Dissociation of amyloid fibrils of alpha-synuclein and transthyretin by pressure reveals their reversible nature and the formation of water-excluded cavities.
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Cavities determine the pressure unfolding of proteinsProtein aggregate structure under high pressure.Comparing the folding and misfolding energy landscapes of phosphoglycerate kinase.Revealing different aggregation pathways of amyloidogenic proteins by ultrasound velocimetry.Reversible aggregation plays a crucial role on the folding landscape of p53 core domain.Structural basis for the dissociation of α-synuclein fibrils triggered by pressure perturbation of the hydrophobic core.The amino-terminal PrP domain is crucial to modulate prion misfolding and aggregation.Fourier transform infrared spectroscopy provides a fingerprint for the tetramer and for the aggregates of transthyretin.The p53 core domain is a molten globule at low pH: functional implications of a partially unfolded structure.Ligand binding and hydration in protein misfolding: insights from studies of prion and p53 tumor suppressor proteins.Physiological IgM class catalytic antibodies selective for transthyretin amyloid.Pressure denaturation of staphylococcal nuclease studied by neutron small-angle scattering and molecular simulationTemperature-dependent structural changes of Parkinson's alpha-synuclein reveal the role of pre-existing oligomers in alpha-synuclein fibrillizationAmyloid features and neuronal toxicity of mature prion fibrils are highly sensitive to high pressureQuaternary structure of pathological prion protein as a determining factor of strain-specific prion replication dynamics.Microbial diversity and adaptation to high hydrostatic pressure in deep-sea hydrothermal vents prokaryotes.Volume and energy folding landscape of prion protein revealed by pressure.Potency under pressure: the impact of hydrostatic pressure on antigenic properties of influenza virus hemagglutininHigh pressure promotes alpha-synuclein aggregation in cultured neuronal cells.The role of the 132-160 region in prion protein conformational transitions.Molecular dynamics simulations of mechanical failure in polymorphic arrangements of amyloid fibrils containing structural defects.Pressure-dissociable reversible assembly of intrinsically denatured lysozyme is a precursor for amyloid fibrils.Pressure to kill or pressure to boost: a review on the various effects and applications of hydrostatic pressure in bacterial biotechnology.Modulation of prion protein oligomerization, aggregation, and beta-sheet conversion by 4,4'-dianilino-1,1'-binaphthyl-5,5'-sulfonate (bis-ANS).Pressure-A Gateway to Fundamental Insights into Protein Solvation, Dynamics, and Function.Fluorescent N-arylaminonaphthalene sulfonate probes for amyloid aggregation of alpha-synuclein.Inflammation protein SAA2.2 spontaneously forms marginally stable amyloid fibrils at physiological temperature.Aggregation and Prion-Like Properties of Misfolded Tumor Suppressors: Is Cancer a Prion Disease?Effects of salt or cosolvent addition on solubility of a hydrophobic solute in water: Relevance to those on thermal stability of a protein.Transthyretin aggregates induce production of reactive nitrogen species.Hydrostatic Pressure Increases the Catalytic Activity of Amyloid Fibril Enzymes.Pressure-accelerated dissociation of amyloid fibrils in wild-type hen lysozyme.Controlling {beta}-amyloid oligomerization by the use of naphthalene sulfonates: trapping low molecular weight oligomeric species.Kinetic analysis of amyloid protofibril dissociation and volumetric properties of the transition state.Effects of solutes on solubilization and refolding of proteins from inclusion bodies with high hydrostatic pressure.Concentration dependence of alpha-synuclein fibril length assessed by quantitative atomic force microscopy and statistical-mechanical theory.Recovery of functional enzyme from amyloid fibrils.Nonequilibrium all-atom molecular dynamics simulation of the bubble cavitation and application to dissociate amyloid fibrils.A comprehensive model for packing and hydration for amyloid fibrils of beta2-microglobulin.Simulation studies on the stabilities of aggregates formed by fibril-forming segments of alpha-Synuclein.
P2860
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P2860
Dissociation of amyloid fibrils of alpha-synuclein and transthyretin by pressure reveals their reversible nature and the formation of water-excluded cavities.
description
2003 nî lūn-bûn
@nan
2003年の論文
@ja
2003年論文
@yue
2003年論文
@zh-hant
2003年論文
@zh-hk
2003年論文
@zh-mo
2003年論文
@zh-tw
2003年论文
@wuu
2003年论文
@zh
2003年论文
@zh-cn
name
Dissociation of amyloid fibril ...... on of water-excluded cavities.
@ast
Dissociation of amyloid fibril ...... on of water-excluded cavities.
@en
type
label
Dissociation of amyloid fibril ...... on of water-excluded cavities.
@ast
Dissociation of amyloid fibril ...... on of water-excluded cavities.
@en
prefLabel
Dissociation of amyloid fibril ...... on of water-excluded cavities.
@ast
Dissociation of amyloid fibril ...... on of water-excluded cavities.
@en
P2093
P2860
P50
P356
P1476
Dissociation of amyloid fibril ...... on of water-excluded cavities.
@en
P2093
Astria D Ferrão-Gonzales
Carla M Einsiedler
Leonardo Palmieri
Marisa C Suarez
Peter T Lansbury
Thais C R Porto
P2860
P304
P356
10.1073/PNAS.1734009100
P407
P577
2003-08-04T00:00:00Z