نتایج جستجو برای: β amyloid aggregation

تعداد نتایج: 265469  

2016
Laura C. López Olga Varea Susanna Navarro José A. Carrodeguas Natalia Sanchez de Groot Salvador Ventura Javier Sancho

Human Amylin, or islet amyloid polypeptide (hIAPP), is a small hormone secreted by pancreatic β-cells that forms aggregates under insulin deficiency metabolic conditions, and it constitutes a pathological hallmark of type II diabetes mellitus. In type II diabetes patients, amylin is abnormally increased, self-assembled into amyloid aggregates, and ultimately contributes to the apoptotic death o...

2015
Susanna Navarro Marta Diaz-Caballero Ricard Illa Salvador Ventura

Misfolding and aggregation of proteins in tissues is linked to the onset of a diverse set of human neurodegenerative disorders, including Alzheimer's and Parkinson's diseases. In these pathologies proteins usually aggregate into highly ordered and β-sheet enriched amyloid fibrils. However, the formation of these toxic structures is not restricted to a reduced set of polypeptides but rather an i...

Journal: :Journal of Alzheimer's disease : JAD 2016
Farida El Gaamouch Ping Jing Jiahong Xia Dongming Cai

Brain lipid homeostasis plays an important role in Alzheimer's disease (AD) and other neurodegenerative disorders. Aggregation of amyloid-β peptide is one of the major events in AD. The complex interplay between lipids and amyloid-β accumulation has been intensively investigated. The proportions of lipid components including phospholipids, sphingolipids, and cholesterol are roughly similar acro...

2014
Georg K. A. Hochberg Heath Ecroyd Cong Liu Michael R. Sawaya Miranda P. Collier James Stroud John A. Carver Andrew J. Baldwin Carol V. Robinson David S. Eisenberg Justin L. P. Benesch Arthur Laganowsky Junichi Sugihara Shiho Kawamura Stefania A. Mari Senthilkumar Cinghu Sailu Yellaboina Johannes M. Freudenberg Swati Ghosh Xiaofeng Zheng Andrew J. Oldfield Brad L. Lackford Dmitri V. Zaykin Guang Hu Raja Jothi

We find that the core domain of the human molecular chaperone αBcrystallin can function effectively in preventing protein aggregation and amyloid toxicity. The core domain represents only half the total sequence of the protein, but it is one of the most potent known inhibitors of the aggregation of amyloid-β, a process implicated in Alzheimer’s disease. We have determined high-resolution struct...

2016
Maryam Hashemi Shabestari Nico J. Meeuwenoord Dmitri. V. Filippov Martina Huber

The amyloid β (A β) peptide is important in the context of Alzheimer's disease, since it is one of the major components of the fibrils that constitute amyloid plaques. Agents that can influence fibril formation are important, and of those, membrane mimics are particularly relevant, because the hydrophobic part of A β suggests a possible membrane activity of the peptide. We employed spin-label E...

2016
Anne-Marie Marzesco Matthias Flötenmeyer Anika Bühler Ulrike Obermüller Matthias Staufenbiel Mathias Jucker Frank Baumann

An early event in Alzheimer's disease (AD) pathogenesis is the formation of extracellular aggregates of amyloid-β peptide (Aβ), thought to be initiated by a prion-like seeding mechanism. However, the molecular nature and location of the Aβ seeds remain rather elusive. Active Aβ seeds are found in crude homogenates of amyloid-laden brains and in the soluble fraction thereof. To analyze the seedi...

Journal: :Macromolecular Rapid Communications 2019

2011
Jiyong Lee Elizabeth K. Culyba Evan T. Powers Jeffery W. Kelly

Amyloid-β amyloidogenesis is reported to occur via a nucleated polymerization mechanism. If this is true, the energetically unfavorable oligomeric nucleus should be very hard to detect. However, many laboratories have detected early nonfibrillar amyloid-β oligomers without observing amyloid fibrils, suggesting that a mechanistic revision may be needed. Here we introduce Cys-Cys-amyloid-β(1-40),...

نمودار تعداد نتایج جستجو در هر سال

با کلیک روی نمودار نتایج را به سال انتشار فیلتر کنید