Evidence map›Paper›PMID 29016650›Full record

ArticlePloS one2017

Protein-protein interactions in paralogues: Electrostatics modulates specificity on a conserved steric scaffold.

Stefan M Ivanov, Andrew Cawley, Roland G Huber, Peter J Bond, Jim Warwicker

Abstract read
In one paragraph

Article in PloS one, 2017. 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. In Silico Isomerization Produces Apt Negative Data for VHTS Validation.Journal of chemical information and modeling · 2026
    Article
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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

5 authors.

Stefan M IvanovManchester Institute of Biotechnology, School of Chemistry, The University of Manchester, Manchester, United Kingdom.ORCID http://orcid.org/0000-0002-6949-2328
Andrew CawleyManchester Institute of Biotechnology, School of Chemistry, The University of Manchester, Manchester, United Kingdom.
Roland G HuberBioinformatics Institute, Agency for Science, Technology and Research (A*STAR), Matrix, Singapore, Singapore.
Peter J BondBioinformatics Institute, Agency for Science, Technology and Research (A*STAR), Matrix, Singapore, Singapore.
Jim WarwickerManchester Institute of Biotechnology, School of Chemistry, The University of Manchester, Manchester, United Kingdom.ORCID http://orcid.org/0000-0002-1302-0815

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

An improved knowledge of protein-protein interactions is essential for better understanding of metabolic and signaling networks, and cellular function. Progress tends to be based on structure determination and predictions using known structures, along with computational methods based on evolutionary information or detailed atomistic descriptions. We hypothesized that for the case of interactions across a common interface, between proteins from a pair of paralogue families or within a family of paralogues, a relatively simple interface description could distinguish between binding and non-binding pairs. Using binding data for several systems, and large-scale comparative modeling based on known template complex structures, it is found that charge-charge interactions (for groups bearing net charge) are generally a better discriminant than buried non-polar surface. This is particularly the case for paralogue families that are less divergent, with more reliable comparative modeling. We suggest that electrostatic interactions are major determinants of specificity in such systems, an observation that could be used to predict binding partners.

Indexed as

Conserved SequenceStatic ElectricityAmino AcidsAmino Acid SequenceBacteriaBacterial ProteinsBacterial ToxinsBinding SitesDNA-Binding ProteinsDNA Topoisomerase IVHumansHydrophobic and Hydrophilic InteractionsKineticsMembrane GlycoproteinsProtein BindingProtein Conformation, alpha-HelicalAmino AcidsBacterial ProteinsBacterial ToxinsDNA-Binding ProteinsDNA Topoisomerase IVMembrane GlycoproteinsparD protein, BacteriaUbiquitin-Conjugating EnzymesUbiquitin-Protein LigasesVapB protein, Bacteria

Identifiers

PMID29016650
PMCPMC5634604

What OpenQuestion holds

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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.