Structural basis for increased toxicity of pathological aβ42:aβ40 ratios in Alzheimer disease. - Test2 - elhamkhani - TriplyDB

Structural basis for increased toxicity of pathological aβ42:aβ40 ratios in Alzheimer disease.

Structural basis for increased toxicity of pathological aβ42:aβ40 ratios in Alzheimer disease.

http://www.wikidata.org/entity/Q35774046

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The coexistence of an equal amount of Alzheimer's amyloid-β 40 and 42 forms structurally stable and toxic oligomers through a distinct pathway Interaction between soluble Aβ-(1-40) monomer and Aβ-(1-42) fibrils probed by paramagnetic relaxation enhancement Assessing the causes and consequences of co-polymerization in amyloid formation Transient dynamics of Aβ contribute to toxicity in Alzheimer's disease β-sheet propensity controls the kinetic pathways and morphologies of seeded peptide aggregation.Alzheimer disease: a tale of two prions Fiber diffraction data indicate a hollow core for the Alzheimer's aβ 3-fold symmetric fibril.Extracellular Vesicle-Associated Aβ Mediates Trans-Neuronal Bioenergetic and Ca2+-Handling Deficits in Alzheimer's Disease Models.A new structural model of Alzheimer's Aβ42 fibrils based on electron paramagnetic resonance data and Rosetta modeling Distinct synthetic Aβ prion strains producing different amyloid deposits in bigenic mice.The spleen tyrosine kinase (Syk) regulates Alzheimer amyloid-β production and Tau hyperphosphorylation.γ-AApeptide-based small-molecule ligands that inhibit Aβ aggregation.Microglia constitute a barrier that prevents neurotoxic protofibrillar Aβ42 hotspots around plaques Synergistic interactions between Alzheimer's Aβ40 and Aβ42 on the surface of primary neurons revealed by single molecule microscopy.Aβ(1-42) fibril structure illuminates self-recognition and replication of amyloid in Alzheimer's disease.The Role of Neutrophil Proteins on the Amyloid Beta-RAGE Axis.Insights into the consequences of co-polymerisation in the early stages of IAPP and Aβ peptide assembly from mass spectrometry.Reduction of amyloid-beta levels in mouse eye tissues by intra-vitreally delivered neprilysin Single-molecule imaging reveals aβ42:aβ40 ratio-dependent oligomer growth on neuronal processes Aβ40 has a subtle effect on Aβ42 protofibril formation, but to a lesser degree than Aβ42 concentration, in Aβ42/Aβ40 mixtures.Amyloid beta oligomers induce neuronal elasticity changes in age-dependent manner: a force spectroscopy study on living hippocampal neurons.Alzheimer's Aβ42 and Aβ40 peptides form interlaced amyloid fibrils Pulsed hydrogen-deuterium exchange mass spectrometry probes conformational changes in amyloid beta (Aβ) peptide aggregation.Alzheimer's disease-associated mutations increase amyloid precursor protein resistance to γ-secretase cleavage and the Aβ42/Aβ40 ratio AβPP processing results in greater toxicity per amount of Aβ1-42 than individually expressed and secreted Aβ1-42 in Drosophila melanogaster.Mechanism of amyloid β-protein dimerization determined using single-molecule AFM force spectroscopy.Signature amyloid β profiles are produced by different γ-secretase complexes.Alzheimer's disease, cholesterol, and statins: the junctions of important metabolic pathways.Apolipoprotein E, amyloid-beta, and neuroinflammation in Alzheimer's disease Distinguishing closely related amyloid precursors using an RNA aptamer.Selenoprotein P and selenoprotein M block Zn2+ -mediated Aβ42 aggregation and toxicity.On the lag phase in amyloid fibril formation.Aβ42 and Aβ40: similarities and differences.Structural, morphological, and functional diversity of amyloid oligomers.Strain phenomenon in protein aggregation: Interplay between sequence and conformation.In silico investigation on the inhibition of Aβ42 aggregation by Aβ40 peptide by potential of mean force study.Charge regulation phenomenon predicted from the modeling of polypeptide electrophoretic mobilities as a relevant mechanism of amyloid-beta peptide oligomerization.Pen-2 is essential for γ-secretase complex stability and trafficking but partially dispensable for endoproteolysis.Structural Biology of PrP Prions.Truncated tau deregulates synaptic markers in rat model for human tauopathy.

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Structural basis for increased toxicity of pathological aβ42:aβ40 ratios in Alzheimer disease.

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Neurotoxicity of Alzheimer's disease Aβ peptides is induced by small changes in the Aβ42 to Aβ40 ratio

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Increased amyloid-beta42(43) in brains of mice expressing mutant presenilin 1

Mutant presenilins of Alzheimer's disease increase production of 42-residue amyloid beta-protein in both transfected cells and transgenic mice

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

Diffusible, nonfibrillar ligands derived from Abeta1-42 are potent central nervous system neurotoxins

Secreted amyloid beta-protein similar to that in the senile plaques of Alzheimer's disease is increased in vivo by the presenilin 1 and 2 and APP mutations linked to familial Alzheimer's disease

3D structure of Alzheimer's amyloid-beta(1-42) fibrils

Soluble pool of Abeta amyloid as a determinant of severity of neurodegeneration in Alzheimer's disease

Using inducible vectors to study intracellular trafficking of GFP-tagged steroid/nuclear receptors in living cells.

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Alzheimer's disease

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