phosphatidylcholines has been researched along with alpha-synuclein in 52 studies
| Studies (phosphatidylcholines) | Trials (phosphatidylcholines) | Recent Studies (post-2010) (phosphatidylcholines) | Studies (alpha-synuclein) | Trials (alpha-synuclein) | Recent Studies (post-2010) (alpha-synuclein) |
|---|---|---|---|---|---|
| 32,204 | 443 | 5,593 | 10,821 | 29 | 8,011 |
| Timeframe | Studies, this research(%) | All Research% |
|---|---|---|
| pre-1990 | 0 (0.00) | 18.7374 |
| 1990's | 1 (1.92) | 18.2507 |
| 2000's | 15 (28.85) | 29.6817 |
| 2010's | 29 (55.77) | 24.3611 |
| 2020's | 7 (13.46) | 2.80 |
| Authors | Studies |
|---|---|
| Clayton, DF; Davidson, WS; George, JM; Jonas, A | 1 |
| Ding, TT; Kessler, JC; Lansbury, PT; Lee, SJ; Rochet, JC; Shtilerman, MD; Volles, MJ | 1 |
| Narayanan, V; Scarlata, S | 1 |
| Jensen, PH; Marsh, D; Ramakrishnan, M | 2 |
| Bussell, R; Eliezer, D | 1 |
| Fink, AL; Hu, D; Munishkina, LA; Qin, ZJ; Zhu, M | 1 |
| Kato, H; Kosaraju, MG; Narayanaswami, V; Raussens, V; Ruysschaert, JM; Tamamizu-Kato, S | 1 |
| Bar-On, P; Crews, L; Hashimoto, M; Keller, SH; Masliah, E; Miller, MA; Platoshyn, O; Sharikov, Y; Tsigelny, IF; Yuan, JX | 1 |
| Cambrea, LR; Haque, F; Hovis, JS; Rochet, JC; Schieler, JL | 1 |
| Antonenko, YN; Cramer, WA; Dutseva, EA; Hulleman, JD; Rochet, JC; Zakharov, SD | 1 |
| Fischer, P; Herrmann, A; Stöckl, M; Wanker, E | 1 |
| Barnham, KJ; Bottomley, SP; Cappai, R; Hill, AF; Masters, CL; Smith, DP; Tew, DJ | 1 |
| Bisaglia, M; Bortolus, M; Bubacco, L; Ferrarini, A; Mammi, S; Maniero, AL; Tessari, I; Tombolato, F | 1 |
| Doig, AJ; Hughes, E; Madine, J; Middleton, DA | 1 |
| Haque, F; Hovis, JS; Pandey, AP; Rochet, JC | 1 |
| Cambrea, LR; Haque, F; Hovis, JS; Pandey, AP; Rochet, JC | 1 |
| Fantini, J; Yahi, N | 1 |
| Claessens, MM; Stöckl, M; Subramaniam, V | 1 |
| Cornell, RB; Lee, JM; Taneva, SG | 1 |
| Drescher, M; Hintze, C; Huber, M; Jüngst, C; Karreman, C; Leist, M; Robotta, M; Schildknecht, S; Subramaniam, V; Zijlstra, N | 1 |
| Campbell, SA; Chen, N; Cornell, RB; Ding, Z; Huang, HK; Semenec, L; Taneva, SG | 1 |
| Cheng, N; Hegde, BG; Langen, R; Mizuno, N; Steven, AC; Varkey, J | 1 |
| Amoussouvi, A; Haralampiev, I; Herrmann, A; Stöckl, M; Wietek, J | 1 |
| de Messieres, M; Jiang, Z; Lee, JC | 1 |
| Bai, J; Dai, C; Li, C; Liu, M; Xu, G; Zhang, Z | 1 |
| Bader, B; Giese, A; Hillmer, A; Högen, T; Kamp, F; Levin, J; Lorenzl, S; Nübling, GS | 1 |
| Claessens, MM; Iyer, A; Petersen, NO; Subramaniam, V | 1 |
| Braun, AR; Ducas, VC; Lacy, MM; Rhoades, E; Sachs, JN | 1 |
