Protein aggregation: mechanisms and functional consequences

Int J Biochem Cell Biol. 2012 Sep;44(9):1541-54. doi: 10.1016/j.biocel.2012.05.023. Epub 2012 Jun 17.

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.

Publication types

  • Research Support, Non-U.S. Gov't
  • Review

MeSH terms

  • Amyloid / chemistry
  • Amyloid / metabolism
  • Animals
  • Disease
  • Humans
  • Models, Molecular
  • Protein Conformation
  • Protein Multimerization*
  • Proteins / chemistry*
  • Proteins / metabolism*

Substances

  • Amyloid
  • Proteins