Amyloids or prions? That is the question

Raimon Sabate, Frederic Rousseau, Joost Schymkowitz, Cristina Batlle, Salvador Ventura

Research output: Contribution to journalArticleResearchpeer-review

27 Citations (Scopus)


© 2015, Taylor & Francis Group, LLC. 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.
Original languageEnglish
Pages (from-to)200-206
Issue number3
Publication statusPublished - 1 Jan 2015


  • Amyloids
  • Neurodegenerative diseases
  • Prions
  • Protein intrinsic disorder
  • Q/N-rich domains
  • Yeast


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