Scutellarin inhibits the uninduced and metal-induced aggregation of α-Synuclein and disaggregates preformed fibrils: implications for Parkinson's disease

نویسندگان
چکیده

برای دانلود باید عضویت طلایی داشته باشید

برای دانلود متن کامل این مقاله و بیش از 32 میلیون مقاله دیگر ابتدا ثبت نام کنید

اگر عضو سایت هستید لطفا وارد حساب کاربری خود شوید

منابع مشابه

Rifampicin Inhibits -Synuclein Fibrillation and Disaggregates Fibrils

mentia development if they had been under antileprosy The aggregation of -synuclein in dopaminergic neutreatment with dapsone or rifampicin (Figure 1) and rons of the substantia nigra is a critical step in the closely related drugs for the preceding several years pathogenesis of Parkinson’s disease. We show that [22, 23]. For example, it has been shown that the overall the antibiotic rifampicin...

متن کامل

The Flavonoid Baicalein Inhibits Fibrillation of -Synuclein and Disaggregates Existing Fibrils*

The aggregation of -synuclein has been implicated as a critical step in the development of Parkinson’s disease. Parkinson’s disease is a progressive neurodegenerative disorder caused by the loss of dopaminergic neurons from the substantia nigra; currently, no cure exists. Baicalein is a flavonoid with antioxidant properties; upon oxidation, it forms several products including quinones. We show ...

متن کامل

Endosulfine-alpha inhibits membrane-induced α-synuclein aggregation and protects against α-synuclein neurotoxicity

Neuropathological and genetic findings suggest that the presynaptic protein α-synuclein (aSyn) is involved in the pathogenesis of synucleinopathy disorders, including Parkinson's disease (PD), dementia with Lewy bodies (DLB) and multiple system atrophy. Evidence suggests that the self-assembly of aSyn conformers bound to phospholipid membranes in an aggregation-prone state plays a key role in a...

متن کامل

Sumoylation inhibits α-synuclein aggregation and toxicity

Posttranslational modification of proteins by attachment of small ubiquitin-related modifier (SUMO) contributes to numerous cellular phenomena. Sumoylation sometimes creates and abolishes binding interfaces, but increasing evidence points to another role for sumoylation in promoting the solubility of aggregation-prone proteins. Using purified α-synuclein, an aggregation-prone protein implicated...

متن کامل

Membrane Lipid Co-Aggregation with α-Synuclein Fibrils

Amyloid deposits from several human diseases have been found to contain membrane lipids. Co-aggregation of lipids and amyloid proteins in amyloid aggregates, and the related extraction of lipids from cellular membranes, can influence structure and function in both the membrane and the formed amyloid deposit. Co-aggregation can therefore have important implications for the pathological consequen...

متن کامل

ذخیره در منابع من


  با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید

ژورنال

عنوان ژورنال: Biochemical Journal

سال: 2020

ISSN: 0264-6021,1470-8728

DOI: 10.1042/bcj20190705