Results 51 to 60 of about 61,554 (301)

Associations of sleep characteristics with alpha‐synuclein in cerebrospinal fluid in older adults

open access: yesAnnals of Clinical and Translational Neurology, 2020
Objective Sleep disorders as a preclinical symptom of synucleinopathies become more prevalent in older adults. Synucleinopathies might be caused by the abnormal aggregation of alpha‐synuclein in the brain, which was indicated by alpha‐synuclein levels in
Xiao‐Tong Wang   +7 more
doaj   +1 more source

Functional and neuropathological changes induced by injection of distinct alpha-synuclein strains: A pilot study in non-human primates

open access: yesNeurobiology of Disease, 2023
The role of alpha-synuclein in Parkinson's disease has been heavily investigated since its discovery as a component of Lewy bodies. Recent rodent data demonstrate that alpha-synuclein strain structure is critical for differential propagation and toxicity.
Audrey Fayard   +15 more
doaj   +1 more source

Parkinson's disease (PD) is the most common neurodegenerative disease

open access: yesУчёные записки Санкт-Петербургского государственного медицинского университета им. Акад. И.П. Павлова, 2015
Metabolic impairment of alpha-synuclein protein is considered to be the central event in PDpathogenesis. Recent studies explored usage of alpha-synuclein in peripheral fluids as a biomarker of PD, however alpha-synuclein level in the CSF and plasma is ...
P. A. Andoskin   +7 more
doaj   +1 more source

The role of glyoxalases for sugar stress and aging, with relevance for dyskinesia, anxiety, dementia and Parkinson's disease [PDF]

open access: yes, 2011
Commentary on: Scheckhuber CQ et al. Modulation of the glyoxalase system in the aging model Podospora anserina: effects on growth and lifespan. Aging.
Auburger, Georg, Kurz, Alexander
core   +1 more source

Intercellular transmission of alpha-synuclein [PDF]

open access: yesFrontiers in Molecular Neuroscience
An emerging theme in Parkinson’s disease (PD) is the propagation of α-synuclein pathology as the disease progresses. Research involving the injection of preformed α-synuclein fibrils (PFFs) in animal models has recapitulated the pathological spread observed in PD patients.
Wu, Shenjie, Schekman, Randy
openaire   +4 more sources

Deciphering transcriptional plasticity in pancreatic ductal adenocarcinoma reveals alterations in sensory neuron innervation

open access: yesMolecular Oncology, EarlyView.
Pancreatic sensory neurons innervating healthy and PDAC tissue were retrogradely labeled and profiled by single‐cell RNA sequencing. Tumor‐associated innervation showed a dominant neurofilament‐positive subtype, altered mitochondrial gene signatures, and reduced non‐peptidergic neurons.
Elena Genova   +14 more
wiley   +1 more source

Electron microscopy analysis of alpha-synuclein and LRRK2 transgenic C. elegans [PDF]

open access: yes, 2013
Thesis (M.A.)--Boston UniversityMutations in alpha-synuclein and leucine-rich repeat kinase 2 (LRRK2) have been implicated in the cause of Parkinson’s disease (PD).
Nguyen, Andrew Huy
core   +1 more source

Chameleon sequences reveal structural effects in proteins representing micelle‐like distribution of hydrophobicity

open access: yesFEBS Open Bio, EarlyView.
Amino acids sequence of two different proteins with the same sequence (chameleon sequence—black boxes) represent in 3D structure of the proteins different secondary structures: HHHH—helical and BBB—Beta‐structural. The chains folded in water environment adopt different III‐order structures in which the chameleon fragments appear to adopt similar status
Irena Roterman   +4 more
wiley   +1 more source

Transcriptional regulation of the beta-synuclein 5'-promoter metal response element by metal transcription factor-1.

open access: yesPLoS ONE, 2011
The progression of many human neurodegenerative disorders is associated with an accumulation of alpha-synuclein. Alpha-synuclein belongs to the homologous synuclein family, which includes beta-synuclein.
Patrick C McHugh   +2 more
doaj   +1 more source

Large‐scale bidirectional arrayed genetic screens identify OXR1 and EMC4 as modifiers of αSynuclein aggregation

open access: yesFEBS Open Bio, EarlyView.
Activation of the mitochondrial protein OXR1 increases pSyn129 αSynuclein aggregation by lowering ATP levels and altering mitochondrial membrane potential, particularly in response to MSA‐derived fibrils. In contrast, ablation of the ER protein EMC4 enhances autophagic flux and lysosomal clearance, broadly reducing α‐synuclein aggregates.
Sandesh Neupane   +11 more
wiley   +1 more source

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