| Furlan, G; Hanagata, N; Kaizuka, Y; Kataoka-Hamai, C; Minowa, T | 1 |
| Auger, M; Bédard, L; Lefèvre, T; Morin-Michaud, É | 1 |
| Banerjee, R; Carvalho, E; Dwivedi, S; Ghosh, D; Kumar, A; Maji, SK; Mohite, GM; Ranjan, P; Sahay, S; Salot, S; Singh, PK | 1 |
| Claessens, MM; Lindhoud, S; Semerdzhiev, SA; Stefanovic, AN; Subramaniam, V | 1 |
| Bartucci, R; Kjær, L; Lillelund, O; Otzen, D; Pantusa, M; Vad, B | 1 |
| Barron, A; Caldwell, GA; Caldwell, KA; Galiano, F; Lee, YJ; Patel, D; Wang, S; Witt, SN; Xu, C; Zhang, S | 1 |
| Braun, AR; Brummel, BE; Sachs, JN | 1 |
| Chaudhary, H; Claessens, MM; Iyer, A; Subramaniam, V | 1 |
| Baumgart, T; Canyurt, M; Cleveland, CL; Daniels, MJ; Haney, CM; Ischiropoulos, H; Owei, L; Petersson, EJ; Robustelli, J; Rodriguez, P; Wissner, RF | 1 |
| Fukui, N; Goto, Y; Ikenoue, T; Kawata, Y; Kinoshita, M; Lee, YH; Lin, Y; Sugiki, T; Terakawa, MS | 1 |
| Broersen, K; Davletov, B; Ruiperez, V | 1 |
| Araki, K; Hayakawa, EH; Kobayashi, I; Mochizuki, H; Nunomura, W; Sawada, K; Sugawara, K; Takahashi, N; Ubukawa, K; Wakui, H | 1 |
| Banerjee, S; Lv, Z; Lyubchenko, YL; Zagorski, K | 1 |
| Banerjee, S; Hashemi, M; Lv, Z; Lyubchenko, YL; Rochet, JC; Zagorski, K | 1 |
| Biswas, SC; Chattopadhyay, K; Mahapatra, A; Sarkar, S | 1 |
| Almásy, L; Bottyán, L; Casalis, L; Merkel, DG; Parisse, P; Perissinotto, F; Rondelli, V; Sajti, S; Tormena, N; Zunino, A | 1 |
| Kaur, U; Lee, JC | 1 |
| Bu, B; Crowe, M; Diao, J; Ji, B; Li, D; Liu, J | 1 |
| Caballero, L; Cornejo, A; Doll, I; Melo, F; Navarro, C; Ventura, N; Zamorano, E; Zamorano, P | 1 |
| Canale, C; Canepa, E; Dante, S; Diaspro, A; Jadavi, S; Relini, A | 1 |
| Dean, NJ; Dzamko, N; Galper, J; Halliday, GM; Kim, WS; Lewis, SJG; Pickford, R | 1 |
| Dou, T; Kurouski, D | 1 |
| Dou, T; Kurouski, D; Matveyenka, M | 1 |
52 other study(ies) available for phosphatidylcholines and alpha-synuclein
| Article | Year |
|---|---|
Stabilization of alpha-synuclein secondary structure upon binding to synthetic membranes.
Topics: alpha-Synuclein; Amino Acid Sequence; Animals; Binding Sites; Canaries; Circular Dichroism; Humans; Liposomes; Molecular Sequence Data; Nerve Tissue Proteins; Osmolar Concentration; Phosphatidic Acids; Phosphatidylcholines; Phosphatidylethanolamines; Phosphatidylinositols; Protein Structure, Secondary; Sequence Alignment; Sequence Homology, Amino Acid; Structure-Activity Relationship; Synucleins | 1998 |
Vesicle permeabilization by protofibrillar alpha-synuclein: implications for the pathogenesis and treatment of Parkinson's disease.
