Thermodynamic selection of steric zipper patterns in the amyloid cross-beta spine
about
Structural Conversion of Aβ17-42 Peptides from Disordered Oligomers to U-Shape Protofilaments via Multiple Kinetic PathwaysMapping the conformational dynamics and pathways of spontaneous steric zipper Peptide oligomerizationA multiscale approach to characterize the early aggregation steps of the amyloid-forming peptide GNNQQNY from the yeast prion sup-35The stability of cylindrin β-barrel amyloid oligomer models-a molecular dynamics study.Amyloid β Protein and Alzheimer's Disease: When Computer Simulations Complement Experimental Studies.Polymorphism in Alzheimer Abeta amyloid organization reflects conformational selection in a rugged energy landscape.Impact of sequence on the molecular assembly of short amyloid peptides.Kinetics of amyloid aggregation: a study of the GNNQQNY prion sequence.Structural characterization of GNNQQNY amyloid fibrils by magic angle spinning NMRStability of Iowa mutant and wild type Aβ-peptide aggregatesRole of sequence and structural polymorphism on the mechanical properties of amyloid fibrilsRole of hydration force in the self-assembly of collagens and amyloid steric zipper filamentsStructural complexity of a composite amyloid fibril.Spontaneous formation of twisted Aβ(16-22) fibrils in large-scale molecular-dynamics simulations.Effect of single point mutations in a form of systemic amyloidosis.In silico cross seeding of Aβ and amylin fibril-like oligomers.Mutations and seeding of amylin fibril-like oligomers.Yeast cell adhesion molecules have functional amyloid-forming sequences.A kinetic approach to the sequence-aggregation relationship in disease-related protein assemblyThermodynamic analysis of structural transitions during GNNQQNY aggregation.Probing the role of aromatic residues in the self-assembly of Aβ(16-22) in fluorinated alcohols and their aqueous mixtures.Binding of ACE-inhibitors to in vitro and patient-derived amyloid-β fibril models.Nucleation process of a fibril precursor in the C-terminal segment of amyloid-β.Amyloid and the origin of life: self-replicating catalytic amyloids as prebiotic informational and protometabolic entities.Structural, thermodynamical, and dynamical properties of oligomers formed by the amyloid NNQQ peptide: Insights from coarse-grained simulations
P2860
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P2860
Thermodynamic selection of steric zipper patterns in the amyloid cross-beta spine
description
2009 nî lūn-bûn
@nan
2009 թուականի Սեպտեմբերին հրատարակուած գիտական յօդուած
@hyw
2009 թվականի սեպտեմբերին հրատարակված գիտական հոդված
@hy
2009年の論文
@ja
2009年論文
@yue
2009年論文
@zh-hant
2009年論文
@zh-hk
2009年論文
@zh-mo
2009年論文
@zh-tw
2009年论文
@wuu
name
Thermodynamic selection of steric zipper patterns in the amyloid cross-beta spine
@ast
Thermodynamic selection of steric zipper patterns in the amyloid cross-beta spine
@en
type
label
Thermodynamic selection of steric zipper patterns in the amyloid cross-beta spine
@ast
Thermodynamic selection of steric zipper patterns in the amyloid cross-beta spine
@en
prefLabel
Thermodynamic selection of steric zipper patterns in the amyloid cross-beta spine
@ast
Thermodynamic selection of steric zipper patterns in the amyloid cross-beta spine
@en
P2860
P1476
Thermodynamic selection of steric zipper patterns in the amyloid cross-beta spine
@en
P2093
Byungnam Kahng
Wonmuk Hwang
P2860
P304
P356
10.1371/JOURNAL.PCBI.1000492
P50
P577
2009-09-04T00:00:00Z