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

doi 10.1101/759472

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September 12, 2019

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Cold Spring Harbor Laboratory

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

Full Text

Abstract

Date

Authors

Publisher

Related search

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

339 Keratin 1–keratin 10 Helix 1B Tetramer Crystal Structures Reveal a Knob-Pocket Mechanism Important for Proper Assembly of Intermediate Filaments

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

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

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

Microglial Inhibitory Mechanism of Coenzyme Q10 Against Aβ (1-42) Induced Cognitive Dysfunctions: Possible Behavioral, Biochemical, Cellular, and Histopathological Alterations

CprK Crystal Structures Reveal Mechanism for Transcriptional Control of Halorespiration

Crystal and Electron Microscopy Structures of Sticholysin II Actinoporin Reveal Insights Into the Mechanism of Membrane Pore Formation

Cryo-Em Structures of ASC and NLRC4 CARD Filaments Reveal a Unified Mechanism of Nucleation and Activation of Caspase-1