Results 51 to 60 of about 50,704 (271)

Multifaceted role of sialylation in prion diseases

Frontiers in Neuroscience, 2016
Mammalian prion or PrPSc is a proteinaceous infectious agent that consists of a misfolded, self-replicating state of a sialoglycoprotein called the prion protein or PrPC. Sialylation of the prion protein N-linked glycans was discovered more than 30 years
Ilia V Baskakov, Ilia V Baskakov, Elizaveta Katorcha, Elizaveta Katorcha   +3 more
doaj   +1 more source

Construction of pathogenic Sec16a mutation mouse model using CRISPR/Cas9

Animal Models and Experimental Medicine, EarlyView.
Yaqiang Hu et al. engineered a pathogenic Sec16a mutant mouse model using CRISPR/Cas9 technology. They observed that the Sec16a mutant mice displayed diminished learning and memory capabilities, along with a limb‐clasping phenotype upon tail suspension.
Yaqiang Hu, Zhiyang Zeng, Xinyu Ming, Shuming Yin, Yuting Guan, Liangcai Gao, Dali Li   +6 more
wiley   +1 more source

Protein-lipid interactions and protein anchoring modulate the modes of association of the globular domain of the Prion protein and Doppel protein to model membrane patches

Frontiers in Bioinformatics
The Prion protein is the molecular hallmark of the incurable prion diseases affecting mammals, including humans. The protein-only hypothesis states that the misfolding, accumulation, and deposition of the Prion protein play a critical role in toxicity ...
Patricia Soto, Davis T. Thalhuber, Frank Luceri, Jamie Janos, Mason R. Borgman, Noah M. Greenwood, Sofia Acosta, Hunter Stoffel   +7 more
doaj   +1 more source

Reversible symptoms and clearance of mutant prion protein in an inducible model of a genetic prion disease in Drosophila melanogaster

Neurobiology of Disease, 2014
Prion diseases are progressive disorders that affect the central nervous system leading to memory loss, personality changes, ataxia and neurodegeneration.
A. Murali, R.A. Maue, P.J. Dolph
doaj   +1 more source

Prion peptide-mediated calcium level alteration governs neuronal cell damage through AMPK-autophagy flux

Cell Communication and Signaling, 2020
Background The distinctive molecular structure of the prion protein, PrPsc, is established only in mammals with infectious prion diseases. Prion protein characterizes either the transmissible pathogen itself or a primary constituent of the disease.
Ji-Hong Moon, Sang-Youel Park
doaj   +1 more source

Cytosolic Prion Protein Toxicity Is Independent of Cellular Prion Protein Expression and Prion Propagation [PDF]

Journal of Virology, 2007
ABSTRACT Prion diseases are transmissible neurodegenerative diseases caused by a conformational isoform of the prion protein (PrP), a host-encoded cell surface sialoglycoprotein. Recent evidence suggests a cytosolic fraction of PrP (cyPrP) functions either as an initiating factor or toxic element of prion disease.
Eric M, Norstrom, Mark F, Ciaccio, Benjamin, Rassbach, Robert, Wollmann, James A, Mastrianni   +4 more
openaire   +2 more sources

Clinical–Radiological Spectrum of Cerebral Amyloid Angiopathy‐Related Inflammation

Annals of Neurology, EarlyView.
Objective To identify clinical and radiological features of cerebral amyloid angiopathy‐related inflammation (CAA‐ri), and compare these features with those of sporadic CAA, to improve the understanding, diagnosis, and clinical care of CAA‐ri. Methods We retrospectively reviewed routine clinical data from 37 patients with CAA‐ri and 158 patients with ...
Larysa Panteleienko, Gargi Banerjee, Dermot Mallon, Kitti Thiankhaw, Rupert Oliver, Victoria Harvey, Gareth Ambler, Michael Zandi, Hans Rolf Jäger, David J. Werring   +9 more
wiley   +1 more source

Prion-Like Proteins in Phase Separation and Their Link to Disease

Biomolecules, 2021
Aberrant protein folding underpins many neurodegenerative diseases as well as certain myopathies and cancers. Protein misfolding can be driven by the presence of distinctive prion and prion-like regions within certain proteins. These prion and prion-like
Macy L. Sprunger, Meredith E. Jackrel
doaj   +1 more source

Metabolism of minor isoforms of prion proteins: Cytosolic prion protein and transmembrane prion protein.

Neural regeneration research, 2013
Transmissible spongiform encephalopathy or prion disease is triggered by the conversion from cellular prion protein to pathogenic prion protein. Growing evidence has concentrated on prion protein configuration changes and their correlation with prion disease transmissibility and pathogenicity.
Song, Zhiqi, Zhao, Deming, Yang, Lifeng
openaire   +2 more sources

Conformational conversion of prion protein in prion diseases [PDF]

Acta Biochimica et Biophysica Sinica, 2013
Prion diseases are a group of infectious fatal neurodegenerative diseases. The conformational conversion of a cellular prion protein (PrP(C)) into an abnormal misfolded isoform (PrP(Sc)) is the key event in prion diseases pathology. Under normal conditions, the high-energy barrier separates PrP(C) from PrP(Sc) isoform.
Zheng, Zhou, Gengfu, Xiao
openaire   +2 more sources