Cargando…

Redox-Dependent Copper Ion Modulation of Amyloid-β (1-42) Aggregation In Vitro

Plaque deposits composed of amyloid-β (Aβ) fibrils are pathological hallmarks of Alzheimer’s disease (AD). Although copper ion dyshomeostasis is apparent in AD brains and copper ions are found co-deposited with Aβ peptides in patients’ plaques, the molecular effects of copper ion interactions and re...

Descripción completa

Detalles Bibliográficos
Autores principales:	Sasanian, Nima, Bernson, David, Horvath, Istvan, Wittung-Stafshede, Pernilla, Esbjörner, Elin K.
Formato:	Online Artículo Texto
Lenguaje:	English
Publicado:	MDPI 2020
Materias:	Article
Acceso en línea:	https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7355640/ https://www.ncbi.nlm.nih.gov/pubmed/32570820 http://dx.doi.org/10.3390/biom10060924

Ejemplares similares

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

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

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)

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

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)

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

Copper Chaperone Atox1 Interacts with Cell Cycle Proteins
por: Matson Dzebo, Maria, et al.
Publicado: (2018)

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)

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

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

Amyloids of α-Synuclein Promote Chemical Transformations of Neuronal Cell Metabolites
por: Horvath, Istvan, et al.
Publicado: (2023)

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

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)

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

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

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

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)

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

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

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

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

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

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

Direct Observations of Amyloid β Self-Assembly in Live Cells Provide Insights into Differences in the Kinetics of Aβ(1–40) and Aβ(1–42) Aggregation
por: Esbjörner, Elin K., et al.
Publicado: (2014)

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

A Luminal Loop of Wilson Disease Protein Binds Copper and Is Required for Protein Activity
por: Köhn, Birgit, et al.
Publicado: (2018)

The Caenorhabditis elegans homolog of human copper chaperone Atox1, CUC-1, aids in distal tip cell migration
por: Zhang, Xiaolu, et al.
Publicado: (2020)

Endocytic uptake of monomeric amyloid-β peptides is clathrin- and dynamin-independent and results in selective accumulation of Aβ(1–42) compared to Aβ(1–40)
por: Wesén, Emelie, et al.
Publicado: (2017)

ATP7A-Regulated Enzyme Metalation and Trafficking in the Menkes Disease Puzzle
por: Horn, Nina, 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)

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

Influence of denaturants on amyloid β42 aggregation kinetics
por: Weiffert, Tanja, et al.
Publicado: (2022)

Determinants for Simultaneous Binding of Copper and Platinum to Human Chaperone Atox1: Hitchhiking not Hijacking
por: Palm-Espling, Maria E., et al.
Publicado: (2013)

Effect of Ovocystatin on Amyloid β 1-42 Aggregation—In Vitro Studies
por: Stańczykiewicz, Bartłomiej, et al.
Publicado: (2023)

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

Amyloid formation of bovine insulin is retarded in moderately acidic pH and by addition of short-chain alcohols
por: Bernson, David, et al.
Publicado: (2020)

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

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

Solvent exposure of Tyr10 as a probe of structural differences between monomeric and aggregated forms of the amyloid-β peptide
por: Aran Terol, Pablo, et al.
Publicado: (2015)

Reciprocal modulation of Aβ42 aggregation by copper and homocysteine
por: Keskitalo, Salla, et al.
Publicado: (2014)

Cannot write session to /tmp/vufind_sessions/sess_4pbe9gkkrmgr8730hnv41mv0nd