| scholarly article | Q13442814 |
| P50 | author | Alice Soragni | Q52617115 |
| P2093 | author name string | Roland Riek | |
| Stefan Seeger | |||
| Dorinel Verdes | |||
| Nicholas P Reynolds | |||
| Michael Rabe | |||
| Ennio Liverani | |||
| P2860 | cites work | Mutation in the alpha-synuclein gene identified in families with Parkinson's disease | Q27860459 |
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| Clustering of alpha-synuclein on supported lipid bilayers: role of anionic lipid, protein, and divalent ion concentration | Q30374521 | ||
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| The UCH-L1 gene encodes two opposing enzymatic activities that affect alpha-synuclein degradation and Parkinson's disease susceptibility | Q34157005 | ||
| Analyzing thioflavin T binding to amyloid fibrils by an equilibrium microdialysis-based technique | Q34181516 | ||
| Amyloid β-protein aggregation produces highly reproducible kinetic data and occurs by a two-phase process | Q34332006 | ||
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| The biochemistry of Parkinson's disease | Q34426026 | ||
| Effect of familial Parkinson's disease point mutations A30P and A53T on the structural properties, aggregation, and fibrillation of human alpha-synuclein | Q34517780 | ||
| Sulfated glycosaminoglycans accelerate transthyretin amyloidogenesis by quaternary structural conversion | Q34561167 | ||
| Low-resolution structure of a vesicle disrupting α-synuclein oligomer that accumulates during fibrillation | Q34602533 | ||
| In vivo demonstration that alpha-synuclein oligomers are toxic | Q34652122 | ||
| Acceleration of oligomerization, not fibrillization, is a shared property of both alpha-synuclein mutations linked to early-onset Parkinson's disease: implications for pathogenesis and therapy | Q34964783 | ||
| Nucleation of protein fibrillation by nanoparticles | Q35785510 | ||
| Fibril specific, conformation dependent antibodies recognize a generic epitope common to amyloid fibrils and fibrillar oligomers that is absent in prefibrillar oligomers | Q36178075 | ||
| Cell systems and the toxic mechanism(s) of alpha-synuclein | Q36440972 | ||
| The fold of alpha-synuclein fibrils | Q36735295 | ||
| Branching in amyloid fibril growth | Q37279173 | ||
| The two-fold aspect of the interplay of amyloidogenic proteins with lipid membranes. | Q37341219 | ||
| Kinetics of insulin aggregation in aqueous solutions upon agitation in the presence of hydrophobic surfaces | Q37610662 | ||
| Alpha-synuclein, lipids and Parkinson's disease | Q37767943 | ||
| Amyloidogenic protein-membrane interactions: mechanistic insight from model systems | Q37771927 | ||
| Assays for α-synuclein aggregation | Q37821550 | ||
| Α-synuclein misfolding and Parkinson's disease | Q37949158 | ||
| Alpha-synuclein, especially the Parkinson's disease-associated mutants, forms pore-like annular and tubular protofibrils | Q39632694 | ||
| Adsorption of alpha-synuclein on lipid bilayers: modulating the structure and stability of protein assemblies | Q40062265 | ||
| Fluorescence imaging of amyloid formation in living cells by a functional, tetracysteine-tagged alpha-synuclein | Q40160660 | ||
| Models of amyloid seeding in Alzheimer's disease and scrapie: mechanistic truths and physiological consequences of the time-dependent solubility of amyloid proteins | Q41550219 | ||
| alpha-synuclein fibrillogenesis is nucleation-dependent. Implications for the pathogenesis of Parkinson's disease | Q41676981 | ||
| The aggregation kinetics of Alzheimer's beta-amyloid peptide is controlled by stochastic nucleation | Q41839526 | ||
| Thioflavine T interaction with synthetic Alzheimer's disease beta-amyloid peptides: detection of amyloid aggregation in solution | Q42153291 | ||
| Heparin binds 8 kDa gelsolin cross-β-sheet oligomers and accelerates amyloidogenesis by hastening fibril extension | Q42203354 | ||
| Membrane interaction of α-synuclein in different aggregation states | Q42442931 | ||
| Fibrils formed in vitro from alpha-synuclein and two mutant forms linked to Parkinson's disease are typical amyloid | Q42620617 | ||
| In vitro formation of amyloid from alpha-synuclein is dominated by reactions at hydrophobic interfaces. | Q43005488 | ||
