In silico characterization of human prion-like proteins: Beyond neurological diseases

Valentin Iglesias, Lisanna Paladin, Teresa Juan-Blanco, Irantzu Pallarès, Patrick Aloy, Silvio C.E. Tosatto, Salvador Ventura

Research output: Contribution to journalArticleResearch

3 Citations (Scopus)

Abstract

© 2019 Iglesias, Paladin, Juan-Blanco, Pallarès, Aloy, Tosatto and Ventura. Prion-like behavior has been in the spotlight since it was first associated with the onset of mammalian neurodegenerative diseases. However, a growing body of evidence suggests that this mechanism could be behind the regulation of processes such as transcription and translation in multiple species. Here, we perform a stringent computational survey to identify prion-like proteins in the human proteome. We detected 242 candidate polypeptides and computationally assessed their function, protein-protein interaction networks, tissular expression, and their link to disease. Human prion-like proteins constitute a subset of modular polypeptides broadly expressed across different cell types and tissues, significantly associated with disease, embedded in highly connected interaction networks, and involved in the flow of genetic information in the cell. Our analysis suggests that these proteins might play a relevant role not only in neurological disorders, but also in different types of cancer and viral infections.
Original languageEnglish
Article number314
JournalFrontiers in Physiology
Volume10
DOIs
Publication statusPublished - 1 Jan 2019

Keywords

  • Amyloid
  • Bioinformatics
  • Disease
  • Prion-like proteins
  • Protein aggregation
  • Protein-protein interaction

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