Half a century of amyloids: past, present and future

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 a...

Celý popis

Uloženo v:
Podrobná bibliografie
Vydáno v:Chemical Society reviews Ročník 49; číslo 15; s. 5473
Hlavní autoři: Ke, Pu Chun, Zhou, Ruhong, Serpell, Louise C, Riek, Roland, Knowles, Tuomas P J, Lashuel, Hilal A, Gazit, Ehud, Hamley, Ian W, Davis, Thomas P, Fändrich, Marcus, Otzen, Daniel Erik, Chapman, Matthew R, Dobson, Christopher M, Eisenberg, David S, Mezzenga, Raffaele
Médium: Journal Article
Jazyk:angličtina
Vydáno: England 07.08.2020
Témata:
Alzheimer Disease - metabolism
Amyloid - chemistry
Amyloid - metabolism
Amyloidosis
Cations, Divalent - chemistry
Cross-Linking Reagents - chemistry
Humans
Models, Molecular
Molecular Conformation
Printing, Three-Dimensional
Protein Folding
Protein Processing, Post-Translational
ISSN:1460-4744, 1460-4744
On-line přístup:Zjistit podrobnosti o přístupu
Tagy: Přidat tag
Žádné tagy, Buďte první, kdo vytvoří štítek k tomuto záznamu!
Popis
Shrnutí: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.
Bibliografie:ObjectType-Article-1
SourceType-Scholarly Journals-1
ObjectType-Feature-2
ObjectType-Review-3
content type line 23
ISSN:1460-4744
1460-4744
DOI:10.1039/c9cs00199a