High-Pressure-Driven Reversible Dissociation of α-Synuclein Fibrils Reveals Structural Hierarchy.

scientific article published in October 2017

High-Pressure-Driven Reversible Dissociation of α-Synuclein Fibrils Reveals Structural Hierarchy. is …
instance of (P31):
scholarly articleQ13442814

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P356DOI10.1016/J.BPJ.2017.08.042
P932PMC publication ID5647593
P698PubMed publication ID29045863

P50authorNicoletta PlotegherQ55030167
Marco BrucaleQ57061159
Isabella TessariQ57247794
Francesco SpinozziQ63694367
Valeria MilitelloQ114399822
Federica PiccirilliQ117251432
Mariano BeltraminiQ117251434
Stefano LupiQ117251436
Andrea PerucchiQ117251438
Luigi BubaccoQ38543824
Paolo MarianiQ41619738
Maria Grazia OrtoreQ43052907
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Alpha-synuclein promotes SNARE-complex assembly in vivo and in vitroQ24629968
Alpha-synuclein in Lewy bodiesQ27860680
Immunoelectron-microscopic demonstration of NACP/alpha-synuclein-epitopes on the filamentous component of Lewy bodies in Parkinson's disease and in dementia with Lewy bodiesQ28287237
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Molecular recycling within amyloid fibrilsQ30160171
Oxidative dimer formation is the critical rate-limiting step for Parkinson's disease alpha-synuclein fibrillogenesisQ30881832
Structural basis for the dissociation of α-synuclein fibrils triggered by pressure perturbation of the hydrophobic coreQ31145567
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Mapping Long-Range Interactions in α-Synuclein using Spin-Label NMR and Ensemble Molecular Dynamics SimulationsQ57976902
Preparation and Characterization of Purified Amyloid FibrilsQ58374790
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Increased expression of alpha-synuclein reduces neurotransmitter release by inhibiting synaptic vesicle reclustering after endocytosisQ35058315
Progressive aggregation of alpha-synuclein and selective degeneration of lewy inclusion-bearing neurons in a mouse model of parkinsonismQ35151971
Structured regions of α-synuclein fibrils include the early-onset Parkinson's disease mutation sites.Q35168339
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Dissociation of amyloid fibrils of alpha-synuclein and transthyretin by pressure reveals their reversible nature and the formation of water-excluded cavitiesQ35813797
Structure of the toxic core of α-synuclein from invisible crystalsQ36685232
The fold of alpha-synuclein fibrilsQ36735295
Pressure-induced protein-folding/unfolding kineticsQ36774807
NACP, a protein implicated in Alzheimer's disease and learning, is natively unfoldedQ36830682
Reducing C-terminal truncation mitigates synucleinopathy and neurodegeneration in a transgenic model of multiple system atrophyQ37213903
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 toxicityQ38180144
Structural disorder of monomeric α-synuclein persists in mammalian cells.Q38799574
α-Synuclein strains cause distinct synucleinopathies after local and systemic administrationQ41681113
α-Synuclein inhibits intersynaptic vesicle mobility and maintains recycling-pool homeostasisQ41901772
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
P433issue8
P407language of work or nameEnglishQ1860
P921main subjectSynucleinQ24767155
P304page(s)1685-1696
P577publication date2017-10-01
P1433published inBiophysical JournalQ2032955
P1476titleHigh-Pressure-Driven Reversible Dissociation of α-Synuclein Fibrils Reveals Structural Hierarchy
P478volume113

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cites work (P2860)
Q61797140Early Stage Alpha-Synuclein Amyloid Fibrils are Reservoirs of Membrane-Binding Species
Q64869800Multi-Pronged Interactions Underlie Inhibition of α-Synuclein Aggregation by β-Synuclein
Q90161028Pressure dependence of vibrational optical activity of model biomolecules. A computational study

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