Literature DB >> 22162214

Autoproteolytic fragments are intermediates in the oligomerization/aggregation of the Parkinson's disease protein alpha-synuclein as revealed by ion mobility mass spectrometry.

Camelia Vlad1, Kathrin Lindner, Christiaan Karreman, Stefan Schildknecht, Marcel Leist, Nick Tomczyk, John Rontree, James Langridge, Karin Danzer, Thomas Ciossek, Alina Petre, Michael L Gross, Bastian Hengerer, Michael Przybylski.   

Abstract

Gas-phase protein separation by ion mobility: With its ability to separate the Parkinson's disease protein α-synuclein and its autoproteolytic products-despite the small concentrations of the latter-ion-mobility MS has enabled the characterization of intermediate fragments in in vitro oligomerization-aggregation. In particular, a possible key fragment, the highly aggregating C-terminal fragment, αSyn(72-140), has been revealed.
Copyright © 2011 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim.

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Year:  2011        PMID: 22162214      PMCID: PMC3461308          DOI: 10.1002/cbic.201100569

Source DB:  PubMed          Journal:  Chembiochem        ISSN: 1439-4227            Impact factor:   3.164


  56 in total

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4.  Ion mobility-mass spectrometry analysis of large protein complexes.

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5.  Conformational behavior of human alpha-synuclein is modulated by familial Parkinson's disease point mutations A30P and A53T.

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7.  On-line bioaffinity-electrospray mass spectrometry for simultaneous detection, identification, and quantification of protein-ligand interactions.

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8.  Interplay of alpha-synuclein binding and conformational switching probed by single-molecule fluorescence.

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10.  Ion mobility spectrometry/mass spectrometry snapshots for assessing the molecular compositions of complex polymeric systems.

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  13 in total

1.  Dopamine-induced α-synuclein oligomers show self- and cross-propagation properties.

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2.  Identification and affinity-quantification of ß-amyloid and α-synuclein polypeptides using on-line SAW-biosensor-mass spectrometry.

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Review 3.  Implications of peptide assemblies in amyloid diseases.

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4.  Stabilization of Alpha-Synuclein Oligomers In Vitro by the Neurotransmitters, Dopamine and Norepinephrine: The Effect of Oxidized Catecholamines.

Authors:  Andrew F Fischer; Kathryn Mansfield Matera
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6.  Prion-Like Seeding of Misfolded α-Synuclein in the Brains of Dementia with Lewy Body Patients in RT-QUIC.

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7.  Exploring the Structural Diversity in Inhibitors of α-Synuclein Amyloidogenic Folding, Aggregation, and Neurotoxicity.

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8.  Vibrio cholerae biofilm scaffolding protein RbmA shows an intrinsic, phosphate-dependent autoproteolysis activity.

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Review 9.  Advances in ion mobility spectrometry-mass spectrometry reveal key insights into amyloid assembly.

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