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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...
| Autores principales: | , , , , , , |
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| Formato: | Online Artículo Texto |
| Lenguaje: | English |
| Publicado: |
Nature Publishing Group UK
2019
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| Materias: | |
| 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 |