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Protein Aggregation Landscape in Neurodegenerative Diseases: Clinical Relevance and Future Applications. | LitMetric

AI Article Synopsis

  • * Misfolded proteins can follow various pathways based on their amino acid composition and environment, producing different structures that may influence physiological and pathological signaling.
  • * This review discusses the diverse structures from intrinsically disordered protein domains, the formation of physiological droplets and pathogenic aggregates, and the implications for understanding neurodegenerative diseases.

Article Abstract

Intrinsic disorder is a natural feature of polypeptide chains, resulting in the lack of a defined three-dimensional structure. Conformational changes in intrinsically disordered regions of a protein lead to unstable β-sheet enriched intermediates, which are stabilized by intermolecular interactions with other β-sheet enriched molecules, producing stable proteinaceous aggregates. Upon misfolding, several pathways may be undertaken depending on the composition of the amino acidic string and the surrounding environment, leading to different structures. Accumulating evidence is suggesting that the conformational state of a protein may initiate signalling pathways involved both in pathology and physiology. In this review, we will summarize the heterogeneity of structures that are produced from intrinsically disordered protein domains and highlight the routes that lead to the formation of physiological liquid droplets as well as pathogenic aggregates. The most common proteins found in aggregates in neurodegenerative diseases and their structural variability will be addressed. We will further evaluate the clinical relevance and future applications of the study of the structural heterogeneity of protein aggregates, which may aid the understanding of the phenotypic diversity observed in neurodegenerative disorders.

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Source
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC8199687PMC
http://dx.doi.org/10.3390/ijms22116016DOI Listing

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