Cargando…

Two 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 diseases. Although the roles of metabolites have been extensively studied with regard to ce...

Descripción completa

Detalles Bibliográficos
Autores principales:	Joshi, Priyanka, Perni, Michele, Limbocker, Ryan, Mannini, Benedetta, Casford, Sam, Chia, Sean, Habchi, Johnny, Labbadia, Johnathan, Dobson, Christopher M., 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/PMC8263720/ https://www.ncbi.nlm.nih.gov/pubmed/34234268 http://dx.doi.org/10.1038/s42003-021-02218-7

Ejemplares similares

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)

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

Combinations of Vitamin A and Vitamin E Metabolites Confer Resilience against Amyloid-β Aggregation
por: Joshi, Priyanka, et al.
Publicado: (2023)

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)

Exogenous misfolded protein oligomers can cross the intestinal barrier and cause a disease phenotype in C. elegans
por: Perni, Michele, et al.
Publicado: (2021)

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

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

Expression of the amyloid-β peptide in a single pair of C. elegans sensory neurons modulates the associated behavioural response
por: Sinnige, Tessa, et al.
Publicado: (2019)

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)

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

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

Bacterial production and direct functional screening of expanded molecular libraries for discovering inhibitors of protein aggregation
por: Delivoria, Dafni C., et al.
Publicado: (2019)

Cytosolic aggregation of mitochondrial proteins disrupts cellular homeostasis by stimulating the aggregation of other proteins
por: Nowicka, Urszula, et al.
Publicado: (2021)

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

An anticancer drug suppresses the primary nucleation reaction that initiates the production of the toxic Aβ42 aggregates linked with Alzheimer’s disease
por: Habchi, Johnny, et al.
Publicado: (2016)

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

Structure-Based Discovery of Small-Molecule Inhibitors of the Autocatalytic Proliferation of α-Synuclein Aggregates
por: Chia, Sean, et al.
Publicado: (2022)

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)

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

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

Surface-Catalyzed Secondary Nucleation Dominates the Generation of Toxic IAPP Aggregates
por: Rodriguez Camargo, Diana C., et al.
Publicado: (2021)

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

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

Microfluidic deposition for resolving single-molecule protein architecture and heterogeneity
por: Ruggeri, Francesco Simone, et al.
Publicado: (2018)

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

Infrared nanospectroscopy reveals the molecular interaction fingerprint of an aggregation inhibitor with single Aβ42 oligomers
por: Ruggeri, Francesco Simone, et al.
Publicado: (2021)

The inverted free energy landscape of an intrinsically disordered peptide by simulations and experiments
por: Granata, Daniele, et al.
Publicado: (2015)

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)

Screening of small molecules using the inhibition of oligomer formation in α-synuclein aggregation as a selection parameter
por: Staats, Roxine, et al.
Publicado: (2020)

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)

ADP ribosylation adapts an ER chaperone response to short-term fluctuations in unfolded protein load
por: Chambers, Joseph E., et al.
Publicado: (2012)

ADP ribosylation adapts an ER chaperone response to short-term fluctuations in unfolded protein load
por: Chambers, Joseph E., et al.
Publicado: (2014)

Folding Mitochondrial-Mediated Cytosolic Proteostasis Into the Mitochondrial Unfolded Protein Response
por: Jenkins, Edmund Charles, et al.
Publicado: (2021)

Crosstalk between endoplasmic reticulum and cytosolic unfolded protein response in tomato
por: Löchli, Karin, et al.
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)

Comparative Studies in the A30P and A53T α-Synuclein C. elegans Strains to Investigate the Molecular Origins of Parkinson's Disease
por: Perni, Michele, et al.
Publicado: (2021)

Cell adaptation to aneuploidy by the environmental stress response dampens induction of the cytosolic unfolded-protein response
por: Kane, Andrew J., et al.
Publicado: (2021)

Human PERK rescues unfolded protein response-deficient yeast cells
por: Yap, Wei Sheng, et al.
Publicado: (2022)

Cannot write session to /tmp/vufind_sessions/sess_t7q34kbo5rocjuvfse2mlkucae