Cargando…

Strikingly different effects of cholesterol and 7-ketocholesterol on lipid bilayer-mediated aggregation of amyloid beta (1-42)

Oxidized cholesterol has been widely reported to contribute to the pathogenesis of Alzheimer's disease (AD). However, the mechanism by which they affect the disease is not fully understood. Herein, we aimed to investigate the effect of 7-ketocholesterol (7keto) on membrane-mediated aggregation...

Descripción completa

Detalles Bibliográficos
Autores principales:	Phan, Huong T.T., Shimokawa, Naofumi, Sharma, Neha, Takagi, Masahiro, Vestergaard, Mun'delanji C.
Formato:	Online Artículo Texto
Lenguaje:	English
Publicado:	Elsevier 2018
Materias:	Research Article
Acceso en línea:	https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5986554/ https://www.ncbi.nlm.nih.gov/pubmed/29872741 http://dx.doi.org/10.1016/j.bbrep.2018.04.007

Ejemplares similares

Effects of Capsaicin on Biomimetic Membranes †
por: Sharma, Neha, et al.
Publicado: (2019)

Polyphenols Modulate Alzheimer’s Amyloid Beta Aggregation in a Structure-Dependent Manner
por: Phan, Huong T. T., et al.
Publicado: (2019)

Glycosyl chains and 25‐hydroxycholesterol contribute to the intracellular transport of amyloid beta (Aβ‐42) in Jurkat T cells
por: Sharma, Neha, et al.
Publicado: (2017)

An Overview of Label-free Electrochemical Protein Sensors
por: Vestergaard, Mun'delanji, et al.
Publicado: (2007)

Printable Electrochemical Biosensors: A Focus on Screen-Printed Electrodes and Their Application
por: Yamanaka, Keiichiro, et al.
Publicado: (2016)

Carbon-Based Nanomaterials in Biomass-Based Fuel-Fed Fuel Cells
por: Hoa, Le Quynh, et al.
Publicado: (2017)

Dynamic Morphological Changes Induced By GM1 and Protein Interactions on the Surface of Cell-Sized Liposomes
por: Dhingra, Shruti, et al.
Publicado: (2013)

Immuno-Dipstick for Colletotrichum gloeosporioides Detection: Towards On-Farm Application
por: Oussou-Azo, Fifame Auriane, et al.
Publicado: (2022)

Antifungal Potential of Nanostructured Crystalline Copper and Its Oxide Forms
por: Oussou-Azo, Auriane Fifame, et al.
Publicado: (2020)

7-Ketocholesterol in disease and aging
por: Anderson, Amelia, et al.
Publicado: (2019)

Effect of Ergothioneine on 7-Ketocholesterol-Induced Endothelial Injury
por: Koh, Sally Shuxian, et al.
Publicado: (2020)

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

7-Ketocholesterol Induces Lipid Metabolic Reprogramming and Enhances Cholesterol Ester Accumulation in Cardiac Cells
por: Cheng, Mei-Ling, et al.
Publicado: (2021)

Oxysterols Versus Cholesterol in Model Neuronal Membrane. I. The Case of 7-Ketocholesterol. The Langmuir Monolayer Study
por: Wnętrzak, Anita, et al.
Publicado: (2017)

Stability of Cholesterol, 7-Ketocholesterol and β-Sitosterol during Saponification: Ramifications for Artifact Monitoring of Sterol Oxide Products
por: Busch, T. P., et al.
Publicado: (2010)

Lipoprotein-Induced Increases in Cholesterol and 7-Ketocholesterol Result in Opposite Molecular-Scale Biophysical Effects on Membrane Structure
por: Ayee, Manuela A.A., et al.
Publicado: (2021)

RRY Inhibits Amyloid-β(1–42) Peptide Aggregation and Neurotoxicity
por: Sun, Xicui, et al.
Publicado: (2021)

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

Cholesterol-sensing role of phenylalanine in the interaction of human islet amyloid polypeptide with lipid bilayers
por: Hao, Ruijie, et al.
Publicado: (2018)

