Evidence map›Paper›PMID 32169820›Full record

ArticleiScience2020

MutaBind2: Predicting the Impacts of Single and Multiple Mutations on Protein-Protein Interactions.

Ning Zhang, Yuting Chen, Haoyu Lu, Feiyang Zhao, Roberto Vera Alvarez, Alexander Goncearenco, Anna R Panchenko, Minghui Li

Abstract read
In one paragraph

Article in iScience, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 117 papers.

0numbers the graph read from it
0cells of the map it votes in
117citing 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

117 citing papers in PubMed.

  1. Article
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  5. International journal of molecular sciences · 2026
    Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. An interpretable molecular framework for predicting cancer driver missense mutations.Proceedings of the National Academy of Sciences of the United States of America · 2026
    Article
  11. Article
  12. Multiscale Computational Dissection of CCRL2-Mediated Chemerin Presentation.Journal of chemical information and modeling · 2025
    Article
  13. Calmodulin Interaction Interface with Plasma Membrane CaInternational journal of molecular sciences · 2025
    Article
  14. Article
  15. Article
  16. Journal of chemical information and modeling · 2025
    Article
  17. