Results 41 to 50 of about 49,072 (180)

p300 Degradation by the p53‐SIAH1 Axis Relieves TBK1 Acetylation to Enhance Innate Antiviral Immunity

open access: yesAdvanced Science, EarlyView.
This study identifies p300 as the acetyltransferase that acetylates TBK1 and inhibits its phosphorylation. Activation of the p53‐SIAH1 axis by immune response downregulates p300 expression to sustain innate antiviral immunity. Conditional p300 knockout in alveolar epithelial cells in vivo promotes antiviral responses and suppresses virus replication ...
Huidi Yu   +6 more
wiley   +1 more source

Deposition pattern and subcellular distribution of disease-associated prion protein in cerebellar organotypic slice cultures infected with scrapie

open access: yesFrontiers in Neuroscience, 2015
Organotypic cerebellar slices represent a suitable model for characterizing and manipulating prion replication in complex cell environments. Organotypic slices recapitulate prion pathology and are amenable to drug testing in the absence of a blood-brain ...
Hanna eWolf   +7 more
doaj   +1 more source

[PSI+] maintenance is dependent on the composition, not primary sequence, of the oligopeptide repeat domain. [PDF]

open access: yesPLoS ONE, 2011
[PSI(+)], the prion form of the yeast Sup35 protein, results from the structural conversion of Sup35 from a soluble form into an infectious amyloid form.
James A Toombs   +4 more
doaj   +1 more source

A Phase‐Resolved Geometric Deep Learning Framework Maps Structural Determinants of Disease‐Associated Protein Aggregation and Guides Suppressor Design

open access: yesAdvanced Science, EarlyView.
SKALE 2.0 maps disease‐associated protein aggregation as a phase‐resolved structural process, linking mutation‐induced geometric perturbations to nucleation, elongation, and suppressor design. Across neurodegenerative proteins, the framework reveals cryptic aggregation vulnerabilities, separates phase‐concordant and phase‐switching mutations, and ...
Jia Shen Sio   +6 more
wiley   +1 more source

Prion strains depend on different endocytic routes for productive infection

open access: yesScientific Reports, 2017
Prions are unconventional agents composed of misfolded prion protein that cause fatal neurodegenerative diseases in mammals. Prion strains induce specific neuropathological changes in selected brain areas. The mechanism of strain-specific cell tropism is
Andrea Fehlinger   +12 more
doaj   +1 more source

Intraperitoneal Infection of Wild-Type Mice with Synthetically Generated Mammalian Prion. [PDF]

open access: yesPLoS Pathogens, 2015
The prion hypothesis postulates that the infectious agent in transmissible spongiform encephalopathies (TSEs) is an unorthodox protein conformation based agent.
Xinhe Wang   +6 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

Ayer, Hoy y Mañana, La Teoría del Prión.

open access: yesMedicina, 2004
<p><span><strong>(Reproducido con autorización de Acta Neurológica Colombiana Vol. 18 No. 4, 2002).</strong></span></p><h3>Introducción</h3><p>La creencia mejor respaldada actualmente nos indica que ...
Gabriel Toro González   +2 more
doaj  

RNA-seq and network analysis reveal unique glial gene expression signatures during prion infection

open access: yesMolecular Brain, 2020
Background Prion diseases and prion-like disorders, including Alzheimer’s disease and Parkinson’s disease, are characterized by gliosis and accumulation of misfolded aggregated host proteins.
James A. Carroll   +4 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

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