Copper(II)-induced self-oligomerization of alpha-synuclein.
about
Curcumin and its derivatives: their application in neuropharmacology and neuroscience in the 21st centuryUntangling the Manganese-α-Synuclein WebNeuronal response in Alzheimer's and Parkinson's disease: the effect of toxic proteins on intracellular pathwaysCatecholamine autotoxicity. Implications for pharmacology and therapeutics of Parkinson disease and related disordersMechanisms of cholinesterase inhibition by inorganic mercuryThe Synaptic Function of α-SynucleinProtein-metal interactions of calmodulin and alpha-synuclein monitored by selective noncovalent adduct protein probing mass spectrometry.MOAG-4 promotes the aggregation of α-synuclein by competing with self-protective electrostatic interactions.Phosphorylation at S87 is enhanced in synucleinopathies, inhibits alpha-synuclein oligomerization, and influences synuclein-membrane interactionsSelf-oligomerization and protein aggregation of alpha-synuclein in the presence of Coomassie Brilliant Blue.Copper-triggered aggregation of ubiquitin.Alpha-synuclein in Lewy body disease and Alzheimer's disease.Divalent metal ions enhance DOPAL-induced oligomerization of alpha-synuclein.Alpha-synuclein is a cellular ferrireductase.Transcriptional regulation of the beta-synuclein 5'-promoter metal response element by metal transcription factor-1.Structural characterization of copper(II) binding to alpha-synuclein: Insights into the bioinorganic chemistry of Parkinson's disease.α-Synuclein in central nervous system and from erythrocytes, mammalian cells, and Escherichia coli exists predominantly as disordered monomerNeuropathology, biochemistry, and biophysics of alpha-synuclein aggregation.The crucial role of metal ions in neurodegeneration: the basis for a promising therapeutic strategy.Mechanism of copper(II)-induced misfolding of Parkinson's disease protein.The N Terminus of α-Synuclein Forms Cu(II)-Bridged Oligomers.Phosphorylation of α-Synuclein at Y125 and S129 alters its metal binding properties: implications for understanding the role of α-Synuclein in the pathogenesis of Parkinson's Disease and related disordersStructural changes in alpha-synuclein affect its chaperone-like activity in vitro.Interactions between metals and alpha-synuclein--function or artefact?Spermine binding to Parkinson's protein alpha-synuclein and its disease-related A30P and A53T mutantsCopper(II) binding to alpha-synuclein, the Parkinson's protein.Bivalent Copper Ions Promote Fibrillar Aggregation of KCTD1 and Induce CytotoxicityTargeting the progression of Parkinson's disease.Copper and copper proteins in Parkinson's disease.Insight into α-synuclein plasticity and misfolding from differential micelle binding.Antioxidant gene therapy against neuronal cell death.Metallothionein, Copper and Alpha-Synuclein in Alpha-Synucleinopathies.Metalloproteins and neuronal death.Insights into the thermodynamics of copper association with amyloid-β, α-synuclein and prion proteins.The potential application of iron chelators for the treatment of neurodegenerative diseases.Metal-mediated targeting in the body.The function of α-synuclein.Protein phosphorylation in neurodegeneration: friend or foe?Can the propensity of protein crystallization be increased by using systematic screening with metals?Implication of Alpha-Synuclein Phosphorylation at S129 in Synucleinopathies: What Have We Learned in the Last Decade?
P2860
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P2860
Copper(II)-induced self-oligomerization of alpha-synuclein.
description
1999 nî lūn-bûn
@nan
1999年の論文
@ja
1999年論文
@yue
1999年論文
@zh-hant
1999年論文
@zh-hk
1999年論文
@zh-mo
1999年論文
@zh-tw
1999年论文
@wuu
1999年论文
@zh
1999年论文
@zh-cn
name
Copper(II)-induced self-oligomerization of alpha-synuclein.
@en
type
label
Copper(II)-induced self-oligomerization of alpha-synuclein.
@en
altLabel
Copper(II)-induced self-oligomerization of α-synuclein
@en
prefLabel
Copper(II)-induced self-oligomerization of alpha-synuclein.
@en
P2093
P2860
P1433
P1476
Copper(II)-induced self-oligomerization of alpha-synuclein
@en
P2093
P2860
P304
P356
10.1042/0264-6021:3400821
P407
P478
340 ( Pt 3)
P50
P577
1999-06-01T00:00:00Z