Observation of metastable Abeta amyloid protofibrils by atomic force microscopy (Q73431442)

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3 November 2019

title

Observation of metastable Abeta amyloid protofibrils by atomic force microscopy (English)

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3 November 2019

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J D Harper

1

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3 November 2019

S S Wong

series ordinal

2

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3 November 2019

C M Lieber

series ordinal

3

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3 November 2019

P T Lansbury

series ordinal

4

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3 November 2019

publication date

1 February 1997

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3 November 2019

published in

Chemistry and Biology

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3 November 2019

volume

4

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issue

2

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3 November 2019

page(s)

119-125

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describes a project that uses

3 November 2019

atomic force microscopy

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Scavenger receptor-mediated adhesion of microglia to beta-amyloid fibrils

inferred from title

cites work

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Correlative Memory Deficits, Abeta Elevation, and Amyloid Plaques in Transgenic Mice

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

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

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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

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An increased percentage of long amyloid beta protein secreted by familial amyloid beta protein precursor (beta APP717) mutants.

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Familial Alzheimer's disease-linked presenilin 1 variants elevate Abeta1-42/1-40 ratio in vitro and in vivo

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Visualization of A beta 42(43) and A beta 40 in senile plaques with end-specific A beta monoclonals: evidence that an initially deposited species is A beta 42(43).

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The E280A presenilin 1 Alzheimer mutation produces increased A beta 42 deposition and severe cerebellar pathology

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Increased amyloid-beta42(43) in brains of mice expressing mutant presenilin 1

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Amyloid-beta aggregation: selective inhibition of aggregation in mixtures of amyloid with different chain lengths

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Imaging crystals, polymers, and processes in water with the atomic force microscope

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Scanning Force Microscopy in Biology

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Morphology and antibody recognition of synthetic beta-amyloid peptides

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Structural model for the β-amyloid fibril based on interstrand alignment of an antiparallel-sheet comprising a C-terminal peptide

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Molecular determinants of amyloid deposition in Alzheimer's disease: conformational studies of synthetic beta-protein fragments.

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Synchrotron X-ray studies suggest that the core of the transthyretin amyloid fibril is a continuous β-sheet helix

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7 January 2021

Examination of the Structure of the Transthyretin Amyloid Fibril by Image Reconstruction from Electron Micrographs

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pH-dependent structural transitions of Alzheimer amyloid peptides

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Normal and abnormal biology of the beta-amyloid precursor protein

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Native complex formation between apolipoprotein E isoforms and the Alzheimer's disease peptide A beta.

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Gene dose of apolipoprotein E type 4 allele and the risk of Alzheimer's disease in late onset families

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7 January 2021

10.1016/S1074-5521(97)90255-6

Identifiers

DOI

1 reference

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3 November 2019

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