About: Interaction of α-Synuclein with Divalent Metal Ions Reveals Key Differences: A Link between Structure, Binding Specificity and Fibrillation Enhancement

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About: Interaction of α-Synuclein with Divalent Metal Ions Reveals Key Differences: A Link between Structure, Binding Specificity and Fibrillation Enhancement Goto Sponge NotDistinct Permalink

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scientific article published on 01 August 2006

Attributes	Values
rdf:type	Item
description	wetenschappelijk artikel (nl) article scientifique publié en 2006 (fr) наукова стаття, опублікована в серпні 2006 (uk) im August 2006 veröffentlichter wissenschaftlicher Artikel (de) artículu científicu espublizáu n'agostu de 2006 (ast) scientific article published on 01 August 2006 (en)
publication date	wds:Q58484316-59C04271-1F12-438F-9B1B-4EB09D48F167
publication date	2006-08-01 00:00:00Z (xsd:dateTime)
language of work or name	wds:Q58484316-A30AF83E-3793-4CD5-BB7B-75788AA2DAA4
language of work or name	English
author name string	wds:Q58484316-07B79DDE-FE0D-4015-A356-5818593A2CCE wds:Q58484316-4EF16D59-4B4F-4949-9BDE-F8BB19FF384D wds:Q58484316-E2B32375-8F3F-451D-A83C-992F1C215CB4 wds:Q58484316-E3509022-F4E5-49FE-9320-C6A178F6DBC6
author name string	Christian Griesinger Markus Zweckstetter Thomas M Jovin Andrés Binolfi
rdfs:label	Interaction of α-Synuclein with Divalent Metal Ions Reveals Key Differences: A Link between Structure, Binding Specificity and Fibrillation Enhancement (en) Interaction of α-Synuclein with Divalent Metal Ions Reveals Key Differences: A Link between Structure, Binding Specificity and Fibrillation Enhancement (nl)
skos:prefLabel	Interaction of α-Synuclein with Divalent Metal Ions Reveals Key Differences: A Link between Structure, Binding Specificity and Fibrillation Enhancement (en) Interaction of α-Synuclein with Divalent Metal Ions Reveals Key Differences: A Link between Structure, Binding Specificity and Fibrillation Enhancement (nl)
name	Interaction of α-Synuclein with Divalent Metal Ions Reveals Key Differences: A Link between Structure, Binding Specificity and Fibrillation Enhancement (en) Interaction of α-Synuclein with Divalent Metal Ions Reveals Key Differences: A Link between Structure, Binding Specificity and Fibrillation Enhancement (nl)
author	wds:Q58484316-35974154-3A0A-4BA9-89D7-AFCE8B295169 wds:Q58484316-47ACFADA-EA48-41E6-9984-03168D024E65 wds:Q58484316-575D7551-9D5D-44D3-842A-5483B8FA2060 wds:Q58484316-6BCD0A4D-1F6B-43F8-8701-986E5E0E0200
author	Marcelo Ceolín Carlos W. Bertoncini Rodolfo M Rasia Claudio O. Fernandez
title	wds:Q58484316-A560FE3D-AE07-4983-8705-46D40E9B9543
title	Interaction of alpha-synuclein with divalent metal ions reveals key differences: a link between structure, binding specificity and fibrillation enhancement (en)
page(s)	wds:Q58484316-769BB2F9-B04B-4D7C-AE7A-25A54557AA67
page(s)	9893-9901
instance of	wds:Q58484316-418C3C3D-4FBA-4B5D-8C41-3F7B9B27BA37
instance of	scholarly article
main subject	wds:Q58484316-8EFF1A70-9084-49E5-865C-D8AC32480656 wds:Q58484316-94D251F0-E139-4E3F-B196-E1A4558FB863
main subject	fibrillation Synuclein
PubMed ID	wds:Q58484316-68EC8191-033C-4BCA-86B1-F906998BF5B1
PubMed ID	http://rdf.ncbi.nlm.nih.gov/pubchem/reference/16866548
PubMed ID	16866548
published in	wds:Q58484316-0615FAC5-D4F7-42AD-96D1-2AB7E81B5BB0
published in	Journal of the American Chemical Society
issue	wds:Q58484316-B86C3F6E-9ECB-4517-BEE8-417C77398D0B
volume	wds:Q58484316-F82580C3-1AC4-4FA3-8076-D624674D2369
issue	30
volume	128
DOI	wds:Q58484316-69D45D1B-3E7C-437D-9405-8ED1EAAEA74B
DOI	http://dx.doi.org/10.1021/JA0618649
DOI	10.1021/JA0618649
is about of	https://www.wikidata.org/wiki/Special:EntityData/Q58484316
