Cargando…

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

Misfolded protein oligomers are increasingly recognized as highly cytotoxic agents in a wide range of human disorders associated with protein aggregation. In this study, we assessed the possible uptake and resulting toxic effects of model protein oligomers administered to C. elegans through the cult...

Descripción completa

Detalles Bibliográficos
Autores principales:	Perni, Michele, Mannini, Benedetta, Xu, Catherine K., Kumita, Janet R., Dobson, Christopher M., Chiti, Fabrizio, Vendruscolo, Michele
Formato:	Online Artículo Texto
Lenguaje:	English
Publicado:	Nature Publishing Group UK 2021
Materias:	Article
Acceso en línea:	https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8277765/ https://www.ncbi.nlm.nih.gov/pubmed/34257326 http://dx.doi.org/10.1038/s41598-021-93527-8

Ejemplares similares

Distinct responses of human peripheral blood cells to different misfolded protein oligomers
por: Leal‐Lasarte, Magdalena, et al.
Publicado: (2021)

Chaperones as Suppressors of Protein Misfolded Oligomer Toxicity
por: Mannini, Benedetta, et al.
Publicado: (2017)

Trodusquemine displaces protein misfolded oligomers from cell membranes and abrogates their cytotoxicity through a generic mechanism
por: Limbocker, Ryan, et al.
Publicado: (2020)

Characterization of Pairs of Toxic and Nontoxic Misfolded Protein Oligomers Elucidates the Structural Determinants of Oligomer Toxicity in Protein Misfolding Diseases
por: Limbocker, Ryan, et al.
Publicado: (2023)

Therapeutic Strategies to Reduce the Toxicity of Misfolded Protein Oligomers
por: Kreiser, Ryan P., et al.
Publicado: (2020)

Aβ Oligomers Dysregulate Calcium Homeostasis by Mechanosensitive Activation of AMPA and NMDA Receptors
por: Fani, Giulia, et al.
Publicado: (2021)

Misfolded protein oligomers induce an increase of intracellular Ca(2+) causing an escalation of reactive oxidative species
por: Fani, Giulia, et al.
Publicado: (2022)

Delivery of Native Proteins into C. elegans Using a Transduction Protocol Based on Lipid Vesicles
por: Perni, Michele, et al.
Publicado: (2017)

A dopamine metabolite stabilizes neurotoxic amyloid-β oligomers
por: Cataldi, Rodrigo, et al.
Publicado: (2021)

Publisher Correction: A dopamine metabolite stabilizes neurotoxic amyloid-β oligomers
por: Cataldi, Rodrigo, et al.
Publicado: (2021)

Rationally Designed Antibodies as Research Tools to Study the Structure–Toxicity Relationship of Amyloid-β Oligomers
por: Limbocker, Ryan, et al.
Publicado: (2020)

Two human metabolites rescue a C. elegans model of Alzheimer’s disease via a cytosolic unfolded protein response
por: Joshi, Priyanka, et al.
Publicado: (2021)

Publisher Correction: Two human metabolites rescue a C. elegans model of Alzheimer’s disease via a cytosolic unfolded protein response
por: Joshi, Priyanka, et al.
Publicado: (2021)

Quantitative Measurement of the Affinity of Toxic and Nontoxic Misfolded Protein Oligomers for Lipid Bilayers and of its Modulation by Lipid Composition and Trodusquemine
por: Errico, Silvia, et al.
Publicado: (2021)

Trodusquemine enhances Aβ(42) aggregation but suppresses its toxicity by displacing oligomers from cell membranes
por: Limbocker, Ryan, et al.
Publicado: (2019)

Squalamine and Its Derivatives Modulate the Aggregation of Amyloid-β and α-Synuclein and Suppress the Toxicity of Their Oligomers
por: Limbocker, Ryan, et al.
Publicado: (2021)

