Evidence map›Paper›PMID 28510303›Full record

ArticleAngewandte Chemie (International ed. in English)2017

A Binary Bivalent Supramolecular Assembly Platform Based on Cucurbit[8]uril and Dimeric Adapter Protein 14-3-3.

Pim J de Vink, Jeroen M Briels, Thomas Schrader, Lech-Gustav Milroy, Luc Brunsveld, Christian Ottmann

Abstract read
In one paragraph

Article in Angewandte Chemie (International ed. in English), 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 32 papers.

0numbers the graph read from it
0cells of the map it votes in
32citing 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

32 citing papers in PubMed.

  1. Review
  2. Making and Breaking Supramolecular Synthons for Modular Protein Frameworks.Chemistry (Weinheim an der Bergstrasse, Germany) · 2025
    Article
  3. Review
  4. Article
  5. Article
  6. Article
  7. Article
  8. Review
  9. Article
  10. Article
  11. Toward Light-Controlled Supramolecular Peptide Dimerization.The Journal of organic chemistry · 2021
    Article
  12. Article
  13. Article
  14. Article
  15. Facile Fabrication of Protein-Macrocycle Frameworks.Journal of the American Chemical Society · 2021
    Article
  16. Article
  17. Review
  18. A new soaking procedure for X-ray crystallographic structural determination of protein-peptide complexes.Acta crystallographica. Section F, Structural biology communications · 2020
    Article
  19. Review
  20. Article
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

6 authors.

Pim J de VinkLaboratory of Chemical Biology and Institute of Complex Molecular Systems, Department of Biomedical Engineering, Eindhoven University of Technology, Den Dolech 2, 5612 AZ, Eindhoven, The Netherlands.ORCID 0000-0001-6822-6995
Jeroen M BrielsLaboratory of Chemical Biology and Institute of Complex Molecular Systems, Department of Biomedical Engineering, Eindhoven University of Technology, Den Dolech 2, 5612 AZ, Eindhoven, The Netherlands.
Thomas SchraderDepartment of Chemistry, University of Duisburg-Essen, Universitätsstrasse 7, 45117, Essen, Germany.
Lech-Gustav MilroyLaboratory of Chemical Biology and Institute of Complex Molecular Systems, Department of Biomedical Engineering, Eindhoven University of Technology, Den Dolech 2, 5612 AZ, Eindhoven, The Netherlands.ORCID 0000-0003-4601-0936
Luc BrunsveldLaboratory of Chemical Biology and Institute of Complex Molecular Systems, Department of Biomedical Engineering, Eindhoven University of Technology, Den Dolech 2, 5612 AZ, Eindhoven, The Netherlands.ORCID 0000-0001-5675-511X
Christian OttmannLaboratory of Chemical Biology and Institute of Complex Molecular Systems, Department of Biomedical Engineering, Eindhoven University of Technology, Den Dolech 2, 5612 AZ, Eindhoven, The Netherlands.ORCID 0000-0001-7315-0315

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Interactions between proteins frequently involve recognition sequences based on multivalent binding events. Dimeric 14-3-3 adapter proteins are a prominent example and typically bind partner proteins in a phosphorylation-dependent mono- or bivalent manner. Herein we describe the development of a cucurbit[8]uril (Q8)-based supramolecular system, which in conjunction with the 14-3-3 protein dimer acts as a binary and bivalent protein assembly platform. We fused the phenylalanine-glycine-glycine (FGG) tripeptide motif to the N-terminus of the 14-3-3-binding epitope of the estrogen receptor α (ERα) for selective binding to Q8. Q8-induced dimerization of the ERα epitope augmented its affinity towards 14-3-3 through a binary bivalent binding mode. The crystal structure of the Q8-induced ternary complex revealed molecular insight into the multiple supramolecular interactions between the protein, the peptide, and Q8.

Indexed as

14-3-3 ProteinsAmino Acid MotifsBinding, CompetitiveBinding SitesBridged-Ring CompoundsCrystallography, X-RayCucurbit(n)urilsDimerizationEpitopesFluorescent DyesFluorometryImidazolesMacrocyclic CompoundsMolecular Dynamics SimulationPhosphopeptidesProtein Binding14-3-3 ProteinsBridged-Ring Compoundscucurbit(8)urilCucurbit(n)urilsEpitopesFluorescent DyesImidazolesMacrocyclic CompoundsPhosphopeptidesadapter proteinscooperativitycucurbiturilshost-guest systemssupramolecular chemistry

Identifiers

PMID28510303
PMCPMC5575475

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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.