Results 91 to 100 of about 659,948 (302)

Additional file 5: of Prion-like propagation of human brain-derived alpha-synuclein in transgenic mice expressing human wild-type alpha-synuclein

open access: yes, 2016
Phosphorylated alpha-synuclein in inclusion bodies colocalizes with sequestosome-1/p62.
Maria Bernis (3553610)   +5 more
core   +1 more source

Extracellular Alpha-Synuclein Promotes a Neuroinhibitory Secretory Phenotype in Astrocytes

open access: yes, 2020
Multiple system atrophy (MSA) and dementia with Lewy bodies (DLB) are α-synucleinopathies that exhibit widespread astrogliosis as a component of the neuroinflammatory response.
Ben Greenaway   +17 more
core   +1 more source

A Correlative SICM‐OPM Platform for Surface and Volumetric Imaging in Live Cells

open access: yesAdvanced Science, EarlyView.
A multifunctional correlative imaging platform integrating Scanning Ion Conductance Microscopy (SICM) with Oblique Plane Microscopy (OPM) enables simultaneous surface topography, mechanical mapping, and 3D volumetric fluorescence imaging in live cells.
Wenzhi Hong   +13 more
wiley   +1 more source

Inhibition and Formation of Amyloid Fibrils in the Bulk and at the Interface of Biomolecular Condensates

open access: yesAngewandte Chemie, EarlyView.
In this review, we discuss how biomolecular condensates can inhibit amyloid aggregation in their interior, while still facilitating fibril formation at the interface between the dense and dilute phases, where molecular and mesoscale properties are likely optimal to promote protein aggregation.
Marcell Papp   +3 more
wiley   +2 more sources

Spatiotemporal Control of Formation of Dynamic Protein Fiber Assemblies via Photophysical Effects of a Focused Laser Beam

open access: yesAdvanced Science, EarlyView.
Tightly focused laser irradiation can accumulate tubulin proteins at/around the laser focus, which leads to the formation of highly ordered microtubule assemblies. The assemblies can exhibit various dynamic behaviors such as radial motion, bundling, and flagella‐like rotation with motor protein and chemical energy, highlighting as a unique tool for ...
Hiroshi Y. Yoshikawa   +16 more
wiley   +1 more source

Nigrostriatal dynein changes in A53T alpha-synuclein transgenic mice [v1; ref status: indexed, http://f1000r.es/2wb]

open access: yesF1000Research, 2014
The accumulation of misfolded a-synuclein is mechanistically linked to neurodegeneration in Parkinson’s disease (PD) and other alpha-synucleinopathies. However, how alpha-synuclein causes neurodegeneration is unresolved.
Yan Liu   +5 more
doaj   +1 more source

PRMT9 Aggravated Dopaminergic Neurodegeneration in Parkinson's Disease Model by Facilitating the Degradation of DUSP26 and Inducing Mitochondrial Dysfunction

open access: yesAdvanced Science, EarlyView.
In the pathological state of PD induced by MPP+, the upregulated PRMT9 in dopaminergic neurons translocates into mitochondrion and interacts with DUSP26 and catalyzes its arginine methylation, leading to the ubiquitin‐proteasomal degradation of DUSP26 mediated by Trim32.
Tengfei Liu   +13 more
wiley   +1 more source

Protein-Protein Interactions in Alpha-Synuclein Biogenesis: New Potential Targets in Parkinson’s Disease

open access: yesFrontiers in Aging Neuroscience, 2020
Parkinson’s disease (PD) is a debilitating neurodegenerative disorder defined by a loss of dopamine-producing neurons in the substantia nigra in the brain. It is associated with cytosolic inclusions known as Lewy bodies.
Sarah M. Hernandez   +2 more
doaj   +1 more source

Additional file 2: of Prion-like propagation of human brain-derived alpha-synuclein in transgenic mice expressing human wild-type alpha-synuclein

open access: yes, 2016
Brains of MSA and probable iLBD cases contain phosphorylated alpha-synuclein in the sarkosyl-insoluble fraction.
Maria Bernis (3553610)   +5 more
core   +1 more source

TDP‐43 Aggregation: The Healthy‐Toxic Balance of the Prion‐Like Domain

open access: yesAdvanced Science, EarlyView.
TDP‐43 function relies on a delicate balance between reversible phase‐separated states and irreversible aggregation. Under physiological conditions, TDP‐43 forms dynamic droplets and oligomers that support normal cellular functions. In pathological contexts, this balance shifts toward aberrant aggregation, leading to toxic species.
Luca Zangrando   +2 more
wiley   +1 more source

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