Suppression of Amyloid-β Adsorption on Endoplasmic Reticulum Stress-Mimicking Membranes by α-Tocopherol and α-Tocotrienol
por: Nakatani, Yusuke, et al.
Publicado: (2022)

The Binding of Aβ42 Peptide Monomers to Sphingomyelin/Cholesterol/Ganglioside Bilayers Assayed by Density Gradient Ultracentrifugation
por: Ahyayauch, Hasna, et al.
Publicado: (2020)

Amyloid-β peptide 37, 38 and 40 individually and cooperatively inhibit amyloid-β 42 aggregation
por: Braun, Gabriel A., et al.
Publicado: (2022)

Critical aggregation concentration for the formation of early Amyloid-β (1–42) oligomers
por: Novo, Mercedes, et al.
Publicado: (2018)

Interaction of the Molecular Chaperone DNAJB6 with Growing Amyloid-beta 42 (Aβ42) Aggregates Leads to Sub-stoichiometric Inhibition of Amyloid Formation
por: Månsson, Cecilia, et al.
Publicado: (2014)

Tyrosine Hydroxylase Binding to Phospholipid Membranes Prompts Its Amyloid Aggregation and Compromises Bilayer Integrity
por: Baumann, Anne, et al.
Publicado: (2016)

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

The calcium-free form of atorvastatin inhibits amyloid-β(1–42) aggregation in vitro
por: Nedaei, Hadi, et al.
Publicado: (2022)

Hypochlorite-induced oxidation promotes aggregation and reduces toxicity of amyloid beta 1-42
por: Mañucat-Tan, Noralyn B., et al.
Publicado: (2023)

How Do the Size, Charge and Shape of Nanoparticles Affect Amyloid β Aggregation on Brain Lipid Bilayer?
por: Kim, Yuna, et al.
Publicado: (2016)

The Production of Matchout-Deuterated Cholesterol and the Study of Bilayer-Cholesterol Interactions
por: Waldie, Sarah, et al.
Publicado: (2019)

7-Ketocholesterol: Effects on viral infections and hypothetical contribution in COVID-19
por: Ghzaiel, Imen, et al.
Publicado: (2021)

Detection of Amyloid-β(1–42) Aggregation With a Nanostructured Electrochemical Sandwich Immunoassay Biosensor
por: Wang, Bing-Yu, et al.
Publicado: (2022)

α-Synuclein Aggregation Is Triggered by Oligomeric Amyloid-β 42 via Heterogeneous Primary Nucleation
por: Vadukul, Devkee M., et al.
Publicado: (2023)

Erratum: How Do the Size, Charge and Shape of Nanoparticles Affect Amyloid β Aggregation on Brain Lipid Bilayer?
por: Kim, Yuna, et al.
Publicado: (2016)

Electrografting a Hybrid Bilayer Membrane via Diazonium Chemistry for Electrochemical Impedance Spectroscopy of Amyloid-β Aggregation
por: Fini, Hamid, et al.
Publicado: (2022)

Amyloid-β 1–24 C-terminal truncated fragment promotes amyloid-β 1–42 aggregate formation in the healthy brain
por: Mazzitelli, Sonia, et al.
Publicado: (2016)

Cu(2+) Affects Amyloid-β (1–42) Aggregation by Increasing Peptide-Peptide Binding Forces
por: Hane, Francis, et al.
Publicado: (2013)

Investigating in Vitro Amyloid Peptide 1–42 Aggregation: Impact of Higher Molecular Weight Stable Adducts
por: De Simone, Angela, et al.
Publicado: (2019)

Complete aggregation pathway of amyloid β (1-40) and (1-42) resolved on an atomically clean interface
por: Nirmalraj, Peter Niraj, et al.
Publicado: (2020)

Exploring the Early Stages of the Amyloid Aβ(1–42) Peptide Aggregation Process: An NMR Study
por: Santoro, Angelo, et al.
Publicado: (2021)

Cannot write session to /tmp/vufind_sessions/sess_mui63ihfharqaptnrh4heb7klv