Protein Misfolding, Amyloid Formation, and Human Disease: A Summary of Progress Over the Last Decade
University of Florence · University of Cambridge
Abstract
Peptides and proteins have been found to possess an inherent tendency to convert from their native functional states into intractable amyloid aggregates. This phenomenon is associated with a range of increasingly common human disorders, including Alzheimer and Parkinson diseases, type II diabetes, and a number of systemic amyloidoses. In this review, we describe this field of science with particular reference to the advances that have been made over the last decade in our understanding of its fundamental nature and consequences. We list the proteins that are known to be deposited as amyloid or other types of aggregates in human tissues and the disorders with which they are associated, as well as the proteins…
Citation impact
- FWCI
- 144.18
- Percentile
- 100%
- References
- 242
Authors
2Topics & keywords
- Proteostasis
- Amyloid (mycology)
- Amyloid fibril
- Protein aggregation
- Disease
- Protein folding
- Amyloid disease
- Computational biology
- Good health and well-being