Evidence map›Paper›PMID 31814236›Full record

ArticleAngewandte Chemie (International ed. in English)2020

A Supramolecular Stabilizer of the 14-3-3ζ/ERα Protein-Protein Interaction with a Synergistic Mode of Action.

Alba Gigante, Eline Sijbesma, Pedro A Sánchez-Murcia, Xiaoyu Hu, David Bier, Sandra Bäcker, Shirley Knauer, Federico Gago, Christian Ottmann, Carsten Schmuck

Open access · hybridAbstract read
In one paragraph

Article in Angewandte Chemie (International ed. in English), 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.

0numbers the graph read from it
0cells of the map it votes in
11citing papers in PubMed
1.1field-weighted citation impact, top 22% 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

11 citing papers in PubMed, 17 citations in OpenAlex.

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  11. NMR Spectroscopy of supramolecular chemistry on protein surfaces.Beilstein journal of organic chemistry · 2020
    Review
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 4 countries.

Alba GiganteDepartment of Organic Chemistry, University of Duisburg Essen, Universitätstr. 7, 45141, Essen, Germany.ORCID 0000-0003-2606-665X
Eline SijbesmaDepartment of Biomedical Engineering, Eindhoven University of Technology, P.O. Box 513, 5600 MB, Eindhoven, The Netherlands.ORCID 0000-0002-4837-7574
Pedro A Sánchez-MurciaDepartamento de Ciencias Biomédicas, Universidad de Alcalá, 28805, Alcalá de Henares, Spain.
Xiaoyu HuDepartment of Organic Chemistry, University of Duisburg Essen, Universitätstr. 7, 45141, Essen, Germany.
David BierDepartment of Organic Chemistry, University of Duisburg Essen, Universitätstr. 7, 45141, Essen, Germany.
Sandra BäckerCentre for Medical Biotechnology, University of Duisburg Essen, Universitätstr. 7, 45141, Essen, Germany.
Shirley KnauerCentre for Medical Biotechnology, University of Duisburg Essen, Universitätstr. 7, 45141, Essen, Germany.
Federico GagoDepartamento de Ciencias Biomédicas, Universidad de Alcalá, 28805, Alcalá de Henares, Spain.
Christian OttmannDepartment of Organic Chemistry, University of Duisburg Essen, Universitätstr. 7, 45141, Essen, Germany.ORCID 0000-0001-7315-0315
Carsten SchmuckDepartment of Organic Chemistry, University of Duisburg Essen, Universitätstr. 7, 45141, Essen, Germany.
University of Duisburg-Essen · DEEindhoven University of Technology · NLUniversidad de Alcalá · ESUniversity of Vienna · AT

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

We report on a stabilizer of the interaction between 14-3-3ζ and the Estrogen Receptor alpha (ERα). ERα is a driver in the majority of breast cancers and 14-3-3 proteins are negative regulators of this nuclear receptor, making the stabilization of this protein-protein interaction (PPI) an interesting strategy. The stabilizer (1) consists of three symmetric peptidic arms containing an arginine mimetic, previously described as the GCP motif. 1 stabilizes the 14-3-3ζ/ERα interaction synergistically with the natural product Fusicoccin-A and was thus hypothesized to bind to a different site. This is supported by computational analysis of 1 binding to the binary complex of 14-3-3 and an ERα-derived phosphopeptide. Furthermore, 1 shows selectivity towards 14-3-3ζ/ERα interaction over other 14-3-3 client-derived phosphomotifs. These data provide a solid support of a new binding mode for a supramolecular 14-3-3ζ/ERα PPI stabilizer.

Indexed as

14-3-3 ProteinsAmino Acid MotifsAmino Acid SequenceArginineBreast NeoplasmsEstrogen Receptor alphaGlycosidesHumansMolecular Dynamics SimulationPeptidesProtein Binding14-3-3 ProteinsArginineEstrogen Receptor alphafusicoccinGlycosidesPeptides14-3-3ERαprotein-protein interactionstabilizerssupramolecular systems

Identifiers

PMID31814236
PMCPMC7155037
OpenAlexW2994348454

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.