Evidence map›Paper›PMID 38175787›Full record

ArticleBioinformatics (Oxford, England)2024

M-Ionic: prediction of metal-ion-binding sites from sequence using residue embeddings.

Aditi Shenoy, Yogesh Kalakoti, Durai Sundar, Arne Elofsson

Open access · goldAbstract read
In one paragraph

Article in Bioinformatics (Oxford, England), 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.

0numbers the graph read from it
0cells of the map it votes in
11citing papers in PubMed
5.4field-weighted citation impact, top 4% of its field
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

11 citing papers in PubMed, 23 citations in OpenAlex.

  1. PrOMet: Accurate and Robust Metal-Binding Site and Type Prediction.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2026
    Article
  2. MBPBERT: A Large Language Model for Metal-Binding Peptide Discovery.Interdisciplinary sciences, computational life sciences · 2026
    Article
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  9. Interpretable prediction of zinc ion location in proteins with ZincSight.Protein science : a publication of the Protein Society · 2025
    Article
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  11. bindNode24: Competitive binding residue prediction with 60 % smaller model.Computational and structural biotechnology journal · 2025
    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

4 authors at 2 institutions in 2 countries.

Aditi ShenoyScience for Life Laboratory and Department of Biochemistry and Biophysics, Stockholm University, Solna 17121, Sweden.ORCID 0000-0001-7748-2501
Yogesh KalakotiDepartment of Biochemical Engineering & Biotechnology, Indian Institute of Technology (IIT) Delhi, New Delhi 110016, India.
Durai SundarDepartment of Biochemical Engineering & Biotechnology, Indian Institute of Technology (IIT) Delhi, New Delhi 110016, India.ORCID 0000-0002-6549-6663
Arne ElofssonScience for Life Laboratory and Department of Biochemistry and Biophysics, Stockholm University, Solna 17121, Sweden.ORCID 0000-0002-7115-9751
Indian Institute of Technology Delhi · INStockholm University · SE

Funding

Knut and Alice Wallenberg FoundationSNICVetenskapsrådet 2021-03979
6 · The paper itself

Abstract

motivationUnderstanding metal-protein interaction can provide structural and functional insights into cellular processes. As the number of protein sequences increases, developing fast yet precise computational approaches to predict and annotate metal-binding sites becomes imperative. Quick and resource-efficient pre-trained protein language model (pLM) embeddings have successfully predicted binding sites from protein sequences despite not using structural or evolutionary features (multiple sequence alignments). Using residue-level embeddings from the pLMs, we have developed a sequence-based method (M-Ionic) to identify metal-binding proteins and predict residues involved in metal binding.

resultsOn independent validation of recent proteins, M-Ionic reports an area under the curve (AUROC) of 0.83 (recall = 84.6%) in distinguishing metal binding from non-binding proteins compared to AUROC of 0.74 (recall = 61.8%) of the next best method. In addition to comparable performance to the state-of-the-art method for identifying metal-binding residues (Ca2+, Mg2+, Mn2+, Zn2+), M-Ionic provides binding probabilities for six additional ions (i.e. Cu2+, Po43-, So42-, Fe2+, Fe3+, Co2+). We show that the pLM embedding of a single residue contains sufficient information about its neighbours to predict its binding properties. AVAILABILITY AND IMPLEMENTATION: M-Ionic can be used on your protein of interest using a Google Colab Notebook (https://bit.ly/40FrRbK). The GitHub repository (https://github.com/TeamSundar/m-ionic) contains all code and data.

Indexed as

MetalsProteinsAmino Acid SequenceBinding SitesIonsProtein DomainsIonsMetalsProteins

Identifiers

PMID38175787
PMCPMC10792727
OpenAlexW4390631588

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.