Evidence map›Paper›PMID 28994715›Full record

ReviewMolecules (Basel, Switzerland)2017

β-Amyloid and the Pathomechanisms of Alzheimer's Disease: A Comprehensive View.

Botond Penke, Ferenc Bogár, Lívia Fülöp

Open access · goldAbstract readReview
In one paragraph

Review in Molecules (Basel, Switzerland), 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 58 papers, 3 of them syntheses that pooled it.

0numbers the graph read from it
0cells of the map it votes in
58citing papers in PubMed, 3 pooled it
6.7field-weighted citation impact, top 3% of its field
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

58 citing papers in PubMed, 3 syntheses or guidelines pooled it, 120 citations in OpenAlex.

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  16. IBRO neuroscience reports · 2025
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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

3 authors at 1 institution in 1 country.

Botond PenkeDepartment of Medical Chemistry, University of Szeged, H-6720 Szeged, Dóm Square 8, Hungary. penke.botond@med.u-szeged.hu.
Ferenc BogárMTA-SZTE Biomimetic Systems Research Group and Department of Medical Chemistry, University of Szeged, H-6720 Szeged, Dóm Square 8, Hungary. bogar@sol.cc.u-szeged.hu.
Lívia FülöpDepartment of Medical Chemistry, University of Szeged, H-6720 Szeged, Dóm Square 8, Hungary. fulop.livia@med.u-szeged.hu.
University of Szeged · HU

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Protein dyshomeostasis is the common mechanism of neurodegenerative diseases such as Alzheimer's disease (AD). Aging is the key risk factor, as the capacity of the proteostasis network declines during aging. Different cellular stress conditions result in the up-regulation of the neurotrophic, neuroprotective amyloid precursor protein (APP). Enzymatic processing of APP may result in formation of toxic Aβ aggregates (β-amyloids). Protein folding is the basis of life and death. Intracellular Aβ affects the function of subcellular organelles by disturbing the endoplasmic reticulum-mitochondria cross-talk and causing severe Ca

Indexed as

Alzheimer DiseaseAmyloid beta-PeptidesAmyloid beta-Protein PrecursorAmyloid Precursor Protein SecretasesAnimalsAspartic Acid EndopeptidasesBlood-Brain BarrierBrainEndoplasmic ReticulumHumansMitochondriaProtein Aggregation, PathologicalSignal TransductionUp-RegulationAmyloid beta-PeptidesAmyloid beta-Protein PrecursorAmyloid Precursor Protein SecretasesAspartic Acid EndopeptidasesBACE1 protein, humanAlzheimer’s diseaseAPPautophagyAβ-clearanceCa2+ dysregulationER-mitochondrial axisintracellular Aβmolecular chaperonesneuroinflammationprotein and lipid dyshomeostasis

Identifiers

PMID28994715
PMCPMC6151811
OpenAlexW2762897579

What OpenQuestion holds

Textmetadata
LicenceCC BY
Read underepoch 390

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.