The neurotoxic carboxy-terminal fragment of the Alzheimer amyloid precursor binds specifically to a neuronal cell surface molecule: pH dependence of the neurotoxicity and the binding.

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Back to search

Article

The neurotoxic carboxy-terminal fragment of the Alzheimer amyloid precursor binds specifically to a neuronal cell surface molecule: pH dependence of the neurotoxicity and the binding.

The Journal of neuroscience : the official journal of the Society for Neuroscience - 1 May 1992

Kozlowski M R, Spanoyannis A, Manly S P, Fidel S A, Neve R L

Abstract excerpt

One of the hallmarks of Alzheimer's disease neurodegeneration is the accumulation of deposits of amyloid in neuritic plaques and in the cerebral vasculature. Recent studies have implicated carboxy-terminal fragments of the Alzheimer amyloid precursor protein (beta APP) in the processes of amyloidogenesis and neurodegeneration. In particular, the carboxy-terminal 104 amino acids of beta APP (beta APP-C104) have...

Topics

Alzheimer Disease
Amyloid beta-Protein Precursor
Animals
Cell Differentiation
Cell Line, Transformed
Cell Membrane
Culture Media
Hydrogen-Ion Concentration
Mutation
Nerve Growth Factors

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Nervous System

Neurons

PC12 Cells

Peptide Fragments

Tachykinins

Transfection

Source

Open in PubMed Open full text

Identifiers

PMID: 1578262
PMCID: PMC6575880

Genes

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 29 Aug 2026. Prepared record publication-1578262-2026-08-29.1. Manifest publication-graph-cohort-2026-08-29.1.

Source receipt: PubMed via Helena Literature Corpus, retrieved 29 Aug 2026.

Community interpretation

Discuss the evidence

Ask a question, add context or challenge an interpretation. Community activity is separate from scientific evidence strength.

discussions

replies

Citations encouraged

Claims remain attributable.

No discussion yet

Be the first to add a careful, cited interpretation.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 10 closest

The neurotoxic carboxy-terminal fragment of the Alzheimer amyloid precursor binds specifically to a neuronal cell surface molecule: pH dependence of the neurotoxicity and the binding.PMID 1578262Read ↗

PC12 cells release stimulatory factors after transfection with beta/A4-C-terminal DNA of the Alzheimer amyloid precursor protein.Semantic proximity Read ↗

The amyloid precursor protein shows a pH-dependent conformational switch in its E1 domain.Semantic proximity Read ↗

The phosphorylation of Hsp20 enhances its association with amyloid-β to increase protection against neuronal cell death.Semantic proximity Read ↗

Role of phosphorylation of Alzheimer's amyloid precursor protein during neuronal differentiation.Semantic proximity Read ↗

Peptides containing the RERMS sequence of amyloid beta/A4 protein precursor bind cell surface and promote neurite extensionSemantic proximity Read ↗

Cysteine 27 variant of the delta-opioid receptor affects amyloid precursor protein processing through altered endocytic trafficking.Semantic proximity Read ↗

Cell surface receptor function of amyloid precursor protein that activates Ser/Thr kinases.Semantic proximity Read ↗

Localization of structural elements of bee venom phospholipase A2 involved in N-type receptor binding and neurotoxicity.Semantic proximity Read ↗

Localization of a fibrillar amyloid beta-protein binding domain on its precursor.Semantic proximity Read ↗

Regulated cleavage of Alzheimer beta-amyloid precursor protein in the absence of the cytoplasmic tail.Semantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.