Evidence map›Paper›PMID 29671834›Full record

ReviewMolecules (Basel, Switzerland)2018

Using Peptidomimetics and Constrained Peptides as Valuable Tools for Inhibiting Protein⁻Protein Interactions.

Naomi S Robertson, David R Spring

Abstract readReview
In one paragraph

Review in Molecules (Basel, Switzerland), 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 40 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
40citing papers in PubMed, 1 pooled it
–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

40 citing papers in PubMed, 1 synthesis or guideline pooled it.

  1. Pooled it
  2. Article
  3. RSC chemical biology · 2026
    Article
  4. Article
  5. Article
  6. Review
  7. Article
  8. β-Hairpin Peptidomimetics for Protein-Protein Interaction Inhibition.Methods in molecular biology (Clifton, N.J.) · 2025
    Article
  9. Review
  10. Non-symmetric stapling of native peptides.Nature reviews. Chemistry · 2024
    Review
  11. Article
  12. Article
  13. Article
  14. Review
  15. Article
  16. Article
  17. Article
  18. 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

2 authors.

Naomi S RobertsonDepartment of Chemistry, University of Cambridge, Lensfield Road, Cambridge CB2 1EW, UK. nsr32@cam.ac.uk.ORCID 0000-0001-5519-9158
David R SpringDepartment of Chemistry, University of Cambridge, Lensfield Road, Cambridge CB2 1EW, UK. spring@ch.cam.ac.uk.ORCID 0000-0001-7355-2824

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Protein⁻protein interactions (PPIs) are tremendously important for the function of many biological processes. However, because of the structure of many protein⁻protein interfaces (flat, featureless and relatively large), they have largely been overlooked as potential drug targets. In this review, we highlight the current tools used to study the molecular recognition of PPIs through the use of different peptidomimetics, from small molecules and scaffolds to peptides. Then, we focus on constrained peptides, and in particular, ways to constrain α-helices through stapling using both one- and two-component techniques.

Indexed as

PeptidesPeptidomimeticsProtein BindingPeptidesPeptidomimeticsmacrocyclespeptidomimeticsprotein–protein interactionsproteomimeticsstapled peptides

Identifiers

PMID29671834
PMCPMC6017787

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.