Evidence map›Paper›PMID 27467859›Full record

ArticleAngewandte Chemie (International ed. in English)2016

An α-Helix-Mimicking 12,13-Helix: Designed α/β/γ-Foldamers as Selective Inhibitors of Protein-Protein Interactions.

Claire M Grison, Jennifer A Miles, Sylvie Robin, Andrew J Wilson, David J Aitken

Open access · hybridAbstract read
In one paragraph

Article in Angewandte Chemie (International ed. in English), 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.

0numbers the graph read from it
0cells of the map it votes in
24citing papers in PubMed
4.7field-weighted citation impact, top 5% 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

24 citing papers in PubMed, 64 citations in OpenAlex.

  1. RSC chemical biology · 2026
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  4. Review
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  8. Review
  9. Dissecting Solvent Effects on Hydrogen Bonding.Angewandte Chemie (International ed. in English) · 2022
    Article
  10. Article
  11. A Sustainable Approach for Synthesizing (Frontiers in bioengineering and biotechnology · 2021
    Article
  12. Aromatic Foldamer Helices as α-Helix Extended Surface Mimetics.Chemistry (Weinheim an der Bergstrasse, Germany) · 2020
    Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. Article
  20. Chemical science · 2018
    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

5 authors at 2 institutions in 2 countries.

Claire M GrisonCP3A Organic Synthesis Group, ICMMO, CNRS, Université Paris Sud, Université Paris Saclay, 15 Rue George Clemenceau, 91405, Orsay Cedex, France.
Jennifer A MilesSchool of Chemistry, University of Leeds, Woodhouse Lane, Leeds, LS2 9JT, UK.
Sylvie RobinCP3A Organic Synthesis Group, ICMMO, CNRS, Université Paris Sud, Université Paris Saclay, 15 Rue George Clemenceau, 91405, Orsay Cedex, France.
Andrew J WilsonSchool of Chemistry, University of Leeds, Woodhouse Lane, Leeds, LS2 9JT, UK. A.J.Wilson@leeds.ac.uk.ORCID 0000-0001-9852-6366
David J AitkenCP3A Organic Synthesis Group, ICMMO, CNRS, Université Paris Sud, Université Paris Saclay, 15 Rue George Clemenceau, 91405, Orsay Cedex, France. david.aitken@u-psud.fr.
Université Paris-Sud · FRUniversity of Leeds · GB

Funding

European Research Council 632207Wellcome TrustWellcome Trust 104920/Z/14/Z
6 · The paper itself

Abstract

A major current challenge in bioorganic chemistry is the identification of effective mimics of protein secondary structures that act as inhibitors of protein-protein interactions (PPIs). In this work, trans-2-aminocyclobutanecarboxylic acid (tACBC) was used as the key β-amino acid component in the design of α/β/γ-peptides to structurally mimic a native α-helix. Suitably functionalized α/β/γ-peptides assume an α-helix-mimicking 12,13-helix conformation in solution, exhibit enhanced proteolytic stability in comparison to the wild-type α-peptide parent sequence from which they are derived, and act as selective inhibitors of the p53/hDM2 interaction.

Indexed as

Carboxylic AcidsCyclobutanesHumansProtein BindingProtein Conformation, alpha-HelicalRNA-Binding ProteinsTumor Suppressor Protein p532-aminocyclobutanecarboxylic acidCarboxylic AcidsCNBP protein, humanCyclobutanesRNA-Binding ProteinsTumor Suppressor Protein p53foldamersinhibitorspeptidomimeticsprotein-protein interactionsα-helix mimetics

Identifiers

PMID27467859
PMCPMC5014220
OpenAlexW2505601816

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.