The amyloid interactome: Exploring protein aggregation
| Autor: | Chara V. Mastrokalou, Katerina C. Nastou, Konstantina V. Biza, Vassiliki A. Iconomidou, Stavros J. Hamodrakas, Paraskevi L. Tsiolaki |
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| Rok vydání: | 2016 |
| Předmět: |
0301 basic medicine
Proteomics Amyloid Computer and Information Sciences Serum Proteins lcsh:Medicine Computational biology Protein aggregation Biology Interactome Protein Aggregation Pathological Biochemistry Protein–protein interaction Amyloidogenic Proteins 03 medical and health sciences Interaction network Humans Computational analysis Protein Interaction Maps lcsh:Science Protein Interactions Multidisciplinary lcsh:R Biology and Life Sciences Proteins Amyloidosis Protein Aggregation Chaperone Proteins 030104 developmental biology Protein-Protein Interactions Amyloid Proteins lcsh:Q Protein folding Protein Interaction Networks Network Analysis Research Article |
| Zdroj: | PLoS ONE PLoS ONE, Vol 12, Iss 3, p e0173163 (2017) |
| ISSN: | 1932-6203 |
| Popis: | Protein-protein interactions are the quintessence of physiological activities, but also participate in pathological conditions. Amyloid formation, an abnormal protein-protein interaction process, is a widespread phenomenon in divergent proteins and peptides, resulting in a variety of aggregation disorders. The complexity of the mechanisms underlying amyloid formation/amyloidogenicity is a matter of great scientific interest, since their revelation will provide important insight on principles governing protein misfolding, self-assembly and aggregation. The implication of more than one protein in the progression of different aggregation disorders, together with the cited synergistic occurrence between amyloidogenic proteins, highlights the necessity for a more universal approach, during the study of these proteins. In an attempt to address this pivotal need we constructed and analyzed the human amyloid interactome, a protein-protein interaction network of amyloidogenic proteins and their experimentally verified interactors. This network assembled known interconnections between well-characterized amyloidogenic proteins and proteins related to amyloid fibril formation. The consecutive extended computational analysis revealed significant topological characteristics and unraveled the functional roles of all constituent elements. This study introduces a detailed protein map of amyloidogenicity that will aid immensely towards separate intervention strategies, specifically targeting sub-networks of significant nodes, in an attempt to design possible novel therapeutics for aggregation disorders. |
| Databáze: | OpenAIRE |
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