Evidence map›Paper›PMID 42141350›Full record

ArticleMolecular neurobiology2026

Amyloid Plaques Ameliorate Memory Deficits and Hippocampal Neuron Loss in an Aβ4-42-Driven Alzheimer's Disease Mouse Model.

Silvia Zampar, Merle Fricke, Florian Kremser, Ivan Talucci, Hans Michael Maric, Hans-Wolfgang Klafki, Agueda Rostagno, Olaf Jahn, Sascha Weggen, Jorge Ghiso and 1 more

Abstract read
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In one paragraph

Article in Molecular neurobiology, 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

11 authors.

Silvia Zampar *Department of Psychiatry and Psychotherapy, University Medical Center (UMG), Georg-August-University, Von-Siebold-Str. 5, 37075, Göttingen, Germany.
Merle Fricke *Department of Psychiatry and Psychotherapy, University Medical Center (UMG), Georg-August-University, Von-Siebold-Str. 5, 37075, Göttingen, Germany.
Florian KremserDepartment of Psychiatry and Psychotherapy, University Medical Center (UMG), Georg-August-University, Von-Siebold-Str. 5, 37075, Göttingen, Germany.
Ivan TalucciRudolf Virchow Center for Integrative and Translational Bioimaging, University of Würzburg, Würzburg, Germany.
Hans Michael MaricRudolf Virchow Center for Integrative and Translational Bioimaging, University of Würzburg, Würzburg, Germany.
Hans-Wolfgang KlafkiDepartment of Psychiatry and Psychotherapy, University Medical Center (UMG), Georg-August-University, Von-Siebold-Str. 5, 37075, Göttingen, Germany.
Agueda RostagnoDepartment of Pathology, New York University School of Medicine, New York, NY, USA.
Olaf JahnDepartment of Psychiatry and Psychotherapy, University Medical Center (UMG), Georg-August-University, Von-Siebold-Str. 5, 37075, Göttingen, Germany.
Sascha WeggenDepartment of Neuropathology, Heinrich-Heine-University, Düsseldorf, Germany.
Jorge GhisoDepartment of Pathology, New York University School of Medicine, New York, NY, USA.
Oliver WirthsDepartment of Psychiatry and Psychotherapy, University Medical Center (UMG), Georg-August-University, Von-Siebold-Str. 5, 37075, Göttingen, Germany. owirths@gwdg.de.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Extracellular deposition of amyloid-β (Aβ) peptides in the form of plaques is the most prominent pathological hallmark of Alzheimer's disease (AD). The postulated central pathophysiological role of fibrillary Aβ plaques has, however, been questioned, and small, soluble, pre-fibrillar Aβ aggregates (oligomers) have been implicated as the crucial neurotoxic species in AD etiology. While the relationship between insoluble amyloid plaques and soluble Aβ oligomers remains unclear, it has been hypothesized that plaques may serve as reservoirs, sequestering toxic Aβ oligomers in the initial stages of the disease. Next to the canonical "full-length" Aβ1-40 and Aβ1-42 peptides, a variety of N-terminally truncated Aβ variants are present in AD brain tissue, with Aβ4-42 peptides showing high abundance. The detrimental effects of these N-terminally truncated peptides have been previously studied using the Tg4-42

Indexed as

Alzheimer DiseaseAmyloid beta-PeptidesHippocampusMemory DisordersNeuronsPeptide FragmentsPlaque, AmyloidAnimalsDisease Models, AnimalMaleMiceMice, TransgenicAmyloid beta-PeptidesPeptide FragmentsAbetaAlzheimer’s diseaseAmyloid pathologyBehaviorMouse modelNeuron lossN-terminal truncation

Identifiers

PMID42141350
PMCPMC13179277

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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.