Results 111 to 120 of about 3,255,404 (222)

Molecular Editing Reveals a Bilobalide Chemotype that Attenuates Prolyl Endopeptidase (PREP)‐Linked Neuroinflammation

open access: yesAdvanced Science, EarlyView.
Molecular editing of bilobalide uncovers BB56, a PREP‐engaging chemotype with enhanced anti‐inflammatory activity in microglia. Integrated CETSA‐MS, SAR, and pathway analyses link BB56 to attenuation of p38 MAPK/NF‐κB and NLRP3‐associated inflammatory signaling, highlighting bilobalide editing as a strategy for developing neuroinflammation‐modulating ...
Chanin Sillapachaiyaporn   +20 more
wiley   +1 more source

Neuropathogenic role of astrocyte‐derived extracellular vesicles in HIV‐associated neurocognitive disorders

open access: yesJournal of Extracellular Vesicles
Our previous findings demonstrated that astrocytic HIF‐1α plays a major role in HIV‐1 Tat‐mediated amyloidosis which can lead to Alzheimer's‐like pathology‐a comorbidity of HIV‐Associated Neurocognitive Disorders (HAND). These amyloids can be shuttled in
Divya T. Chemparathy   +8 more
doaj   +1 more source

Early Retinal UCHL1 Dysregulation Coupled With Synaptic Loss Reflects Alzheimer's Disease Severity

open access: yesAdvanced Science, EarlyView.
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

Biological Amyloids Chemically Damage DNA [Elektronisk resurs]

open access: yes
Amyloid fibrils are protein polymers noncovalently assembled through beta-strands arranged in a cross-beta structure. Biological amyloids were considered chemically inert until we and others recently demonstrated their ability to catalyze chemical ...
Rehnberg, Nikita,   +7 more
core   +1 more source

Structures of Pathological and Functional Amyloids and Prions, a Solid-State NMR Perspective. [PDF]

open access: yesFront Mol Neurosci, 2021
Daskalov A   +16 more
europepmc   +1 more source

Entorhinal Astrocyte Transplants Restore Spatial Exploration and Alleviate Amyloid‐Beta Pathology in Alzheimer's Mice

open access: yesAdvanced Science, EarlyView.
Impaired MEC astrocytic Ca2+ signaling is associated with fragmented spatial exploration in AD mice. Region‐specific glial progenitor transplantation generates engrafted astrocytes that are accompanied by improved AQP4 polarization, reduced amyloid‐β‐associated pathology, attenuated neuroinflammation, preserved synaptic integrity, and ameliorated ...
Fengjuan Wu   +16 more
wiley   +1 more source

α‐Synuclein Forms Distinct Micelle‐Like Assemblies at Low Ionic Strengths

open access: yesAdvanced Science, EarlyView.
At high ionic strength, α‐synuclein forms diverse assemblies, including oligomers, fibrils, and condensates. Here, we show that at low ionic strength, α‐synuclein adopts a distinct, low‐abundance assembly state. These assemblies maintain a constant size above a critical concentration and do not coalesce, suggesting a micelle‐like organization ...
Sophie Hertel   +10 more
wiley   +1 more source

Early Spatial and Contextual Coding Deficits in Hippocampal CA1 Precede Performance Decline in an Alzheimer's Disease Model

open access: yesAdvanced Science, EarlyView.
Two‐photon calcium imaging in behaving 5xFAD mice reveals early CA1 coding deficits before behavioral decline. Task‐related place cell activity and splitter cell trajectory coding are impaired, with reduced retrospective dominance and greater prospective weighting.
Yimei Li   +8 more
wiley   +1 more source

Natural protective amyloids

open access: yes, 2008
Amyloidoses are a group of diseases including neurodegenerative diseases like Alzheimer's disease and also type II diabetes, spongiform encephalopathies and many others, believed to be caused by protein aggregation and subsequent amyloid fibril ...
Iconomidou, V.A., Hamodrakas, S.J.
core  

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