Co-existence of two different α-synuclein oligomers with different core structures determined by hydrogen/deuterium exchange mass spectrometry. (Q46904618)

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scientific article published on 16 April 2014

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English	Co-existence of two different α-synuclein oligomers with different core structures determined by hydrogen/deuterium exchange mass spectrometry.	scientific article published on 16 April 2014

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14 March 2020

Co-existence of two different α-synuclein oligomers with different core structures determined by hydrogen/deuterium exchange mass spectrometry (English)

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14 March 2020

Wojciech Paslawski

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14 March 2020

Thomas J.D. Jørgensen

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Karen Thomsen

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14 March 2020

Angewandte Chemie International Edition

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14 March 2020

7560-7563

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14 March 2020

Protein folding and misfolding

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The new mutation, E46K, of alpha-synuclein causes Parkinson and Lewy body dementia

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Low-resolution structure of a vesicle disrupting α-synuclein oligomer that accumulates during fibrillation

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Acceleration of oligomerization, not fibrillization, is a shared property of both alpha-synuclein mutations linked to early-onset Parkinson's disease: implications for pathogenesis and therapy

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In vivo demonstration that alpha-synuclein oligomers are toxic

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alpha-Synuclein in filamentous inclusions of Lewy bodies from Parkinson's disease and dementia with lewy bodies

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Protein aggregation: folding aggregates, inclusion bodies and amyloid

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Vesicle permeabilization by protofibrillar alpha-synuclein: implications for the pathogenesis and treatment of Parkinson's disease

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Mapping of a gene for Parkinson's disease to chromosome 4q21-q23

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Alpha-synuclein in Lewy bodies

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Mutation in the alpha-synuclein gene identified in families with Parkinson's disease

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Progress towards a molecular-level structural understanding of amyloid fibrils

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Atomic structure and hierarchical assembly of a cross- amyloid fibril

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Unique identification of supramolecular structures in amyloid fibrils by solid-state NMR spectroscopy

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High-resolution molecular structure of a peptide in an amyloid fibril determined by magic angle spinning NMR spectroscopy

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The fold of alpha-synuclein fibrils

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Structural characterization of beta-amyloid oligomer-aggregates by ion mobility mass spectrometry and electron spin resonance spectroscopy

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Characterization of oligomerization-aggregation products of neurodegenerative target proteins by ion mobility mass spectrometry

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Human islet amyloid polypeptide monomers form ordered beta-hairpins: a possible direct amyloidogenic precursor

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Ligand binding to distinct states diverts aggregation of an amyloid-forming protein

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Mysterious oligomerization of the amyloidogenic proteins

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Oligomeric intermediates in amyloid formation: structure determination and mechanisms of toxicity

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Characterizing the dynamics of α-synuclein oligomers using hydrogen/deuterium exchange monitored by mass spectrometry

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HDX-ESI-MS reveals enhanced conformational dynamics of the amyloidogenic protein beta(2)-microglobulin upon release from the MHC-1.

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Structural differences between Abeta(1-40) intermediate oligomers and fibrils elucidated by proteolytic fragmentation and hydrogen/deuterium exchange

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Experimental characterization of disordered and ordered aggregates populated during the process of amyloid fibril formation

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Conserved core of amyloid fibrils of wild type and A30P mutant α-synuclein

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Structure and properties of alpha-synuclein and other amyloids determined at the amino acid level

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Protein structure change studied by hydrogen-deuterium exchange, functional labeling, and mass spectrometry.

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Tryptophan fluorescence reveals structural features of alpha-synuclein oligomers

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Membrane Permeabilization by Oligomeric α-Synuclein: In Search of the Mechanism

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Direct observation of the interconversion of normal and toxic forms of α-synuclein

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10.1002/ANIE.201400491

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Europe PubMed Central

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https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:24740651%20AND%20SRC:MED&resulttype=core&format=json

14 March 2020

PubMed publication ID

1 reference

Europe PubMed Central

PubMed publication ID

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:24740651%20AND%20SRC:MED&resulttype=core&format=json

14 March 2020

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