Amyloids or prions? That is the question.


Por: Sabate R, Rousseau F, Schymkowitz J, Batlle C and Ventura S

Publicada: 1 ene 2015
Resumen:
Despite major efforts devoted to understanding the phenomenon of prion transmissibility, it is still poorly understood how this property is encoded in the amino acid sequence. In recent years, experimental data on yeast prion domains allow to start at least partially decrypting the sequence requirements of prion formation. These experiments illustrate the need for intrinsically disordered sequence regions enriched with a particularly high proportion of glutamine and asparagine. Bioinformatic analysis suggests that these regions strike a balance between sufficient amyloid nucleation propensity on the one hand and disorder on the other, which ensures availability of the amyloid prone regions but entropically prevents unwanted nucleation and facilitates brittleness required for propagation.

Filiaciones:
Sabate R:
 a Departament de Fisicoquímica

 Facultat de Farmàcia

 and Institut de Nanociència i Nanotecnologia (IN2UB)

 Universitat de Barcelona

 Barcelona , Spain
ISSN: 19336896





Prion
Editorial
TAYLOR & FRANCIS INC, 530 WALNUT STREET, STE 850, PHILADELPHIA, PA 19106, Estados Unidos America
Tipo de documento: Article
Volumen: 9 Número: 3
Páginas: 200-206
WOS Id: 000356878400005
ID de PubMed: 26039159
imagen gold, Green Published

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