Aβ(1-42) fibril structure illuminates self-recognition and replication of amyloid in Alzheimer's disease.
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Atomic Resolution Structure of Monomorphic Aβ42 Amyloid FibrilsMolecular Structure of Aggregated Amyloid-β: Insights from Solid-State Nuclear Magnetic ResonanceStructural Characterization of Fibrils from Recombinant Human Islet Amyloid Polypeptide by Solid-State NMR: The Central FGAILS Segment Is Part of the β-Sheet CoreStructural Polymorphism of Alzheimer's β-Amyloid Fibrils as Controlled by an E22 Switch: A Solid-State NMR StudyAtomic-resolution structure of a disease-relevant Aβ(1-42) amyloid fibril.Structure of fully protonated proteins by proton-detected magic-angle spinning NMRA new structural model of Alzheimer's Aβ42 fibrils based on electron paramagnetic resonance data and Rosetta modelingN-Terminal Extensions Retard Aβ42 Fibril Formation but Allow Cross-Seeding and Coaggregation with Aβ42Structural Changes of Amyloid Beta in Hippocampus of Rats Exposed to Ozone: A Raman Spectroscopy Study.Membrane-Induced Dichotomous Conformation of Amyloid β with the Disordered N-Terminal Segment Followed by the Stable C-Terminal β Structure.A molecular tweezer antagonizes seminal amyloids and HIV infection.Discovery of DNA dyes Hoechst 34580 and 33342 as good candidates for inhibiting amyloid beta formation: in silico and in vitro study.N-terminal lipid conjugation of amyloid β(1-40) leads to the formation of highly ordered N-terminally extended fibrils.Alzheimer's amyloid-β A2T variant and its N-terminal peptides inhibit amyloid-β fibrillization and rescue the induced cytotoxicity.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.Amylin-Aβ oligomers at atomic resolution using molecular dynamics simulations: a link between Type 2 diabetes and Alzheimer's diseaseMechanism of C-Terminal Fragments of Amyloid β-Protein as Aβ Inhibitors: Do C-Terminal Interactions Play a Key Role in Their Inhibitory Activity?X-ray Crystallographic Structures of a Trimer, Dodecamer, and Annular Pore Formed by an Aβ17-36 β-Hairpin.Conformational Dynamics of Specific Aβ Oligomers Govern Their Ability To Replicate and Induce Neuronal ApoptosisWhat amyloid ligands can tell us about molecular polymorphism and disease.Amino acid substitutions [K16A] and [K28A] distinctly affect amyloid β-protein oligomerization.The amyloid fold of Gad m 1 epitopes governs IgE binding.Solid-state NMR structure of a pathogenic fibril of full-length human α-synuclein.Amyloid-β 1-24 C-terminal truncated fragment promotes amyloid-β 1-42 aggregate formation in the healthy brain.Polymorphism of fibrillar structures depending on the size of assembled Aβ17-42 peptides.Structure of Crenezumab Complex with Aβ Shows Loss of β-Hairpin.Structural variation in amyloid-β fibrils from Alzheimer's disease clinical subtypes.Imaging β-amyloid using [(18)F]flutemetamol positron emission tomography: from dosimetry to clinical diagnosis.Molecular insights into Aβ42 protofibril destabilization with a fluorinated compound D744: A molecular dynamics simulation study.Propagation of Aß pathology: hypotheses, discoveries, and yet unresolved questions from experimental and human brain studies.The potential inhibitory effect of β-casein on the aggregation and deposition of Aβ1-42 fibrils in Alzheimer's disease: insight from in-vitro and in-silico studies.Decreasing amyloid toxicity through an increased rate of aggregation.An Account of Amyloid Oligomers: Facts and Figures Obtained from Experiments and Simulations.LRP/LR Antibody Mediated Rescuing of Amyloid-β-Induced Cytotoxicity is Dependent on PrPc in Alzheimer's Disease.Elongation affinity, activation barrier, and stability of Aβ42 oligomers/fibrils in physiological saline.Conformational selection in amyloid-based immunotherapy: Survey of crystal structures of antibody-amyloid complexes.The activities of amyloids from a structural perspective.The Exceptional Vulnerability of Humans to Alzheimer's Disease.Benzothiazole-Based Neutral Ratiometric Fluorescence Sensor for Amyloid Fibrils.
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P2860
Aβ(1-42) fibril structure illuminates self-recognition and replication of amyloid in Alzheimer's disease.
description
2015 nî lūn-bûn
@nan
2015年の論文
@ja
2015年論文
@yue
2015年論文
@zh-hant
2015年論文
@zh-hk
2015年論文
@zh-mo
2015年論文
@zh-tw
2015年论文
@wuu
2015年论文
@zh
2015年论文
@zh-cn
name
Aβ(1-42) fibril structure illu ...... myloid in Alzheimer's disease.
@ast
Aβ(1-42) fibril structure illu ...... myloid in Alzheimer's disease.
@en
type
label
Aβ(1-42) fibril structure illu ...... myloid in Alzheimer's disease.
@ast
Aβ(1-42) fibril structure illu ...... myloid in Alzheimer's disease.
@en
prefLabel
Aβ(1-42) fibril structure illu ...... myloid in Alzheimer's disease.
@ast
Aβ(1-42) fibril structure illu ...... myloid in Alzheimer's disease.
@en
P2093
P2860
P50
P356
P1476
Aβ(1-42) fibril structure illu ...... myloid in Alzheimer's disease.
@en
P2093
Dan McElheny
Minako Hoshi
Sudhakar Parthasarathy
Yiling Xiao
P2860
P2888
P304
P356
10.1038/NSMB.2991
P577
2015-05-04T00:00:00Z