In vivo cross-linking reveals principally oligomeric forms of α-synuclein and β-synuclein in neurons and non-neural cells
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α-Synuclein as an intrinsically disordered monomer--fact or artefact?α-Synuclein assembles into higher-order multimers upon membrane binding to promote SNARE complex formationPhysicochemical properties of cells and their effects on intrinsically disordered proteins (IDPs)Biophysical characterization of α-synuclein and its controversial structureExploring the accessible conformations of N-terminal acetylated α-synucleinThe complex relationships between microglia, alpha-synuclein, and LRRK2 in Parkinson's diseaseAlpha-Synuclein Oligomers-Neurotoxic Molecules in Parkinson's Disease and Other Lewy Body DisordersThe contribution of alpha synuclein to neuronal survival and function - Implications for Parkinson's diseaseSeeking a mechanism for the toxicity of oligomeric α-synucleinCharacterization of α-Synuclein Multimer Stoichiometry in Complex Biological Samples by Electrophoresisα-Synuclein mutations cluster around a putative protein loop.The dual functions of the extreme N-terminus of TDP-43 in regulating its biological activity and inclusion formation.Molecular basis for preventing α-synuclein aggregation by a molecular tweezer.Molecular chaperones and protein folding as therapeutic targets in Parkinson's disease and other synucleinopathiesSoluble, prefibrillar α-synuclein oligomers promote complex I-dependent, Ca2+-induced mitochondrial dysfunction.Molecular chaperone dysfunction in neurodegenerative diseases and effects of curcumin.A pipeline for determining protein-protein interactions and proximities in the cellular milieuPurification of α-synuclein from human brain reveals an instability of endogenous multimers as the protein approaches purity.Mitochondria-associated endoplasmic reticulum membrane (MAM) regulates steroidogenic activity via steroidogenic acute regulatory protein (StAR)-voltage-dependent anion channel 2 (VDAC2) interactionA new method for quantitative immunoblotting of endogenous α-synuclein.Zonisamide attenuates α-synuclein neurotoxicity by an aggregation-independent mechanism in a rat model of familial Parkinson's diseaseN-alpha-acetylation of α-synuclein increases its helical folding propensity, GM1 binding specificity and resistance to aggregation.Molecular details of α-synuclein membrane association revealed by neutrons and photons.Overexpression of alpha-synuclein at non-toxic levels increases dopaminergic cell death induced by copper exposure via modulation of protein degradation pathways.Parkinson-causing α-synuclein missense mutations shift native tetramers to monomers as a mechanism for disease initiationThe Interplay between Alpha-Synuclein Clearance and SpreadingCysteine cathepsins are essential in lysosomal degradation of α-synuclein.KTKEGV repeat motifs are key mediators of normal α-synuclein tetramerization: Their mutation causes excess monomers and neurotoxicity.Distinct clinical and neuropathological features of G51D SNCA mutation cases compared with SNCA duplication and H50Q mutationRBM45 homo-oligomerization mediates association with ALS-linked proteins and stress granulesExPLAining early synucleinopathies.An Outer Mitochondrial Translocase, Tom22, Is Crucial for Inner Mitochondrial Steroidogenic Regulation in Adrenal and Gonadal Tissues.Inhibition of Protein Ubiquitination by Paraquat and 1-Methyl-4-Phenylpyridinium Impairs Ubiquitin-Dependent Protein Degradation Pathways.Preparation and Characterization of Stable α-Synuclein Lipoprotein ParticlesSerine 129 phosphorylation of membrane-associated α-synuclein modulates dopamine transporter function in a G protein-coupled receptor kinase-dependent manner.Poststroke Induction of α-Synuclein Mediates Ischemic Brain Damage.Nuclear Magnetic Resonance Observation of α-Synuclein Membrane Interaction by Monitoring the Acetylation Reactivity of Its Lysine Side Chains.Presynaptic alpha-synuclein aggregation in a mouse model of Parkinson's disease.Evidence of native α-synuclein conformers in the human brain.The function of α-synuclein.
P2860
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P2860
In vivo cross-linking reveals principally oligomeric forms of α-synuclein and β-synuclein in neurons and non-neural cells
description
2013 nî lūn-bûn
@nan
2013 թուականի Յունուարին հրատարակուած գիտական յօդուած
@hyw
2013 թվականի հունվարին հրատարակված գիտական հոդված
@hy
2013年の論文
@ja
2013年論文
@yue
2013年論文
@zh-hant
2013年論文
@zh-hk
2013年論文
@zh-mo
2013年論文
@zh-tw
2013年论文
@wuu
name
In vivo cross-linking reveals ...... n neurons and non-neural cells
@ast
In vivo cross-linking reveals ...... n neurons and non-neural cells
@en
In vivo cross-linking reveals ...... n neurons and non-neural cells
@nl
type
label
In vivo cross-linking reveals ...... n neurons and non-neural cells
@ast
In vivo cross-linking reveals ...... n neurons and non-neural cells
@en
In vivo cross-linking reveals ...... n neurons and non-neural cells
@nl
prefLabel
In vivo cross-linking reveals ...... n neurons and non-neural cells
@ast
In vivo cross-linking reveals ...... n neurons and non-neural cells
@en
In vivo cross-linking reveals ...... n neurons and non-neural cells
@nl
P2093
P2860
P356
P1476
In vivo cross-linking reveals ...... n neurons and non-neural cells
@en
P2093
Andrew J Newman
Dennis Selkoe
Eric S Luth
Tim Bartels
Ulf Dettmer
P2860
P304
P356
10.1074/JBC.M112.403311
P407
P577
2013-01-14T00:00:00Z