Every reference with a DOI in the deposited reference list resolved to a known
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The 90 checked references that resolve
resolves10.1007/BF00493487Histochemical demonstration of copper in normal rat brain and spinal cord
resolves10.1007/s10653-011-9373-7Bioelements and mineral matter in human livers from the highly industrialized region of the Upper Silesia Coal Basin (Poland)
resolves10.1042/CS20150153Copper dyshomoeostasis in Parkinson's disease: implications for pathogenesis and indications for novel therapeutics
resolves10.14336/AD.2017.1018Superoxide Radical Dismutation as New Therapeutic Strategy in Parkinson’s Disease
resolves10.1002/mds.870080116Parkinson's disease mortality and the industrial use of heavy metals in Michigan
resolves10.1212/WNL.48.3.650Occupational exposures to metals as risk factors for Parkinson's disease
resolves10.1002/jat.1460Mechanisms underlying the inhibition of the cytochrome P450 system by copper ions
resolves10.1016/0006-2952(85)90710-5Effects of heavy metal cations, sulfhydryl reagents and other chemical agents on striatal D2 dopamine receptors
resolves10.1002/mds.26103Presynaptic effects of levodopa and their possible role in dyskinesia
resolves10.1002/anie.201811122Dopamine, Oxidative Stress and Protein–Quinone Modifications in Parkinson's and Other Neurodegenerative Diseases
resolves10.1039/C2MT20151HLocalization of copper and copper transporters in the human brain
resolves10.1073/pnas.1009932108Calcium-dependent copper redistributions in neuronal cells revealed by a fluorescent copper sensor and X-ray fluorescence microscopy
resolves10.1089/ars.2015.6343Alpha-Synuclein Oligomers Interact with Metal Ions to Induce Oxidative Stress and Neuronal Death in Parkinson's Disease
resolves10.1007/s10571-018-0587-4Parkinson Disease from Mendelian Forms to Genetic Susceptibility: New Molecular Insights into the Neurodegeneration Process
resolves10.1096/fj.08-119784Structural insights on physiological functions and pathological effects of ±‐synuclein
resolves10.1074/jbc.M105343200Metal-triggered Structural Transformations, Aggregation, and Fibrillation of Human α-Synuclein
resolves10.1021/ja0618649Interaction of α-Synuclein with Divalent Metal Ions Reveals Key Differences: A Link between Structure, Binding Specificity and Fibrillation Enhancement
resolves10.1039/C7MT00046DCross talk between neurometals and amyloidogenic proteins at the synapse and the pathogenesis of neurodegenerative diseases
resolves10.1039/c6mt00026fAlpha-synuclein: relating metals to structure, function and inhibition
resolves10.1073/pnas.0407881102Structural characterization of copper(II) binding to α-synuclein: Insights into the bioinorganic chemistry of Parkinson's disease
resolves10.1016/j.bbrc.2007.05.060Thermodynamics imprinting reveals differential binding of metals to α-synuclein: Relevance to parkinson’s disease
resolves10.1021/ja107842fExploring the Structural Details of Cu(I) Binding to α-Synuclein by NMR Spectroscopy
resolves10.1021/ja103338nStructural Characterization of a High Affinity Mononuclear Site in the Copper(II)-α-Synuclein Complex
resolves10.1021/bi101912qCoordination Features and Affinity of the Cu<sup>2+</sup> Site in the α-Synuclein Protein of Parkinson’s Disease
resolves10.1021/ic302050mCopper(I)-α-Synuclein Interaction: Structural Description of Two Independent and Competing Metal Binding Sites
resolves10.1074/jbc.M600933200Phosphorylation of Ser-129 Is the Dominant Pathological Modification of α-Synuclein in Familial and Sporadic Lewy Body Disease
resolves10.1038/nature10324α-Synuclein occurs physiologically as a helically folded tetramer that resists aggregation
