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Article
Amyloid formation as a protein phase transition
The formation of amyloid fibrils is a general class of protein self-assembly behaviour, which is associated with both functional biology and the development of a number of disorders, such as Alzheimer and Park...
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Article
Open AccessCorrection to: Galectin-3, a novel endogenous TREM2 ligand, detrimentally regulates inflammatory response in Alzheimer’s disease
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Article
Open AccessPublisher Correction: A dopamine metabolite stabilizes neurotoxic amyloid-β oligomers
A Correction to this paper has been published: https://doi.org/10.1038/s42003-021-01680-7.
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Article
Open AccessA dopamine metabolite stabilizes neurotoxic amyloid-β oligomers
Aberrant soluble oligomers formed by the amyloid-β peptide (Aβ) are major pathogenic agents in the onset and progression of Alzheimer’s disease. A variety of biomolecules can influence the formation of these o...
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Article
Open AccessScreening of small molecules using the inhibition of oligomer formation in α-synuclein aggregation as a selection parameter
The aggregation of α-synuclein is a central event in Parkinsons’s disease and related synucleinopathies. Since pharmacologically targeting this process, however, has not yet resulted in approved disease-modify...
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Article
Kinetic fingerprints differentiate the mechanisms of action of anti-Aβ antibodies
The amyloid cascade hypothesis, according to which the self-assembly of amyloid-β peptide (Aβ) is a causative process in Alzheimer’s disease, has driven many therapeutic efforts for the past 20 years. Failures...
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Article
Open AccessBenefits and constrains of covalency: the role of loop length in protein stability and ligand binding
Protein folding is governed by non-covalent interactions under the benefits and constraints of the covalent linkage of the backbone chain. In the current work we investigate the influence of loop length variat...
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Article
Direct measurement of lipid membrane disruption connects kinetics and toxicity of Aβ42 aggregation
The formation of amyloid deposits in human tissues is a defining feature of more than 50 medical disorders, including Alzheimer’s disease. Strong genetic and histological evidence links these conditions to the...
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Article
Author Correction: Dynamics of oligomer populations formed during the aggregation of Alzheimer’s Aβ42 peptide
An amendment to this paper has been published and can be accessed via a link at the top of the paper.
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Article
Dynamics of oligomer populations formed during the aggregation of Alzheimer’s Aβ42 peptide
Oligomeric species populated during the aggregation of the Aβ42 peptide have been identified as potent cytotoxins linked to Alzheimer’s disease, but the fundamental molecular pathways that control their dynami...
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Protocol
Single Step Purification of Glycogen Synthase Kinase Isoforms from Small Scale Transient Expression in HEK293 Cells with a Calcium-Dependent Fragment Complementation System
Purification of proteins for the biophysical analysis of protein interactions occurring in human cells can benefit from methods that facilitate the capture of small amounts of natively processed protein obtain...
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Protocol
Expression and Purification of Intrinsically Disordered Aβ Peptide and Setup of Reproducible Aggregation Kinetics Experiment
High purity and sequence homogeneity of intrinsically disordered proteins are prerequisites for reproducible studies of the kinetics and equilibrium of their self-assembly reactions. Starting from the pure sta...
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Article
Open AccessAutocatalytic amplification of Alzheimer-associated Aβ42 peptide aggregation in human cerebrospinal fluid
Alzheimer’s disease is linked to amyloid β (Aβ) peptide aggregation in the brain, and a detailed understanding of the molecular mechanism of Aβ aggregation may lead to improved diagnostics and therapeutics. Wh...
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Article
Open AccessGalectin-3, a novel endogenous TREM2 ligand, detrimentally regulates inflammatory response in Alzheimer’s disease
Alzheimer’s disease (AD) is a progressive neurodegenerative disease in which the formation of extracellular aggregates of amyloid beta (Aβ) peptide, fibrillary tangles of intraneuronal tau and microglial activ...
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Article
Open AccessA method of predicting the in vitro fibril formation propensity of Aβ40 mutants based on their inclusion body levels in E. coli
Overexpression of recombinant proteins in bacteria may lead to their aggregation and deposition in inclusion bodies. Since the conformational properties of proteins in inclusion bodies exhibit many of the char...
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Article
Open AccessTrodusquemine enhances Aβ42 aggregation but suppresses its toxicity by displacing oligomers from cell membranes
Transient oligomeric species formed during the aggregation process of the 42-residue form of the amyloid-β peptide (Aβ42) are key pathogenic agents in Alzheimer’s disease (AD). To investigate the relationship bet...
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Article
Open AccessProtein stabilization with retained function of monellin using a split GFP system
Sweet proteins are an unexploited resource in the search for non-carbohydrate sweeteners mainly due to their low stability towards heating. Variants of the sweet protein monellin, with increased stability, wer...
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Article
Cholesterol catalyses Aβ42 aggregation through a heterogeneous nucleation pathway in the presence of lipid membranes
Alzheimer’s disease is a neurodegenerative disorder associated with the aberrant aggregation of the amyloid-β peptide. Although increasing evidence implicates cholesterol in the pathogenesis of Alzheimer’s diseas...
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Article
Distinct thermodynamic signatures of oligomer generation in the aggregation of the amyloid-β peptide
Map** free-energy landscapes has proved to be a powerful tool for studying reaction mechanisms. Many complex biomolecular assembly processes, however, have remained challenging to access using this approach,...
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Protocol
Production and Use of Recombinant Aβ for Aggregation Studies
The amyloid β-protein (Aβ) is believed to play a central role in Alzheimer’s disease (AD) pathogenesis and there is great interest in understanding the process of Aβ aggregation, its underlying mechanism and t...
