(Q46109204)

19 December 2017

title

Amino-terminal deletions enhance aggregation of beta-amyloid peptides in vitro (English)

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19 December 2017

author name string

Pike CJ

series ordinal

1

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19 December 2017

Overman MJ

series ordinal

2

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19 December 2017

Cotman CW

series ordinal

3

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19 December 2017

language of work or name

English

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publication date

1 October 1995

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19 December 2017

Journal of Biological Chemistry

published in

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19 December 2017

volume

270

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19 December 2017

page(s)

23895-23898

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19 December 2017

issue

41

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19 December 2017

The molecular pathology of 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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Cultured GABA-immunoreactive neurons are resistant to toxicity induced by beta-amyloid

21 January 2018

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Calretinin-immunoreactive neurons are resistant to beta-amyloid toxicity in vitro

21 January 2018

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In vitro aging of beta-amyloid protein causes peptide aggregation and neurotoxicity

21 January 2018

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21 January 2018

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21 January 2018

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Synthetic peptide homologous to beta protein from Alzheimer disease forms amyloid-like fibrils in vitro

21 January 2018

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Beta-amyloid neurotoxicity requires fibril formation and is inhibited by congo red.

21 January 2018

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21 January 2018

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The alpha-helical to beta-strand transition in the amino-terminal fragment of the amyloid beta-peptide modulates amyloid formation

21 January 2018

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21 January 2018

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The metabolic pathway generating p3, an A beta-peptide fragment, is probably non-amyloidogenic.

21 January 2018

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21 January 2018

Identifiers

DOI

10.1074/JBC.270.41.23895

1 reference

19 December 2017

PubMed ID

7592576

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19 December 2017