Alzheimer's disease amyloid propagation by a template-dependent dock-lock mechanism.
about
Gerstmann-Sträussler-Scheinker disease amyloid protein polymerizes according to the "dock-and-lock" modelInteraction between soluble Aβ-(1-40) monomer and Aβ-(1-42) fibrils probed by paramagnetic relaxation enhancementMechanism of prion propagation: amyloid growth occurs by monomer additionTargeting the proper amyloid-beta neuronal toxins: a path forward for Alzheimer's disease immunotherapeuticsTransient dynamics of Aβ contribute to toxicity in Alzheimer's diseaseA mathematical model of the kinetics of beta-amyloid fibril growth from the denatured stateStepwise dynamics of epitaxially growing single amyloid fibrils.Computational design of new Peptide inhibitors for amyloid Beta (aβ) aggregation in Alzheimer's disease: application of a novel methodologyAβ peptide fibrillar architectures controlled by conformational constraints of the monomerThe role of dynamic conformational ensembles in biomolecular recognitionβ-sheet propensity controls the kinetic pathways and morphologies of seeded peptide aggregation.Stepwise organization of the β-structure identifies key regions essential for the propagation and cytotoxicity of insulin amyloid fibrils.Fibronectins, their fibrillogenesis, and in vivo functions.Role of aggregation conditions in structure, stability, and toxicity of intermediates in the Abeta fibril formation pathwayDynamic imaging by fluorescence correlation spectroscopy identifies diverse populations of polyglutamine oligomers formed in vivo.Increased in vivo amyloid-β42 production, exchange, and loss in presenilin mutation carriersProbing the origins of increased activity of the E22Q "Dutch" mutant Alzheimer's beta-amyloid peptide.High-speed atomic force microscopy reveals structural dynamics of amyloid β1-42 aggregates.Selection of peptides binding to the amyloid b-protein reveals potential inhibitors of amyloid formation.Structural reorganisation and potential toxicity of oligomeric species formed during the assembly of amyloid fibrils.Model discrimination and mechanistic interpretation of kinetic data in protein aggregation studies.Principles governing oligomer formation in amyloidogenic peptides.Computational backbone mutagenesis of Abeta peptides: probing the role of backbone hydrogen bonds in aggregation.Differences in nucleation behavior underlie the contrasting aggregation kinetics of the Aβ40 and Aβ42 peptidesMolecular dynamics simulations of anti-aggregation effect of ibuprofen.Polymorphism in Alzheimer Abeta amyloid organization reflects conformational selection in a rugged energy landscape.Probing solvent accessibility of amyloid fibrils by solution NMR spectroscopyA peptide that binds specifically to the β-amyloid of Alzheimer's disease: selection and assessment of anti-β-amyloid neurotoxic effects.polyglutamine aggregation nucleation: thermodynamics of a highly unfavorable protein folding reactionRecognition between flexible protein molecules: induced and assisted folding.Fibril elongation by Aβ(17-42): kinetic network analysis of hybrid-resolution molecular dynamics simulationsCharacterization of the interaction of β-amyloid with transthyretin monomers and tetramers.Huntington's disease age-of-onset linked to polyglutamine aggregation nucleation.Mechanism of fiber assembly: treatment of Aβ peptide aggregation with a coarse-grained united-residue force field.Thermodynamic perspective on the dock-lock growth mechanism of amyloid fibrils.Kinetics of amyloid aggregation: a study of the GNNQQNY prion sequence.Nonsteroidal anti-inflammatory drug naproxen destabilizes Aβ amyloid fibrils: a molecular dynamics investigation.Macrocyclic β-sheet peptides that inhibit the aggregation of a tau-protein-derived hexapeptide.Exploring the role of hydration and confinement in the aggregation of amyloidogenic peptides Aβ(16-22) and Sup35(7-13) in AOT reverse micellesTRPM8 and Nav1.8 sodium channels are required for transthyretin-induced calcium influx in growth cones of small-diameter TrkA-positive sensory neurons.
P2860
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P2860
Alzheimer's disease amyloid propagation by a template-dependent dock-lock mechanism.
description
2000 nî lūn-bûn
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2000 թուականի Մայիսին հրատարակուած գիտական յօդուած
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2000 թվականի մայիսին հրատարակված գիտական հոդված
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2000年の論文
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2000年論文
@yue
2000年論文
@zh-hant
2000年論文
@zh-hk
2000年論文
@zh-mo
2000年論文
@zh-tw
2000年论文
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name
Alzheimer's disease amyloid propagation by a template-dependent dock-lock mechanism.
@ast
Alzheimer's disease amyloid propagation by a template-dependent dock-lock mechanism.
@en
type
label
Alzheimer's disease amyloid propagation by a template-dependent dock-lock mechanism.
@ast
Alzheimer's disease amyloid propagation by a template-dependent dock-lock mechanism.
@en
prefLabel
Alzheimer's disease amyloid propagation by a template-dependent dock-lock mechanism.
@ast
Alzheimer's disease amyloid propagation by a template-dependent dock-lock mechanism.
@en
P2093
P356
P1433
P1476
Alzheimer's disease amyloid propagation by a template-dependent dock-lock mechanism.
@en
P2093
Ghilardi JR
Jennings JM
Stimson ER
Vinters HV
P304
P356
10.1021/BI992933H
P407
P577
2000-05-01T00:00:00Z