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Article
Open AccessPublisher Correction: Two human metabolites rescue a C. elegans model of Alzheimer’s disease via a cytosolic unfolded protein response
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Article
Open AccessTwo human metabolites rescue a C. elegans model of Alzheimer’s disease via a cytosolic unfolded protein response
Age-related changes in cellular metabolism can affect brain homeostasis, creating conditions that are permissive to the onset and progression of neurodegenerative disorders such as Alzheimer’s and Parkinson’s ...
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Article
Quantifying misfolded protein oligomers as drug targets and biomarkers in Alzheimer and Parkinson diseases
Protein misfolding and aggregation are characteristic of a wide range of neurodegenerative disorders, including Alzheimer and Parkinson diseases. A hallmark of these diseases is the aggregation of otherwise so...
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Article
Structural and dynamics analysis of intrinsically disordered proteins by high-speed atomic force microscopy
Intrinsically disordered proteins (IDPs) are ubiquitous proteins that are disordered entirely or partly and play important roles in diverse biological phenomena. Their structure dynamically samples a multitude...
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Article
Open AccessInfrared nanospectroscopy reveals the molecular interaction fingerprint of an aggregation inhibitor with single Aβ42 oligomers
Significant efforts have been devoted in the last twenty years to develo** compounds that can interfere with the aggregation pathways of proteins related to misfolding disorders, including Alzheimer’s and Pa...
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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
Open AccessTrodusquemine displaces protein misfolded oligomers from cell membranes and abrogates their cytotoxicity through a generic mechanism
The onset and progression of numerous protein misfolding diseases are associated with the presence of oligomers formed during the aberrant aggregation of several different proteins, including amyloid-β (Aβ) in...
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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 AccessMicrofluidic deposition for resolving single-molecule protein architecture and heterogeneity
Scanning probe microscopy provides a unique window into the morphology, mechanics, and structure of proteins and their complexes on the nanoscale. Such measurements require, however, deposition of samples onto...
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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
Open AccessThe inverted free energy landscape of an intrinsically disordered peptide by simulations and experiments
The free energy landscape theory has been very successful in rationalizing the folding behaviour of globular proteins, as this representation provides intuitive information on the number of states involved in ...
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Article
Molecular Basis for Structural Heterogeneity of an Intrinsically Disordered Protein Bound to a Partner by Combined ESI-IM-MS and Modeling
Intrinsically disordered proteins (IDPs) form biologically active complexes that can retain a high degree of conformational disorder, esca** structural characterization by conventional approaches. An example...
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Chapter
Order and Disorder in the Replicative Complex of Paramyxoviruses
In this review we summarize available data showing the abundance of structural disorder within the nucleoprotein (N) and phosphoprotein (P) from three paramyxoviruses, namely the measles (MeV), Nipah (NiV) and...
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Protocol
Monitoring Structural Transitions in IDPs by Vibrational Spectroscopy of Cyanylated Cysteine
The fast intrinsic time scale of infrared absorption and the sensitivity of molecular vibrational frequencies to their environments can be applied with site-specificity by introducing the artificial amino acid...
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Protocol
Monitoring Structural Transitions in IDPs by Site-Directed Spin Labeling EPR Spectroscopy
Electron paramagnetic resonance (EPR) spectroscopy is a technique that specifically detects unpaired electrons. EPR sensitive reporter groups (spin labels or spin probes) can be introduced into biological syst...
