Evidence map›Paper›PMID 31525028›Full record

ArticleACS chemical biology2019

Predicting and Experimentally Validating Hot-Spot Residues at Protein-Protein Interfaces.

Amaurys A Ibarra, Gail J Bartlett, Zsöfia Hegedüs, Som Dutt, Fruzsina Hobor, Katherine A Horner, Kristina Hetherington, Kirstin Spence, Adam Nelson, Thomas A Edwards and 3 more

Abstract read
In one paragraph

Article in ACS chemical biology, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 57 papers.

0numbers the graph read from it
0cells of the map it votes in
57citing 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

57 citing papers in PubMed.

  1. Article
  2. RSC chemical biology · 2026
    Article
  3. Article
  4. Article
  5. Article
  6. The Structural Analogy of MASP-2 with Thrombin and MASP-1 Reveals Strong Binding with PAR4.Anti-inflammatory & anti-allergy agents in medicinal chemistry · 2026
    Article
  7. Article
  8. Article
  9. Review
  10. Article
  11. Review
  12. Article
  13. Article
  14. Mapping the interaction surface between CaNature communications · 2025
    Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. Review
  20. PPI-hotspoteLife · 2024
    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

13 authors.

Amaurys A IbarraSchool of Biochemistry , University of Bristol , Medical Sciences Building, University Walk , Bristol BS8 1TD , U.K.
Gail J BartlettSchool of Chemistry , University of Bristol , Cantock's Close , Bristol BS8 1TS , U.K.
Zsöfia HegedüsSchool of Chemistry , University of Leeds , Woodhouse Lane , Leeds LS2 9JT , U.K.
Som DuttSchool of Chemistry , University of Leeds , Woodhouse Lane , Leeds LS2 9JT , U.K.
Fruzsina HoborAstbury Centre for Structural Molecular Biology , University of Leeds , Woodhouse Lane , Leeds LS2 9JT , U.K.
Katherine A HornerSchool of Chemistry , University of Leeds , Woodhouse Lane , Leeds LS2 9JT , U.K.
Kristina HetheringtonSchool of Chemistry , University of Leeds , Woodhouse Lane , Leeds LS2 9JT , U.K.
Kirstin SpenceAstbury Centre for Structural Molecular Biology , University of Leeds , Woodhouse Lane , Leeds LS2 9JT , U.K.
Adam NelsonSchool of Chemistry , University of Leeds , Woodhouse Lane , Leeds LS2 9JT , U.K.
Thomas A EdwardsAstbury Centre for Structural Molecular Biology , University of Leeds , Woodhouse Lane , Leeds LS2 9JT , U.K.
Derek N WoolfsonSchool of Biochemistry , University of Bristol , Medical Sciences Building, University Walk , Bristol BS8 1TD , U.K.ORCID 0000-0002-0394-3202
Richard B SessionsSchool of Biochemistry , University of Bristol , Medical Sciences Building, University Walk , Bristol BS8 1TD , U.K.ORCID 0000-0003-0320-0895
Andrew J WilsonSchool of Chemistry , University of Leeds , Woodhouse Lane , Leeds LS2 9JT , U.K.ORCID 0000-0001-9852-6366

Funding

Biotechnology and Biological Sciences Research Council BB/L01386X/1Wellcome Trust 094232/Z/10/ZWellcome Trust 097827/Z/11/AWellcome Trust WT094232M
6 · The paper itself

Abstract

Protein-protein interactions (PPIs) are vital to all biological processes. These interactions are often dynamic, sometimes transient, typically occur over large topographically shallow protein surfaces, and can exhibit a broad range of affinities. Considerable progress has been made in determining PPI structures. However, given the above properties, understanding the key determinants of their thermodynamic stability remains a challenge in chemical biology. An improved ability to identify and engineer PPIs would advance understanding of biological mechanisms and mutant phenotypes and also provide a firmer foundation for inhibitor design.

Indexed as

Amino AcidsAnimalsHumansMagnetic Resonance SpectroscopyMiceMolecular Dynamics SimulationMutagenesis, Site-DirectedMyeloid Cell Leukemia Sequence 1 ProteinNerve Tissue ProteinsProtein BindingProtein MultimerizationProteinsRatsSAP90-PSD95 Associated ProteinsSmall Ubiquitin-Related Modifier ProteinsAmino AcidsMcl1 protein, mouseMyeloid Cell Leukemia Sequence 1 ProteinNerve Tissue ProteinsProteinsSAP90-PSD95 Associated ProteinsSmall Ubiquitin-Related Modifier Proteins

Identifiers

PMID31525028
PMCPMC6804253

What OpenQuestion holds

Textmetadata
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.