Amyloid beta -protein (Abeta) assembly: Abeta 40 and Abeta 42 oligomerize through distinct pathways. - Wikidata - wikimedia - TriplyDB

Amyloid beta -protein (Abeta) assembly: Abeta 40 and Abeta 42 oligomerize through distinct pathways.

Amyloid beta -protein (Abeta) assembly: Abeta 40 and Abeta 42 oligomerize through distinct pathways.

http://www.wikidata.org/entity/Q34468169

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Rationally designed turn promoting mutation in the amyloid-β peptide sequence stabilizes oligomers in solution The coexistence of an equal amount of Alzheimer's amyloid-β 40 and 42 forms structurally stable and toxic oligomers through a distinct pathway Gerstmann-Sträussler-Scheinker disease amyloid protein polymerizes according to the "dock-and-lock" model Mapping out the multistage fibrillation of glucagon Efficient reversal of Alzheimer's disease fibril formation and elimination of neurotoxicity by a small molecule Soluble oligomers of the amyloid beta-protein impair synaptic plasticity and behavior Simulating oligomerization at experimental concentrations and long timescales: A Markov state model approach Amyloid beta-protein monomer folding: free-energy surfaces reveal alloform-specific differences Stabilization of neurotoxic soluble beta-sheet-rich conformations of the Alzheimer's disease amyloid-beta peptide Effects of grape seed-derived polyphenols on amyloid beta-protein self-assembly and cytotoxicity The Alzheimer's peptides Abeta40 and 42 adopt distinct conformations in water: a combined MD / NMR study Mechanism of prion propagation: amyloid growth occurs by monomer addition Inflammatory cytokine levels correlate with amyloid load in transgenic mouse models of Alzheimer's disease Multi-Target Directed Donepezil-Like Ligands for Alzheimer's Disease Structural evolution and membrane interactions of Alzheimer's amyloid-beta peptide oligomers: new knowledge from single-molecule fluorescence studies Alzheimer's disease--a panorama glimpse Wireless-electrodeless quartz-crystal-microbalance biosensors for studying interactions among biomolecules: a review.Preclinical Pharmacokinetic Studies of the Tritium Labelled D-Enantiomeric Peptide D3 Developed for the Treatment of Alzheimer´s Disease Dimer formation enhances structural differences between amyloid β-protein (1-40) and (1-42): an explicit-solvent molecular dynamics study Structural Conversion of Aβ17-42 Peptides from Disordered Oligomers to U-Shape Protofilaments via Multiple Kinetic Pathways Molecular Structure of β-Amyloid Fibrils in Alzheimer’s Disease Brain Tissue Amyloid properties of the leader peptide of variant B cystatin C: implications for Alzheimer and macular degeneration Modulating self-assembly of amyloidogenic proteins as a therapeutic approach for neurodegenerative diseases: strategies and mechanisms Ectoine and hydroxyectoine inhibit aggregation and neurotoxicity of Alzheimer's beta-amyloid Real-time imaging and quantification of amyloid-beta peptide aggregates by novel quantum-dot nanoprobes Sequestration of the Abeta peptide prevents toxicity and promotes degradation in vivo Direct observation of single amyloid-β(1-40) oligomers on live cells: binding and growth at physiological concentrations Halogenation generates effective modulators of amyloid-Beta aggregation and neurotoxicity.Shaking alone induces de novo conversion of recombinant prion proteins to β-sheet rich oligomers and fibrils Systematic Aβ Analysis in Drosophila Reveals High Toxicity for the 1-42, 3-42 and 11-42 Peptides, and Emphasizes N- and C-Terminal Residues Probing protein aggregation using discrete molecular dynamics Design and Characterization of Chemically Stabilized Aβ42 Oligomers Amyloid β-Protein Assembly: The Effect of Molecular Tweezers CLR01 and CLR03 Electrostatic effects in the folding of the SH3 domain of the c-Src tyrosine kinase: pH-dependence in 3D-domain swapping and amyloid formation Modulation of the stability of amyloidogenic precursors by anion binding strongly influences the rate of amyloid nucleation.Microcanonical thermostatistics of coarse-grained proteins with amyloidogenic propensity.Characterization of oligomers of heterogeneous size as precursors of amyloid fibril nucleation of an SH3 domain: an experimental kinetics study.Lysine-Specific Molecular Tweezers Are Broad-Spectrum Inhibitors of Assembly and Toxicity of Amyloid Proteins Analysis of the stabilities of hexameric amyloid-β(1-42) models using discrete molecular dynamics simulations Environmental conditions affect the kinetics of nucleation of amyloid fibrils and determine their morphology.

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Amyloid beta -protein (Abeta) assembly: Abeta 40 and Abeta 42 oligomerize through distinct pathways.

http://www.wikidata.org/entity/Q34468169

description

2002 nî lūn-bûn

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2002 թուականի Դեկտեմբերին հրատարակուած գիտական յօդուած

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2002 թվականի դեկտեմբերին հրատարակված գիտական հոդված

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2002年の論文

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Amyloid beta -protein (Abeta) ...... ize through distinct pathways.

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Amyloid beta -protein (Abeta) ...... ize through distinct pathways.

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Proceedings of the National Academy of Sciences of the United States of America

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Amyloid beta -protein (Abeta) ...... ize through distinct pathways.

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Aleksey Lomakin

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David B Teplow

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Gal Bitan

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George B Benedek

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Marina D Kirkitadze

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Sabrina S Vollers

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P2860

Amyloid plaque core protein in Alzheimer disease and Down syndrome

Naturally secreted oligomers of amyloid beta protein potently inhibit hippocampal long-term potentiation in vivo

The carboxy terminus of the beta amyloid protein is critical for the seeding of amyloid formation: implications for the pathogenesis of Alzheimer's disease

Alzheimer's disease: the amyloid cascade hypothesis

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

Alzheimer's disease: initial report of the purification and characterization of a novel cerebrovascular amyloid protein

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

High-level neuronal expression of abeta 1-42 in wild-type human amyloid protein precursor transgenic mice: synaptotoxicity without plaque formation

Monitoring protein assembly using quasielastic light scattering spectroscopy.

Translating cell biology into therapeutic advances in Alzheimer's disease.

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330-335

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10.1073/PNAS.222681699

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1

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100

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2002-12-27T00:00:00Z

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10970099

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12506200

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140968

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