Results 31 to 40 of about 6,958 (184)

The cellular prion protein interacts with and promotes the activity of Na,K-ATPases.

open access: yesPLoS ONE, 2021
The prion protein (PrP) is best known for its ability to cause fatal neurodegenerative diseases in humans and animals. Here, we revisited its molecular environment in the brain using a well-developed affinity-capture mass spectrometry workflow that ...
Declan Williams   +10 more
doaj   +1 more source

Prion therapeutics: Lessons from the past

open access: yesPrion, 2022
Prion diseases are a group of incurable zoonotic neurodegenerative diseases (NDDs) in humans and other animals caused by the prion proteins. The abnormal folding and aggregation of the soluble cellular prion proteins (PrPC) into scrapie isoform (PrPSc ...
Kyu Hwan Shim   +2 more
doaj   +1 more source

New insights into cellular prion protein (PrPc) functions: The “ying and yang” of a relevant protein [PDF]

open access: yesBrain Research Reviews, 2009
The conversion of cellular prion protein (PrP(c)), a GPI-anchored protein, into a protease-K-resistant and infective form (generally termed PrP(sc)) is mainly responsible for Transmissible Spongiform Encephalopathies (TSEs), characterized by neuronal degeneration and progressive loss of basic brain functions.
Nicolás i Pallejà, Josep Oriol   +2 more
openaire   +4 more sources

Post-translational modifications in prion diseases

open access: yesFrontiers in Molecular Neuroscience
More than 650 reversible and irreversible post-translational modifications (PTMs) of proteins have been listed so far. Canonical PTMs of proteins consist of the covalent addition of functional or chemical groups on target backbone amino-acids or the ...
Chloé Bizingre   +12 more
doaj   +1 more source

Synaptic Dysfunction in Prion Diseases: A Trafficking Problem?

open access: yesInternational Journal of Cell Biology, 2013
Synaptic dysfunction is an important cause of neurological symptoms in prion diseases, a class of clinically heterogeneous neurodegenerative disorders caused by misfolding of the cellular prion protein (PrPC).
Assunta Senatore   +2 more
doaj   +1 more source

An antipsychotic drug exerts anti-prion effects by altering the localization of the cellular prion protein.

open access: yesPLoS ONE, 2017
Prion diseases are neurodegenerative conditions characterized by the conformational conversion of the cellular prion protein (PrPC), an endogenous membrane glycoprotein of uncertain function, into PrPSc, a pathological isoform that replicates by imposing
Claudia Stincardini   +16 more
doaj   +1 more source

Prominent Stress Response of Purkinje Cells in Creutzfeldt–Jakob Disease

open access: yesNeurobiology of Disease, 2001
To examine the role of stress-related 70-kDa heat shock proteins (Hsp-s) in Creutzfeldt–Jakob disease (CJD), we performed immunocytochemistry to detect Hsp-72 and Hsp-73, together with the abnormal (PrPSc) and the presumed cellular form (PrPC) of the ...
Gábor G. Kovács   +9 more
doaj   +1 more source

Enhanced Sensitivity of a Modified Quaking‐Induced Conversion Diagnostic Test for the Broad Detection of Sporadic and Inherited Prion Diseases: A Retrospective Study

open access: yesAnnals of Neurology, EarlyView.
Objective Quaking‐induced conversion (QuIC) tests, which detect prion‐seeding activity in cerebrospinal fluid (CSF), have markedly advanced the antemortem diagnosis of prion diseases such as Creutzfeldt‐Jakob disease (CJD). These tests provide high diagnostic accuracy and enable timely differentiation from other rapidly progressive neurodegenerative ...
Jennifer Myskiw   +13 more
wiley   +1 more source

Common themes in PrP signaling: the Src remains the same

open access: yesFrontiers in Cell and Developmental Biology, 2014
The ability of the cellular prion protein (PrPC) to trigger intracellular signals appears central to neurodegeneration pathways, yet the physiological significance of such signals is rather puzzling.
Katharina eOchs   +2 more
doaj   +1 more source

Alterations in the brain interactome of the intrinsically disordered N-terminal domain of the cellular prion protein (PrPC) in Alzheimer's disease. [PDF]

open access: yesPLoS ONE, 2018
The cellular prion protein (PrPC) is implicated in neuroprotective signaling and neurotoxic pathways in both prion diseases and Alzheimer's disease (AD). Specifically, the intrinsically disordered N-terminal domain (N-PrP) has been shown to interact with
Sarah Ulbrich   +9 more
doaj   +1 more source

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