Topics: Adsorption; alpha-Synuclein; Cytotoxins; Humans; Lewy Bodies; Nerve Tissue Proteins; Parkinson Disease; Permeability; Phosphatidic Acids; Phosphatidylcholines; Phosphatidylglycerols; Phospholipids; Protein Binding; Protein Structure, Secondary; Synucleins; Time Factors | 2001 |
Membrane binding and self-association of alpha-synucleins.
Topics: alpha-Synuclein; beta-Synuclein; Blotting, Western; Cell Membrane; Circular Dichroism; Dose-Response Relationship, Drug; Electrophoresis, Polyacrylamide Gel; Escherichia coli; Humans; Hydrogen-Ion Concentration; Lipids; Nerve Tissue Proteins; Neurodegenerative Diseases; Phosphatidylcholines; Phosphatidylethanolamines; Phosphorylation; Protein Binding; Protein Structure, Secondary; Protein Structure, Tertiary; Silver Staining; Spectrometry, Fluorescence; Synucleins | 2001 |
Alpha-synuclein association with phosphatidylglycerol probed by lipid spin labels.
Topics: alpha-Synuclein; Electron Spin Resonance Spectroscopy; Humans; Hydrophobic and Hydrophilic Interactions; Lipid Bilayers; Models, Chemical; Nerve Tissue Proteins; Phosphatidylcholines; Phosphatidylglycerols; Phosphoproteins; Protein Binding; Recombinant Proteins; Spin Labels; Static Electricity; Synucleins; Titrimetry | 2003 |
Effects of Parkinson's disease-linked mutations on the structure of lipid-associated alpha-synuclein.
Topics: Alanine; alpha-Synuclein; Humans; Lipid Metabolism; Liposomes; Micelles; Mutation, Missense; Nerve Tissue Proteins; Nuclear Magnetic Resonance, Biomolecular; Parkinson Disease; Phosphatidic Acids; Phosphatidylcholines; Proline; Protein Binding; Protein Structure, Secondary; Recombinant Proteins; Synucleins; Threonine | 2004 |
Association of alpha-synuclein and mutants with lipid membranes: spin-label ESR and polarized IR.
Topics: alpha-Synuclein; Circular Dichroism; Electron Spin Resonance Spectroscopy; Humans; Lipid Bilayers; Lipids; Membranes; Phosphatidylcholines; Phosphatidylglycerols; Protein Binding; Protein Conformation; Proteins; Recombinant Proteins; Spectrophotometry, Infrared; Spin Labels; Titrimetry | 2006 |
Alpha-synuclein can function as an antioxidant preventing oxidation of unsaturated lipid in vesicles.
Topics: alpha-Synuclein; Antioxidants; Boron Compounds; Circular Dichroism; Fluorescence; Kinetics; Liposomes; Oxidation-Reduction; Phosphatidylcholines; Phosphatidylglycerols | 2006 |
Calcium-triggered membrane interaction of the alpha-synuclein acidic tail.
Topics: Adenosine; alpha-Synuclein; Amino Acid Sequence; Calcium; Cell Membrane; Circular Dichroism; Fluorescence; Glycerophospholipids; Humans; Hydrogen-Ion Concentration; Lipid Bilayers; Membrane Lipids; Molecular Sequence Data; Phosphatidylcholines; Protein Conformation; Pyrenes; Recombinant Proteins | 2006 |
Dynamics of alpha-synuclein aggregation and inhibition of pore-like oligomer development by beta-synuclein.
Topics: alpha-Synuclein; beta-Synuclein; Cations; Cell Line; Computer Simulation; Electrophysiology; Humans; Ion Channels; Microscopy, Electron, Scanning; Models, Molecular; Phosphatidylcholines; Protein Binding; Protein Conformation; Protein Structure, Quaternary; Protein Structure, Secondary; Static Electricity; Transfection; Zinc | 2007 |
Effect of ions on the organization of phosphatidylcholine/phosphatidic acid bilayers.
