نتایج جستجو برای: syn
تعداد نتایج: 6081 فیلتر نتایج به سال:
Lewy bodies (LBs) are intraneuronal inclusions consisting primarily of fibrillized human α-synuclein (hα-Syn) protein, which represent the major pathological hallmark of Parkinson's disease (PD). Although doubling hα-Syn expression provokes LB pathology in humans, hα-Syn overexpression does not trigger the formation of fibrillar LB-like inclusions in mice. We hypothesized that interactions betw...
A pre-phylogenetic revision of the family Phalacridae at the genus level is presented. Twenty-eight new generic synonymies are established as follows: Acylomus Sharp 1888 (=Liophalacrus Sharp 1888, syn. nov.; Ganyrus Guillebeau 1894, syn. nov.; Podocesus Guillebeau 1894, syn. nov.; Tinodemus Guillebeau 1894, syn. nov.; Ledorus Guillebeau 1895, syn. nov.; Astenulus Guillebeau 1896, syn. nov.; Af...
We present ANEMONA: a language for distributed network management programming. The compilation of an ANEMONA program generates code for configuring DisMan MIB’s thus automating a complex task that is prone to errors if done manually. The language allows the definition of expressions of managed objects that are monitored, as well as triggers that when fired may indicate the occurrence of associa...
A taxonomic revision of the genus Megalostomis Chevrolat, 1836 (Coleoptera: Chrysomelidae: Cryptocephalinae: Clytrini: Megalostomina) is provided, including new data on geographic ranges. Two new species and 34 new synonymies are proposed within the genus Megalostomis, leaving 42 valid species in the genus. A checklist of the species of Megalostomis is provided, with information on host plants,...
In the healthy brain, less than 5% of α-synuclein (α-syn) is phosphorylated at serine 129 (Ser(P)-129). However, within Parkinson disease (PD) Lewy bodies, 89% of α-syn is Ser(P)-129. The effects of Ser(P)-129 modification on α-syn distribution and solubility are poorly understood. As α-syn normally exists in both membrane-bound and cytosolic compartments, we examined the binding and dissociati...
The choroid plexus maintains the homeostasis of critical molecules in the brain by regulating their transport between the blood and cerebrospinal fluid (CSF). The current study was designed to investigate the potential role of the blood-CSF barrier (BCSFB) in α-synuclein (a-Syn) transport in the brain as affected by exposure to manganese (Mn), the toxic metal implicated in Parkinsonian disorder...
Accumulation of α-synuclein (α-syn) fibrils in Lewy bodies and Lewy neurites is the pathological hallmark of Parkinson disease (PD). Ligands that bind α-syn fibrils could be utilized as imaging agents to improve the diagnosis of PD and to monitor disease progression. However, ligands for α-syn fibrils in PD brain tissue have not been previously identified and the feasibility of quantifying α-sy...
Alpha-synuclein (a-Syn), a protein implicated in Parkinson disease, contributes significantly to dopamine metabolism. a-Syn binding inhibits the activity of tyrosine hydroxylase (TH), the rate-limiting enzyme in catecholamine synthesis. Phosphorylation of TH stimulates its activity, an effect that is reversed by protein phosphatase 2A (PP2A). In cells, a-Syn overexpression activates PP2A. Here ...
Early α-synuclein (α-Syn)-induced alterations are neurite pathologies resulting in Lewy neurites. α-Syn oligomers are a toxic species in synucleinopathies and are suspected to cause neuritic pathology. To investigate how α-Syn oligomers may be linked to aberrant neurite pathology, we modeled different stages of α-Syn aggregation in vitro and investigated the interplay of α-Syn aggregates with p...
Neurodegenerative disorders such as Parkinson's Disease (PD), PD dementia (PDD) and Dementia with Lewy bodies (DLB) are characterized by progressive accumulation of α-synuclein (α-syn) in neurons. Recent studies have proposed that neuron-to-neuron propagation of α-syn plays a role in the pathogenesis of these disorders. We have previously shown that antibodies against the C-terminus of α-syn re...
نمودار تعداد نتایج جستجو در هر سال
با کلیک روی نمودار نتایج را به سال انتشار فیلتر کنید