4.8 Review

Half a century of amyloids: past, present and future

Journal

CHEMICAL SOCIETY REVIEWS
Volume 49, Issue 15, Pages 5473-5509

Publisher

ROYAL SOC CHEMISTRY
DOI: 10.1039/c9cs00199a

Keywords

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Funding

  1. HHMI
  2. NIH
  3. NSF
  4. BBSRC
  5. MRC
  6. Alzheimer's Society
  7. Alzheimer's Research UK
  8. ARC
  9. AFTAM Research Collaboration Award
  10. EPSRC [EP/L020599/1]
  11. Independent Research Council Denmark-Natural Sciences grant [8021-00208B]
  12. Independent Research Council Denmark-Technical Sciences grant [6111-00241]
  13. NIH [R01GM118651]
  14. DFG [FA 456/27]
  15. EPSRC [EP/L020599/1] Funding Source: UKRI

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Amyloid diseases are global epidemics with profound health, social and economic implications and yet remain without a cure. This dire situation calls for research into the origin and pathological manifestations of amyloidosis to stimulate continued development of new therapeutics. In basic science and engineering, the cross-beta architecture has been a constant thread underlying the structural characteristics of pathological and functional amyloids, and realizing that amyloid structures can be both pathological and functional in nature has fuelled innovations in artificial amyloids, whose use today ranges from water purification to 3D printing. At the conclusion of a half century since Eanes and Glenner's seminal study of amyloids in humans, this review commemorates the occasion by documenting the major milestones in amyloid research to date, from the perspectives of structural biology, biophysics, medicine, microbiology, engineering and nanotechnology. We also discuss new challenges and opportunities to drive this interdisciplinary field moving forward.

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