Topics: alpha-Synuclein; Dihydroxyphenylalanine; Escherichia coli; Fluorescence Recovery After Photobleaching; Ions; Lipid Bilayers; Lipids; Microscopy, Fluorescence; Phosphatidic Acids; Phosphatidylcholines; Protein Structure, Tertiary; Spectroscopy, Fourier Transform Infrared; Static Electricity; Time Factors | 2007 |
Helical alpha-synuclein forms highly conductive ion channels.
Topics: alpha-Synuclein; Amino Acid Sequence; Circular Dichroism; Dimerization; Humans; Ion Channels; Lipids; Membrane Proteins; Models, Biological; Molecular Sequence Data; Mutation; Phosphatidylcholines; Phosphatidylethanolamines; Phosphatidylserines; Protein Conformation; Protein Structure, Secondary | 2007 |
Alpha-synuclein selectively binds to anionic phospholipids embedded in liquid-disordered domains.
Topics: alpha-Synuclein; Amino Acid Sequence; Anions; Binding Sites; Cell Membrane; Fatty Acids; Fluorescent Dyes; Hydrophobic and Hydrophilic Interactions; Lipids; Microscopy, Fluorescence; Molecular Sequence Data; Molecular Weight; Mutation; Parkinson Disease; Phosphatidic Acids; Phosphatidylcholines; Phosphatidylglycerols; Phosphatidylinositol 4,5-Diphosphate; Phosphatidylserines; Phospholipids; Protein Binding; Protein Conformation; Protein Structure, Secondary; Protein Structure, Tertiary; Rhodamines; Static Electricity; Surface Properties; Unilamellar Liposomes | 2008 |
Formation of a high affinity lipid-binding intermediate during the early aggregation phase of alpha-synuclein.
Topics: alpha-Synuclein; Circular Dichroism; Humans; Lipids; Microscopy, Electron; Phosphatidylcholines; Phosphatidylserines; Protein Structure, Quaternary; Protein Structure, Secondary; Surface Plasmon Resonance; Unilamellar Liposomes | 2008 |
Broken helix in vesicle and micelle-bound alpha-synuclein: insights from site-directed spin labeling-EPR experiments and MD simulations.
Topics: alpha-Synuclein; Amino Acid Sequence; Computer Simulation; Electron Spin Resonance Spectroscopy; Humans; Lipid Bilayers; Micelles; Models, Molecular; Molecular Sequence Data; Nuclear Magnetic Resonance, Biomolecular; Phosphatidylcholines; Protein Structure, Secondary; Sodium Dodecyl Sulfate; Spin Labels | 2008 |
The effects of alpha-synuclein on phospholipid vesicle integrity: a study using 31P NMR and electron microscopy.
Topics: alpha-Synuclein; Liposomes; Magnetic Resonance Spectroscopy; Manganese; Membrane Fusion; Microscopy, Electron; Models, Biological; Peptide Fragments; Permeability; Phosphatidylcholines; Phosphatidylglycerols; Phospholipids; Phosphorus Isotopes; Synapses | 2008 |
Clustering of alpha-synuclein on supported lipid bilayers: role of anionic lipid, protein, and divalent ion concentration.
Topics: alpha-Synuclein; Calcium; Cations, Divalent; Cyclic AMP; Fluorescence Recovery After Photobleaching; Humans; Lipid Bilayers; Membrane Lipids; Microscopy, Fluorescence; Phosphatidylcholines; Phosphatidylglycerols; Phospholipids; Protein Binding; Protein Conformation; Proteins | 2009 |
Adsorption of alpha-synuclein on lipid bilayers: modulating the structure and stability of protein assemblies.
Topics: Adsorption; alpha-Synuclein; Hydrogen-Ion Concentration; Kinetics; Lipid Bilayers; Phosphatidylcholines; Protein Stability; Thermodynamics | 2010 |
Molecular basis for the glycosphingolipid-binding specificity of α-synuclein: key role of tyrosine 39 in membrane insertion.
