Cargando…

Amyloidogenic cross-seeding of Tau protein: Transient emergence of structural variants of fibrils

Amyloid aggregates of Tau protein have been implicated in etiology of many neurodegenerative disorders including Alzheimer's disease (AD). When amyloid growth is induced by seeding with preformed fibrils assembled from the same protein, structural characteristics of the seed are usually imprint...

Descripción completa

Detalles Bibliográficos
Autores principales:	Nizynski, Bartosz, Nieznanska, Hanna, Dec, Robert, Boyko, Solomiia, Dzwolak, Wojciech, Nieznanski, Krzysztof
Formato:	Online Artículo Texto
Lenguaje:	English
Publicado:	Public Library of Science 2018
Materias:	Research Article
Acceso en línea:	https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6053212/ https://www.ncbi.nlm.nih.gov/pubmed/30024984 http://dx.doi.org/10.1371/journal.pone.0201182

Ejemplares similares

Multiscale Modeling of Amyloid Fibrils Formed by Aggregating Peptides Derived from the Amyloidogenic Fragment of the A-Chain of Insulin
por: Koliński, Michał, et al.
Publicado: (2021)

Revisiting the conformational state of albumin conjugated to gold nanoclusters: A self-assembly pathway to giant superstructures unraveled
por: Kluz, Michał, et al.
Publicado: (2019)

Extremely Amyloidogenic Single-Chain Analogues of Insulin’s H-Fragment: Structural Adaptability of an Amyloid Stretch
por: Dec, Robert, et al.
Publicado: (2020)

The emergence of superstructural order in insulin amyloid fibrils upon multiple rounds of self-seeding
por: Surmacz-Chwedoruk, Weronika, et al.
Publicado: (2016)

Covalent Defects Restrict Supramolecular Self-Assembly of Homopolypeptides: Case Study of β(2)-Fibrils of Poly-L-Glutamic Acid
por: Fulara, Aleksandra, et al.
Publicado: (2014)

On the Heat Stability of Amyloid-Based Biological Activity: Insights from Thermal Degradation of Insulin Fibrils
por: Surmacz-Chwedoruk, Weronika, et al.
Publicado: (2014)

Self-Assembly of Insulin-Derived Chimeric Peptides into Two-Component Amyloid Fibrils: The Role of Coulombic Interactions
por: Fortunka, Mateusz, et al.
Publicado: (2023)

Mellitate: A multivalent anion with extreme charge density causes rapid aggregation and misfolding of wild type lysozyme at neutral pH
por: Ścibisz, Grzegorz, et al.
Publicado: (2017)

Prelysosomal Compartments in the Unconventional Secretion of Amyloidogenic Seeds
por: Borland, Helena, et al.
Publicado: (2017)

Domain-specific modulatory effects of phosphomimetic substitutions on liquid-liquid phase separation of tau protein
por: Boyko, Solomiia, et al.
Publicado: (2023)

Virtual Quasi-2D Intermediates as Building Blocks for Plausible Structural Models of Amyloid Fibrils from Proteins with Complex Topologies: A Case Study of Insulin
por: Puławski, Wojciech, et al.
Publicado: (2022)

Amyloidogenicity assessment of transthyretin gene variants
por: Grether, Nicolai B., et al.
Publicado: (2022)

Amplification of Tau Fibrils from Minute Quantities of Seeds
por: Meyer, Virginia, et al.
Publicado: (2014)

Camouflaged Fluorescent Silica Nanoparticles Target Aggregates and Condensates of the Amyloidogenic Protein Tau
por: Barracchia, Carlo Giorgio, et al.
Publicado: (2022)

Heterotypic seeding of Tau fibrillization by pre-aggregated Abeta provides potent seeds for prion-like seeding and propagation of Tau-pathology in vivo
por: Vasconcelos, Bruno, et al.
Publicado: (2016)

Oligomerization Profile of Human Transthyretin Variants with Distinct Amyloidogenicity
por: Frangolho, Ana, et al.
Publicado: (2020)

Competition between crystal and fibril formation in molecular mutations of amyloidogenic peptides
por: Reynolds, Nicholas P., et al.
Publicado: (2017)

