About: Structural properties of pore-forming oligomers of alpha-synuclein

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article by Hai-Young Kim et al published 2 December 2009 in Journal of the American Chemical Society

Attributes	Values
rdf:type	Item
description	wetenschappelijk artikel (nl) article scientifique publié en 2009 (fr) наукова стаття, опублікована в грудні 2009 (uk) im Dezember 2009 veröffentlichter wissenschaftlicher Artikel (de) article by Hai-Young Kim et al published 2 December 2009 in Journal of the American Chemical Society (en)
publication date	wds:Q57185914-AC58E04E-FF1B-46B2-B8F5-2F76DD6055B0
publication date	2009-12-02 00:00:00Z (xsd:dateTime)
language of work or name	wds:Q57185914-C3716AD2-F7D5-4223-A20A-0012F624E94C
language of work or name	English
author name string	wds:Q57185914-332FD275-DCC4-4D53-BBEB-B4CA868C7846 wds:Q57185914-6D939B27-791B-4EED-B1A3-1E70FB949E5A wds:Q57185914-C47792F1-78CC-4B35-B817-6026E89BA52C wds:Q57185914-C6254F43-6FD8-481A-A7BF-C7D4F0C52159 wds:Q57185914-DD77AEEC-368B-4807-B6D8-C0CD1D504CE5
author name string	Ashutosh Kumar Stefan Becker Hai-Young Kim Elke Maier Carsten Siebenhaar
rdfs:label	Structural properties of pore-forming oligomers of alpha-synuclein (en) Structural properties of pore-forming oligomers of alpha-synuclein (nl)
skos:prefLabel	Structural properties of pore-forming oligomers of alpha-synuclein (en) Structural properties of pore-forming oligomers of alpha-synuclein (nl)
name	Structural properties of pore-forming oligomers of alpha-synuclein (en) Structural properties of pore-forming oligomers of alpha-synuclein (nl)
author	wds:Q57185914-0E4C7D91-FB43-439B-8815-896DBCD6DA6E wds:Q57185914-435F376D-7747-49BB-A63C-B53BC1502CBB wds:Q57185914-4F4EBB0F-DC51-4C3C-8FF2-BA4E5B9B5936 wds:Q57185914-973B917D-2208-459F-A351-DD166C96DF36 wds:Q57185914-9914E987-45E3-4AE9-AE83-2E2C6917B090 wds:Q57185914-A75D1286-46A1-4A78-8F2E-3330B34CAF71 wds:Q57185914-AE176DA1-3807-418C-AA8B-A76055984994 wds:Q57185914-F3F78A43-ADDE-4EEC-B21E-88AC3EB5DFE1
author	Hilal Lashuel Roland Benz Markus Zweckstetter Adam Lange Min-Kyu Cho Claudio O. Fernandez
title	wds:Q57185914-4F887D25-0DD6-4C18-8080-656143EDD423 wds:Q57185914-5B52B731-913A-4C31-B37A-144C8D74C253
title	Structural Properties of Pore-Forming Oligomers of α-Synuclein (en) Structural properties of pore-forming oligomers of alpha-synuclein (en)
page(s)	wds:Q57185914-70AD99F6-4057-4F69-95EE-F2251522F020 wds:Q57185914-DC3D19AE-049E-4B84-A1FA-743D8E620AD2
page(s)	17482-17489 17482-9
instance of	wds:Q57185914-2A1BC9F6-4DCA-4EFA-B8DE-7F507CC327B5
instance of	scholarly article
main subject	wds:Q57185914-886547EF-5701-4AC9-B9B3-F05ED8C72377
main subject	Synuclein
PubMed ID	wds:Q57185914-AB98E460-B076-400E-92A9-628765D0F425
PubMed ID	http://rdf.ncbi.nlm.nih.gov/pubchem/reference/19888725
PubMed ID	19888725
published in	wds:Q57185914-8A20C7FC-367C-4E92-974C-6B0DCA2F949D
published in	Journal of the American Chemical Society
issue	wds:Q57185914-CEAD6CE4-4E33-4F53-9524-8E53B25D31CD
volume	wds:Q57185914-4C88CFC7-0DB1-482A-9215-C03587D34B74
issue	47
volume	131
DOI	wds:Q57185914-3C5E5AE1-D12F-4155-B97D-2D1A76B3F7C5
DOI	http://dx.doi.org/10.1021/JA9077599
DOI	10.1021/JA9077599
skos:altLabel	Structural Properties of Pore-Forming Oligomers of α-Synuclein (en) Structural Properties of Pore-Forming Oligomers of α-Synuclein (nl)
is owl:sameAs of	Structural properties of pore-forming oligomers of alpha-synuclein
is about of	https://www.wikidata.org/wiki/Special:EntityData/Q57185914
is cites work of	Passive immunization reduces behavioral and neuropathological deficits in an alpha-synuclein transgenic model of Lewy body disease Formation kinetics and structural features of Beta-amyloid aggregates by sedimented solute NMR. Activity and architecture of pyroglutamate-modified amyloid-β (AβpE3-42) pores The chaperone-like protein 14-3-3η interacts with human α-synuclein aggregation intermediates rerouting the amyloidogenic pathway and reducing α-synuclein cellular toxicity A soluble α-synuclein construct forms a dynamic tetramer Biophysical groundwork as a hinge to unravel the biology of α-synuclein aggregation and toxicity Solid-state NMR spectroscopy on complex biomolecules High resolution structural characterization of Aβ42 amyloid fibrils by magic angle spinning NMR. Specificity and kinetics of alpha-synuclein binding to model membranes determined with fluorescent excited state intramolecular proton transfer (ESIPT) probe Drosophila histone deacetylase 6 protects dopaminergic neurons against {alpha}-synuclein toxicity by promoting inclusion formation Differential phospholipid binding of alpha-synuclein variants implicated in Parkinson's disease revealed by solution NMR spectroscopy α-Synuclein senses lipid packing defects and induces lateral expansion of lipids leading to membrane remodeling Direct visualization of alpha-synuclein oligomers reveals previously undetected pathology in Parkinson's disease brain Biophysics of α-synuclein membrane interactions. Tau oligomers impair artificial membrane integrity and cellular viability The structure of dopamine induced alpha-synuclein oligomers. Supramolecular non-amyloid intermediates in the early stages of α-synuclein aggregation α-Synuclein oligomers induced by docosahexaenoic acid affect membrane integrity Exploring the accessible conformations of N-terminal acetylated α-synuclein Protein misfolding and aggregation in Alzheimer's disease and type 2 diabetes mellitus Stable alpha-synuclein oligomers strongly inhibit chaperone activity of the Hsp70 system by weak interactions with J-domain co-chaperones Insights on the interaction of alpha-synuclein and metals in the pathophysiology of Parkinson's disease Cu(II) promotes amyloid pore formation Structural intermediates during α-synuclein fibrillogenesis on phospholipid vesicles α-Synuclein oligomers: an amyloid pore? Insights into mechanisms of α-synuclein oligomer-lipid interactions Two different binding modes of α-synuclein to lipid vesicles depending on its aggregation state Toxic prefibrillar α-synuclein amyloid oligomers adopt a distinctive antiparallel β-sheet structure. Structural characterization of toxic oligomers that are kinetically trapped during α-synuclein fibril formation. Identification of fibril-like tertiary contacts in soluble monomeric α-synuclein Extracellular α-synuclein alters synaptic transmission in brain neurons by perforating the neuronal plasma membrane. Features of alpha-synuclein that could explain the progression and irreversibility of Parkinson's disease Structural, morphological, and functional diversity of amyloid oligomers

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