Cargando…

Amyloids of α-Synuclein Promote Chemical Transformations of Neuronal Cell Metabolites

The assembly of α-synuclein into cross-β structured amyloid fibers results in Lewy body deposits and neuronal degeneration in Parkinson’s disease patients. As the cell environment is highly crowded, interactions between the formed amyloid fibers and a range of biomolecules can occur in cells. Althou...

Descripción completa

Detalles Bibliográficos
Autores principales:	Horvath, Istvan, Mohamed, Khadra A., Kumar, Ranjeet, Wittung-Stafshede, Pernilla
Formato:	Online Artículo Texto
Lenguaje:	English
Publicado:	MDPI 2023
Materias:	Communication
Acceso en línea:	https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10454467/ https://www.ncbi.nlm.nih.gov/pubmed/37629028 http://dx.doi.org/10.3390/ijms241612849

Ejemplares similares

Macromolecular crowding modulates α-synuclein amyloid fiber growth
por: Horvath, Istvan, et al.
Publicado: (2021)

Amyloid Fibers of α-Synuclein Catalyze Chemical Reactions
por: Horvath, Istvan, et al.
Publicado: (2023)

Abundant fish protein inhibits α-synuclein amyloid formation
por: Werner, Tony, et al.
Publicado: (2018)

Differential effects of Cu(2+) and Fe(3+) ions on in vitro amyloid formation of biologically-relevant α-synuclein variants
por: Lorentzon, Emma, et al.
Publicado: (2020)

Synaptic vesicle mimics affect the aggregation of wild-type and A53T α-synuclein variants differently albeit similar membrane affinity
por: Rocha, Sandra, et al.
Publicado: (2019)

Effects of the Toxic Metals Arsenite and Cadmium on α-Synuclein Aggregation In Vitro and in Cells
por: Lorentzon, Emma, et al.
Publicado: (2021)

Crosstalk Between Alpha-Synuclein and Other Human and Non-Human Amyloidogenic Proteins: Consequences for Amyloid Formation in Parkinson’s Disease
por: Werner, Tony, et al.
Publicado: (2020)

Chemical catalysis by biological amyloids
por: Wittung-Stafshede, Pernilla
Publicado: (2023)

Orientation of α-Synuclein at Negatively Charged Lipid Vesicles: Linear Dichroism Reveals Time-Dependent Changes in Helix Binding Mode
por: Rocha, Sandra, et al.
Publicado: (2021)

Direct Correlation Between Ligand-Induced α-Synuclein Oligomers and Amyloid-like Fibril Growth
por: Nors Perdersen, Martin, et al.
Publicado: (2015)

Mechanisms of Protein Oligomerization: Inhibitor of Functional Amyloids Templates α-Synuclein Fibrillation
por: Horvath, Istvan, et al.
Publicado: (2012)

Corrigendum: Direct Correlation Between Ligand-Induced α-Synuclein Oligomers and Amyloid-like Fibril Growth
por: Nors Pedersen, Martin, et al.
Publicado: (2015)

A gut bacterial amyloid promotes α-synuclein aggregation and motor impairment in mice
por: Sampson, Timothy R, et al.
Publicado: (2020)

Response to crowded conditions reveals compact nucleus for amyloid formation of folded protein
por: Werner, Tony E.R., et al.
Publicado: (2021)

Crossroads between copper ions and amyloid formation in Parkinson’s disease
por: Wittung-Stafshede, Pernilla
Publicado: (2022)

Redox-Dependent Copper Ion Modulation of Amyloid-β (1-42) Aggregation In Vitro
por: Sasanian, Nima, et al.
Publicado: (2020)

Bacterial Chaperones CsgE and CsgC Differentially Modulate Human α-Synuclein Amyloid Formation via Transient Contacts
por: Chorell, Erik, et al.
Publicado: (2015)

Insulin-degrading enzyme prevents α-synuclein fibril formation in a nonproteolytical manner
por: Sharma, Sandeep K., et al.
Publicado: (2015)

Single-vesicle imaging reveals lipid-selective and stepwise membrane disruption by monomeric α-synuclein
por: Hannestad, Jonas K., et al.
Publicado: (2020)

Memo1 binds reduced copper ions, interacts with copper chaperone Atox1, and protects against copper-mediated redox activity in vitro
por: Zhang, Xiaolu, et al.
Publicado: (2022)

Single injection of small-molecule amyloid accelerator results in cell death of nigral dopamine neurons in mice
por: Chermenina, Maria, et al.
Publicado: (2015)

Alpha‐Synuclein Modulates the Physical Properties of DNA
por: Jiang, Kai, et al.
Publicado: (2018)

Disease-causing point-mutations in metal-binding domains of Wilson disease protein decrease stability and increase structural dynamics
por: Kumar, Ranjeet, et al.
Publicado: (2016)

Identification of New Potential Interaction Partners for Human Cytoplasmic Copper Chaperone Atox1: Roles in Gene Regulation?
por: Öhrvik, Helena, et al.
Publicado: (2015)

Roles of Copper-Binding Proteins in Breast Cancer
por: Blockhuys, Stéphanie, et al.
Publicado: (2017)

ATP7A-Regulated Enzyme Metalation and Trafficking in the Menkes Disease Puzzle
por: Horn, Nina, et al.
Publicado: (2021)

Amyloid formation of fish β-parvalbumin involves primary nucleation triggered by disulfide-bridged protein dimers
por: Werner, Tony E. R., et al.
Publicado: (2020)

Effects of small-molecule amyloid modulators on a Drosophila model of Parkinson’s disease
por: Pokrzywa, Małgorzata, et al.
Publicado: (2017)

Folding, Stability and Shape of Proteins in Crowded Environments: Experimental and Computational Approaches
por: Samiotakis, Antonios, et al.
Publicado: (2009)

The C-Terminus of Human Copper Importer Ctr1 Acts as a Binding Site and Transfers Copper to Atox1
por: Kahra, Dana, et al.
Publicado: (2016)

The six metal binding domains in human copper transporter, ATP7B: molecular biophysics and disease-causing mutations
por: Ariöz, Candan, et al.
Publicado: (2017)

Synergistic Effects of Copper Sites on Apparent Stability of Multicopper Oxidase, Fet3p
por: Sedlák, Erik, et al.
Publicado: (2018)

Single-cell tracking demonstrates copper chaperone Atox1 to be required for breast cancer cell migration
por: Blockhuys, Stéphanie, et al.
Publicado: (2020)

A large ‘discovery’ experiment: Gender Initiative for Excellence (Genie) at Chalmers University of Technology
por: Saline, Maria, et al.
Publicado: (2021)

In Vitro Thermodynamic Dissection of Human Copper Transfer from Chaperone to Target Protein
por: Niemiec, Moritz S., et al.
Publicado: (2012)

Evaluation of copper chaperone ATOX1 as prognostic biomarker in breast cancer
por: Blockhuys, Stéphanie, et al.
Publicado: (2020)

Med8, Med18, and Med20 subunits of the Mediator head domain are interdependent upon each other for folding and complex formation
por: Adler, David, et al.
Publicado: (2009)

Enthalpy-entropy compensation at play in human copper ion transfer
por: Niemiec, Moritz S., et al.
Publicado: (2015)

Impact of crowded environments on binding between protein and single-stranded DNA
por: Köhn, Birgit, et al.
Publicado: (2021)

α-Synuclein-derived lipoparticles in the study of α-Synuclein amyloid fibril formation
por: Falke, Marcel, et al.
Publicado: (2019)

Cannot write session to /tmp/vufind_sessions/sess_264cpot22uu5clqdfqt8im2f31