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| Surface-catalyzed amyloid fibril formation | Q44146881 | ||
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| Lipid bilayer disruption by oligomeric alpha-synuclein depends on bilayer charge and accessibility of the hydrophobic core. | Q45908123 | ||
| Islet amyloid polypeptide forms rigid lipid-protein amyloid fibrils on supported phospholipid bilayers | Q46835677 | ||
| Visualization and classification of amyloid beta supramolecular assemblies | Q46877303 | ||
| Rapid Anionic Micelle-mediated α-Synuclein Fibrillization in Vitro | Q47609800 | ||
| Accelerated in vitro fibril formation by a mutant alpha-synuclein linked to early-onset Parkinson disease | Q48353748 | ||
| Revealing two-state protein-protein interactions of calmodulin by single-molecule spectroscopy. | Q50726225 | ||
| A comprehensive study of concepts and phenomena of the nonspecific adsorption of beta-lactoglobulin. | Q51918943 | ||
| Mechanism of membrane interaction and disruption by α-synuclein. | Q52617078 | ||
| Formation of a High Affinity Lipid-Binding Intermediate during the Early Aggregation Phase of α-Synuclein† | Q57092800 | ||
| Nanometer Axial Resolution by Three-Dimensional Supercritical Angle Fluorescence Microscopy | Q58819494 | ||
| Surface Organization and Cooperativity during Nonspecific Protein Adsorption Events | Q58819502 | ||
| alpha-Synuclein membrane interactions and lipid specificity | Q74071513 | ||
| Phospholipid translocation from the outer to the inner leaflet of synaptic vesicle membranes isolated from the electric organ of Japanese electric ray Narke japonica | Q77359104 | ||
| Molecular crowding accelerates fibrillization of alpha-synuclein: could an increase in the cytoplasmic protein concentration induce Parkinson's disease? | Q77784550 | ||
| Secondary structure of alpha-synuclein oligomers: characterization by raman and atomic force microscopy | Q81515488 | ||
| P433 | issue | 3 | |
| P921 | main subject | Synuclein | Q24767155 |
| P304 | page(s) | 408-417 | |
| P577 | publication date | 2013-01-22 | |
| P1433 | published in | ACS Chemical Neuroscience | Q2819059 |
| P1476 | title | On-surface aggregation of α-synuclein at nanomolar concentrations results in two distinct growth mechanisms | |
| P478 | volume | 4 |
| Q36327854 | A novel pathway for amyloids self-assembly in aggregates at nanomolar concentration mediated by the interaction with surfaces. |
| Q35048929 | Acceleration of α-synuclein aggregation by exosomes |
| Q41142736 | Amyloids of alpha-synuclein affect the structure and dynamics of supported lipid bilayers. |
| Q22061724 | Digested disorder: Quarterly intrinsic disorder digest (January/February/March, 2013). |
| Q35529960 | Direct Detection of α-Synuclein Dimerization Dynamics: Single-Molecule Fluorescence Analysis |
| Q92942047 | Effect of Terminal Modifications on the Adsorption and Assembly of hIAPP(20-29) |
| Q46259884 | Factors affecting the physical stability (aggregation) of peptide therapeutics |
| Q57636158 | Membranes as modulators of amyloid protein misfolding and target of toxicity |
| Q46024871 | Nanoscale Dynamics of Amyloid β-42 Oligomers As Revealed by High-Speed Atomic Force Microscopy. |
| Q26823798 | Physicochemical properties of cells and their effects on intrinsically disordered proteins (IDPs) |
| Q38669105 | Review: Spreading the word: precise animal models and validated methods are vital when evaluating prion-like behaviour of alpha-synuclein |
| Q46242764 | Secondary nucleation of monomers on fibril surface dominates α-synuclein aggregation and provides autocatalytic amyloid amplification |
| Q58819456 | Solid supported lipid bilayers from artificial and natural lipid mixtures – long-term stable, homogeneous and reproducible |
| Q55122147 | Structural insights from lipid-bilayer nanodiscs link α-Synuclein membrane-binding modes to amyloid fibril formation |
| Q57149569 | Supercritical angle Raman microscopy: a surface-sensitive nanoscale technique without field enhancement |
| Q41549497 | The Impact of N-terminal Acetylation of α-Synuclein on Phospholipid Membrane Binding and Fibril Structure. |
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