Intracellular A beta 1-42 aggregates stimulate the accumulation of stable, insoluble amyloidogenic fragments of the amyloid precursor protein in transfected cells. (Q45956646)

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scientific article published in June 1995

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English	Intracellular A beta 1-42 aggregates stimulate the accumulation of stable, insoluble amyloidogenic fragments of the amyloid precursor protein in transfected cells.	scientific article published in June 1995

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scholarly article

1 reference

Europe PubMed Central

PubMed publication ID

18 December 2017

http://europepmc.org/abstract/MED/7782344

Intracellular A beta 1-42 aggregates stimulate the accumulation of stable, insoluble amyloidogenic fragments of the amyloid precursor protein in transfected cells. (English)

1 reference

Europe PubMed Central

PubMed publication ID

18 December 2017

http://europepmc.org/abstract/MED/7782344

author name string

A J Yang

1

1 reference

Europe PubMed Central

PubMed publication ID

18 December 2017

http://europepmc.org/abstract/MED/7782344

M Knauer

2

1 reference

Europe PubMed Central

PubMed publication ID

18 December 2017

http://europepmc.org/abstract/MED/7782344

D A Burdick

3

1 reference

Europe PubMed Central

PubMed publication ID

18 December 2017

http://europepmc.org/abstract/MED/7782344

C Glabe

4

1 reference

Europe PubMed Central

PubMed publication ID

18 December 2017

http://europepmc.org/abstract/MED/7782344

language of work or name

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publication date

1 June 1995

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Europe PubMed Central

PubMed publication ID

18 December 2017

http://europepmc.org/abstract/MED/7782344

Journal of Biological Chemistry

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Europe PubMed Central

PubMed publication ID

18 December 2017

http://europepmc.org/abstract/MED/7782344

270

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Europe PubMed Central

PubMed publication ID

18 December 2017

http://europepmc.org/abstract/MED/7782344

24

1 reference

Europe PubMed Central

PubMed publication ID

18 December 2017

http://europepmc.org/abstract/MED/7782344

14786-14792

1 reference

Europe PubMed Central

PubMed publication ID

18 December 2017

http://europepmc.org/abstract/MED/7782344

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Potentially Amyloidogenic, Carboxyl-Terminal Derivatives of the Amyloid Protein Precursor

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Processing of the Amyloid Protein Precursor to Potentially Amyloidogenic Derivatives

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Evidence for lysosomal processing of amyloid beta-protein precursor in cultured cells.

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Targeting of cell-surface beta-amyloid precursor protein to lysosomes: alternative processing into amyloid-bearing fragments.

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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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Alzheimer beta/A4 amyloid precursor protein in human brain: aging-associated increases in holoprotein and in a proteolytic fragment

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The immunohistochemical demonstration of subsequences of the precursor of the amyloid A4 protein in senile plaques in Alzheimer's disease.

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Immunoreactivity of neuronal lipofuscin with monoclonal antibodies to the amyloid beta-protein.

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The amyloid precursor protein is concentrated in neuronal lysosomes in normal and Alzheimer disease subjects.

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Amyloid beta-protein precursor accumulates in dystrophic neurites of senile plaques in Alzheimer-type dementia

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Accumulation of amyloid precursor fragment in Alzheimer plaques

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Senile plaque neurites in Alzheimer disease accumulate amyloid precursor protein

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Two types of dystrophic neurites in senile plaques of Alzheimer disease and elderly non-demented cases

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In vitro production of beta-amyloid in smooth muscle cells isolated from amyloid angiopathy-affected vessels.

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Abnormal and deficient processing of beta-amyloid precursor protein in familial Alzheimer's disease lymphoblastoid cells

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Altered processing characteristics of beta-amyloid-containing peptides in cytosol and in media of familial Alzheimer's disease cells

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Overexpression of amyloid precursor protein alters its normal processing and is associated with neurotoxicity

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Transgenic animal models for Alzheimer's disease

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Overexpression of a C-terminal portion of the beta-amyloid precursor protein in mouse brains by transplantation of transformed neuronal cells

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Identifiers

10.1074/JBC.270.24.14786

1 reference

Europe PubMed Central

PubMed publication ID

18 December 2017

http://europepmc.org/abstract/MED/7782344

PubMed publication ID

1 reference

Europe PubMed Central

PubMed publication ID

18 December 2017

http://europepmc.org/abstract/MED/7782344

ResearchGate publication ID

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