Evidence map›Paper›PMID 35639953›Full record

ArticleBioinformatics (Oxford, England)2022

mebipred: identifying metal-binding potential in protein sequence.

A A Aptekmann, J Buongiorno, D Giovannelli, M Glamoclija, D U Ferreiro, Y Bromberg

Open access · hybridAbstract read
In one paragraph

Article in Bioinformatics (Oxford, England), 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.

0numbers the graph read from it
0cells of the map it votes in
16citing papers in PubMed
5.2field-weighted citation impact, top 3% 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

16 citing papers in PubMed, 48 citations in OpenAlex.

  1. Article
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  4. Bioinformatic study of copper-associated proteins of bread wheat.Biometals : an international journal on the role of metal ions in biology, biochemistry, and medicine · 2026
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  7. Interpretable prediction of zinc ion location in proteins with ZincSight.Protein science : a publication of the Protein Society · 2025
    Article
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  10. Polymorphism rs259983 of theThe Egyptian journal of medical human genetics · 2025
    Article
  11. MgbioRxiv : the preprint server for biology · 2024
    Article
  12. Review
  13. Article
  14. 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

6 authors at 3 institutions in 3 countries.

A A AptekmannDepartment of Biochemistry and Microbiology, Rutgers University, New Brunswick, NJ 08873, USA.ORCID 0000-0001-8822-4372
J BuongiornoDivision of Natural Sciences, Maryville College, Maryville, TN 37804, USA.
D GiovannelliInstitute of Marine and Coastal Sciences, Rutgers University, New Brunswick, NJ 08901, USA.
M GlamoclijaDepartment of Earth and Environmental Sciences, Rutgers University, Newark, NJ 07102, USA.
D U FerreiroProtein Physiology Lab, Departamento de Quimica Biologica, Facultad de Ciencias Exactas y Naturales, Universidad de Buenos Aires-CONICET-IQUIBICEN, 1428 Buenos Aires, Argentina.
Y BrombergDepartment of Biochemistry and Microbiology, Rutgers University, New Brunswick, NJ 08873, USA.ORCID 0000-0002-8351-0844
Rutgers, The State University of New Jersey · USConsejo Nacional de Investigaciones Científicas y Técnicas · ARMaryville College · US

Funding

AVA,Dx: Analysis of Variation for Association with DiseaseR01GM115486 · NIGMS · RUTGERS, THE STATE UNIV OF N.J. · PI BROMBERG, YANA · 2019 to 2019
$306k
Astrobiology Institute 80NSSC18M0093European Research CouncilEuropean Union's Horizon 2020 948972NASANational Science FoundationNational Scientific and Technical Research CouncilNIGMS NIH HHS R01 GM115486NSF 1553289
6 · The paper itself

Abstract

motivationmetal-binding proteins have a central role in maintaining life processes. Nearly one-third of known protein structures contain metal ions that are used for a variety of needs, such as catalysis, DNA/RNA binding, protein structure stability, etc. Identifying metal-binding proteins is thus crucial for understanding the mechanisms of cellular activity. However, experimental annotation of protein metal-binding potential is severely lacking, while computational techniques are often imprecise and of limited applicability.

resultswe developed a novel machine learning-based method, mebipred, for identifying metal-binding proteins from sequence-derived features. This method is over 80% accurate in recognizing proteins that bind metal ion-containing ligands; the specific identity of 11 ubiquitously present metal ions can also be annotated. mebipred is reference-free, i.e. no sequence alignments are involved, and is thus faster than alignment-based methods; it is also more accurate than other sequence-based prediction methods. Additionally, mebipred can identify protein metal-binding capabilities from short sequence stretches, e.g. translated sequencing reads, and, thus, may be useful for the annotation of metal requirements of metagenomic samples. We performed an analysis of available microbiome data and found that ocean, hot spring sediments and soil microbiomes use a more diverse set of metals than human host-related ones. For human microbiomes, physiological conditions explain the observed metal preferences. Similarly, subtle changes in ocean sample ion concentration affect the abundance of relevant metal-binding proteins. These results highlight mebipred's utility in analyzing microbiome metal requirements. AVAILABILITY AND IMPLEMENTATION: mebipred is available as a web server at services.bromberglab.org/mebipred and as a standalone package at https://pypi.org/project/mymetal/. SUPPLEMENTARY INFORMATION: Supplementary data are available at Bioinformatics online.

Indexed as

MetalsProteinsAmino Acid SequenceHumansIonsProtein BindingSequence AlignmentIonsMetalsProteins

Identifiers

PMID35639953
PMCPMC9272798
OpenAlexW4281750795

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.