Structural basis of β-amyloid-dependent synaptic dysfunctions. - Wikidata - wikimedia - TriplyDB

Structural basis of β-amyloid-dependent synaptic dysfunctions.

Structural basis of β-amyloid-dependent synaptic dysfunctions.

http://www.wikidata.org/entity/Q30318220

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Molecular basis of -amyloid oligomer recognition with a conformational antibody fragment Enhanced Fibril Fragmentation of N-Terminally Truncated and Pyroglutamyl-Modified Aβ Peptides.Oligomer-targeting with a conformational antibody fragment promotes toxicity in Aβ-expressing flies.Antiparallel triple-strand architecture for prefibrillar Aβ42 oligomers Comparisons with amyloid-β reveal an aspartate residue that stabilizes fibrils of the aortic amyloid peptide medin.Amyloid β Protein and Alzheimer's Disease: When Computer Simulations Complement Experimental Studies.Specific Binding of Cu(II) Ions to Amyloid-Beta Peptides Bound to Aggregation-Inhibiting Molecules or SDS Micelles Creates Complexes that Generate Radical Oxygen Species.SDS-PAGE analysis of Aβ oligomers is disserving research into Alzheimer´s disease: appealing for ESI-IM-MS Nanoprobing of the effect of Cu(2+) cations on misfolding, interaction and aggregation of amyloid β peptide.N-truncated amyloid β (Aβ) 4-42 forms stable aggregates and induces acute and long-lasting behavioral deficits.N-truncated Abeta starting with position four: early intraneuronal accumulation and rescue of toxicity using NT4X-167, a novel monoclonal antibody.Deciphering the molecular profile of plaques, memory decline and neuron loss in two mouse models for Alzheimer's disease by deep sequencing.Alzheimer's disease Aβ assemblies mediating rapid disruption of synaptic plasticity and memory.Neuropathology and biochemistry of Aβ and its aggregates in Alzheimer's disease.Amyloid misfolding, aggregation, and the early onset of protein deposition diseases: insights from AFM experiments and computational analyses.Phosphorylation Interferes with Maturation of Amyloid-β Fibrillar Structure in the N Terminus.Phosphorylation modifies the molecular stability of β-amyloid deposits.Isotope-edited FTIR reveals distinct aggregation and structural behaviors of unmodified and pyroglutamylated amyloid β peptides.Solid-Phase Synthesis and Characterization of N-Terminally Elongated Aβ-3-x -Peptides.Introduction of d-Glutamate at a Critical Residue of Aβ42 Stabilizes a Prefibrillary Aggregate with Enhanced Toxicity.Solid-state NMR reveals a close structural relationship between amyloid-β protofibrils and oligomers.Role of the N-terminus for the stability of an amyloid-β fibril with three-fold symmetry.Formation kinetics and structural features of Beta-amyloid aggregates by sedimented solute NMR.Amyloid-β dimers in the absence of plaque pathology impair learning and synaptic plasticity.Using an NMR metabolomics approach to investigate the pathogenicity of amyloid-beta and alpha-synuclein.Cu²⁺ accentuates distinct misfolding of Aβ₁₋₄₀ and Aβ₁₋₄₂ peptides, and potentiates membrane disruption.Impact of membrane curvature on amyloid aggregation.Structural, thermodynamical, and dynamical properties of oligomers formed by the amyloid NNQQ peptide: Insights from coarse-grained simulations Side-chain moieties from the N-terminal region of Aβ are Involved in an oligomer-stabilizing network of interactions

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P2860

Structural basis of β-amyloid-dependent synaptic dysfunctions.

http://www.wikidata.org/entity/Q30318220

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2012 nî lūn-bûn

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2012 թուականի Յունուարին հրատարակուած գիտական յօդուած

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2012年の論文

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2012年論文

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Structural basis of β-amyloid-dependent synaptic dysfunctions.

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Structural basis of β-amyloid-dependent synaptic dysfunctions.

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Structural basis of β-amyloid-dependent synaptic dysfunctions.

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Structural basis of β-amyloid-dependent synaptic dysfunctions.

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Structural basis of β-amyloid-dependent synaptic dysfunctions.

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Structural basis of β-amyloid-dependent synaptic dysfunctions.

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Angewandte Chemie International Edition

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Structural basis of β-amyloid-dependent synaptic dysfunctions.

@en

P2093

Christian Haupt

http://www.w3.org/2001/XMLSchema#string

Jay K Yadav

http://www.w3.org/2001/XMLSchema#string

Jessica Meinhardt

http://www.w3.org/2001/XMLSchema#string

Jörg Leppert

http://www.w3.org/2001/XMLSchema#string

Klaus G Reymann

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Marcus Fändrich

http://www.w3.org/2001/XMLSchema#string

Matthias Görlach

http://www.w3.org/2001/XMLSchema#string

Oliver Ohlenschläger

http://www.w3.org/2001/XMLSchema#string

Raik Rönicke

http://www.w3.org/2001/XMLSchema#string

Ramadurai Ramachandran

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P2860

Structural conversion of neurotoxic amyloid-beta(1-42) oligomers to fibrils

Soluble protein oligomers in neurodegeneration: lessons from the Alzheimer's amyloid beta-peptide

A structural model for Alzheimer's beta -amyloid fibrils based on experimental constraints from solid state NMR

Recent progress in understanding Alzheimer's β-amyloid structures.

Structural properties of Abeta protofibrils stabilized by a small molecule.

Directed selection of a conformational antibody domain that prevents mature amyloid fibril formation by stabilizing Abeta protofibrils.

Effects of the English (H6R) and Tottori (D7N) familial Alzheimer disease mutations on amyloid beta-protein assembly and toxicity.

Amyloid beta-protein dimers rapidly form stable synaptotoxic protofibrils.

Abeta42 neurotoxicity is mediated by ongoing nucleated polymerization process rather than by discrete Abeta42 species.

Soluble amyloid beta-protein dimers isolated from Alzheimer cortex directly induce Tau hyperphosphorylation and neuritic degeneration.

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1576-1579

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10.1002/ANIE.201105638

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7

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51

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2012-01-10T00:00:00Z

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221738305

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22234970

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