Topics: alpha-Synuclein; Amino Acid Sequence; Amyloid beta-Peptides; Cell Membrane; Gangliosides; Glycosphingolipids; Humans; Membrane Microdomains; Molecular Dynamics Simulation; Molecular Sequence Data; Peptide Fragments; Phosphatidylcholines; Protein Binding; Protein Conformation; Sphingomyelins; Tyrosine | 2011 |
Kinetic measurements give new insights into lipid membrane permeabilization by α-synuclein oligomers.
Topics: 4-Chloro-7-nitrobenzofurazan; alpha-Synuclein; Dithionite; Humans; Kinetics; Membrane Lipids; Permeability; Phosphatidylcholines; Protein Structure, Quaternary; Unilamellar Liposomes | 2012 |
The amphipathic helix of an enzyme that regulates phosphatidylcholine synthesis remodels membranes into highly curved nanotubules.
Topics: alpha-Synuclein; Amino Acid Motifs; Animals; Caenorhabditis elegans; Caenorhabditis elegans Proteins; Choline-Phosphate Cytidylyltransferase; Membranes, Artificial; Nanotubes; Phosphatidylcholines; Rats | 2012 |
Locally resolved membrane binding affinity of the N-terminus of α-synuclein.
Topics: alpha-Synuclein; Cell Membrane; Electron Spin Resonance Spectroscopy; Humans; Lewy Bodies; Membranes, Artificial; Mutation; Phosphatidylcholines; Phosphatidylglycerols; Phospholipids | 2012 |
A 22-mer segment in the structurally pliable regulatory domain of metazoan CTP: phosphocholine cytidylyltransferase facilitates both silencing and activating functions.
Topics: alpha-Synuclein; Amino Acid Motifs; Amino Acid Sequence; Animals; Catalysis; Catalytic Domain; Choline-Phosphate Cytidylyltransferase; Computational Biology; Cytidine Triphosphate; Enzyme Activation; Gene Silencing; Kinetics; Lipids; Molecular Sequence Data; Phosphatidylcholines; Protein Conformation; Protein Structure, Secondary; Protein Structure, Tertiary; Rats; Sequence Homology, Amino Acid | 2012 |
α-Synuclein oligomers with broken helical conformation form lipoprotein nanoparticles.
Topics: alpha-Synuclein; Cholesterol; Chromatography, Gel; Cryoelectron Microscopy; Fluorescence Resonance Energy Transfer; Humans; Lipoproteins; Membranes, Artificial; Mitochondrial Membranes; Nanoparticles; Particle Size; Phosphatidylcholines; Phosphatidylglycerols; Phosphatidylserines; Protein Structure, Quaternary; Protein Structure, Secondary | 2013 |
Membrane bound α-synuclein is fully embedded in the lipid bilayer while segments with higher flexibility remain.
Topics: Acrylamide; alpha-Synuclein; Amino Acid Sequence; Cell Membrane; Humans; Lipid Bilayers; Lipids; Micelles; Molecular Sequence Data; Parkinson Disease; Phosphatidylcholines; Phosphatidylserines; Protein Binding; Protein Structure, Tertiary; Tryptophan | 2013 |
Membrane remodeling by α-synuclein and effects on amyloid formation.
Topics: Adenosine; alpha-Synuclein; Amyloid; Cholesterol; Circular Dichroism; Glycerophospholipids; Indicators and Reagents; Lipid Bilayers; Lipids; Membranes, Artificial; Microscopy, Electron, Transmission; Microtubules; Neutrons; Phosphatidylcholines; Spectrophotometry, Ultraviolet; Tryptophan | 2013 |
Ca(2+) modulating α-synuclein membrane transient interactions revealed by solution NMR spectroscopy.
