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.
Original language | English |
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Journal | International Journal of Biochemistry & Cell Biology |
Volume | 44 |
Issue number | 9 |
Pages (from-to) | 1541-1554 |
Number of pages | 14 |
ISSN | 1357-2725 |
DOIs | |
Publication status | Published - Sept 2012 |
Externally published | Yes |
Keywords
- Amyloid
- Animals
- Disease
- Humans
- Models, Molecular
- Protein Conformation
- Protein Multimerization
- Proteins