Half a century of amyloids: past, present and future

Publikation: Bidrag til tidsskrift/Konferencebidrag i tidsskrift /Bidrag til avisReviewForskningpeer review

DOI

  • Pu Chun Ke, Shanghai Fudan Univ, Fudan University
  • ,
  • Ruhong Zhou, Zhejiang Univ, Zhejiang University, Dept Phys
  • ,
  • Louise C Serpell, Univ Sussex, University of Sussex, Sch Psychol
  • ,
  • Roland Riek, Edwards LifeSciences, Nyon, Switzerland Léman Research Institute, Switzerland.
  • ,
  • Tuomas P J Knowles, Department of Biochemistry, University of Cambridge, Cambridge, United Kingdom; Cambridge Systems Biology Centre, University of Cambridge, Cambridge, United Kingdom;
  • ,
  • Hilal A Lashuel, Brain Mind Institute
  • ,
  • Ehud Gazit, Tel Aviv University (TAU), Tel Aviv
  • ,
  • Ian W Hamley, Univ Reading, University of Reading, Dept Meteorol
  • ,
  • Thomas P Davis, Monash Med Ctr, Monash University, Monash Heart
  • ,
  • Marcus Fändrich, Ulm Univ, Ulm University
  • ,
  • Daniel Erik Otzen
  • Matthew R Chapman, Univ Michigan, University of Michigan System, University of Michigan, Leinweber Ctr Theoret Phys
  • ,
  • Christopher M Dobson, Department of Biochemistry, University of Cambridge, Cambridge, United Kingdom; Cambridge Systems Biology Centre, University of Cambridge, Cambridge, United Kingdom;
  • ,
  • David S Eisenberg, UCLA-DOE Institute and Howard Hughes Medical Institute
  • ,
  • Raffaele Mezzenga, Edwards LifeSciences, Nyon, Switzerland Léman Research Institute, Switzerland.

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-β 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.

OriginalsprogEngelsk
TidsskriftChemical Society Reviews
Vol/bind49
Nummer15
Sider (fra-til)5473-5509
ISSN0306-0012
DOI
StatusUdgivet - 7 aug. 2020

Se relationer på Aarhus Universitet Citationsformater

ID: 192152045