Release of amino-terminal fragments from amyloid precursor protein reporter and mutated derivatives in cultured cells.

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Article

Release of amino-terminal fragments from amyloid precursor protein reporter and mutated derivatives in cultured cells.

The Journal of biological chemistry - 15 Dec 1992

Sahasrabudhe S R, Spruyt M A, Muenkel H A, Blume A J, Vitek M P, Jacobsen J S

Abstract excerpt

Abnormal proteolytic processing of amyloid precursor protein (APP) is thought to be central to the formation and deposition of beta amyloid peptide in Alzheimer's disease. A putative "secretase" activity normally releases an amino-terminal APP fragment by cleaving APP at residues within the beta...

Topics

Amino Acid Sequence
Amyloid Precursor Protein Secretases
Amyloid beta-Protein Precursor
Animals
Aspartic Acid Endopeptidases
CHO Cells
Cell Line
Cell Membrane
Cloning, Molecular
Cricetinae
Endopeptidases

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Enkephalin, Methionine

Epitopes

Humans

Kinetics

Molecular Sequence Data

Molecular Weight

Mutation

Source

Open in PubMed

Identifiers

PMID: 1281162

Genes

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 30 Aug 2026. Prepared record publication-1281162-2026-08-30.1. Manifest publication-graph-cohort-2026-08-30.1.

Source receipt: PubMed via Helena Literature Corpus, retrieved 30 Aug 2026.

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