Evidence map›Paper›PMID 41917388›Full record

ReviewAdvances in experimental medicine and biology2026

Unique Expression and Glycosylation of Amyloid Precursor Protein in Alzheimer's Disease.

Yuriko Tachida, Shinobu Kitazume

Abstract readReview
PubMed Publisher
In one paragraph

Review in Advances in experimental medicine and biology, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

0numbers the graph read from it
0cells of the map it votes in
0citing papers in PubMed
–field-weighted citation impact
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

0 citing papers in PubMed.

No citing paper in PubMed yet.

4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

2 authors.

Yuriko TachidaGlycan and Life Systems Integration Center (GaLSIC), Soka University, Hachiōji, Japan.
Shinobu KitazumeDepartment of Clinical Laboratory Sciences, School of Health Sciences, Fukushima Medical University School of Medicine, Fukushima, Japan. shinobuk@fmu.ac.jp.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Accumulation of amyloid β (Aβ) peptide in the brain is a characteristic pathological feature of Alzheimer's disease that occurs several decades before the onset of symptoms. Aβ is produced from the membrane-bound amyloid β precursor protein (APP) by β-secretase 1 (BACE1) and γ-secretase-mediated proteolytic cleavage. Alternatively, ADAM10/17 α-secretase and γ-secretase cleavage does not generate Aβ. Accumulating evidence indicates that intracellular trafficking of APP to each secretase determines the level of Aβ production. In this chapter, we summarize how glycosylation affects the Aβ production, possibly by modulating the intracellular localization of APP and its secretases.

Indexed as

Alzheimer DiseaseAmyloid beta-Protein PrecursorBrainAmyloid beta-PeptidesAmyloid Precursor Protein SecretasesAnimalsGlycosylationHumansProtein TransportAmyloid beta-PeptidesAmyloid beta-Protein PrecursorAmyloid Precursor Protein SecretasesAlzheimer’s disease (AD)Amyloid precursor protein (APP)Amyloid β (Aβ)Cerebral amyloid angiopathy (CAA)Intracellular traffickingN-,O-glycosylation

Identifiers

PMID41917388

What OpenQuestion holds

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Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.