An asymmetric dimer as the basic subunit in Alzheimer's disease amyloid β fibrils.
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Atomic Resolution Structure of Monomorphic Aβ42 Amyloid FibrilsUnlike twins: an NMR comparison of two α-synuclein polymorphs featuring different toxicityStructural 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 StudyCryo-EM reveals the steric zipper structure of a light chain-derived amyloid fibrilSolid-State NMR Spectroscopy of Functional Amyloid from a Fungal Hydrophobin: A Well-Ordered β-Sheet Core Amidst Structural HeterogeneitySolid-state NMR structure determination from diagonal-compensated, sparsely nonuniform-sampled 4D proton-proton restraints.Solid-state NMR studies of metal-free SOD1 fibrillar structures.Molecular architecture of Aβ fibrils grown in cerebrospinal fluid solution and in a cell culture model of Aβ plaque formation.Peptide dimer structure in an Aβ(1-42) fibril visualized with cryo-EM.Structural Mechanism of the Interaction of Alzheimer Disease Aβ Fibrils with the Non-steroidal Anti-inflammatory Drug (NSAID) Sulindac SulfideNMR studies of active-site properties of human carbonic anhydrase II by using (15) N-labeled 4-methylimidazole as a local probe and histidine hydrogen-bond correlations.Amyloid β Protein and Alzheimer's Disease: When Computer Simulations Complement Experimental Studies.Locating folds of the in-register parallel β-sheet of the Sup35p prion domain infectious amyloid.Local interactions influence the fibrillation kinetics, structure and dynamics of Aβ(1-40) but leave the general fibril structure unchanged.Alternative salt bridge formation in Aβ-a hallmark of early-onset Alzheimer's disease?Aβ(1-42) fibril structure illuminates self-recognition and replication of amyloid in Alzheimer's disease.Atomic-resolution three-dimensional structure of amyloid β fibrils bearing the Osaka mutation.High resolution structural characterization of Aβ42 amyloid fibrils by magic angle spinning NMR.Molecular structures of amyloid and prion fibrils: consensus versus controversyPolymorph-specific kinetics and thermodynamics of β-amyloid fibril growth.Force spectroscopy reveals the presence of structurally modified dimers in transthyretin amyloid annular oligomers.Spectral editing at ultra-fast magic-angle-spinning in solid-state NMR: facilitating protein sequential signal assignment by HIGHLIGHT approach.Nucleotide-type chemical shift assignment of the encapsulated 40 kbp dsDNA in intact bacteriophage T7 by MAS solid-state NMR.Effect of the Tottori familial disease mutation (D7N) on the monomers and dimers of Aβ40 and Aβ42.Protein-RNA interfaces probed by 1H-detected MAS solid-state NMR spectroscopy.Formation kinetics and structural features of Beta-amyloid aggregates by sedimented solute NMR.Structural characterization of supramolecular assemblies by ¹³C spin dilution and 3D solid-state NMR.The molecular structure of Alzheimer β-amyloid fibrils formed in the presence of phospholipid vesicles.Amyloid fibril polymorphism - a challenge for molecular imaging and therapy.Fibril structure of amyloid-β(1-42) by cryo-electron microscopy.A long-lived Aβ oligomer resistant to fibrillization.Covalent Tethering and Residues with Bulky Hydrophobic Side Chains Enable Self-Assembly of Distinct Amyloid Structures.Purification of recombinant Aβ(1-42) and pGlu-Aβ(3-42) using preparative SDS-PAGE.Cryogenic solid state NMR studies of fibrils of the Alzheimer's disease amyloid-β peptide: perspectives for DNP.Hydrogen bonding involving side chain exchangeable groups stabilizes amyloid quarternary structure.SedNMR: a web tool for optimizing sedimentation of macromolecular solutes for SSNMR.Solid-state NMR sequential assignment of Osaka-mutant amyloid-beta (Aβ1−40 E22Δ) fibrilsDynamics in the solid-state: perspectives for the investigation of amyloid aggregates, membrane proteins and soluble protein complexesSSNMR of biosilica-entrapped enzymes permits an easy assessment of preservation of native conformation in atomic detail
P2860
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P2860
An asymmetric dimer as the basic subunit in Alzheimer's disease amyloid β fibrils.
description
2012 nî lūn-bûn
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2012年の論文
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2012年学术文章
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2012年学术文章
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2012年学术文章
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2012年学术文章
@zh-hans
2012年学术文章
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2012年学术文章
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2012年學術文章
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2012年學術文章
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name
An asymmetric dimer as the basic subunit in Alzheimer's disease amyloid β fibrils.
@en
An asymmetric dimer as the basic subunit in Alzheimer's disease amyloid β fibrils.
@nl
type
label
An asymmetric dimer as the basic subunit in Alzheimer's disease amyloid β fibrils.
@en
An asymmetric dimer as the basic subunit in Alzheimer's disease amyloid β fibrils.
@nl
prefLabel
An asymmetric dimer as the basic subunit in Alzheimer's disease amyloid β fibrils.
@en
An asymmetric dimer as the basic subunit in Alzheimer's disease amyloid β fibrils.
@nl
P2093
P2860
P356
P1476
An asymmetric dimer as the basic subunit in Alzheimer's disease amyloid β fibrils
@en
P2093
Marcus Fändrich
Matthias Schmidt
Muralidar Dasari
P2860
P304
P356
10.1002/ANIE.201200965
P407
P577
2012-05-08T00:00:00Z