resolves10.1002/pro.2088N‐terminal acetylation of α‐synuclein induces increased transient helical propensity and decreased aggregation rates in the intrinsically disordered monomer
resolves10.1021/bi300642hImpact of N-Terminal Acetylation of α-Synuclein on Its Random Coil and Lipid Binding Properties
resolves10.1074/jbc.M113.512459N-terminal Acetylation Stabilizes N-terminal Helicity in Lipid- and Micelle-bound α-Synuclein and Increases Its Affinity for Physiological Membranes
resolves10.1021/jacs.5b01911Copper Binding to the N-Terminally Acetylated, Naturally Occurring Form of Alpha-Synuclein Induces Local Helical Folding
resolves10.1021/acs.biochem.6b00708Copper Binding and Subsequent Aggregation of α-Synuclein Are Modulated by N-Terminal Acetylation and Ablated by the H50Q Missense Mutation
resolves10.1039/c1mt00106jRole of metal ions in aggregation of intrinsically disordered proteins in neurodegenerative diseases
resolves10.1007/s12017-009-8082-1Interaction Between α-Synuclein and Metal Ions, Still Looking for a Role in the Pathogenesis of Parkinson’s Disease
resolves10.1017/S0317167100029140Regional Metal Concentrations in Parkinson's Disease, Other Chronic Neurological Diseases, and Control Brains
resolves10.1002/ana.23817Ceruloplasmin dysfunction and therapeutic potential for Parkinson disease
resolves10.1093/ajcn/67.5.972SAceruloplasminemia: an inherited neurodegenerative disease with impairment of iron homeostasis
resolves10.1196/annals.1306.024Aceruloplasminemia: An Inherited Neurodegenerative Disease with Impairment of Iron Homeostasis
resolves10.1007/s00401-017-1726-6Amyotrophic lateral sclerosis-like superoxide dismutase 1 proteinopathy is associated with neuronal loss in Parkinson’s disease brain
resolves10.1007/BF00571500Cu/Zn superoxide dismutase-like immunoreactivity is present in Lewy bodies from Parkinson disease: a light and electron microscopic immunocytochemical study
resolves10.1002/elps.201500187Reduced net charge and heterogeneity of p<i>I</i> isoforms in familial amyotrophic lateral sclerosis mutants of copper/zinc superoxide dismutase
resolves10.1038/s41598-017-01402-2Brain iron chelation by deferiprone in a phase 2 randomised double-blinded placebo controlled clinical trial in Parkinson’s disease
resolves10.1007/s00702-006-0499-1The copper chelator, D-penicillamine, does not attenuate MPTP induced dopamine depletion in mice
resolves10.1016/j.jinorgbio.2017.02.020A moderate metal-binding hydrazone meets the criteria for a bioinorganic approach towards Parkinson's disease: Therapeutic potential, blood-brain barrier crossing evaluation and preliminary toxicological studies
resolves10.1523/JNEUROSCI.4196-13.2014Oral Treatment with CuII(atsm) Increases Mutant SOD1 In Vivo but Protects Motor Neurons and Improves the Phenotype of a Transgenic Mouse Model of Amyotrophic Lateral Sclerosis
resolves10.1016/j.nbd.2016.01.020Copper delivery to the CNS by CuATSM effectively treats motor neuron disease in SODG93A mice co-expressing the Copper-Chaperone-for-SOD
resolves10.1038/srep42292CuII(atsm) improves the neurological phenotype and survival of SOD1G93A mice and selectively increases enzymatically active SOD1 in the spinal cord
resolves10.1039/b705989bCu–ATSM: A radiopharmaceutical for the PET imaging of hypoxia
resolves10.1016/j.nucmedbio.2011.08.008Radiolabeled Cu-ATSM as a novel indicator of overreduced intracellular state due to mitochondrial dysfunction: studies with mitochondrial DNA-less ρ0 cells and cybrids carrying MELAS mitochondrial DNA mutation
resolves10.1084/jem.20112285The hypoxia imaging agent CuII(atsm) is neuroprotective and improves motor and cognitive functions in multiple animal models of Parkinson’s disease
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