(PDF) Ramachandran Map Analysis of the Monomeric Aβ 1-40

Ramachandran Map Analysis of the Monomeric Aβ 1-40 and Aβ 1-42 Peptides by Solution NMR

Biophysical Journal - United States

doi 10.1016/j.bpj.2016.11.2605

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Date

February 1, 2017

Authors

Julien Roche

Publisher

Elsevier BV

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Ramachandran Map Analysis of the Monomeric Aβ 1-40 and Aβ 1-42 Peptides by Solution NMR

Biophysical Journal - United States

doi 10.1016/j.bpj.2016.11.2605

Full Text

Abstract

Categories

Date

Authors

Publisher

Related search

Regenerable and Simultaneous Surface Plasmon Resonance Detection of Aβ(1−40) and Aβ(1−42) Peptides in Cerebrospinal Fluids With Signal Amplification by Streptavidin Conjugated to an N-Terminus-Specific Antibody

A Chemometric Approach Towards Predicting the Relative Aggregation Propensity: Aβ(1-42)

Alzheimer's Aβ(1-40) Amyloid Fibrils Feature Size-Dependent Mechanical Properties

Atomic-Resolution Structure of a Disease-Relevant Aβ(1–42) Amyloid Fibril

NMR Solution Structure of Rat Aβ(1–16): Toward Understanding the Mechanism of Rats' Resistance to Alzheimer's Disease

Low-Dose Γ-Secretase Inhibition Increases Secretion of Aβ Peptides and Intracellular Oligomeric Aβ

Protective Effect of Quercetin in Primary Neurons Against Aβ(1–42): Relevance to Alzheimer's Disease

Small Molecule NPT-440-1 Inhibits Ionic Flux Through Aβ 1-42 Pores: Implications for Alzheimer's Disease Therapeutics

Aβ(1-42) Tetramer and Octamer Structures Reveal Edge Pores as a Mechanism for Membrane Damage