Topics: Adenosine; alpha-Synuclein; Apolipoprotein A-I; Calcium; Cell Membrane; Glycerophospholipids; Humans; Lipid Bilayers; Magnetic Resonance Spectroscopy; Phosphatidylcholines; Protein Binding | 2014 |
Modelling Ser129 phosphorylation inhibits membrane binding of pore-forming alpha-synuclein oligomers.
Topics: 1,2-Dipalmitoylphosphatidylcholine; alpha-Synuclein; Cell Membrane; Humans; Mutation; Phosphatidylcholines; Phosphorylation; Porosity; Protein Binding; Protein Multimerization; Protein Structure, Quaternary; Serine; Temperature; Unilamellar Liposomes | 2014 |
Amyloids of alpha-synuclein affect the structure and dynamics of supported lipid bilayers.
Topics: Adsorption; alpha-Synuclein; Amyloid; Benzothiazoles; Lipid Bilayers; Liposomes; Mutant Proteins; Phosphatidylcholines; Phosphatidylglycerols; Protein Aggregates; Protein Binding; Staining and Labeling; Thiazoles | 2014 |
α-Synuclein-induced membrane remodeling is driven by binding affinity, partition depth, and interleaflet order asymmetry.
Topics: alpha-Synuclein; Lipids; Membranes, Artificial; Phosphatidylcholines; Phosphatidylglycerols | 2014 |
Phosphatase CD45 both positively and negatively regulates T cell receptor phosphorylation in reconstituted membrane protein clusters.
Topics: alpha-Synuclein; Animals; Baculoviridae; Escherichia coli; Gene Expression Regulation; Genes, Reporter; Green Fluorescent Proteins; Humans; Jurkat Cells; Leukocyte Common Antigens; Lipid Bilayers; Liposomes; Lymphocyte Specific Protein Tyrosine Kinase p56(lck); Molecular Imaging; Phosphatidylcholines; Phosphatidylserines; Phosphorylation; Receptors, Antigen, T-Cell; Recombinant Proteins; Sf9 Cells; Signal Transduction; Spodoptera | 2014 |
Besides fibrillization: putative role of the peptide fragment 71-82 on the structural and assembly behavior of α-synuclein.
Topics: alpha-Synuclein; Amyloid; Circular Dichroism; Humans; Lipid Bilayers; Models, Molecular; Nuclear Magnetic Resonance, Biomolecular; Osmolar Concentration; Peptide Fragments; Phosphatidylcholines; Phosphatidylglycerols; Protein Aggregation, Pathological; Protein Conformation; Protein Interaction Domains and Motifs; Protein Stability; Protein Structure, Secondary; Protein Unfolding; Solubility; Temperature | 2014 |
The newly discovered Parkinson's disease associated Finnish mutation (A53E) attenuates α-synuclein aggregation and membrane binding.
Topics: alpha-Synuclein; Amino Acid Substitution; Amyloid; Circular Dichroism; Finland; Fluorescent Dyes; Humans; Kinetics; Lipid Bilayers; Microscopy, Atomic Force; Mutation; Parkinson Disease; Phosphatidylcholines; Phosphatidylethanolamines; Protein Aggregation, Pathological; Protein Structure, Secondary; Recombinant Proteins; Spectrometry, Fluorescence; Surface Plasmon Resonance; Surface Properties | 2014 |
Oligomers of Parkinson's Disease-Related α-Synuclein Mutants Have Similar Structures but Distinctive Membrane Permeabilization Properties.
Topics: alpha-Synuclein; Cell Membrane Permeability; Fluoresceins; Humans; Membranes, Artificial; Multiprotein Complexes; Mutation, Missense; Parkinson Disease; Phosphatidylcholines; Phosphatidylethanolamines; Phosphatidylglycerols; Protein Binding; Scattering, Small Angle; X-Ray Diffraction | 2015 |
Alpha-synuclein and familial variants affect the chain order and the thermotropic phase behavior of anionic lipid vesicles.
