A soluble α-synuclein construct forms a dynamic tetramer. - Wikidata - wikimedia - TriplyDB

A soluble α-synuclein construct forms a dynamic tetramer.

A soluble α-synuclein construct forms a dynamic tetramer.

http://www.wikidata.org/entity/Q34050129

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Determining biophysical protein stability in lysates by a fast proteolysis assay, FASTpp Diverse metastable structures formed by small oligomers of α-synuclein probed by force spectroscopy The chaperone-like protein 14-3-3η interacts with human α-synuclein aggregation intermediates rerouting the amyloidogenic pathway and reducing α-synuclein cellular toxicity α-Synuclein as an intrinsically disordered monomer--fact or artefact?Direct visualization of alpha-synuclein oligomers reveals previously undetected pathology in Parkinson's disease brain α-Synuclein assembles into higher-order multimers upon membrane binding to promote SNARE complex formation Native α-synuclein induces clustering of synaptic-vesicle mimics via binding to phospholipids and synaptobrevin-2/VAMP2 Dynamic structural flexibility of α-synuclein Physicochemical properties of cells and their effects on intrinsically disordered proteins (IDPs)Biophysical characterization of α-synuclein and its controversial structure Exploring the accessible conformations of N-terminal acetylated α-synuclein The complex relationships between microglia, alpha-synuclein, and LRRK2 in Parkinson's disease Pathogenesis of synaptic degeneration in Alzheimer's disease and Lewy body disease Integrated control of protein degradation in C. elegans muscle Function and dysfunction of α-synuclein: probing conformational changes and aggregation by single molecule fluorescence The Synaptic Function of α-Synuclein Synthetic Proteins and Peptides for the Direct Interrogation of α-Synuclein Posttranslational Modifications ATP13A2 and Alpha-synuclein: a Metal Taste in Autophagy Modulating self-assembly of amyloidogenic proteins as a therapeutic approach for neurodegenerative diseases: strategies and mechanisms Common features at the start of the neurodegeneration cascade In-cell NMR characterization of the secondary structure populations of a disordered conformation of α-synuclein within E. coli cells Investigation of intramolecular dynamics and conformations of α-, β- and γ-synuclein Total α-synuclein levels in human blood cells, CSF, and saliva determined by a lipid-ELISA.Membrane remodeling by amyloidogenic and non-amyloidogenic proteins studied by EPR.Bacterial in-cell NMR of human α-synuclein: a disordered monomer by nature?α-Synuclein mutations cluster around a putative protein loop.Assessing the subcellular dynamics of alpha-synuclein using photoactivation microscopy.Structural basis for the dissociation of α-synuclein fibrils triggered by pressure perturbation of the hydrophobic core.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 synucleinopathies Mechanisms of Parkinson's disease-related proteins in mediating secondary brain damage after cerebral ischemia.Soluble, prefibrillar α-synuclein oligomers promote complex I-dependent, Ca2+-induced mitochondrial dysfunction.Potential pharmacological chaperones targeting cancer-associated MCL-1 and Parkinson disease-associated α-synuclein.Residue histidine 50 plays a key role in protecting α-synuclein from aggregation at physiological pH.α-Synuclein in central nervous system and from erythrocytes, mammalian cells, and Escherichia coli exists predominantly as disordered monomer Monomeric synucleins generate membrane curvature.In vivo cross-linking reveals principally oligomeric forms of α-synuclein and β-synuclein in neurons and non-neural cells γ-Synuclein interacts with phospholipase Cβ2 to modulate G protein activation.Quantitative analysis of α-synuclein solubility in living cells using split GFP complementation Covalent α-synuclein dimers: chemico-physical and aggregation properties.

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A soluble α-synuclein construct forms a dynamic tetramer.

http://www.wikidata.org/entity/Q34050129

description

2011 nî lūn-bûn

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2011 թուականի Հոկտեմբերին հրատարակուած գիտական յօդուած

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2011 թվականի հոտեմբերին հրատարակված գիտական հոդված

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2011年の論文

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2011年論文

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2011年論文

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2011年論文

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2011年論文

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2011年論文

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2011年论文

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name

A soluble α-synuclein construct forms a dynamic tetramer.

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A soluble α-synuclein construct forms a dynamic tetramer.

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A soluble α-synuclein construct forms a dynamic tetramer.

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A soluble α-synuclein construct forms a dynamic tetramer.

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A soluble α-synuclein construct forms a dynamic tetramer.

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A soluble α-synuclein construct forms a dynamic tetramer.

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A soluble α-synuclein construct forms a dynamic tetramer.

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A soluble α-synuclein construct forms a dynamic tetramer.

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A soluble α-synuclein construct forms a dynamic tetramer.

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A soluble α-synuclein construct forms a dynamic tetramer.

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Alana K Simorellis

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Alice Kaganovich

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Anuradha Landeru

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Brian N Webb

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Chulhee Kang

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Derrick Johnson

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Francisco J Asturias

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Iva Perovic

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Jared R Auclair

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Jeffrey N Agar

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P2860

Pre-fibrillar alpha-synuclein variants with impaired beta-structure increase neurotoxicity in Parkinson's disease models

α-Synuclein occurs physiologically as a helically folded tetramer that resists aggregation

TALOS+: a hybrid method for predicting protein backbone torsion angles from NMR chemical shifts

Alpha-synuclein blocks ER-Golgi traffic and Rab1 rescues neuron loss in Parkinson's models

Structures of segments of α-synuclein fused to maltose-binding protein suggest intermediate states during amyloid formation

SPIDER and WEB: processing and visualization of images in 3D electron microscopy and related fields

Alpha-synuclein and neurodegenerative diseases

Appion: an integrated, database-driven pipeline to facilitate EM image processing

SPARX, a new environment for Cryo-EM image processing.

Methods for protein characterization by mass spectrometry, thermal shift (ThermoFluor) assay, and multiangle or static light scattering.

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