Imaging real-time aggregation of amyloid beta protein (1-42) by atomic force microscopy. (Q44071723)

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11 November 2019

title

Imaging real-time aggregation of amyloid beta protein (1-42) by atomic force microscopy (English)

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11 November 2019

1

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11 November 2019

author name string

Hai Lin

series ordinal

2

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11 November 2019

Julian Thimm

series ordinal

3

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Ratneshwar Lal

series ordinal

4

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11 November 2019

publication date

1 July 2002

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11 November 2019

number of pages

6

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inferred from page(s)

published in

Peptides

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volume

23

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issue

7

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11 November 2019

page(s)

1265-1270

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describes a project that uses

11 November 2019

atomic force microscopy

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Giant multilevel cation channels formed by Alzheimer disease amyloid beta-protein [A beta P-(1-40)] in bilayer membranes

inferred from title

cites work

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Dramatic aggregation of Alzheimer abeta by Cu(II) is induced by conditions representing physiological acidosis.

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Amyloid beta-peptide induces cell monolayer albumin permeability, impairs glucose transport, and induces apoptosis in vascular endothelial cells.

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Soluble beta-amyloid induction of Alzheimer's phenotype for human fibroblast K+ channels

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Watching amyloid fibrils grow by time-lapse atomic force microscopy

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Beta-amyloid peptide blocks the fast-inactivating K+ current in rat hippocampal neurons

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Inhibition of fibril formation in beta-amyloid peptide by a novel series of benzofurans

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Structural studies of soluble oligomers of the Alzheimer beta-amyloid peptide

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Zinc-induced Alzheimer's Abeta1-40 aggregation is mediated by conformational factors.

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Monitoring the assembly of Ig light-chain amyloid fibrils by atomic force microscopy.

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Seeding "one-dimensional crystallization" of amyloid: a pathogenic mechanism in Alzheimer's disease and scrapie?

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Alzheimer's disease amyloid beta-protein forms Zn(2+)-sensitive, cation-selective channels across excised membrane patches from hypothalamic neurons

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Properties of cytotoxic peptide-formed ion channels

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Biological applications of atomic force microscopy

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Imaging molecular structure and physiological function of gap junctions and hemijunctions by multimodal atomic force microscopy

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Amyloid beta protein forms ion channels: implications for Alzheimer's disease pathophysiology

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7 January 2021

Amyloid beta protein (1-40) forms calcium-permeable, Zn2+-sensitive channel in reconstituted lipid vesicles

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7 January 2021

Histidine-13 is a crucial residue in the zinc ion-induced aggregation of the A beta peptide of Alzheimer's disease

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7 January 2021

Cellular actions of beta-amyloid precursor protein and its soluble and fibrillogenic derivatives

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Laminin inhibits A beta 40 fibril formation promoted by apolipoprotein E4 in vitro.

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Recognition sequence design for peptidyl modulators of beta-amyloid aggregation and toxicity.

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7 January 2021

Amyloid beta protein-(1-42) forms calcium-permeable, Zn2+-sensitive channel

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7 January 2021

beta-Amyloid peptide induced cytoskeletal reorganization in cultured astrocytes

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7 January 2021

Molecular structure of a fibrillar Alzheimer's A beta fragment.

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7 January 2021

The protofilament substructure of amyloid fibrils11Edited by F. E. Cohen

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7 January 2021

Superoxide free radical and intracellular calcium mediate A beta(1-42) induced endothelial toxicity.

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7 January 2021

In vitro studies of amyloid beta-protein fibril assembly and toxicity provide clues to the aetiology of Flemish variant (Ala692-->Gly) Alzheimer's disease

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7 January 2021

Fresh and nonfibrillar amyloid beta protein(1-40) induces rapid cellular degeneration in aged human fibroblasts: evidence for AbetaP-channel-mediated cellular toxicity

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7 January 2021

10.1016/S0196-9781(02)00061-X

Identifiers

DOI

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11 November 2019

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