated state. To facilitate protein disaggregation, Hsp104 cooperates with Hsp70 and Hsp40 chaperones (Hsp70/40) to form a bi-chaperone system. How Hsp104 recognizes its substrates, particularly the import...
Autores principales: | Lee, Jungsoon, Sung, Nuri, Mercado, Jonathan M., Hryc, Corey F., Chang, Changsoo, Lee, Sukyeong, Tsai, Francis T. F. |
---|---|
Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Nature Publishing Group UK
2017
|
Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5593927/ https://www.ncbi.nlm.nih.gov/pubmed/28894176 http://dx.doi.org/10.1038/s41598-017-11474-9 |
Ejemplares similares
-
Structural determinants for protein unfolding and translocation by the Hsp104 protein disaggregase
por: Lee, Jungsoon, et al.
Publicado: (2017) -
Cryo-EM Structures of the Hsp104 Protein Disaggregase Captured in the ATP Conformation
por: Lee, Sukyeong, et al.
Publicado: (2019) -
Hsp104 N‐terminal domain interaction with substrates plays a regulatory role in protein disaggregation
por: Harari, Anna, et al.
Publicado: (2022) -
Coordinated Hsp110 and Hsp104 Activities Power Protein Disaggregation in Saccharomyces cerevisiae
por: Kaimal, Jayasankar Mohanakrishnan, et al.
Publicado: (2017) -
Molecular chaperones: guardians of the proteome in normal and disease states
por: Jeng, Wilson, et al.
Publicado: (2015)