A prion-like domain in Hsp42 drives chaperone-facilitated aggregation of misfolded proteins

Chaperones with aggregase activity promote and organize the aggregation of misfolded proteins and their deposition at specific intracellular sites. This activity represents a novel cytoprotective strategy of protein quality control systems; however, little is known about its mechanism. In yeast, the...

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Detalles Bibliográficos
Autores principales: Grousl, Tomas, Ungelenk, Sophia, Miller, Stephanie, Ho, Chi-Ting, Khokhrina, Maria, Mayer, Matthias P., Bukau, Bernd, Mogk, Axel
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Rockefeller University Press 2018
Materias:
Research Articles
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5881502/
https://www.ncbi.nlm.nih.gov/pubmed/29362223
http://dx.doi.org/10.1083/jcb.201708116

Internet

https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5881502/
https://www.ncbi.nlm.nih.gov/pubmed/29362223
http://dx.doi.org/10.1083/jcb.201708116

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