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A method for probing the mutational landscape of amyloid structure
Motivation: Proteins of all kinds can self-assemble into highly ordered β-sheet aggregates known as amyloid fibrils, important both biologically and clinically. However, the specific molecular structure of a fibril can vary dramatically depending on sequence and environmental conditions, and mutatio...
Autores principales: | O'Donnell, Charles W., Waldispühl, Jérôme, Lis, Mieszko, Halfmann, Randal, Devadas, Srinivas, Lindquist, Susan, Berger, Bonnie |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Oxford University Press
2011
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3117379/ https://www.ncbi.nlm.nih.gov/pubmed/21685090 http://dx.doi.org/10.1093/bioinformatics/btr238 |
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Author Index
Publicado: (2011)