Topics: alpha-Synuclein; Amino Acid Substitution; Gene Expression; Humans; Lipid Bilayers; Mutation; Phase Transition; Phosphatidylcholines; Phosphatidylglycerols; Protein Binding; Protein Conformation, alpha-Helical; Protein Conformation, beta-Strand; Protein Folding; Protein Interaction Domains and Motifs; Recombinant Proteins; Solutions; Structure-Activity Relationship; Thermodynamics | 2016 |
Chemical Compensation of Mitochondrial Phospholipid Depletion in Yeast and Animal Models of Parkinson's Disease.
Topics: alpha-Synuclein; Animals; Caenorhabditis elegans; Caenorhabditis elegans Proteins; Carboxy-Lyases; Cyclosporine; Disease Models, Animal; Dopaminergic Neurons; Endoplasmic Reticulum Stress; Meclofenoxate; Membrane Proteins; Mitochondria; Mitochondrial Proteins; Parkinson Disease; Phosphatidylcholines; Phosphatidylethanolamines; Protective Agents; Saccharomyces cerevisiae; Solubility; Sulfaphenazole; Transferases (Other Substituted Phosphate Groups) | 2016 |
Polyunsaturated chains in asymmetric lipids disorder raft mixtures and preferentially associate with α-Synuclein.
Topics: 1,2-Dipalmitoylphosphatidylcholine; alpha-Synuclein; Biomimetic Materials; Cholesterol; Humans; Membrane Microdomains; Molecular Conformation; Molecular Dynamics Simulation; Phase Transition; Phosphatidylcholines; Protein Binding; Static Electricity | 2017 |
α-Synuclein Oligomers Stabilize Pre-Existing Defects in Supported Bilayers and Propagate Membrane Damage in a Fractal-Like Pattern.
Topics: alpha-Synuclein; Cell Membrane; Fractals; Lipid Bilayers; Microscopy, Atomic Force; Microscopy, Confocal; Phosphatidylcholines; Phosphatidylserines; Time-Lapse Imaging; Unilamellar Liposomes | 2016 |
Site-Specific Fluorescence Polarization for Studying the Disaggregation of α-Synuclein Fibrils by Small Molecules.
Topics: alpha-Synuclein; Amino Acid Sequence; Catechin; Dopamine; Fluorescence Polarization; Fluorescent Dyes; Humans; Masoprocol; Phosphatidylcholines; Protein Aggregates; Recombinant Proteins; Small Molecule Libraries; Sodium Dodecyl Sulfate; Unilamellar Liposomes; Xanthenes | 2017 |
Membrane-induced initial structure of α-synuclein control its amyloidogenesis on model membranes.
Topics: alpha-Synuclein; Amyloid; Dose-Response Relationship, Drug; Dynamic Light Scattering; Humans; Membrane Lipids; Models, Chemical; Nuclear Magnetic Resonance, Biomolecular; Phosphatidylcholines; Phosphatidylethanolamines; Phosphatidylserines; Protein Binding; Protein Conformation; Sequence Deletion; Unilamellar Liposomes | 2018 |
Structural and Aggregation Properties of Alpha-Synuclein Linked to Phospholipase A2 Action.
Topics: alpha-Synuclein; Animals; Arachidonic Acid; Fatty Acid-Binding Proteins; Fluorescent Dyes; Humans; Liposomes; Mice; Oxidation-Reduction; Parkinson Disease; Phosphatidylcholines; Phospholipases A2; Protein Aggregates; Protein Conformation; RAW 264.7 Cells; Recombinant Proteins | 2018 |
The localization of α-synuclein in the process of differentiation of human erythroid cells.
Topics: Acetylation; alpha-Synuclein; Cell Differentiation; Cell Membrane; Cell Nucleus; Cells, Cultured; Cytoplasm; Erythroblasts; Erythrocytes; Gene Expression; Humans; Liposomes; Phosphatidylcholines; Phosphatidylserines; Protein Binding; Recombinant Proteins; RNA, Messenger | 2018 |
Supported Lipid Bilayers for Atomic Force Microscopy Studies.