Liquid–liquid phase separation of tau protein: The crucial role of electrostatic interactions
por: Boyko, Solomiia, et al.
Publicado: (2019)

Hyperphosphorylation of Intrinsically Disordered Tau Protein Induces an Amyloidogenic Shift in Its Conformational Ensemble
por: Zhu, Shaolong, et al.
Publicado: (2015)

Amyloidogenic and non-amyloidogenic transthyretin variants interact differently with human cardiomyocytes: insights into early events of non-fibrillar tissue damage
por: Manral, Pallavi, et al.
Publicado: (2015)

Glycation Accelerates Fibrillization of the Amyloidogenic W7FW14F Apomyoglobin
por: Iannuzzi, Clara, et al.
Publicado: (2013)

Amyloid β-protein oligomers promote the uptake of tau fibril seeds potentiating intracellular tau aggregation
por: Shin, Woo Shik, et al.
Publicado: (2019)

Fully co-factor-free ClearTau platform produces seeding-competent Tau fibrils for reconstructing pathological Tau aggregates
por: Limorenko, Galina, et al.
Publicado: (2023)

Aptamers targeting amyloidogenic proteins and their emerging role in neurodegenerative diseases
por: Murakami, Kazuma, et al.
Publicado: (2021)

Influence of the Stability of a Fused Protein and Its Distance to the Amyloidogenic Segment on Fibril Formation
por: Buttstedt, Anja, et al.
Publicado: (2010)

Author Correction: Competition between crystal and fibril formation in molecular mutations of amyloidogenic peptides
por: Reynolds, Nicholas P., et al.
Publicado: (2017)

Heparan sulfates facilitate harmless amyloidogenic fibril formation interacting with elastin-like peptides
por: Boraldi, Federica, et al.
Publicado: (2018)

Retraction: Glycation Accelerates Fibrillization of the Amyloidogenic W7FW14F Apomyoglobin
Publicado: (2019)

Structural characterisation of amyloid-like fibrils formed by an amyloidogenic peptide segment of β-lactoglobulin
por: Gowda, Vasantha, et al.
Publicado: (2021)

Amyloidogenicity and toxicity of the reverse and scrambled variants of amyloid‐β 1‐42
por: Vadukul, Devkee M., et al.
Publicado: (2017)

Residue-based propensity of aggregation in the Tau amyloidogenic hexapeptides AcPHF6* and AcPHF6
por: Dangi, Abha, et al.
Publicado: (2020)

Correction to: Amyloid β-protein oligomers promote the uptake of tau fibril seeds potentiating intracellular tau aggregation
por: Shin, Woo Shik, et al.
Publicado: (2021)

How do amino acid substitutions affect the amyloidogenic properties and seeding efficiency of prion peptides
por: Chuang, Chi-Chen, et al.
Publicado: (2013)

Exploiting heterogeneous features to improve in silico prediction of peptide status – amyloidogenic or non-amyloidogenic
por: Nair, Smitha Sunil Kumaran, et al.
Publicado: (2011)

Transthyretin Anti-Amyloidogenic and Fibril Disrupting Activities of Bacopa monnieri (L.) Wettst (Brahmi) Extract
por: Eze, Fredrick Nwude, et al.
Publicado: (2019)

Molecular Determinants of Fibrillation in a Viral Amyloidogenic Domain from Combined Biochemical and Biophysical Studies
por: Nilsson, Juliet F., et al.
Publicado: (2022)

Use of a Novel Grammatical Inference Approach in Classification of Amyloidogenic Hexapeptides
por: Wieczorek, Wojciech, et al.
Publicado: (2016)

Correction: Residue-based propensity of aggregation in the Tau amyloidogenic hexapeptides AcPHF6* and AcPHF6
por: Dangi, Abha, et al.
Publicado: (2022)

The Role of Cholesterol in Amyloidogenic Substrate Binding to the γ-Secretase Complex
por: Orzeł, Urszula, et al.
Publicado: (2021)

Amyloidogenic determinants are usually not buried
por: Frousios, Kimon K, et al.
Publicado: (2009)

Cannot write session to /tmp/vufind_sessions/sess_6d7sjugsiqgstqhh9f5spp7548