Evidence map›Paper›PMID 35596819›Full record

ReviewCellular and molecular neurobiology2023

Tau Aggregation Inhibiting Peptides as Potential Therapeutics for Alzheimer Disease.

Isabelle Aillaud, Susanne Aileen Funke

Open access · hybridFull text readReview
PubMed Full text at PMC Publisher
In one paragraph

Review in Cellular and molecular neurobiology, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 30 papers.

0numbers the graph read from it
0cells of the map it votes in
30citing papers in PubMed
4.6field-weighted citation impact, top 4% 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

30 citing papers in PubMed, 40 citations in OpenAlex.

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  12. Frontiers in neuroscience · 2025
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  17. Precision proteoform design for 4R tau isoform selective templated aggregation.Proceedings of the National Academy of Sciences of the United States of America · 2024
    Article
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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

2 authors at 1 institution in 1 country.

Isabelle AillaudInstitute of Bioanalysis, Coburg University of Applied Sciences, Coburg, Germany.ORCID http://orcid.org/0000-0003-0833-9407
Susanne Aileen FunkeInstitute of Bioanalysis, Coburg University of Applied Sciences, Coburg, Germany. aileen.funke@hs-coburg.de.ORCID http://orcid.org/0000-0002-1160-8762
Coburg University of Applied Sciences · DE

Funding

Alzheimer Forschung Initiative e.V. (AFI) 17001
6 · The paper itself

Abstract

Alzheimer disease (AD) is the most common progressive neurodegenerative disorder. AD causes enormous personal and economic burden to society as currently only limited palliative therapeutic options are available. The pathological hallmarks of the disease are extracellular plaques, composed of fibrillar amyloid-β (Aβ), and neurofibrillary tangles inside neurons, composed of Tau protein. Until recently, the search for AD therapeutics was focussed more on the Aβ peptide and its pathology, but the results were unsatisfying. As an alternative, Tau might be a promising therapeutic target as its pathology is closely correlated to clinical symptoms. In addition, pathological Tau aggregation occurs in a large group of diseases, called Tauopathies, and in most of them Aβ aggregation does not play a role in disease pathogenesis. The formation of Tau aggregates is triggered by two hexapeptide motifs within Tau; PHF6* and PHF6. Both fragments are interesting targets for the development of Tau aggregation inhibitors (TAI). Peptides represent a unique class of pharmaceutical compounds and are reasonable alternatives to chemical substances or antibodies. They are attributed with high biological activity, valuable specificity and low toxicity, and often are developed as drug candidates to interrupt protein-protein interactions. The preparation of peptides is simple, controllable and the peptides can be easily modified. However, their application may also have disadvantages. Currently, a few peptide compounds acting as TAI are described in the literature, most of them developed by structure-based design or phage display. Here, we review the current state of research in this promising field of AD therapy development.

Indexed as

Alzheimer DiseaseTauopathiesAmyloid beta-PeptidesHumansNeurofibrillary Tanglestau ProteinsAmyloid beta-Peptidestau ProteinsAggregation inhibitorsAlzheimer diseasePeptidesTauTauopathies

Identifiers

PMID35596819
PMCPMC10006036
OpenAlexW4281249394

What OpenQuestion holds

Textfull text, public
LicenceCC BY
measurements read3
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.