Results 41 to 50 of about 14,426 (178)

Characterizing Cutaneous α‐Synuclein Deposition and Seeding Activity in Parkinson's Disease Subtypes

open access: yesAnnals of Clinical and Translational Neurology, EarlyView.
ABSTRACT Objective Cutaneous phosphorylated α‐synuclein (p‐syn) and α‐synuclein seeding activity are promising biomarkers for Parkinson's disease (PD), but their clinical value remains uncertain due to disease heterogeneity. This study evaluates these two biomarkers in PD patients to inform phenotype‐specific diagnosis and disease severity assessment ...
Yuting Jin   +8 more
wiley   +1 more source

Aerosols transmit prions to immunocompetent and immunodeficient mice. [PDF]

open access: yesPLoS Pathogens, 2011
Prions, the agents causing transmissible spongiform encephalopathies, colonize the brain of hosts after oral, parenteral, intralingual, or even transdermal uptake. However, prions are not generally considered to be airborne.
Johannes Haybaeck   +11 more
doaj   +1 more source

Stage‐Dependent β‐Synuclein Links MRI and Cognitive Decline in Alzheimer's Disease

open access: yesAnnals of Clinical and Translational Neurology, EarlyView.
ABSTRACT Objective Synaptic degeneration drives cognitive decline in Alzheimer's disease (AD), but synaptic biomarkers are scarce. Brain‐enriched β‐synuclein emerged as a synaptic damage marker. We investigated its diagnostic, prognostic, and structural correlates across the AD continuum.
Ulaş Ay   +15 more
wiley   +1 more source

Prions Ex Vivo: What Cell Culture Models Tell Us about Infectious Proteins

open access: yesInternational Journal of Cell Biology, 2013
Prions are unconventional infectious agents that are composed of misfolded aggregated prion protein. Prions replicate their conformation by template-assisted conversion of the endogenous prion protein PrP.
Sybille Krauss, Ina Vorberg
doaj   +1 more source

The Way forward for the Origin of Life: Prions and Prion-Like Molecules First Hypothesis

open access: yesLife, 2021
In this paper the hypothesis that prions and prion-like molecules could have initiated the chemical evolutionary process which led to the eventual emergence of life is reappraised.
Sohan Jheeta   +3 more
doaj   +1 more source

Structural Polymorphism of polyG Inclusions Revealed by In Situ Cryo‐Electron Tomography

open access: yesAdvanced Science, EarlyView.
Correlative cryo‐electron tomography in primary cortical neurons and NIID mouse brain tissue reveals that polyG inclusions are interconnected ribbon‐like assemblies rather than canonical amyloid fibrils. Multiple compartment‐specific ribbon states show distinct 26S proteasome accessibility, while cytoplasmic ribbons contact and deform ER‐like ...
Yunwen Qian   +12 more
wiley   +1 more source

Distinct patterns of prion strain deposition and toxicity in a novel whole brain organotypic slice culture system

open access: yesScientific Reports
Prion diseases are fatal transmissible neurodegenerative diseases that affect many mammals, including humans, caused by the templated misfolding of the prion protein.
Hailey Pineau, Valerie L. Sim
doaj   +1 more source

Improving the Predictive Value of Prion Inactivation Validation Methods to Minimize the Risks of Iatrogenic Transmission With Medical Instruments

open access: yesFrontiers in Bioengineering and Biotechnology, 2020
Prions are pathogenic infectious agents responsible for fatal, incurable neurodegenerative diseases in animals and humans. Prions are composed exclusively of an aggregated and misfolded form (PrPSc) of the cellular prion protein (PrPC).
Mohammed Moudjou   +9 more
doaj   +1 more source

A Phosphorylation‐Induced Micellization Switch in the Low‐Complexity Domain of TDP‐43

open access: yesAdvanced Science, EarlyView.
Phosphorylation of TAR DNA‐binding protein's 43 kDa (TDP‐43) low‐complexity domain by casein kinase 1 delta (CK1δ) acts as a molecular switch, redirecting its self‐assembly from macroscopic phase separation toward finite‐sized, spherical block‐copolymer micelles of ∼30 nm.
Rodrigo F. Dillenburg   +16 more
wiley   +1 more source

Native PLGA nanoparticles attenuate Aβ-seed induced tau aggregation under in vitro conditions: potential implication in Alzheimer’s disease pathology

open access: yesScientific Reports
Evidence suggests that beta-amyloid (Aβ)-induced phosphorylation/aggregation of tau protein plays a critical role in the degeneration of neurons and development of Alzheimer’s disease (AD), the most common cause of dementia affecting the elderly ...
Pallabi Sil Paul   +9 more
doaj   +1 more source

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