Results 101 to 110 of about 616,892 (193)

Tracking tau and cellular responses in human iPSC‐microglia: from uptake to seedable secretion, including in extracellular vesicles

open access: yesAlzheimer's &Dementia, Volume 22, Issue 4, April 2026.
Abstract INTRODUCTION Microglia have been implicated in the templated spread of tau aggregates in tauopathies through mouse studies. However, it is unclear whether these findings translate to human disease. METHODS We challenged human induced pluripotent stem cell (iPSC)‐derived microglia‐like‐cells (iMGL) with monomeric and fibrillar recombinant tau ...
Maria Kreger Karabova   +22 more
wiley   +1 more source

Detection of prions in skin punch biopsies of Creutzfeldt–Jakob disease patients [PDF]

open access: yes, 2020
Prion real-time quaking-induced conversion (RT-QuIC) is an ultrasensitive assay detecting pathological aggregates of misfolded prion protein in biospecimens.
Baiardi S.   +7 more
core   +1 more source

Preparation of mouse tissue homogenates for RT-QuIC assay v1

open access: yes, 2023
This protocol is designed for a standardized and efficient procedure to homogenize mouse tissue, conducive for RT-QuIC analysis. The process involves treating samples with PBS mixed with Triton-X100, followed by homogenization using a prob-tip sonicator.
arpine.sokratian not provided   +1 more
openaire   +1 more source

The Phenotypic Spectrum of Sporadic Creutzfeldt‐Jakob Disease Cortical Subtype

open access: yesAnnals of Neurology, Volume 99, Issue 4, Page 883-896, April 2026.
Objective The objective of this study was to characterize the phenotypic spectrum of the rare sporadic Creutzfeldt‐Jakob disease cortical subtype (sCJDMM/MV2C) in a large multicentric autopsy cohort. Methods We evaluated clinical histories, biofluid markers, brain diffusion‐weighted (DW)‐magnetic resonance imaging (MRI), and electroencephalogram (EEG ...
Simone Baiardi   +16 more
wiley   +1 more source

In vitro amplification of H-type atypical bovine spongiform encephalopathy by protein misfolding cyclic amplification [PDF]

open access: yes, 2016
The in vitro amplification of prions by serial protein misfolding cyclic amplification has been shown to detect PrPSc to levels at least as sensitive as rodent bioassay but in a fraction of the time.
Ben C. Maddison   +5 more
core   +2 more sources

Towards an improved early diagnosis of neurodegenerative diseases: The emerging role of in vitro conversion assays for protein amyloids [PDF]

open access: yes, 2020
Tissue accumulation of abnormal aggregates of amyloidogenic proteins such as prion protein, α-synuclein, and tau represents the hallmark of most common neurodegenerative disorders and precedes the onset of symptoms by years.
Baiardi S.   +4 more
core   +1 more source

The Brain‐Gut Axis in Parkinson's Disease Pathology

open access: yesComprehensive Physiology, Volume 16, Issue 2, April 2026.
Exposure to environmental toxins induces gut dysbiosis, increases intestinal epithelial barrier permeability, immune activation, and oxidative stress, promoting α‐syn misfolding and propagation. Brainstem DMV neurons exhibit α‐syn pathology, dysregulating neuronal excitability and vagal control of GI functions.
Kudret Selin Ozkaya   +1 more
wiley   +1 more source

Aggregation studies on the transactive response DNA binding protein of 43 KDA (TDP-43) [PDF]

open access: yes, 2020
The pathological deposition of the transactive response DNA-binding protein of 43 kDa (TDP-43) occurs in the majority (\uf07e97%) of amyotrophic lateral sclerosis (ALS) and in around 45% of frontotemporal lobar degeneration cases (FTLD).
Scial\uf2, Carlo
core  

Optimizing Ultrasensitive RT‐QuiC assay on AD tau seed‐monomer reactions [PDF]

open access: yesAlzheimers Dement
AbstractBackgroundAlzheimer’s disease (AD) is pathologically defined by the presence of extracellular Aβ plaque and intracellular tau inclusions. Emerging evidence shows that tau aggregates contain pathogenic bioactivities of templating monomeric tau into filamentous fibrils and propagating through cells.
Chen J, Lee V, Xu H.
europepmc   +2 more sources

In vitro, cellular and in vivo studies of amyloid oligomers structure and toxicity: Challenges and advances

open access: yesProtein Science, Volume 35, Issue 4, April 2026.
Abstract Oligomeric assemblies of amyloidogenic proteins, such as Aβ, tau, α‐synuclein, amylin, transthyretin, and TDP‐43, are increasingly recognized as key drivers of cellular dysfunction across a range of neurodegenerative and systemic disorders.
Magdalena I. Ivanova   +2 more
wiley   +1 more source

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