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107 Result(s)
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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
Generic nature of the condensed states of proteins
Proteins undergoing liquid–liquid phase separation are being discovered at an increasing rate. Since at the high concentrations present in the cell most proteins would be expected to form a liquid condensed st...
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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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Open AccessThe docking of synaptic vesicles on the presynaptic membrane induced by α-synuclein is modulated by lipid composition
α-Synuclein (αS) is a presynaptic disordered protein whose aberrant aggregation is associated with Parkinson’s disease. The functional role of αS is still debated, although it has been involved in the regulati...
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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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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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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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A kinetic ensemble of the Alzheimer’s Aβ peptide
The conformational and thermodynamic properties of disordered proteins are commonly described in terms of structural ensembles and free energy landscapes. To provide information on the transition rates between...
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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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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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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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Open AccessA rationally designed bicyclic peptide remodels Aβ42 aggregation in vitro and reduces its toxicity in a worm model of Alzheimer’s disease
Bicyclic peptides have great therapeutic potential since they can bridge the gap between small molecules and antibodies by combining a low molecular weight of about 2 kDa with an antibody-like binding specific...
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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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Open AccessSingle molecule secondary structure determination of proteins through infrared absorption nanospectroscopy
The chemical and structural properties of biomolecules determine their interactions, and thus their functions, in a wide variety of biochemical processes. Innovative imaging methods have been developed to char...
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Assessing motor-related phenotypes of Caenorhabditis elegans with the wide field-of-view nematode tracking platform
Caenorhabditis elegans is a valuable model organism in biomedical research that has led to major discoveries in the fields of neurodegeneration, cancer and aging. Because movement phenotypes are commonly used and...
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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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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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Open AccessA single ultrasensitive assay for detection and discrimination of tau aggregates of Alzheimer and Pick diseases
Multiple neurodegenerative diseases are characterized by aggregation of tau molecules. Adult humans express six isoforms of tau that contain either 3 or 4 microtubule binding repeats (3R or 4R tau). Different ...
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Chris Dobson (1949–2019)
Chris Dobson passed away on September 8th, leaving a wide-reaching legacy. He is best known for revealing the generality of the phenomenon of protein misfolding and aggregation and has provided inspiration for...
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Open AccessThe N-terminal Acetylation of α-Synuclein Changes the Affinity for Lipid Membranes but not the Structural Properties of the Bound State
The aggregation of α-synuclein (αS), a protein abundant at presynaptic terminals, is associated with a range of highly debilitating neurodegenerative conditions, including Parkinson’s disease (PD), dementia wi...