Positioning of the Alzheimer Abeta(1-40) peptide in SDS micelles using NMR and paramagnetic probes. (Q53387908)

13 May 2018

title

Positioning of the Alzheimer Abeta(1-40) peptide in SDS micelles using NMR and paramagnetic probes. (English)

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13 May 2018

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2

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13 May 2018

Marta Oleszczuk

object named as

Marta Oleszczuk

series ordinal

4

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Jüri Jarvet

object named as

Jüri Jarvet

series ordinal

1

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Astrid Gräslund

series ordinal

5

object named as

Astrid Gräslund

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13 May 2018

Peter Damberg

3

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13 May 2018

publication date

27 July 2007

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Journal of Biomolecular NMR

published in

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13 May 2018

volume

39

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issue

1

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page(s)

63-72

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Structure of amyloid A4-(1-40)-peptide of Alzheimer's disease

cites work

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Solution structures of micelle-bound amyloid beta-(1-40) and beta-(1-42) peptides of Alzheimer's disease

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Autoinsertion of soluble oligomers of Alzheimer's Abeta(1-42) peptide into cholesterol-containing membranes is accompanied by relocation of the sterol towards the bilayer surface.

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Common structure of soluble amyloid oligomers implies common mechanism of pathogenesis

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Folding proteins in fatal ways

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Cholesterol is an important factor affecting the membrane insertion of beta-amyloid peptide (A beta 1-40), which may potentially inhibit the fibril formation

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Dynamics of hard-sphere suspensions

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15N relaxation study of the amyloid beta-peptide: structural propensities and persistence length

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Synaptic targeting by Alzheimer's-related amyloid beta oligomers.

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Insertion of Alzheimer's A beta 40 peptide into lipid monolayers

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Copper binding to the amyloid-beta (Abeta) peptide associated with Alzheimer's disease: folding, coordination geometry, pH dependence, stoichiometry, and affinity of Abeta-(1-28): insights from a range of complementary spectroscopic techniques

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Soluble amyloid oligomers increase bilayer conductance by altering dielectric structure

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High-resolution NMR studies of the zinc-binding site of the Alzheimer's amyloid beta-peptide.

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Two types of Alzheimer's beta-amyloid (1-40) peptide membrane interactions: aggregation preventing transmembrane anchoring versus accelerated surface fibril formation.

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12 December 2020

Solution structure of residues 1-28 of the amyloid beta-peptide

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12 December 2020

Amyloid ion channels: a common structural link for protein-misfolding disease

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Targeting small Abeta oligomers: the solution to an Alzheimer's disease conundrum?

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Ion channel formation by Alzheimer's disease amyloid beta-peptide (Abeta40) in unilamellar liposomes is determined by anionic phospholipids

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Molecular understanding of Abeta peptide interaction with isoflurane, propofol, and thiopental: NMR spectroscopic study

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Solution structure of the Alzheimer amyloid beta-peptide (1-42) in an apolar microenvironment. Similarity with a virus fusion domain

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A specific amyloid-beta protein assembly in the brain impairs memory

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Permeabilization of lipid bilayers is a common conformation-dependent activity of soluble amyloid oligomers in protein misfolding diseases

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Alzheimer's disease amyloid-beta binds copper and zinc to generate an allosterically ordered membrane-penetrating structure containing superoxide dismutase-like subunits

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Effect of sterols on beta-amyloid peptide (AbetaP 1-40) channel formation and their properties in planar lipid membranes

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Alzheimer's disease: halothane induces Abeta peptide to oligomeric form--solution NMR studies

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Accurate measurement of translational diffusion coefficients: a practical method to account for nonlinear gradients.

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Three-dimensional structures of the amyloid beta peptide (25-35) in membrane-mimicking environment

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Architecture of the Alzheimer's A beta P ion channel pore

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Calcium dysregulation and membrane disruption as a ubiquitous neurotoxic mechanism of soluble amyloid oligomers

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Surface behavior and lipid interaction of Alzheimer beta-amyloid peptide 1-42: a membrane-disrupting peptide

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Alzheimer beta-amyloid peptide 25-35: electrostatic interactions with phospholipid membranes.

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12 December 2020

10.1007/S10858-007-9176-4

Identifiers

DOI

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13 May 2018

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13 May 2018