head-bent resistant Hsc70 variants show reduced Hsp40 affinity and altered protein folding activity

The molecular chaperone Hsc70 performs essential tasks by folding proteins. Hsc70 is driven by the hydrolysis of ATP and tuned by the association with various co-chaperones. One such cofactor is the nematode nucleotide exchange factor UNC-23, whose mutation disrupts muscle attachment and induces a s...

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Detalles Bibliográficos
Autores principales: Papsdorf, Katharina, Sima, Siyuan, Schmauder, Lukas, Peter, Sebastian, Renner, Lisa, Hoffelner, Patrica, Richter, Klaus
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Nature Publishing Group UK 2019
Materias:
Article
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6697693/
https://www.ncbi.nlm.nih.gov/pubmed/31420580
http://dx.doi.org/10.1038/s41598-019-48109-0

Internet

https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6697693/
https://www.ncbi.nlm.nih.gov/pubmed/31420580
http://dx.doi.org/10.1038/s41598-019-48109-0

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