scholarly article | Q13442814 |
P50 | author | Nicoletta Plotegher | Q55030167 |
Marco Brucale | Q57061159 | ||
Isabella Tessari | Q57247794 | ||
Francesco Spinozzi | Q63694367 | ||
Valeria Militello | Q114399822 | ||
Federica Piccirilli | Q117251432 | ||
Mariano Beltramini | Q117251434 | ||
Stefano Lupi | Q117251436 | ||
Andrea Perucchi | Q117251438 | ||
Luigi Bubacco | Q38543824 | ||
Paolo Mariani | Q41619738 | ||
Maria Grazia Ortore | Q43052907 | ||
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α-Synuclein occurs physiologically as a helically folded tetramer that resists aggregation | Q24605589 | ||
Alpha-synuclein promotes SNARE-complex assembly in vivo and in vitro | Q24629968 | ||
Alpha-synuclein in Lewy bodies | Q27860680 | ||
Immunoelectron-microscopic demonstration of NACP/alpha-synuclein-epitopes on the filamentous component of Lewy bodies in Parkinson's disease and in dementia with Lewy bodies | Q28287237 | ||
Stabilization of alpha-synuclein secondary structure upon binding to synthetic membranes | Q29617606 | ||
Molecular recycling within amyloid fibrils | Q30160171 | ||
Oxidative dimer formation is the critical rate-limiting step for Parkinson's disease alpha-synuclein fibrillogenesis | Q30881832 | ||
Structural basis for the dissociation of α-synuclein fibrils triggered by pressure perturbation of the hydrophobic core | Q31145567 | ||
Dissociation of amyloid fibrils of alpha-synuclein in supercooled water. | Q31157430 | ||
Early aggregation steps in alpha-synuclein as measured by FCS and FRET: evidence for a contagious conformational change. | Q33550002 | ||
Role of alpha-synuclein carboxy-terminus on fibril formation in vitro | Q47762431 | ||
Decoding vibrational states of Concanavalin A amyloid fibrils | Q57160336 | ||
Structural properties of pore-forming oligomers of alpha-synuclein | Q57185914 | ||
Mapping Long-Range Interactions in α-Synuclein using Spin-Label NMR and Ensemble Molecular Dynamics Simulations | Q57976902 | ||
Preparation and Characterization of Purified Amyloid Fibrils | Q58374790 | ||
Dityrosine cross-linking promotes formation of stable alpha -synuclein polymers. Implication of nitrative and oxidative stress in the pathogenesis of neurodegenerative synucleinopathies | Q73626218 | ||
Cold denaturation of α-synuclein amyloid fibrils | Q88061055 | ||
Synucleins in synaptic plasticity and neurodegenerative disorders | Q33734797 | ||
The behavior of the hydrophobic effect under pressure and protein denaturation | Q33795513 | ||
Simultaneous monitoring of light-induced changes in protein side-group protonation, chromophore isomerization, and backbone motion of bacteriorhodopsin by time-resolved Fourier-transform infrared spectroscopy | Q33926063 | ||
The infrared absorption of amino acid side chains | Q34166914 | ||
Determination of the volume changes for pressure-induced transitions of apomyoglobin between the native, molten globule, and unfolded states | Q34168480 | ||
A general model for amyloid fibril assembly based on morphological studies using atomic force microscopy | Q34182333 | ||
Covalent α-synuclein dimers: chemico-physical and aggregation properties | Q34524912 | ||
In vivo demonstration that alpha-synuclein oligomers are toxic | Q34652122 | ||
Perturbation of the stability of amyloid fibrils through alteration of electrostatic interactions | Q35051211 | ||
Increased expression of alpha-synuclein reduces neurotransmitter release by inhibiting synaptic vesicle reclustering after endocytosis | Q35058315 | ||
Progressive aggregation of alpha-synuclein and selective degeneration of lewy inclusion-bearing neurons in a mouse model of parkinsonism | Q35151971 | ||
Structured regions of α-synuclein fibrils include the early-onset Parkinson's disease mutation sites. | Q35168339 | ||
Parkinson's disease and related alpha-synucleinopathies are brain amyloidoses | Q35171003 | ||
Fiber diffraction of synthetic alpha-synuclein filaments shows amyloid-like cross-beta conformation | Q35700288 | ||
Aggregation of α-synuclein is kinetically controlled by intramolecular diffusion | Q35786977 | ||
Dissociation of amyloid fibrils of alpha-synuclein and transthyretin by pressure reveals their reversible nature and the formation of water-excluded cavities | Q35813797 | ||
Structure of the toxic core of α-synuclein from invisible crystals | Q36685232 | ||
The fold of alpha-synuclein fibrils | Q36735295 | ||
Pressure-induced protein-folding/unfolding kinetics | Q36774807 | ||
NACP, a protein implicated in Alzheimer's disease and learning, is natively unfolded | Q36830682 | ||
Reducing C-terminal truncation mitigates synucleinopathy and neurodegeneration in a transgenic model of multiple system atrophy | Q37213903 | ||
Solid-state NMR structure of a pathogenic fibril of full-length human α-synuclein. | Q37278078 | ||
Biophysical groundwork as a hinge to unravel the biology of α-synuclein aggregation and toxicity | Q38180144 | ||
Structural disorder of monomeric α-synuclein persists in mammalian cells. | Q38799574 | ||
α-Synuclein strains cause distinct synucleinopathies after local and systemic administration | Q41681113 | ||
α-Synuclein inhibits intersynaptic vesicle mobility and maintains recycling-pool homeostasis | Q41901772 | ||
Tyrosine 125 of alpha-synuclein plays a critical role for dimerization following nitrative stress. | Q44006670 | ||
Role of different regions of alpha-synuclein in the assembly of fibrils. | Q46027264 | ||
Pressure effects on α-synuclein amyloid fibrils: An experimental investigation on their dissociation and reversible nature. | Q46348663 | ||
The reaction of alpha-synuclein with tyrosinase: possible implications for Parkinson disease. | Q46663033 | ||
P433 | issue | 8 | |
P407 | language of work or name | English | Q1860 |
P921 | main subject | Synuclein | Q24767155 |
P304 | page(s) | 1685-1696 | |
P577 | publication date | 2017-10-01 | |
P1433 | published in | Biophysical Journal | Q2032955 |
P1476 | title | High-Pressure-Driven Reversible Dissociation of α-Synuclein Fibrils Reveals Structural Hierarchy | |
P478 | volume | 113 |
Q61797140 | Early Stage Alpha-Synuclein Amyloid Fibrils are Reservoirs of Membrane-Binding Species |
Q64869800 | Multi-Pronged Interactions Underlie Inhibition of α-Synuclein Aggregation by β-Synuclein |
Q90161028 | Pressure dependence of vibrational optical activity of model biomolecules. A computational study |
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