Atomic structure and hierarchical assembly of a cross-β amyloid fibril

Fitzpatrick, Anthony W. P.; Debelouchina, Galia T.; Bayro, Marvin J.; Clare, Daniel K.; Caporini, Marc A.; Bajaj, Vikram S.; Jaroniec, Christopher P.; Wang, Luchun; Ladizhansky, Vladimir; Müller, Shirley A.; MacPhee, Cait E.; Waudby, Christopher A.; Mott, Helen R.; Simone, Alfonso De; Knowles, Tuomas P. J.; Saibil, Helen R.; Vendruscolo, Michele; Orlova, Elena V.; Griffin, Robert G.; Dobson, Christopher M.

doi:10.1073/pnas.1219476110

articleProceedings of the National Academy of SciencesMar 19, 2013BRONZE OA

Atomic structure and hierarchical assembly of a cross-β amyloid fibril

AWAnthony W. P. Fitzpatrick GTGalia T. Debelouchina MJMarvin J. Bayro DKDaniel K. Clare MAMarc A. Caporini

University of Cambridge · Massachusetts Institute of Technology · +5 more institutions

PubMed

Indexed incrossrefpubmed

Abstract

The cross-β amyloid form of peptides and proteins represents an archetypal and widely accessible structure consisting of ordered arrays of β-sheet filaments. These complex aggregates have remarkable chemical and physical properties, and the conversion of normally soluble functional forms of proteins into amyloid structures is linked to many debilitating human diseases, including several common forms of age-related dementia. Despite their importance, however, cross-β amyloid fibrils have proved to be recalcitrant to detailed structural analysis. By combining structural constraints from a series of experimental techniques spanning five orders of magnitude in length scale--including magic angle spinning nuclear…

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Keywords

Fibril
Magic angle spinning
Crystallography
Amyloid (mycology)
Transmission electron microscopy
Amyloid fibril
Chemistry
Fiber diffraction

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