Evidence map›Paper›PMID 38966365›Full record

ArticleChemical science2024

Understanding β-strand mediated protein-protein interactions: tuning binding behaviour of intrinsically disordered sequences by backbone modification.

Emma E Cawood, Emily Baker, Thomas A Edwards, Derek N Woolfson, Theodoros K Karamanos, Andrew J Wilson

Abstract read
In one paragraph

Article in Chemical science, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.

0numbers the graph read from it
0cells of the map it votes in
5citing 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

5 citing papers in PubMed.

  1. MinimalRSC chemical biology · 2026
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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.

Emma E CawoodAstbury Centre for Structural Molecular Biology, University of Leeds Woodhouse Lane Leeds LS2 9JT UK a.j.wilson.1@bham.ac.uk.ORCID https://orcid.org/0000-0002-2707-8022
Emily BakerSchool of Biochemistry, University of Bristol Medical Sciences Building, University Walk Bristol BS8 1TD UK d.n.woolfson@bristol.ac.uk.
Thomas A EdwardsAstbury Centre for Structural Molecular Biology, University of Leeds Woodhouse Lane Leeds LS2 9JT UK a.j.wilson.1@bham.ac.uk.ORCID https://orcid.org/0000-0002-1467-3674
Derek N WoolfsonSchool of Chemistry, University of Leeds Woodhouse Lane Leeds LS2 9JT UK.ORCID https://orcid.org/0000-0002-0394-3202
Theodoros K KaramanosDepartment of Life Sciences, Imperial College London London SW7 2BX UK t.karamanos@imperial.ac.uk.ORCID https://orcid.org/0000-0003-2297-540X
Andrew J WilsonAstbury Centre for Structural Molecular Biology, University of Leeds Woodhouse Lane Leeds LS2 9JT UK a.j.wilson.1@bham.ac.uk.ORCID https://orcid.org/0000-0001-9852-6366

Funding

Biotechnology and Biological Sciences Research Council BB/L01386X/1
6 · The paper itself

Abstract

A significant challenge in chemical biology is to understand and modulate protein-protein interactions (PPIs). Given that many PPIs involve a folded protein domain and a peptide sequence that is intrinsically disordered in isolation, peptides represent powerful tools to understand PPIs. Using the interaction between small ubiquitin-like modifier (SUMO) and SUMO-interacting motifs (SIMs), here we show that

Identifiers

PMID38966365
PMCPMC11220606

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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.