Atomic-resolution structure of a disease-relevant Aβ(1-42) amyloid fibril.
about
Nano-assembly of amyloid β peptide: role of the hairpin fold.Line-Broadening in Low-Temperature Solid-State NMR Spectra of Fibrils.Phage display and kinetic selection of antibodies that specifically inhibit amyloid self-replication.N-terminal lipid conjugation of amyloid β(1-40) leads to the formation of highly ordered N-terminally extended fibrils.Quenched hydrogen-deuterium exchange NMR of a disease-relevant Aβ(1-42) amyloid polymorphWater Distribution, Dynamics, and Interactions with Alzheimer's β-Amyloid Fibrils Investigated by Solid-State NMR.Elucidating the structure of an infectious protein.Elucidating the Aβ42 Anti-Aggregation Mechanism of Action of Tramiprosate in Alzheimer's Disease: Integrating Molecular Analytical Methods, Pharmacokinetic and Clinical DataZinc-binding structure of a catalytic amyloid from solid-state NMR.Implications for Alzheimer's disease of an atomic resolution structure of amyloid-β(1-42) fibrils.Structure of Crenezumab Complex with Aβ Shows Loss of β-Hairpin.Structural variation in amyloid-β fibrils from Alzheimer's disease clinical subtypes.Amyloid plaque structure and cell surface interactions of β-amyloid fibrils revealed by electron tomography.Rosetta Stone for Amyloid Fibrils: The Key Role of Ring-Like Oligomers in Amyloidogenesis.Nucleation and growth of a bacterial functional amyloid at single-fiber resolution.High-Resolution Structures of the Amyloid-β 1-42 Dimers from the Comparison of Four Atomistic Force Fields.Elongation affinity, activation barrier, and stability of Aβ42 oligomers/fibrils in physiological saline.The activities of amyloids from a structural perspective.Modulation of amyloid assembly by glycosaminoglycans: from mechanism to biological significance.Impact of a discordant helix on β-amyloid structure, aggregation ability and toxicity.Selective targeting of primary and secondary nucleation pathways in Aβ42 aggregation using a rational antibody scanning method.Identification of proteins that specifically recognize and bind protofibrillar aggregates of amyloid-β.MAK33 antibody light chain amyloid fibrils are similar to oligomeric precursors.Ring-like N-fold Models of Aβ42 fibrils.Limits of Resolution and Sensitivity of Proton Detected MAS Solid-State NMR Experiments at 111 kHz in Deuterated and Protonated Proteins.Alzheimer's disease: Structure of aggregates revealed.Emergence of Alternative Structures in Amyloid Beta 1-42 Monomeric Landscape by N-terminal Hexapeptide Amyloid Inhibitors.Monomer-dependent secondary nucleation in amyloid formation.Cryo-EM structures of tau filaments from Alzheimer's disease.Assembly of Peptides Derived from β-Sheet Regions of β-Amyloid.Coassembly of Peptides Derived from β-Sheet Regions of β-AmyloidEffects of Mutations on the Aggregation Propensity of the Human Prion-Like Protein hnRNPA2B1.A Toxic Conformer of Aβ42 with a Turn at 22-23 is a Novel Therapeutic Target for Alzheimer's DiseaseAtomic Scale Structural Studies of Macromolecular Assemblies by Solid-state Nuclear Magnetic Resonance Spectroscopy.Few Ramachandran Angle Changes Provide Interaction Strength Increase in Aβ42 versus Aβ40 Amyloid FibrilsIdentification of key regions and residues controlling Aβ folding and assembly.Nucleobindin 1 binds to multiple types of pre-fibrillar amyloid and inhibits fibrillization.Familial Alzheimer's Disease Mutations within the Amyloid Precursor Protein Alter the Aggregation and Conformation of the Amyloid-β Peptide.Cross-seeding between Aβ40 and Aβ42 in Alzheimer's disease.Conformational Ensembles of the Wild-Type and S8C Aβ1-42 Dimers.
P2860
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P2860
Atomic-resolution structure of a disease-relevant Aβ(1-42) amyloid fibril.
description
2016 nî lūn-bûn
@nan
2016 թուականի Յուլիսին հրատարակուած գիտական յօդուած
@hyw
2016 թվականի հուլիսին հրատարակված գիտական հոդված
@hy
2016年の論文
@ja
2016年論文
@yue
2016年論文
@zh-hant
2016年論文
@zh-hk
2016年論文
@zh-mo
2016年論文
@zh-tw
2016年论文
@wuu
name
Atomic-resolution structure of a disease-relevant Aβ(1-42) amyloid fibril.
@ast
Atomic-resolution structure of a disease-relevant Aβ(1-42) amyloid fibril.
@en
type
label
Atomic-resolution structure of a disease-relevant Aβ(1-42) amyloid fibril.
@ast
Atomic-resolution structure of a disease-relevant Aβ(1-42) amyloid fibril.
@en
altLabel
Atomic-resolution structure of a disease-relevant Aβ(1–42) amyloid fibril
@en
prefLabel
Atomic-resolution structure of a disease-relevant Aβ(1-42) amyloid fibril.
@ast
Atomic-resolution structure of a disease-relevant Aβ(1-42) amyloid fibril.
@en
P2093
P2860
P356
P1476
Atomic-resolution structure of a disease-relevant Aβ(1-42) amyloid fibril.
@en
P2093
Anja Böckmann
Charles G Glabe
Francesco Ravotti
Hiromi Arai
Joseph S Wall
Marielle Aulikki Wälti
Peter Güntert
Roland Riek
P2860
P304
P356
10.1073/PNAS.1600749113
P407
P50
P577
2016-07-28T00:00:00Z