Preparation and Characterization of Stable α-Synuclein Lipoprotein Particles - Test2 - elhamkhani - TriplyDB

Preparation and Characterization of Stable α-Synuclein Lipoprotein Particles

Preparation and Characterization of Stable α-Synuclein Lipoprotein Particles

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Chemical Compensation of Mitochondrial Phospholipid Depletion in Yeast and Animal Models of Parkinson's Disease Membrane remodeling by amyloidogenic and non-amyloidogenic proteins studied by EPR.Diabetic Risk Factors Promote Islet Amyloid Polypeptide Misfolding by a Common, Membrane-mediated Mechanism.Nuclear Magnetic Resonance Observation of α-Synuclein Membrane Interaction by Monitoring the Acetylation Reactivity of Its Lysine Side Chains.Biomolecular NMR: Past and future.Nanodiscs in Membrane Biochemistry and Biophysics.The Role of Lipids Interacting with α-Synuclein in the Pathogenesis of Parkinson's Disease.Commentary: α-Synuclein Interacts with Lipoproteins in Plasma.α-Synuclein Interacts with Lipoproteins in Plasma.Physical Chemistry in Biomedical Research: From Cuvettes toward Cellular Insights.High-density lipoprotein-like particle formation of Synuclein variants.Stimulation of α-synuclein amyloid formation by phosphatidylglycerol micellar tubules.Structural insights from lipid-bilayer nanodiscs link α-Synuclein membrane-binding modes to amyloid fibril formation

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P2860

Preparation and Characterization of Stable α-Synuclein Lipoprotein Particles

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2016 nî lūn-bûn

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2016年の論文

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2016年論文

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2016年論文

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2016年論文

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2016年論文

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2016年论文

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2016年论文

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2016年论文

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Preparation and Characterization of Stable α-Synuclein Lipoprotein Particles

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Preparation and Characterization of Stable α-Synuclein Lipoprotein Particles

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Preparation and Characterization of Stable α-Synuclein Lipoprotein Particles

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JBC.M115.707968

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Journal of Biological Chemistry

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Preparation and Characterization of Stable α-Synuclein Lipoprotein Particles

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Innokentiy Maslennikov

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Joeri Verasdonck

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Juan Gerez

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Nadezhda Nespovitaya

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Roland Riek

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Senyon Choe

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Silvia Campioni

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Xiaoxia Liu

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P2860

Human α-synuclein modulates vesicle trafficking through its interaction with prenylated Rab acceptor protein 1

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

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

Alpha-synuclein promotes SNARE-complex assembly in vivo and in vitro

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

Attenuated T2 relaxation by mutual cancellation of dipole-dipole coupling and chemical shift anisotropy indicates an avenue to NMR structures of very large biological macromolecules in solution

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

α-Synuclein assembles into higher-order multimers upon membrane binding to promote SNARE complex formation

The 13C chemical-shift index: a simple method for the identification of protein secondary structure using 13C chemical-shift data

The program XEASY for computer-supported NMR spectral analysis of biological macromolecules

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Henning Stahlberg

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2016-02-04T00:00:00Z

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