keyword
https://read.qxmd.com/read/33222922/semaglutide-mediated-protection-against-a%C3%AE-correlated-with-enhancement-of-autophagy-and-inhibition-of-apotosis
#1
JOURNAL ARTICLE
Yan-Fang Chang, Di Zhang, Wei-Min Hu, Dong-Xing Liu, Lin Li
BACKGROUND: Semaglutide, a glucagon-like peptide-1 (GLP-1) analogue with an extended half-life of approximately 1 week has being come into clinic trial to treat parkingson's disease but little is known about its effect to prevent against Alzheimer's disease (AD). The goal of the present study was to explore the potential mechanisms of semaglutide to protect against AD. METHODS: We treated SH-SY5Y cell line with Aβ25-35 as an AD model. Further, SH-SY5Y cells damaged by Aβ25-35 were treated by semaglutide...
November 2020: Journal of Clinical Neuroscience: Official Journal of the Neurosurgical Society of Australasia
https://read.qxmd.com/read/25063512/degradation-of-misfolded-proteins-by-autophagy-is-it-a-strategy-for-huntington-s-disease-treatment
#2
REVIEW
Fang Lin, Zheng-Hong Qin
Autophagy is a degradation pathway for long-lived cytoplasmic proteins, protein complexes, or damaged organelles. The accumulation and aggregation of misfolded proteins are hallmarks of several neurodegenerative diseases. Many researchers have reported that autophagy degrades disease-causing misfolded and aggregated proteins, including mutant huntingtin (Htt) in Huntington's disease, mutant synuclein in familial Parkingson's disease, mutant Cu, Zn-Superoxide dismutase (SOD1) in familial amyotrophic lateral sclerosis...
2013: Journal of Huntington's Disease
https://read.qxmd.com/read/23123341/conversion-of-natively-unstructured-%C3%AE-synuclein-to-its-%C3%AE-helical-conformation-significantly-attenuates-production-of-reactive-oxygen-species
#3
JOURNAL ARTICLE
Binbin Zhou, Yuanqiang Hao, Chengshan Wang, Ding Li, You-Nian Liu, Feimeng Zhou
The intracellular α-synuclein (α-syn) protein, whose conformational change and aggregation have been closely linked to the pathology of Parkingson's disease (PD), is highly populated at the presynaptic termini and remains there in the α-helical conformation. In this study, circular dichroism confirmed that natively unstructured α-syn in aqueous solution was transformed to its α-helical conformation upon addition of trifluoroethanol (TFE). Electrochemical and UV-visible spectroscopic experiments reveal that both Cu (I) and Cu (II) are stabilized, with the former being stabilized by about two orders of magnitude...
January 2013: Journal of Inorganic Biochemistry
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