Results 1 to 10 of about 95,864 (160)

A dopamine metabolite stabilizes neurotoxic amyloid-β oligomers

Communications Biology, 2021
Cataldi et al. investigates the impact of the dopamine derivative DOPAL on the Aβ peptide oligomer formation. They report that DOPAL promotes the formation of stable Aβ oligomers that exert toxicity on neuroblastoma cells by increasing cytosolic calcium ...
Rodrigo Cataldi, Sean Chia, Katarina Pisani, Francesco S. Ruggeri, Catherine K. Xu, Tomas Šneideris, Michele Perni, Sunehera Sarwat, Priyanka Joshi, Janet R. Kumita, Sara Linse, Johnny Habchi, Tuomas P. J. Knowles, Benedetta Mannini, Christopher M. Dobson, Michele Vendruscolo   +15 more
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Publisher Correction: A dopamine metabolite stabilizes neurotoxic amyloid-β oligomers

Communications Biology, 2021
A Correction to this paper has been published: https://doi.org/10.1038/s42003-021-01680 ...
Rodrigo Cataldi, Sean Chia, Katarina Pisani, Francesco S. Ruggeri, Catherine K. Xu, Tomas Šneideris, Michele Perni, Sunehera Sarwat, Priyanka Joshi, Janet R. Kumita, Sara Linse, Johnny Habchi, Tuomas P. J. Knowles, Benedetta Mannini, Christopher M. Dobson, Michele Vendruscolo   +15 more
doaj   +1 more source

Infrared nanospectroscopy reveals the molecular interaction fingerprint of an aggregation inhibitor with single Aβ42 oligomers

Nature Communications, 2021
Our understanding of the molecular mechanisms underlying pathological protein aggregation remains incomplete. Here, single molecule infrared nanospectroscopy (AFM-IR) offers insight into the structure of Aβ42 oligomeric and fibrillar species and their ...
Francesco Simone Ruggeri, Johnny Habchi, Sean Chia, Robert I. Horne, Michele Vendruscolo, Tuomas P. J. Knowles   +5 more
doaj   +1 more source

Two human metabolites rescue a C. elegans model of Alzheimer’s disease via a cytosolic unfolded protein response

Communications Biology, 2021
Joshi et al. identify two human metabolites, carnosine and kynurenic acid, that rescue a C. elegans model of Alzheimer’s disease by inhibiting the aggregation of the amyloid beta peptide in vivo.
Priyanka Joshi, Michele Perni, Ryan Limbocker, Benedetta Mannini, Sam Casford, Sean Chia, Johnny Habchi, Johnathan Labbadia, Christopher M. Dobson, Michele Vendruscolo   +9 more
doaj   +1 more source

The Hsc70 disaggregation machinery removes monomer units directly from α-synuclein fibril ends

Nature Communications, 2021
Molecular chaperones from the Hsp70 family can break up protein aggregates, including amyloids. Here, the authors utilize microfluidic diffusional sizing to assess the mechanism of α-synuclein (αS) disaggregation by the Hsc70–DnaJB1–Apg2 system, and show
Matthias M. Schneider, Saurabh Gautam, Therese W. Herling, Ewa Andrzejewska, Georg Krainer, Alyssa M. Miller, Victoria A. Trinkaus, Quentin A. E. Peter, Francesco Simone Ruggeri, Michele Vendruscolo, Andreas Bracher, Christopher M. Dobson, F. Ulrich Hartl, Tuomas P. J. Knowles   +13 more
doaj   +1 more source

Screening of small molecules using the inhibition of oligomer formation in α-synuclein aggregation as a selection parameter

Communications Chemistry, 2020
Promising treatments for neurogenerative disorders may involve targeting kinetic intermediates, including α-synuclein oligomers. Here a kinetic method for quantifying oligomer populations is used to screen small molecule inhibitors of oligomerisation and
Roxine Staats, Thomas C. T. Michaels, Patrick Flagmeier, Sean Chia, Robert I. Horne, Johnny Habchi, Sara Linse, Tuomas P. J. Knowles, Christopher M. Dobson, Michele Vendruscolo   +9 more
doaj   +1 more source

Rationally Designed Bicyclic Peptides Prevent the Conversion of Aβ42 Assemblies Into Fibrillar Structures

Frontiers in Neuroscience, 2021
There is great interest in drug discovery programs targeted at the aggregation of the 42-residue form of the amyloid β peptide (Aβ42), since this molecular process is closely associated with Alzheimer’s disease.
Tatsuya Ikenoue, Francesco A. Aprile, Francesco A. Aprile, Pietro Sormanni, Michele Vendruscolo   +4 more
doaj   +1 more source

Exogenous misfolded protein oligomers can cross the intestinal barrier and cause a disease phenotype in C. elegans

Scientific Reports, 2021
Misfolded protein oligomers are increasingly recognized as highly cytotoxic agents in a wide range of human disorders associated with protein aggregation.
Michele Perni, Benedetta Mannini, Catherine K. Xu, Janet R. Kumita, Christopher M. Dobson, Fabrizio Chiti, Michele Vendruscolo   +6 more
doaj   +1 more source

Heterologous prion-forming proteins interact to cross-seed aggregation in Saccharomyces cerevisiae [PDF]

, 2017
The early stages of protein misfolding remain incompletely understood, as most mammalian proteinopathies are only detected after irreversible protein aggregates have formed.
Keefer, Kathryn M, Stein, Kevin C, true, Heather L   +2 more
core   +2 more sources

An open-source automated PEG precipitation assay to measure the relative solubility of proteins with low material requirement

Scientific Reports, 2021
The solubility of proteins correlates with a variety of their properties, including function, production yield, pharmacokinetics, and formulation at high concentrations.
Marc Oeller, Pietro Sormanni, Michele Vendruscolo   +2 more
doaj   +1 more source