Results 91 to 100 of about 75,180 (286)
Quaternary Structure Defines a Large Class of Amyloid-β Oligomers Neutralized by Sequestration
Cell Reports, 2015 The accumulation of amyloid-β (Aβ) as amyloid fibrils and toxic oligomers is an important step in the development of Alzheimer’s disease (AD). However, there are numerous potentially toxic oligomers and little is known about their neurological effects ...
Peng Liu +13 more
doaj +1 more source
Advanced Science, EarlyView.This study presents the de novo design and directed evolution of a mirror‐image D‐protein inhibitor targeting human interleukin‐4 (IL‐4). The engineered molecule exhibits nanomolar binding affinity for IL‐4 and effectively inhibits IL‐4–mediated signaling.
Liqing Xu +7 more
wiley +1 more source
Elevated temperatures accelerate the formation of toxic amyloid fibrils of hen egg‐white lysozyme
Veterinary Medicine and Science, 2021 The formation of amyloid fibrils is critical for neurodegenerative diseases. Some physiochemical conditions can promote the conversion of proteins from soluble globular shapes into insoluble well‐organized amyloid fibrils.
Zili Feng, Ying Li, Yu Bai
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Different Amyloid-β Self-Assemblies Have Distinct Effects on Intracellular Tau Aggregation. [PDF]
, 2019 Alzheimer's disease (AD) pathology is characterized by the aggregation of beta-amyloid (Aβ) and tau in the form of amyloid plaques and neurofibrillary tangles in the brain.
Bitan, Gal +6 more
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Advanced Science, EarlyView.Emerging evidence suggests that intraneuronal Aβ accumulation represents an early pathogenic event in Alzheimer's disease (AD). Using Drosophila AD model, this study shows that a nonsecreted serine protease Yip7 physically interacts with Aβ. This causes intraneuronal Aβ accumulation but surprisingly reduces the associated neurotoxicity, arguing that ...
Jingyun Su +4 more
wiley +1 more source
Cell Death and DiseaseThe tumor microenvironment is a complex ecosystem that plays a critical role in cancer progression and treatment response. Recently, extracellular amyloid fibrils have emerged as novel components of the tumor microenvironment; however, their function ...
Francesco Farris +12 more
doaj +1 more source
Exploring the mechanism of formation of native-like and precursor amyloid oligomers for the native acylphosphatase from Sulfolobus solfataricus [PDF]
, 2006 Over 40 human diseases are associated with the formation of well-defined proteinaceous fibrillar aggregates. Since the oligomers precursors to the fibrils are increasingly recognized to be the causative agents of such diseases, it is important to ...
BEMPORAD F +5 more
core +1 more source
Advanced Science, EarlyView.This study tests NeuroD1 AAV‐based gene therapy in a non‐human primate Alzheimer's disease model. The therapy prevents neuronal damage, inhibits hippocampal atrophy, and reduces neuroinflammation. It also repairs vascular and blood‐brain barrier damage, restores cerebrospinal fluid biomarkers, enhances hippocampal glucose metabolism, and improves ...
Zhouquan Jiang +21 more
wiley +1 more source
Amyloid-like fibrils labeled with magnetic nanoparticles
Biomolecular Concepts, 2013 A number of human diseases are associated with the formation of insoluble protein aggregates commonly known as amyloid fibrils or amyloid plaques. Similar materials can be prepared in vitro resulting in so-called amyloid-like fibrils. Herein is discussed
Solin Niclas
doaj +1 more source
Without magic bullets: the biological basis for public health interventions against protein folding disorders [PDF]
, 2010 Protein folding disorders of aging like Alzheimer's and Parkinson's diseases currently present intractable medical challenges. 'Small molecule' interventions - drug treatments - often have, at best, palliative impact, failing to alter
Rodrick Wallace
core +2 more sources