Results 81 to 90 of about 160,241 (252)
Preparation of Amyloid Fibril Networks
Networks of amyloid nanofibrils fabricated from common globular proteins such as lysozyme and β-lactoglobulin have material properties that mimic the extracellular microenvironment of many cell types. Cells cultured on such amyloid fibril networks show improved attachment, spreading and in the case of mesenchymal stem cells improved differentiation ...
Charnley, Mirren +3 more
openaire +5 more sources
Early Retinal UCHL1 Dysregulation Coupled With Synaptic Loss Reflects Alzheimer's Disease Severity
This study identifies synapse‐enriched deubiquitinase UCHL1 as an early Aβ‐responsive regulator of retinal synaptopathy in Alzheimer's disease. Retinal UCHL1 loss accompanies excitatory synapse degeneration, p75NTR activation, and neuroinflammation, and predicts Braak stage and cognitive decline. Aβ42 fibrils trigger synaptic and UCHL1 depletion before
Altan Rentsendorj +25 more
wiley +1 more source
Amyloid fibrils can form biologically relevant functional assemblies. The RIP homotypic interaction motifs (RHIMs) in receptor-interacting protein kinases 1 and 3 (RIPK1 and RIPK3) orchestrate the formation of amyloid-like fibrils essential for ...
Paula Polonio +7 more
doaj +1 more source
Quaternary Structure Defines a Large Class of Amyloid-β Oligomers Neutralized by Sequestration
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
The question of strains in AA amyloidosis
The existence of transmissible amyloid fibril strains has long intrigued the scientific community. The strain theory originates from prion disorders, but here, we provide evidence of strains in systemic amyloidosis.
Gunilla T. Westermark +5 more
doaj +1 more source
Elevated temperatures accelerate the formation of toxic amyloid fibrils of hen egg‐white lysozyme
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
doaj +1 more source
The protein aggregates and gene expression in the middle temporal gyrus (MTG) and somatosensory cortex (SOM) of the postmortem brains of 13 Alzheimer's disease patients were studied in detail, revealing that small hyperphosphorylated tau aggregates increase with Braak stage driven by microglial inflammation.
Elizabeth A. English +9 more
wiley +1 more source
Here, we report a novel NIR fluorescent PROTAC platform that enables real‐time imaging and targeted degradation of Alzheimer's p‐Tau. Our lead compound effectively clears p‐Tau, reduces APP/Aβ, and alleviates cognitive deficits in AD mice. This work demonstrates a theranostic strategy for visualizing degradation and developing next‐generation AD ...
Ziwei Ren +11 more
wiley +1 more source
The 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
Amyloid-like fibrils labeled with magnetic nanoparticles
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

