Results 51 to 60 of about 67,783 (305)

A53T-alpha-synuclein overexpression impairs dopamine signaling and striatal synaptic plasticity in old mice [PDF]

open access: yes, 2010
BACKGROUND: Parkinson's disease (PD), the second most frequent neurodegenerative disorder at old age, can be caused by elevated expression or the A53T missense mutation of the presynaptic protein alpha-synuclein (SNCA). PD is characterized pathologically
Auburger, Georg   +17 more
core   +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

Lenalidomide reduces microglial activation and behavioral deficits in a transgenic model of Parkinson's disease. [PDF]

open access: yes, 2015
BackgroundParkinson's disease (PD) is one of the most common causes of dementia and motor deficits in the elderly. PD is characterized by the abnormal accumulation of the synaptic protein alpha-synuclein (α-syn) and degeneration of dopaminergic neurons ...
Anderson, Scott   +4 more
core   +2 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

SIRT3 Protects Rotenone-induced Injury in SH-SY5Y Cells by Promoting Autophagy through the LKB1-AMPK-mTOR Pathway. [PDF]

open access: yes, 2018
SIRT3 is a class III histone deacetylase that modulates energy metabolism, genomic stability and stress resistance. It has been implicated as a potential therapeutic target in a variety of neurodegenerative diseases, including Parkinson's disease (PD ...
Deng, Yong-Ning   +6 more
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

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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