Evidence map›Paper›PMID 41158105›Full record

ArticleProtein science : a publication of the Protein Society2025

PPISHES-an enhanced physicochemical approach for predicting protein interaction sites using graph neural networks.

Darpan Khanna, Abdullah Abdul Sattar Shaikh, Luis Rueda

Abstract read
In one paragraph

Article in Protein science : a publication of the Protein Society, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.

0numbers the graph read from it
0cells of the map it votes in
1citing 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

1 citing paper in PubMed.

  1. 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

3 authors.

Darpan KhannaSchool of Computer Science, University of Windsor, Ontario, Canada.
Abdullah Abdul Sattar ShaikhSchool of Computer Science, University of Windsor, Ontario, Canada.
Luis RuedaSchool of Computer Science, University of Windsor, Ontario, Canada.ORCID 0000-0001-7988-2058

Funding

Natural Sciences and Engineering Research Council of Canada RGPIN-2019-04696Vector Institute
6 · The paper itself

Abstract

Accurate prediction of protein interaction sites is crucial for understanding biological processes. Many existing methods capture structural, evolutionary, and sequence features; however, they overlook important physicochemical properties, limiting their performance. We propose Prediction of protein interaction sites based on solvent accessible surface area, hydrogen-bonding propensity, and electrostatic potential sites, an enhanced model that incorporates the three physicochemical features to improve site prediction for both obligate and non-obligate complexes. Feature ablation and other analyses identified key features to improve model performance. The model achieved up to 42.8% and 29.3% improvements in Area Under the Precision-Recall Curve for Test_315 and Test_71, respectively. The model also outperforms current state-of-the-art methods across other key metrics, such as Recall, Area Under the Curve, and Matthews Correlation Coefficient.

Indexed as

Computational BiologyNeural Networks, ComputerProtein Interaction MappingProteinsDatabases, ProteinGraph Neural NetworksHydrogen BondingStatic ElectricityProteinselectrostatic potentialhydrogen‐bonding propensityphysicochemical featuresprotein interaction site predictionresidual graph convolutional networksolvent‐accessible surface area

Identifiers

PMID41158105
PMCPMC12569455

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-ND
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.