A multiscale approach to characterize the early aggregation steps of the amyloid-forming peptide GNNQQNY from the yeast prion sup-35
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An Atomistic View of Amyloidogenic Self-assembly: Structure and Dynamics of Heterogeneous Conformational States in the Pre-nucleation Phase.Lattice model for amyloid peptides: OPEP force field parametrization and applications to the nucleus size of Alzheimer's peptides.Nanomaterials design and tests for neural tissue engineering.Amyloid β Protein and Alzheimer's Disease: When Computer Simulations Complement Experimental Studies.C-terminal domain swapping of SSB changes the size of the ssDNA binding siteKinetics of amyloid aggregation: a study of the GNNQQNY prion sequence.Exploring the role of hydration and confinement in the aggregation of amyloidogenic peptides Aβ(16-22) and Sup35(7-13) in AOT reverse micellesThe OPEP protein model: from single molecules, amyloid formation, crowding and hydrodynamics to DNA/RNA systemsComputational modeling of the relationship between amyloid and disease.SAHBNET, an accessible surface-based elastic network: an application to membrane protein.Protein Simulations in Fluids: Coupling the OPEP Coarse-Grained Force Field with HydrodynamicsThe architecture of amyloid-like peptide fibrils revealed by X-ray scattering, diffraction and electron microscopy.Role of monomer arrangement in the amyloid self-assembly.A kinetic approach to the sequence-aggregation relationship in disease-related protein assemblyStudying interactions by molecular dynamics simulations at high concentration.Importance of the ion-pair interactions in the OPEP coarse-grained force field: parametrization and validation.Thermodynamic analysis of structural transitions during GNNQQNY aggregation.Hydrodynamic effects on β-amyloid (16-22) peptide aggregation.Inhibition of GNNQQNY prion peptide aggregation by trehalose: a mechanistic view.Nucleation process of a fibril precursor in the C-terminal segment of amyloid-β.Understanding Amyloid-β Oligomerization at the Molecular Level: The Role of the Fibril Surface.Inhibitory effect of hydrophobic fullerenes on the β-sheet-rich oligomers of a hydrophilic GNNQQNY peptide revealed by atomistic simulationsStructural, thermodynamical, and dynamical properties of oligomers formed by the amyloid NNQQ peptide: Insights from coarse-grained simulations
P2860
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P2860
A multiscale approach to characterize the early aggregation steps of the amyloid-forming peptide GNNQQNY from the yeast prion sup-35
description
2011 nî lūn-bûn
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2011 թուականի Մայիսին հրատարակուած գիտական յօդուած
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2011 թվականի մայիսին հրատարակված գիտական հոդված
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2011年の論文
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2011年論文
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2011年論文
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2011年論文
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2011年論文
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2011年論文
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2011年论文
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name
A multiscale approach to chara ...... NY from the yeast prion sup-35
@ast
A multiscale approach to chara ...... NY from the yeast prion sup-35
@en
A multiscale approach to chara ...... NY from the yeast prion sup-35
@nl
type
label
A multiscale approach to chara ...... NY from the yeast prion sup-35
@ast
A multiscale approach to chara ...... NY from the yeast prion sup-35
@en
A multiscale approach to chara ...... NY from the yeast prion sup-35
@nl
prefLabel
A multiscale approach to chara ...... NY from the yeast prion sup-35
@ast
A multiscale approach to chara ...... NY from the yeast prion sup-35
@en
A multiscale approach to chara ...... NY from the yeast prion sup-35
@nl
P2860
P50
P3181
P1476
A multiscale approach to chara ...... NY from the yeast prion sup-35
@en
P2093
Jessica Nasica-Labouze
Philippe Derreumaux
P2860
P304
P3181
P356
10.1371/JOURNAL.PCBI.1002051
P407
P577
2011-05-01T00:00:00Z