Evidence map›Paper›PMID 32872553›Full record

ArticleInternational journal of molecular sciences2020

Tetrapeptide Ac-HAEE-NH

Evgeny P Barykin, Aleksandra I Garifulina, Anna P Tolstova, Anastasia A Anashkina, Alexei A Adzhubei, Yuri V Mezentsev, Irina V Shelukhina, Sergey A Kozin, Victor I Tsetlin, Alexander A Makarov

Open access · goldAbstract read
In one paragraph

Article in International journal of molecular sciences, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.

0numbers the graph read from it
0cells of the map it votes in
13citing papers in PubMed
0.8field-weighted citation impact, top 28% 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

13 citing papers in PubMed, 19 citations in OpenAlex.

  1. Review
  2. The Tetrapeptide HAEE Promotes Amyloid-Beta Clearance from the Brain.International journal of molecular sciences · 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

10 authors at 4 institutions in 2 countries.

Evgeny P BarykinEngelhardt Institute of Molecular Biology, Russian Academy of Sciences, Vavilov St. 32, 119991 Moscow, Russia.
Aleksandra I GarifulinaShemyakin-Ovchinnikov Institute of Bioorganic Chemistry, Russian Academy of Sciences, Miklukho-Maklaya Street, 16/10, 117997 Moscow, Russia.
Anna P TolstovaEngelhardt Institute of Molecular Biology, Russian Academy of Sciences, Vavilov St. 32, 119991 Moscow, Russia.
Anastasia A AnashkinaEngelhardt Institute of Molecular Biology, Russian Academy of Sciences, Vavilov St. 32, 119991 Moscow, Russia.ORCID 0000-0003-1763-300X
Alexei A AdzhubeiEngelhardt Institute of Molecular Biology, Russian Academy of Sciences, Vavilov St. 32, 119991 Moscow, Russia.
Yuri V MezentsevOrekhovich Institute of Biomedical Chemistry, Pogodinskaya street 10/8, 119121 Moscow, Russia.
Irina V ShelukhinaShemyakin-Ovchinnikov Institute of Bioorganic Chemistry, Russian Academy of Sciences, Miklukho-Maklaya Street, 16/10, 117997 Moscow, Russia.
Sergey A KozinEngelhardt Institute of Molecular Biology, Russian Academy of Sciences, Vavilov St. 32, 119991 Moscow, Russia.
Victor I TsetlinShemyakin-Ovchinnikov Institute of Bioorganic Chemistry, Russian Academy of Sciences, Miklukho-Maklaya Street, 16/10, 117997 Moscow, Russia.ORCID 0000-0002-7980-6191
Alexander A MakarovEngelhardt Institute of Molecular Biology, Russian Academy of Sciences, Vavilov St. 32, 119991 Moscow, Russia.
Engelhardt Institute of Molecular Biology · RUInstitute of Bioorganic Chemistry · RUInstitute of Biomedical Chemistry · RUUniversity of Vienna · AT

Funding

Russian Science Foundation 19-74-30007
6 · The paper itself

Abstract

The cholinergic deficit in Alzheimer's disease (AD) may arise from selective loss of cholinergic neurons caused by the binding of Aβ peptide to nicotinic acetylcholine receptors (nAChRs). Thus, compounds preventing such an interaction are needed to address the cholinergic dysfunction. Recent findings suggest that the

Indexed as

Alzheimer DiseaseAmino Acid MotifsAmyloid beta-PeptidesAnimalsBinding SitesFemaleHumansModels, MolecularOocytesPeptidesProtein ConformationReceptors, NicotinicSurface Plasmon ResonanceXenopus laevisAmyloid beta-Peptidesnicotinic receptor alpha4beta2PeptidesReceptors, NicotinicAlzheimer’s diseasecholinergic deficitmolecular modelingnicotinic acetylcholine receptorpeptide drugsβ-amyloid

Identifiers

PMID32872553
PMCPMC7504039
OpenAlexW3082378233

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.