техническая эксплуатация автомобилей курсовая работа
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техническая эксплуатация автомобилей курсовая работа, Alpha-synuclein - Wikipedia, Alpha-synuclein structure, functions, and interactions - PMC, Alpha Synuclein - The Science of Parkinson's, Alpha-synuclein in Parkinson’s disease and other - Nature, Physiology, Synuclein - StatPearls - NCBI Bookshelf, Alpha-Synuclein (α-syn) - Physiopedia, Explainer: What is alpha-synuclein? – Van Andel Institute.
Oxidative stress in dopaminergic neurons could initiate the pathological damage leading to PD. This damage is triggered by oxidation of unsaturated phospholipids that consequently damage both cellular and intracellular membranes. The sensitivity of dopaminergic neurons to such damage is caused by the oxidative metabolism of dopamine within these cells. Therefore, dopaminergic cell membranes that are rich in unsaturated fatty acids are more vulnerable to this oxidation and damage. The monomeric form of α-syn by interaction with lipid membranes can protect lipids from oxidation, but the fibrillar form of α-syn does not have this capability. Therefore, it seems that monomeric α-syn could act as an antioxidant that plays an important role in dopaminergic neurons to protect them against oxidative damage.[] Another study suggests that maybe α-syn is not an antioxidant but can prevent apoptosis by binding to cytochrome c oxidase in mitochondrial membrane and inhibits release of cytochrome c from mitochondria to cytosol. Consequently, caspases cannot be activated and thus cannot trigger apoptosis.[] Moreover, hydrogen peroxide cannot damage α-syn expressing neural cells while it is toxic in control cells. Hydrogen peroxide in the absence of α-syn activates c-Jun N-terminal kinase (JNK), a member of mitogen-activated protein kinase (MAPK) family that promotes apoptosis under oxidative stress condition. α-Syn by activation of JNK-interacting protein/islet-brain (JIP-1b/IB1) as an inhibitor of JNK pathway may protect cells from injury.[]Neuronal differentiation, Alpha-synuclein (aSyn) is a protein that in humans is encoded by the SNCA gene. [5] It is a neuronal protein involved in the regulation of synaptic vesicle trafficking and the release of neurotransmitters. [6] [7] Alpha-synuclein is abundant in the brain, with smaller amounts present in the heart, muscles, and other tissues., As a molecular biomarker for the detection of PD in its earlier stages, alpha-synuclein (α-syn), which is a key component of Lewy bodies, in which it is found in an aggregated and fibrillar form, has attracted considerable attention..
Alpha-synuclein is a protein. Proteins make up the many pieces of machinery inside each cell that makes our brains work. In order for each protein to function properly, they must be folded into the correct shape when they are first made., In this review, we will discuss these critical issues, providing a state of the art of the role of this protein in early PD and other synucleinopathies. Alpha-synuclein aggregates perturb, Alpha-synuclein is the product of the SNCA gene. It is a small protein that occurs in neurons near synaptic vesicles within presynaptic terminals. Recent studies have shown that alpha-synuclein functions in synaptic vesicle recycling, but the exact mechanism is unclear., Alpha-synuclein (α-syn) is a small protein encoded by the SNCA gene (the gene that provides instructions for α-syn). It is amply expressed in the nervous system and exists in a natively unfolded state under normal physiological conditions (however its conformation changes depending on its environment and interactions with binding partners)., Alpha-synuclein (α-synuclein) is a protein most known for its involvement in Parkinson’s disease. We have α-synuclein throughout our tissues, with the highest concentrations found in the brain. Although the exact function of α-synuclein is not fully understood, evidence suggests it is involved in the release of neurotransmitters in the brain., Alpha-synuclein is a small, 140-residue presynaptic peripheral membrane protein of indeterminate function that is genetically and pathologically linked to Parkinson’s disease (PD). The membrane-binding domain of alpha-synuclein consists of its N-terminal ~100 residues..