Neurodegenerative disease and the NLRP3 inflammasome

JA Holbrook, HH Jarosz-Griffiths, E Caseley… - Frontiers in …, 2021 - frontiersin.org
The prevalence of neurodegenerative disease has increased significantly in recent years,
and with a rapidly aging global population, this trend is expected to continue. These …

NLRP3 inflammasome in neurological diseases, from functions to therapies

L Song, L Pei, S Yao, Y Wu, Y Shang - Frontiers in cellular …, 2017 - frontiersin.org
Neuroinflammation has been identified as a causative factor of multiple neurological
diseases. The nucleotide-binding oligomerization domain-, leucine-rich repeat-and pyrin …

Cellular and molecular mechanisms of prion disease

CJ Sigurdson, JC Bartz, M Glatzel - Annual Review of Pathology …, 2019 - annualreviews.org
Prion diseases are rapidly progressive, incurable neurodegenerative disorders caused by
misfolded, aggregated proteins known as prions, which are uniquely infectious. Remarkably …

Distinct synthetic Aβ prion strains producing different amyloid deposits in bigenic mice

J Stöhr, C Condello, JC Watts, L Bloch… - Proceedings of the …, 2014 - National Acad Sciences
An increasing number of studies continue to show that the amyloid β (Aβ) peptide adopts an
alternative conformation and acquires transmissibility; hence, it becomes a prion. Here, we …

Evidence of distinct α-synuclein strains underlying disease heterogeneity

SAM Holec, AL Woerman - Acta neuropathologica, 2021 - Springer
Synucleinopathies are a group of neurodegenerative disorders caused by the misfolding
and self-templating of the protein α-synuclein, or the formation of α-synuclein prions. Each …

The NLRP3-caspase 1 inflammasome negatively regulates autophagy via TLR4-TRIF in prion peptide-infected microglia

M Lai, H Yao, SZA Shah, W Wu, D Wang… - Frontiers in aging …, 2018 - frontiersin.org
Prion diseases are neurodegenerative disorders characterized by the accumulation of
misfolded prion protein, spongiform changes in the brain, and brain inflammation as a result …

Evidence that bank vole PrP is a universal acceptor for prions

JC Watts, K Giles, S Patel, A Oehler… - PLoS …, 2014 - journals.plos.org
Bank voles are uniquely susceptible to a wide range of prion strains isolated from many
different species. To determine if this enhanced susceptibility to interspecies prion …

The molecular determinants of a universal prion acceptor

H Arshad, Z Patel, ZAM Al-Azzawi, G Amano, L Li… - PLoS …, 2024 - journals.plos.org
In prion diseases, the species barrier limits the transmission of prions from one species to
another. However, cross-species prion transmission is remarkably efficient in bank voles …

ɑ‐Synuclein strains and the variable pathologies of synucleinopathies

W Peelaerts, V Baekelandt - Journal of neurochemistry, 2016 - Wiley Online Library
Several decades ago, a mysterious transmissible agent was found responsible for a group
of progressive and lethal encephalopathies affecting the nervous system of both animals …

High-resolution structure of infectious prion protein: the final frontier

R Diaz-Espinoza, C Soto - Nature structural & molecular biology, 2012 - nature.com
Prions are the proteinaceous infectious agents responsible for the transmission of prion
diseases. The main or sole component of prions is the misfolded prion protein (PrPSc) …