Binding affinity of amyloid oligomers to cellular membranes is a generic indicator of cellular dysfunction in protein misfolding diseases
por: Evangelisti, Elisa, et al.
Publicado: (2016)

Rational design of a conformation-specific antibody for the quantification of Aβ oligomers
por: Aprile, Francesco A., et al.
Publicado: (2020)

Multiplexed Digital Characterization of Misfolded Protein Oligomers via Solid-State Nanopores
por: Sandler, Sarah E., et al.
Publicado: (2023)

Lipid Homeostasis and Its Links With Protein Misfolding Diseases
por: Vendruscolo, Michele
Publicado: (2022)

Probing the Origin of the Toxicity of Oligomeric Aggregates of α-Synuclein with Antibodies
por: Cascella, Roberta, et al.
Publicado: (2019)

Transthyretin Inhibits Primary and Secondary Nucleations of Amyloid-β Peptide Aggregation and Reduces the Toxicity of Its Oligomers
por: Ghadami, Seyyed Abolghasem, et al.
Publicado: (2020)

Membrane Interactions and Toxicity by Misfolded Protein Oligomers
por: Gonzalez-Garcia, Mario, et al.
Publicado: (2021)

A comparison of the biochemical modifications caused by toxic and non-toxic protein oligomers in cells
por: Zampagni, Mariagioia, et al.
Publicado: (2011)

The Pathological G51D Mutation in Alpha-Synuclein Oligomers Confers Distinct Structural Attributes and Cellular Toxicity
por: Xu, Catherine K., et al.
Publicado: (2022)

SAR by kinetics for drug discovery in protein misfolding diseases
por: Chia, Sean, et al.
Publicado: (2018)

The elusive nature and diagnostics of misfolded Aβ oligomers
por: Cerasoli, Eleonora, et al.
Publicado: (2015)

A rationally designed bicyclic peptide remodels Aβ42 aggregation in vitro and reduces its toxicity in a worm model of Alzheimer’s disease
por: Ikenoue, Tatsuya, et al.
Publicado: (2020)

Structural Characterization of Covalently Stabilized Human Cystatin C Oligomers
por: Chrabąszczewska, Magdalena, et al.
Publicado: (2020)

Proteome-wide observation of the phenomenon of life on the edge of solubility
por: Vecchi, Giulia, et al.
Publicado: (2020)

The Role of Protein Misfolding and Tau Oligomers (TauOs) in Alzheimer’s Disease (AD)
por: Mroczko, Barbara, et al.
Publicado: (2019)

Single molecule secondary structure determination of proteins through infrared absorption nanospectroscopy
por: Ruggeri, Francesco Simone, et al.
Publicado: (2020)

Protein Misfolding and Human Disease
por: Dobson, Christopher
Publicado: (2002)

Small-molecule sequestration of amyloid-β as a drug discovery strategy for Alzheimer’s disease
por: Heller, Gabriella T., et al.
Publicado: (2020)

Amyloid-like Fibrils from an α-Helical Transmembrane Protein
por: Stroobants, Karen, et al.
Publicado: (2017)

Distinct thermodynamic signature of oligomer generation in the aggregation of the amyloid-β peptide
por: Cohen, Samuel I. A., et al.
Publicado: (2018)

Frequent and symmetric deposition of misfolded tau oligomers within presynaptic and postsynaptic terminals in Alzheimer’s disease
por: Tai, Hwan-Ching, et al.
Publicado: (2014)

Mechanosensitivity of N-methyl-D-aspartate receptors (NMDAR) is the key through which amyloid beta oligomers activate them
por: Fani, Giulia, et al.
Publicado: (2021)

Selective targeting of primary and secondary nucleation pathways in Aβ42 aggregation using a rational antibody scanning method
por: Aprile, Francesco A., et al.
Publicado: (2017)

Homage to Chris Dobson
por: Baum, Jean, et al.
Publicado: (2019)

Cannot write session to /tmp/vufind_sessions/sess_7b4gapjbsuj54cuon9ticm3cbs