4.6 Review

Protein aggregation: Mechanisms and functional consequences

Journal

INTERNATIONAL JOURNAL OF BIOCHEMISTRY & CELL BIOLOGY
Volume 44, Issue 9, Pages 1541-1554

Publisher

PERGAMON-ELSEVIER SCIENCE LTD
DOI: 10.1016/j.biocel.2012.05.023

Keywords

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

Funding

  1. Ministerio de Ciencia e Innovacion (Spain) [BFU2010-14901]
  2. AGAUR (Agencia de Gestio d'Ajuts Universitaris i de Recerca-Generalitat de Catalunya) [2009-SGR 760]
  3. University of Milano-Bicocca
  4. Ramon y Cajal Programme from Ministerio de Ciencia e Innovacion
  5. European Commission - Capacites Area - Research Infrastructures
  6. ICREA-ACADEMIA award (Institucio Catalana de Recerca i Estudis Avancats)

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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. (C) 2012 Elsevier Ltd. All rights reserved.

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