Protein misfolding, functional amyloid, and human disease

F Chiti, CM Dobson - Annu. Rev. Biochem., 2006 - annualreviews.org
Peptides or proteins convert under some conditions from their soluble forms into highly
ordered fibrillar aggregates. Such transitions can give rise to pathological conditions ranging …

Spherulites

AG Shtukenberg, YO Punin, E Gunn, B Kahr - Chemical reviews, 2012 - ACS Publications
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Find my institution Log In ACS Publications. Most Trusted. Most Cited. Most Read Chemical …

Binding mode of Thioflavin T and other molecular probes in the context of amyloid fibrils—current status

M Groenning - Journal of chemical biology, 2010 - Springer
Because understanding amyloid fibrillation in molecular detail is essential for development
of strategies to control amyloid formation and overcome neurodegenerative disorders …

The binding of thioflavin-T to amyloid fibrils: localisation and implications

MRH Krebs, EHC Bromley, AM Donald - Journal of structural biology, 2005 - Elsevier
Amyloid fibrils are a polymeric form of protein, involving a continuous β-sheet with the
strands perpendicular to the long axis of the fibril. Although typically implicated in diseases …

Characterization of the nanoscale properties of individual amyloid fibrils

JF Smith, TPJ Knowles, CM Dobson… - Proceedings of the …, 2006 - pnas.org
We report the detailed mechanical characterization of individual amyloid fibrils by atomic
force microscopy and spectroscopy. These self-assembling materials, formed here from the …

Protein aggregation and neurodegenerative diseases: From theory to therapy

V Kumar, N Sami, T Kashav, A Islam, F Ahmad… - European journal of …, 2016 - Elsevier
The study of protein misfolding and aggregation saw resurgence in the last decade.
Aggregation is the main cause of several human neurodegenerative diseases which makes …

Aβ (1-40) fibril polymorphism implies diverse interaction patterns in amyloid fibrils

J Meinhardt, C Sachse, P Hortschansky… - Journal of molecular …, 2009 - Elsevier
Amyloid fibrils characterize a diverse group of human diseases that includes Alzheimer's
disease, Creutzfeldt-Jakob and type II diabetes. Alzheimer's amyloid fibrils consist of …

Structural polymorphism of Alzheimer Aβ and other amyloid fibrils

M Fändrich, J Meinhardt, N Grigorieff - Prion, 2009 - Taylor & Francis
Deposits of amyloid fibrils characterize a diverse group of human diseases that includes
Alzheimer's disease, Creutzfeldt-Jakob disease and type II diabetes. Amyloid fibrils formed …

Polyferrocenylsilane block copolymer spherulites in dilute solution

J Jiang, E Nikbin, G Hicks, S Song, Y Liu… - Journal of the …, 2023 - ACS Publications
Self-assembly of block copolymers (BCP) into uniform 3D structures in solution is an
extremely rare phenomenon. Furthermore, the investigation of general prerequisites for …

Nanomaterials: amyloids reflect their brighter side

S Mankar, A Anoop, S Sen, SK Maji - Nano reviews, 2011 - Taylor & Francis
Amyloid fibrils belong to the group of ordered nanostructures that are self-assembled from a
wide range of polypeptides/proteins. Amyloids are highly rigid structures possessing a high …