Cargando…

In situ kinetic measurements of α-synuclein aggregation reveal large population of short-lived oligomers

Knowledge of the mechanisms of assembly of amyloid proteins into aggregates is of central importance in building an understanding of neurodegenerative disease. Given that oligomeric intermediates formed during the aggregation reaction are believed to be the major toxic species, methods to track such...

Descripción completa

Detalles Bibliográficos
Autores principales:	Zurlo, Enrico, Kumar, Pravin, Meisl, Georg, Dear, Alexander J., Mondal, Dipro, Claessens, Mireille M. A. E., Knowles, Tuomas P. J., Huber, Martina
Formato:	Online Artículo Texto
Lenguaje:	English
Publicado:	Public Library of Science 2021
Materias:	Research Article
Acceso en línea:	https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7822277/ https://www.ncbi.nlm.nih.gov/pubmed/33481908 http://dx.doi.org/10.1371/journal.pone.0245548

Ejemplares similares

Oligomer Diversity during the Aggregation of the Repeat Region of Tau
por: Kjaergaard, Magnus, et al.
Publicado: (2018)

Direct observation of prion protein oligomer formation reveals an aggregation mechanism with multiple conformationally distinct species
por: Sang, Jason C., et al.
Publicado: (2019)

Identification of on- and off-pathway oligomers in amyloid fibril formation
por: Dear, Alexander J., et al.
Publicado: (2020)

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

Quantifying Co-Oligomer Formation by α-Synuclein
por: Iljina, Marija, et al.
Publicado: (2018)

The catalytic nature of protein aggregation
por: Dear, Alexander J., et al.
Publicado: (2020)

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)

β-Synuclein suppresses both the initiation and amplification steps of α-synuclein aggregation via competitive binding to surfaces
por: Brown, James W. P., et al.
Publicado: (2016)

Kinetic analysis reveals that independent nucleation events determine the progression of polyglutamine aggregation in C. elegans
por: Sinnige, Tessa, et al.
Publicado: (2021)

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

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)

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)

Mechanistic Models of Protein Aggregation Across Length-Scales and Time-Scales: From the Test Tube to Neurodegenerative Disease
por: Meisl, Georg, et al.
Publicado: (2022)

The C-terminal tail of α-synuclein protects against aggregate replication but is critical for oligomerization
por: Farzadfard, Azad, et al.
Publicado: (2022)

Cross-seeding of alpha-synuclein aggregation by amyloid fibrils of food proteins
por: Vaneyck, Jonathan, et al.
Publicado: (2021)

Quantitative analysis of intrinsic and extrinsic factors in the aggregation mechanism of Alzheimer-associated Aβ-peptide
por: Meisl, Georg, et al.
Publicado: (2016)

Characterization of full-length p53 aggregates and their kinetics of formation
por: Julian, Linda, et al.
Publicado: (2022)

Early stages of aggregation of engineered α-synuclein monomers and oligomers in solution
por: Li, Xi, et al.
Publicado: (2019)

On the role of sidechain size and charge in the aggregation of Aβ42 with familial mutations
por: Yang, Xiaoting, et al.
Publicado: (2018)

Non-uniform self-assembly: On the anisotropic architecture of α-synuclein supra-fibrillar aggregates
por: Semerdzhiev, Slav A., et al.
Publicado: (2017)

Modulation of electrostatic interactions to reveal a reaction network unifying the aggregation behaviour of the Aβ42 peptide and its variants
por: Meisl, Georg, et al.
Publicado: (2017)

Extrinsic Amyloid-Binding Dyes for Detection of Individual Protein Aggregates in Solution
por: Taylor, Christopher G., et al.
Publicado: (2018)

Effects of sedimentation, microgravity, hydrodynamic mixing and air–water interface on α-synuclein amyloid formation
por: Zhou, Jiangtao, et al.
Publicado: (2020)

Zinc Binding to Tau Influences Aggregation Kinetics and Oligomer Distribution
por: Moreira, Guilherme G., et al.
Publicado: (2019)

Super-resolution imaging reveals α-synuclein seeded aggregation in SH-SY5Y cells
por: Sang, Jason C., et al.
Publicado: (2021)

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

Origin of metastable oligomers and their effects on amyloid fibril self-assembly
por: Hasecke, Filip, et al.
Publicado: (2018)

A mechanistic model of tau amyloid aggregation based on direct observation of oligomers
por: Shammas, Sarah L., et al.
Publicado: (2015)

Quantitative detection of α-Synuclein and Tau oligomers and other aggregates by digital single particle counting
por: Blömeke, Lara, et al.
Publicado: (2022)

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

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

Lighting Up Alpha-synuclein Oligomers
por: Richter, Franziska
Publicado: (2018)

Secondary Processes Dominate the Quiescent, Spontaneous Aggregation of α-Synuclein at Physiological pH with Sodium Salts
por: Horne, Robert I., et al.
Publicado: (2023)

Direct detection of alpha synuclein oligomers in vivo
por: Dimant, Hemi, et al.
Publicado: (2013)

Alpha-synuclein oligomers: a new hope
por: Bengoa-Vergniory, Nora, et al.
Publicado: (2017)

The Role of α-Synuclein Oligomers in Parkinson’s Disease
por: Du, Xiao-yu, et al.
Publicado: (2020)

Stabilization of α-synuclein oligomers using formaldehyde
por: Ruesink, Harm, et al.
Publicado: (2019)

Quantitative analysis of co-oligomer formation by amyloid-beta peptide isoforms
por: Iljina, Marija, et al.
Publicado: (2016)

The Binding of Apolipoprotein E to Oligomers and Fibrils of Amyloid-β Alters the Kinetics of Amyloid Aggregation
por: Garai, Kanchan, et al.
Publicado: (2014)

Spontaneous nucleation and fast aggregate-dependent proliferation of α-synuclein aggregates within liquid condensates at neutral pH
por: Dada, Samuel T., et al.
Publicado: (2023)

Cannot write session to /tmp/vufind_sessions/sess_cc2ihlhh7t4qp4i5865c4kn84s