Evidence map›Paper›PMID 34458778›Full record

ReviewRSC chemical biology2021

Strategies to expand peptide functionality through hybridisation with a small molecule component.

Yuteng Wu, Jack Williams, Ewen D D Calder, Louise J Walport

Abstract readReview
In one paragraph

Review in RSC chemical biology, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.

0numbers the graph read from it
0cells of the map it votes in
10citing 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

10 citing papers in PubMed.

  1. Article
  2. Article
  3. Review
  4. Article
  5. Article
  6. Article
  7. Review
  8. Article
  9. Article
  10. 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

4 authors.

Yuteng WuProtein-Protein Interaction Laboratory, The Francis Crick Institute London UK Louise.walport@crick.ac.uk.ORCID https://orcid.org/0000-0002-8573-9626
Jack WilliamsProtein-Protein Interaction Laboratory, The Francis Crick Institute London UK Louise.walport@crick.ac.uk.ORCID https://orcid.org/0000-0002-6239-9083
Ewen D D CalderProtein-Protein Interaction Laboratory, The Francis Crick Institute London UK Louise.walport@crick.ac.uk.ORCID https://orcid.org/0000-0001-7201-8451
Louise J WalportProtein-Protein Interaction Laboratory, The Francis Crick Institute London UK Louise.walport@crick.ac.uk.ORCID https://orcid.org/0000-0002-3795-8365

Funding

Wellcome Trust FC001748
6 · The paper itself

Abstract

Combining different compound classes gives molecular hybrids that can offer access to novel chemical space and unique properties. Peptides provide ideal starting points for such molecular hybrids, which can be easily modified with a variety of molecular entities. The addition of small molecules can improve the potency, stability and cell permeability of therapeutically relevant peptides. Furthermore, they are often applied to create peptide-based tools in chemical biology. In this review, we discuss general methods that allow the discovery of this compound class and highlight key examples of peptide-small molecule hybrids categorised by the application and function of the small molecule entity.

Identifiers

PMID34458778
PMCPMC8341444

What Socratic 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 Socratic graph.