Evidence map›Paper›PMID 39332048›Full record

ReviewCurrent opinion in structural biology2024

Using residue interaction networks to understand protein function and evolution and to engineer new proteins.

Dariia Yehorova, Bruno Di Geronimo, Michael Robinson, Peter M Kasson, Shina C L Kamerlin

Abstract readReview
In one paragraph

Review in Current opinion in structural biology, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.

0numbers the graph read from it
0cells of the map it votes in
15citing 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

15 citing papers in PubMed.

  1. Review
  2. Article
  3. Article
  4. Structural Features of a Tiny Viral Protein, ORF7b of SARS-CoV-2.International journal of molecular sciences · 2026
    Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. Review
  10. Review
  11. Review
  12. Article
  13. 'Intelligent' proteins.Cellular and molecular life sciences : CMLS · 2025
    Review
  14. Article
  15. Review
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.

Dariia YehorovaSchool of Chemistry and Biochemistry, Georgia Institute of Technology, 901 Atlantic Drive NW, Atlanta, GA-30332, USA.
Bruno Di GeronimoSchool of Chemistry and Biochemistry, Georgia Institute of Technology, 901 Atlantic Drive NW, Atlanta, GA-30332, USA.
Michael RobinsonDepartment of Chemistry - BMC, Uppsala University, BMC Box 576, S-751 23 Uppsala, Sweden.
Peter M KassonSchool of Chemistry and Biochemistry, Georgia Institute of Technology, 901 Atlantic Drive NW, Atlanta, GA-30332, USA; Department of Biomedical Engineering, Georgia Institute of Technology, 313 Fersht Dr NW, Atlanta GA 30332, USA; Department of Cell and Molecular Biology, Uppsala University, BMC Box 596, S-751 24 Uppsala, Sweden.
Shina C L KamerlinSchool of Chemistry and Biochemistry, Georgia Institute of Technology, 901 Atlantic Drive NW, Atlanta, GA-30332, USA; Department of Chemistry - BMC, Uppsala University, BMC Box 576, S-751 23 Uppsala, Sweden. Electronic address: skamerlin3@gatech.edu.

Funding

Simulation-guided spectroscopy and refinement of heterogenous conformational ensemblesR01GM138444 · NIGMS · UNIVERSITY OF VIRGINIA · PI KASSON, PETER M · 2021 to 2024
$1.4M
NIGMS NIH HHS R01 GM138444
6 · The paper itself

Abstract

Residue interaction networks (RINs) provide graph-based representations of interaction networks within proteins, providing important insight into the factors driving protein structure, function, and stability relationships. There exists a wide range of tools with which to perform RIN analysis, taking into account different types of interactions, input (crystal structures, simulation trajectories, single proteins, or comparative analysis across proteins), as well as formats, including standalone software, web server, and a web application programming interface (API). In particular, the ability to perform comparative RIN analysis across protein families using "metaRINs" provides a valuable tool with which to dissect protein evolution. This, in turn, highlights hotspots to avoid (or target) for in vitro evolutionary studies, providing a powerful framework that can be exploited to engineer new proteins.

Indexed as

Evolution, MolecularProtein EngineeringProteinsHumansModels, MolecularProtein ConformationProtein Interaction MapsSoftwareProteins

Identifiers

PMID39332048
PMCPMC12135629

What OpenQuestion holds

Textmetadata
LicenceTDM
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.