Topics: alpha-Synuclein; Aluminum Silicates; Lipid Bilayers; Microscopy, Atomic Force; Phosphatidylcholines; Reproducibility of Results; Time-Lapse Imaging | 2018 |
Assembly of α-synuclein aggregates on phospholipid bilayers.
Topics: alpha-Synuclein; Computer Simulation; Humans; Lipid Bilayers; Models, Chemical; Phosphatidylcholines; Phosphatidylserines; Protein Aggregates | 2019 |
An aminoglycoside antibiotic inhibits both lipid-induced and solution-phase fibrillation of α-synuclein in vitro.
Topics: alpha-Synuclein; Anti-Bacterial Agents; Cell Line, Tumor; Humans; Kanamycin; Phosphatidylcholines; Phosphatidylethanolamines; Phosphatidylserines; Protein Binding; Protein Conformation; Protein Multimerization; Unilamellar Liposomes | 2019 |
GM1 Ganglioside role in the interaction of Alpha-synuclein with lipid membranes: Morphology and structure.
Topics: alpha-Synuclein; Dimyristoylphosphatidylcholine; G(M1) Ganglioside; Humans; Lipid Bilayers; Microscopy, Atomic Force; Neutron Diffraction; Phosphatidylcholines; Protein Aggregates; Protein Binding; Scattering, Small Angle | 2019 |
Membrane Interactions of α-Synuclein Probed by Neutrons and Photons.
Topics: alpha-Synuclein; Amino Acid Sequence; Cell Membrane; Glucosylceramidase; Humans; Lipid Bilayers; Neutrons; Phosphatidylcholines; Photons; Protein Aggregates; Protein Binding | 2021 |
Membrane packing defects in synaptic vesicles recruit complexin and synuclein.
Topics: Adaptor Proteins, Vesicular Transport; alpha-Synuclein; Cholesterol; Hydrogen Bonding; Lipid Bilayers; Molecular Dynamics Simulation; Nerve Tissue Proteins; Phosphatidylcholines; Phosphatidylethanolamines; Phosphatidylserines; Protein Binding; Synaptic Vesicles | 2021 |
The Cytotoxic Effect of α-Synuclein Aggregates.
Topics: alpha-Synuclein; Animals; Cell Line, Tumor; Cell Membrane; Hydrophobic and Hydrophilic Interactions; L-Lactate Dehydrogenase; Lipid Bilayers; Mice; Phosphatidylcholines; Protein Aggregates; Protein Multimerization | 2021 |
α-Synuclein interacts differently with membranes mimicking the inner and outer leaflets of neuronal membranes.
Topics: alpha-Synuclein; Biomimetics; Cell Membrane; Cytoplasm; Humans; Membrane Lipids; Neurons; Parkinson Disease; Phosphatidylcholines; Phosphatidylethanolamines | 2022 |
Lipid pathway dysfunction is prevalent in patients with Parkinson's disease.
Topics: alpha-Synuclein; Biomarkers; Ceramides; Humans; Hydroxymethylglutaryl-CoA Reductase Inhibitors; Insulins; Leucine-Rich Repeat Serine-Threonine Protein Kinase-2; Parkinson Disease; Phosphatidylcholines; Sphingomyelins; Triglycerides | 2022 |
Phosphatidylcholine and Phosphatidylserine Uniquely Modify the Secondary Structure of α-Synuclein Oligomers Formed in Their Presence at the Early Stages of Protein Aggregation.
Topics: alpha-Synuclein; Cryoelectron Microscopy; Phosphatidylcholines; Phosphatidylserines; Protein Aggregates | 2022 |
Elucidation of Secondary Structure and Toxicity of α-Synuclein Oligomers and Fibrils Grown in the Presence of Phosphatidylcholine and Phosphatidylserine.
Topics: alpha-Synuclein; Animals; Cytoskeleton; Phosphatidylcholines; Phosphatidylserines; Phospholipids; Rats | 2023 |