突触核蛋白

表达蛋白经Western杂交证实为a-突触核蛋白。

The expressing proteins of α synuclein were confirmed by Western blot analysis .

α-突触核蛋白N-端结构域参与线粒体功能的调控

N-terminal of α - Synuclein Involved in Regulation of Mitochondrial Function

CHIP可以作为α-突触核蛋白蛋白酶体降解途径和溶酶体降解途径的分子开关。

CHIP acts as a molecular switch between proteasomal and lysosomal degradation pathways .

RNA干扰α-突触核蛋白对多巴胺能神经元的影响及其机制

Effect and Its Mechanism of α - Synuclein Knockdown on Dopaminergic Neurons in Parkinson 's Disease in Vitro Model

本研究结果表明铁可以通过氧化应激和IRE/IRP调控系统增加alpha-突触核蛋白的表达，诱导alpha-突触核蛋白聚集，继而导致DA能细胞的损伤和死亡。

Iron could cause the death of dopaminergic neurons by inducing alpha-synuclein expression and aggregation through IRE / IRP system and oxidative stress .

分子伴侣DJ-1与小肽协同抑制α-突触核蛋白的聚集

Interaction of DJ-1 with Small Peptide to Inhibit the Aggregation of Alpha-synuclein in E.coli

优化人α-突触核蛋白核酸疫苗免疫MPTP帕金森病小鼠的神经保护作用及其机制研究

The Neuroprotective Effects and Mechanism of Optimized α - Synuclein DNA Vaccine Immunize MPTP Inducing on Chronic Mouse Model of Parkinson 's Disease

目的观察蛋白酶体抑制剂诱导大鼠黑质多巴胺能神经元α-突触核蛋白（-αsynuclein，-αSyn）的表达及聚集，探讨蛋白酶体功能在帕金森病（PD）发病中的作用机制。

Objective To investigate α - synuclein expression and aggregation in dopaminergic neurons of rat substantia nigra exposed to proteasome inhibition for the role of proteasome function in the pathogenesis of Parkinson disease .

α-突触核蛋白磷酸化参与小鼠多巴胺能神经元的保护作用

α - Synuclein phosphorylation takes part in mouse dopaminergic neuron protection

帕金森病模型鼠黑质α-突触核蛋白表达升高并集聚

Up-regulation and aggregation of α - synuclein in mouse model of parkinsonism

神经突触核蛋白的生物学特性及其与肿瘤关系的研究进展

Research Progress in Biological Characteristics of Synuclein and Its Correlation with Cancer

α-突触核蛋白促进大鼠原代培养神经元突起生长

α - Synuclein Promotes Neurite Outgrowth of Primarily Cultured Rat Brain Neurons

锰对大鼠大脑α-突触核蛋白表达的影响

Manganese alters α - synuclein expression in rat brain

纳入标准为：①与α-突触核蛋白的作用有关。

Inclusive criteria : ① relevant to the role of α - synuclein ;

帕金森病患者血清对α-突触核蛋白寡聚体形成的促进作用

Enhanced Oligomerization of α - Synuclein in Sera of Patients with Parkinson 's Disease

结论：α-突触核蛋白与线粒体之间存在复杂的相互作用。

CONCLUSION : There is a complex interplay between α - synuclein and mitochondria .

原子力显微镜检测过表达α-突触核蛋白引起的线粒体结构变化

The Influence of α - Synuclein Overexpression on Mitochondrial Membrane Structure with Atomic Force Microscopy

重复急性低氧对小鼠大脑皮质中α-突触核蛋白表达的影响

Effect of repeated acute hypoxic treatment on the expression of a-synuclein in the mouse brain cortex

安坦对帕金森病大鼠脑内突触素和α-突触核蛋白的影响

Expression of Synaptophysin and α - Synuclein in the Brains of Parkinson Disease Rats with Trihexyphenidyl

近年来人们发现铁能够促进alpha-突触核蛋白的聚集，但具体机制还不清楚。

Studies have found that iron could promote alpha-synuclein aggregation , but the exact mechanism is largely unknown .

组蛋白脱乙酰化酶在α-突触核蛋白抑制酪氨酸羟化酶表达中的作用

Histone Deacetylase Maybe Involved in the Mechanism of Inhibition of Tyrosine Hydroxylase Expression in α - Synuclein-Transfected Dopaminergic Neuronal Cells

老年神经变性疾病蛋白基因研究：3种α-突触核蛋白提取纯化方法的比较

Protein and gene of neural degeneration disease in the elderly : comparison of three methods to extract and purify alpha-synuclein

另有实验证实Fe2+和Fe3+可在体外及细胞内促进alpha-突触核蛋白的聚集。

It has been found that high concentration of ferrous and ferric iron can promote alpha-synuclein aggregation in vivo and in vitro .

以往的研究证明α-突触核蛋白是一种在神经退行性病变中起关键作用的毒性蛋白。

Early studies had shown that α - synuclein was a toxic protein which played a key role in the process of neurodegeneration .

在神经细胞核内，靠近核膜部分α突触核蛋白的分布较为密集，细胞核中心部位α突触核蛋白则较为稀疏。在胞浆和轴突中，α突触核蛋白散在分布。

In the nucleus , there was a more dense distribution of α - synuclein inside the nuclear membrane , but a sparse distribution in the center ,α - synuclein scattered in the axons and cytoplasm .