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Cell-free synthesis of amyloid fibrils with infectious properties and amenable to sub-milligram magic-angle spinning NMR analysis
Structural investigations of amyloid fibrils often rely on heterologous bacterial overexpression of the protein of interest. Due to their inherent hydrophobicity and tendency to aggregate as inclusion bodies, many amyloid proteins are challenging to express in bacterial systems. Cell-free protein ex...
Autores principales: | Lends, Alons, Daskalov, Asen, Maleckis, Ansis, Delamare, Aline, Berbon, Mélanie, Grélard, Axelle, Morvan, Estelle, Shenoy, Jayakrishna, Dutour, Antoine, Tolchard, James, Noubhani, Abdelmajid, Giraud, Marie-France, Sanchez, Corinne, Habenstein, Birgit, Guichard, Gilles, Compain, Guillaume, Jaudzems, Kristaps, Saupe, Sven J., Loquet, Antoine |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Nature Publishing Group UK
2022
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9646696/ https://www.ncbi.nlm.nih.gov/pubmed/36352173 http://dx.doi.org/10.1038/s42003-022-04175-1 |
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