Evidence map›Paper›PMID 33686072›Full record

ArticleNature communications2021

Specific inhibition of the Survivin-CRM1 interaction by peptide-modified molecular tweezers.

Annika Meiners, Sandra Bäcker, Inesa Hadrović, Christian Heid, Christine Beuck, Yasser B Ruiz-Blanco, Joel Mieres-Perez, Marius Pörschke, Jean-Noël Grad, Cecilia Vallet and 5 more

Open access · goldAbstract read
In one paragraph

Article in Nature communications, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.

0numbers the graph read from it
0cells of the map it votes in
16citing papers in PubMed
1.8field-weighted citation impact, top 15% 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

16 citing papers in PubMed, 32 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Protein Recognition and Assembly by a Phosphocavitand.Journal of the American Chemical Society · 2025
    Article
  6. Molecular Tweezers Block the Functional Pore of a Protein Machine.Journal of the American Chemical Society · 2025
    Article
  7. Review
  8. Design of an Anti-HMGB1 Synthetic Antibody forJournal of the American Chemical Society · 2023
    Article
  9. Article
  10. Article
  11. Article
  12. Review
  13. Article
  14. Article
  15. Review
  16. 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

15 authors at 1 institution in 1 country.

Annika Meiners *Department of Molecular Biology II, Centre for Medical Biotechnology (ZMB), University of Duisburg-Essen, Essen, Germany.
Sandra Bäcker *Department of Molecular Biology II, Centre for Medical Biotechnology (ZMB), University of Duisburg-Essen, Essen, Germany.ORCID http://orcid.org/0000-0001-6388-7778
Inesa Hadrović *Institute of Organic Chemistry I, Faculty of Chemistry, University of Duisburg-Essen, Essen, Germany.
Christian Heid *Institute of Organic Chemistry I, Faculty of Chemistry, University of Duisburg-Essen, Essen, Germany.
Christine BeuckDepartment of Structural and Medicinal Biology, Centre for Medical Biotechnology (ZMB), University of Duisburg-Essen, Essen, Germany.ORCID http://orcid.org/0000-0001-7513-7384
Yasser B Ruiz-BlancoDepartment of Computational Biochemistry, Centre for Medical Biotechnology (ZMB), University of Duisburg-Essen, Essen, Germany.
Joel Mieres-PerezDepartment of Computational Biochemistry, Centre for Medical Biotechnology (ZMB), University of Duisburg-Essen, Essen, Germany.ORCID http://orcid.org/0000-0002-7875-0886
Marius PörschkeDepartment of Structural and Medicinal Biology, Centre for Medical Biotechnology (ZMB), University of Duisburg-Essen, Essen, Germany.ORCID http://orcid.org/0000-0003-4129-6058
Jean-Noël GradDepartment of Bioinformatics and Computational Biophysics, Centre for Medical Biotechnology (ZMB), University of Duisburg-Essen, Essen, Germany.
Cecilia ValletDepartment of Molecular Biology II, Centre for Medical Biotechnology (ZMB), University of Duisburg-Essen, Essen, Germany.
Daniel HoffmannDepartment of Bioinformatics and Computational Biophysics, Centre for Medical Biotechnology (ZMB), University of Duisburg-Essen, Essen, Germany.ORCID http://orcid.org/0000-0003-2973-7869
Peter BayerDepartment of Structural and Medicinal Biology, Centre for Medical Biotechnology (ZMB), University of Duisburg-Essen, Essen, Germany.ORCID http://orcid.org/0000-0003-0435-7202
Elsa Sánchez-GarcíaDepartment of Computational Biochemistry, Centre for Medical Biotechnology (ZMB), University of Duisburg-Essen, Essen, Germany. elsa.sanchez-garcia@uni-due.de.ORCID http://orcid.org/0000-0002-9211-5803
Thomas SchraderInstitute of Organic Chemistry I, Faculty of Chemistry, University of Duisburg-Essen, Essen, Germany. thomas.schrader@uni-due.de.ORCID http://orcid.org/0000-0002-7003-6362
Shirley K KnauerDepartment of Molecular Biology II, Centre for Medical Biotechnology (ZMB), University of Duisburg-Essen, Essen, Germany. shirley.knauer@uni-due.de.ORCID http://orcid.org/0000-0003-4321-0924
University of Duisburg-Essen · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Survivin's dual function as apoptosis inhibitor and regulator of cell proliferation is mediated via its interaction with the export receptor CRM1. This protein-protein interaction represents an attractive target in cancer research and therapy. Here, we report a sophisticated strategy addressing Survivin's nuclear export signal (NES), the binding site of CRM1, with advanced supramolecular tweezers for lysine and arginine. These were covalently connected to small peptides resembling the natural, self-complementary dimer interface which largely overlaps with the NES. Several biochemical methods demonstrated sequence-selective NES recognition and interference with the critical receptor interaction. These data were strongly supported by molecular dynamics simulations and multiscale computational studies. Rational design of lysine tweezers equipped with a peptidic recognition element thus allowed to address a previously unapproachable protein surface area. As an experimental proof-of-principle for specific transport signal interference, this concept should be transferable to any protein epitope with a flanking well-accessible lysine.

Indexed as

Binding SitesCell ProliferationExportin 1 ProteinHumansInhibitor of Apoptosis ProteinsKaryopherinsModels, MolecularNuclear Export SignalsProtein BindingProtein ConformationProtein Interaction Domains and MotifsReceptors, Cytoplasmic and NuclearSurvivinBIRC5 protein, humanExportin 1 ProteinInhibitor of Apoptosis ProteinsKaryopherinsNuclear Export SignalsReceptors, Cytoplasmic and NuclearSurvivin

Identifiers

PMID33686072
PMCPMC7940618
OpenAlexW3135769053

What OpenQuestion holds

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LicenceCC BY
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Registered trials

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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.