α-Synuclein senses lipid packing defects and induces lateral expansion of lipids leading to membrane remodeling. - Wikidata - wikimedia - TriplyDB

α-Synuclein senses lipid packing defects and induces lateral expansion of lipids leading to membrane remodeling.

α-Synuclein senses lipid packing defects and induces lateral expansion of lipids leading to membrane remodeling.

http://www.wikidata.org/entity/Q42184977

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The N-terminus of α-synuclein is essential for both monomeric and oligomeric interactions with membranes α-Synuclein assembles into higher-order multimers upon membrane binding to promote SNARE complex formation Dynamics and instabilities of lipid bilayer membrane shapes Biophysical characterization of α-synuclein and its controversial structure The Synaptic Function of α-Synuclein Seeking a mechanism for the toxicity of oligomeric α-synuclein Chemical properties of lipids strongly affect the kinetics of the membrane-induced aggregation of α-synuclein Membrane Curvature-sensing and Curvature-inducing Activity of Islet Amyloid Polypeptide and Its Implications for Membrane Disruption.Membrane remodeling by amyloidogenic and non-amyloidogenic proteins studied by EPR.Effect of the interplay between protein and surface on the properties of adsorbed protein layers Real-time measurement of membrane conformational states induced by antimicrobial peptides: balance between recovery and lysis.α-Synuclein structural features inhibit harmful polyunsaturated fatty acid oxidation, suggesting roles in neuroprotection Direct observation of the three regions in α-synuclein that determine its membrane-bound behaviour.N-alpha-acetylation of α-synuclein increases its helical folding propensity, GM1 binding specificity and resistance to aggregation.Structural characterization of toxic oligomers that are kinetically trapped during α-synuclein fibril formation.Effects of impaired membrane interactions on α-synuclein aggregation and neurotoxicity Biophysics of α-synuclein induced membrane remodelling Atomic Force Microscopy Characterization of Protein Fibrils Formed by the Amyloidogenic Region of the Bacterial Protein MinE on Mica and a Supported Lipid Bilayer.The influence of N-terminal acetylation on micelle-induced conformational changes and aggregation of α-Synuclein.High expression of α-synuclein in damaged mitochondria with PLA2G6 dysfunction.Fibril growth and seeding capacity play key roles in α-synuclein-mediated apoptotic cell death.Preparation and Characterization of Stable α-Synuclein Lipoprotein Particles N-terminal acetylation stabilizes N-terminal helicity in lipid- and micelle-bound α-synuclein and increases its affinity for physiological membranes.Helix 8 of the angiotensin- II type 1A receptor interacts with phosphatidylinositol phosphates and modulates membrane insertion.The function of α-synuclein.Synucleinopathies: common features and hippocampal manifestations.Impulse control disorder, lysosomal malfunction and ATP13A2 insufficiency in Parkinsonism.Cell Biology and Pathophysiology of α-Synuclein.Molecular interactions of amyloid nanofibrils with biological aggregation modifiers: implications for cytotoxicity mechanisms and biomaterial design.The Role of Lipids Interacting with α-Synuclein in the Pathogenesis of Parkinson's Disease.Lipid vesicles trigger α-synuclein aggregation by stimulating primary nucleation.Amyloids of alpha-synuclein affect the structure and dynamics of supported lipid bilayers.The number of α-synuclein proteins per vesicle gives insights into its physiological function.The effects of apolipoprotein E genotype, α-synuclein deficiency, and sex on brain synaptic and Alzheimer's disease-related pathology.Unraveling amyloid formation paths of Parkinson's disease protein α-synuclein triggered by anionic vesicles.Alpha-synuclein, proteotoxicity and Parkinson's disease: Search for neuroprotective therapy.Simultaneous IR-Spectroscopic Observation of α-Synuclein, Lipids, and Solvent Reveals an Alternative Membrane-Induced Oligomerization Pathway.Influence of lipid composition of model membranes on methacrylate antimicrobial polymer-membrane interactions.Membrane-Bound Alpha Synuclein Clusters Induce Impaired Lipid Diffusion and Increased Lipid Packing.Endo- and exocytic budding transformation of slow-diffusing membrane domains induced by Alzheimer's amyloid beta.

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P2860

α-Synuclein senses lipid packing defects and induces lateral expansion of lipids leading to membrane remodeling.

http://www.wikidata.org/entity/Q42184977

description

2013 nî lūn-bûn

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2013年の論文

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2013年论文

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name

α-Synuclein senses lipid packi ...... eading to membrane remodeling.

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α-Synuclein senses lipid packi ...... eading to membrane remodeling.

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type

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α-Synuclein senses lipid packi ...... eading to membrane remodeling.

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α-Synuclein senses lipid packi ...... eading to membrane remodeling.

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α-Synuclein senses lipid packi ...... eading to membrane remodeling.

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α-Synuclein senses lipid packi ...... eading to membrane remodeling.

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JBC.M113.478297

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Journal of Biological Chemistry

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α-Synuclein senses lipid packi ...... eading to membrane remodeling.

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Juan Wang

http://www.w3.org/2001/XMLSchema#string

Marcus J Swann

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Mark E Welland

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Myriam M Ouberai

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Tim Guilliams

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P2860

Structure of membrane-bound alpha-synuclein from site-directed spin labeling and computational refinement

Membrane curvature induction and tubulation are common features of synucleins and apolipoproteins.

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

Alpha-synuclein in Lewy bodies

Protein misfolding, functional amyloid, and human disease

Optical anisotropy of supported lipid structures probed by waveguide spectroscopy and its application to study of supported lipid bilayer formation kinetics

Mechanisms of membrane curvature sensing

Membrane-bound alpha-synuclein has a high aggregation propensity and the ability to seed the aggregation of the cytosolic form

Membrane curvature and mechanisms of dynamic cell membrane remodelling

Stabilization of alpha-synuclein secondary structure upon binding to synthetic membranes

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288

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Celine Galvagnion

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