A General Model for Amyloid Fibril Assembly Based on Morphological Studies Using Atomic Force Microscopy
Ritu Khurana,Cristian Ionescu-Zanetti,Maighdlin Pope,Jie Li,Liza Nielson,Marina Ramirez-Alvarado,Lynn Regan,Anthony L. Fink,Sue A. Carter +8 more
TLDR
It is proposed that the hierarchical assembly model describes a general mechanism of assembly for all amyloid fibrils.About:
This article is published in Biophysical Journal.The article was published on 2003-08-01 and is currently open access. It has received 299 citations till now. The article focuses on the topics: Amyloid.read more
Citations
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Molecular mechanism of Thioflavin-T binding to amyloid fibrils.
Matthew Biancalana,Shohei Koide +1 more
TL;DR: Recent progress in the understanding of ThT-fibril interactions at an atomic resolution is reviewed to offer guidance for designing the next generation of amyloid assembly diagnostics, inhibitors, and therapeutics.
Journal ArticleDOI
Mechanism of thioflavin T binding to amyloid fibrils
Ritu Khurana,Chris Coleman,Cristian Ionescu-Zanetti,Sue A. Carter,Vinay Krishna,Rajesh K. Grover,Raja Roy,Shashi Singh +7 more
TL;DR: The data suggests that the micelles of thioflavin T bind amyloid fibrils leading to enhancement of fluorescence emission, which suggests that positive charge on the thioFlavin T molecule has a role in its micelle formation that then bind the amyloids fibril.
Journal ArticleDOI
Solid-state NMR structure of a pathogenic fibril of full-length human α-synuclein
Marcus D. Tuttle,Marcus D. Tuttle,Gemma Comellas,Andrew J. Nieuwkoop,Andrew J. Nieuwkoop,Dustin J. Covell,Deborah A. Berthold,Kathryn D. Kloepper,Kathryn D. Kloepper,Joseph M. Courtney,Jae K Kim,Alexander M. Barclay,Amy Kendall,William Wan,William Wan,Gerald Stubbs,Charles D. Schwieters,Virginia M.-Y. Lee,Jimin George,Chad M. Rienstra +19 more
TL;DR: A high-resolution structure of an α-synuclein fibril, in a form that induces robust pathology in primary neuronal culture, determined by solid-state NMR spectroscopy and validated by EM and X-ray fiber diffraction is presented.
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Protein aggregation kinetics, mechanism, and curve-fitting: A review of the literature
TL;DR: Three problem areas in the protein aggregation kinetic and mechanistic studies area are identified, and a Summary and Conclusions section is provided en route to moving the field forward towards the still unachieved goal of unequivocal elucidation of the mechanism(s) of protein aggregation.
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Binding mode of Thioflavin T and other molecular probes in the context of amyloid fibrils—current status
Minna Groenning,Minna Groenning +1 more
TL;DR: Increased understanding of present molecular probes as well as development of new probes are of utmost importance for development of strategies to control amyloid formation and overcome neurodegenerative disorders.
References
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Effect of Environmental Factors on the Kinetics of Insulin Fibril Formation: Elucidation of the Molecular Mechanism
Liza Nielsen,Ritu Khurana,Alisa C. Coats,Sven Frokjaer,Jens Brange,Sandip Vyas,Vladimir N. Uversky,Anthony L. Fink +7 more
TL;DR: The results indicated that both nucleation and fibril growth were controlled by hydrophobic and electrostatic interactions.
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Evidence for a partially folded intermediate in alpha-synuclein fibril formation.
TL;DR: A model for the fibrillation of α-synuclein is proposed in which the first step is the conformational transformation of the natively unfolded protein into the aggregation-competent partially folded intermediate.
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Instability, unfolding and aggregation of human lysozyme variants underlying amyloid fibrillogenesis
David R. Booth,Margaret Sunde,Vittorio Bellotti,Vittorio Bellotti,Carol V. Robinson,Winston L. Hutchinson,Paul E. Fraser,Philip N. Hawkins,Christopher M. Dobson,Sheena E. Radford,Sheena E. Radford,Colin C.F. Blake,Mark B. Pepys +12 more
TL;DR: Biophysical studies suggest that partly folded intermediates are involved in fibrillogenesis, and this may be relevant to amyloidosis generally.
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Fibrils Formed in Vitro from α-Synuclein and Two Mutant Forms Linked to Parkinson's Disease are Typical Amyloid†
TL;DR: Fibrils generated in vitro from alpha-synuclein, wild-type and both mutant forms, are shown to possess very similar features that are characteristic of amyloid fibrils, including a wound and predominantly unbranched morphology, distinctive dye-binding properties, and antiparallel beta-sheet structure.
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Amyloid fibrils from muscle myoglobin
TL;DR: Even an ordinary globular protein can assume a rogue guise if conditions are right and the molecule can be tricked into thinking it is another protein.