Inhibition of toxic metal-alpha synuclein interactions by human serum albumin
Human serum albumin (HSA), the most abundant protein in plasma and cerebrospinal fluid,
not only serves as a crucial carrier of various exogenous and endogenous ligands but also …
not only serves as a crucial carrier of various exogenous and endogenous ligands but also …
Interaction of α-synuclein with divalent metal ions reveals key differences: A link between structure, binding specificity and fibrillation enhancement
The aggregation of α-synuclein (AS) is characteristic of Parkinson's disease and other
neurodegenerative synucleinopathies. Interactions with metal ions affect dramatically the …
neurodegenerative synucleinopathies. Interactions with metal ions affect dramatically the …
Metal interactions of α-synuclein probed by NMR amide-proton exchange
The aberrant aggregation of α-synuclein (αS), a disordered protein primarily expressed in
neuronal cells, is strongly associated with the underlying mechanisms of Parkinson's …
neuronal cells, is strongly associated with the underlying mechanisms of Parkinson's …
Copper (I)-α-synuclein interaction: structural description of two independent and competing metal binding sites
F Camponeschi, D Valensin, I Tessari… - Inorganic …, 2013 - ACS Publications
The aggregation of α-synuclein (αS) is a critical step in the etiology of Parkinson's disease.
Metal ions such as copper and iron have been shown to bind αS, enhancing its fibrillation …
Metal ions such as copper and iron have been shown to bind αS, enhancing its fibrillation …
Differential effects of Cu2+ and Fe3+ ions on in vitro amyloid formation of biologically-relevant α-synuclein variants
Alterations in metal ion homeostasis appear coupled to neurodegenerative disorders but
mechanisms are unknown. Amyloid formation of the protein α-synuclein in brain cells is a …
mechanisms are unknown. Amyloid formation of the protein α-synuclein in brain cells is a …
[HTML][HTML] Understanding the effect of the membrane-mimetic micelles on the interplay between α-synuclein and Cu (II)/Cu (I) cations
AB Uceda, R Ramis, K Pauwels, M Adrover… - Journal of Inorganic …, 2023 - Elsevier
Abstract α-Synuclein (αS) is a presynaptic protein whose aggregates are considered as a
hallmark of Parkinson's disease (PD). Although its physiological function is still under …
hallmark of Parkinson's disease (PD). Although its physiological function is still under …
Site-specific interactions of Cu (II) with α and β-synuclein: Bridging the molecular gap between metal binding and aggregation
The aggregation of α-synuclein (AS) is a critical step in the etiology of Parkinson's disease
(PD) and other neurodegenerative synucleinopathies. Protein− metal interactions play a …
(PD) and other neurodegenerative synucleinopathies. Protein− metal interactions play a …
Copper2+ Binding to α-Synuclein. Histidine50 Can Form a Ternary Complex with Cu2+ at the N-Terminus but Not a Macrochelate
Y Tian, HF Stanyon, JD Barritt, U Mayet… - Inorganic …, 2019 - ACS Publications
α-Synuclein (αSyn) forms amyloid fibrils in the neurons of Parkinson's disease (PD) patients'.
Despite a role for Cu2+ in accelerating αSyn fibril formation, coupled with reports of copper …
Despite a role for Cu2+ in accelerating αSyn fibril formation, coupled with reports of copper …
Effects of the toxic metals arsenite and cadmium on α-synuclein aggregation in vitro and in cells
Exposure to heavy metals, including arsenic and cadmium, is associated with
neurodegenerative disorders such as Parkinson's disease. However, the mechanistic details …
neurodegenerative disorders such as Parkinson's disease. However, the mechanistic details …
[HTML][HTML] Zinc ions prevent α-synuclein aggregation by enhancing chaperone function of human serum albumin
S Al-Harthi, V Kharchenko, P Mandal… - International Journal of …, 2022 - Elsevier
Metal ions present in cellular microenvironment have been implicated as drivers of
aggregation of amyloid forming proteins. Zinc (Zn 2+) ions have been reported to directly …
aggregation of amyloid forming proteins. Zinc (Zn 2+) ions have been reported to directly …