is cites work of	Role of manganese in neurodegenerative diseases The iron regulatory capability of the major protein participants in prevalent neurodegenerative disorders Conformational equilibria in monomeric alpha-synuclein at the single-molecule level Spermine binding to Parkinson's protein alpha-synuclein and its disease-related A30P and A53T mutants α-Synuclein in central nervous system and from erythrocytes, mammalian cells, and Escherichia coli exists predominantly as disordered monomer Allostery in a disordered protein: oxidative modifications to α-synuclein act distally to regulate membrane binding Coordination of copper to the membrane-bound form of α-synuclein Dynamic structural flexibility of α-synuclein Alpha-Synuclein in Parkinson's Disease: From Pathogenetic Dysfunction to Potential Clinical Application Binding of alpha-synuclein with Fe(III) and with Fe(II) and biological implications of the resultant complexes. Post translational changes to α-synuclein control iron and dopamine trafficking; a concept for neuron vulnerability in Parkinson's disease 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 disorders Structural reorganization of alpha-synuclein at low pH observed by NMR and REMD simulations. Binding of Dopamine to Alpha-Synuclein is Mediated by Specific Conformational States Protein-metal interactions of calmodulin and alpha-synuclein monitored by selective noncovalent adduct protein probing mass spectrometry. Bacterial in-cell NMR of human α-synuclein: a disordered monomer by nature? Explaining the structural plasticity of α-synuclein Structural analysis of intrinsically disordered proteins by small-angle X-ray scattering Physicochemical properties of cells and their effects on intrinsically disordered proteins (IDPs) Werner coordination chemistry and neurodegeneration Plasmonics for the study of metal ion-protein interactions. Effect of dioxygen on copper(II) binding to alpha-synuclein. Evidence for copper-dioxygen reactivity during alpha-synuclein fibril formation. Copper(II) enhances membrane-bound α-synuclein helix formation Metalloproteins and neuronal death Redox reactions of the α-synuclein-Cu(2+) complex and their effects on neuronal cell viability Paramagnetic relaxation enhancement to improve sensitivity of fast NMR methods: application to intrinsically disordered proteins. Advances in electrochemical detection for study of neurodegenerative disorders Changes in interfacial properties of alpha-synuclein preceding its aggregation Alpha-Synuclein Oligomers Interact with Metal Ions to Induce Oxidative Stress and Neuronal Death in Parkinson's Disease Alpha-synuclein is a cellular ferrireductase Interaction between alpha-synuclein and metal ions, still looking for a role in the pathogenesis of Parkinson's disease. α-Synuclein Misfolding Versus Aggregation Relevance to Parkinson's Disease: Critical Assessment and Modeling Small molecule-mediated stabilization of vesicle-associated helical α-synuclein inhibits pathogenic misfolding and aggregation. Insights on the interaction of alpha-synuclein and metals in the pathophysiology of Parkinson's disease Alpha-synuclein: relating metals to structure, function and inhibition Two different binding modes of α-synuclein to lipid vesicles depending on its aggregation state The Interplay between Alpha-Synuclein Clearance and Spreading α-synuclein-lanthanide metal ions interaction: binding sites, conformation and fibrillation Identification of fibril-like tertiary contacts in soluble monomeric α-synuclein Distinct phases of free α-synuclein--a Monte Carlo study Metal attenuating therapies in neurodegenerative disease Expression and Transport of α-Synuclein at the Blood-Cerebrospinal Fluid Barrier and Effects of Manganese Exposure Role of N-terminal methionine residues in the redox activity of copper bound to alpha-synuclein

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