Protein aggregation: Mechanisms and functional consequences

Gaetano Invernizzi, Elena Papaleo, Raimon Sabate, Salvador Ventura

Research output: Contribution to journalReview articleResearchpeer-review

91 Citations (Scopus)

Abstract

Understanding the mechanisms underlying protein misfolding and aggregation has become a central issue in biology and medicine. Compelling evidence show that the formation of amyloid aggregates has a negative impact in cell function and is behind the most prevalent human degenerative disorders, including Alzheimer's Parkinson's and Huntington's diseases or type 2 diabetes. Surprisingly, the same type of macromolecular assembly is used for specialized functions by different organisms, from bacteria to human. Here we address the conformational properties of these aggregates, their formation pathways, their role in human diseases, their functional properties and how bioinformatics tools might be of help to study these protein assemblies. © 2012 Elsevier Ltd.
Original languageEnglish
Pages (from-to)1541-1554
JournalInternational Journal of Biochemistry and Cell Biology
Volume44
Issue number9
DOIs
Publication statusPublished - 1 Sep 2012

Keywords

  • Amyloid fibrils
  • Conformational disorders
  • Functional amyloids
  • Molecular dynamics
  • Protein aggregation
  • Protein misfolding

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