reviewAnnual Review of BiochemistryMay 12, 2017GREEN OA

Protein Misfolding, Amyloid Formation, and Human Disease: A Summary of Progress Over the Last Decade

University of Florence · University of Cambridge

PubMed
Indexed incrossrefpubmed

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

2,652
total citations
FWCI
144.18
Percentile
100%
References
242
Citations per year

Authors

2

Topics & keywords

Keywords
  • Proteostasis
  • Amyloid (mycology)
  • Amyloid fibril
  • Protein aggregation
  • Disease
  • Protein folding
  • Amyloid disease
  • Computational biology
UN Sustainable Development Goals
  • Good health and well-being
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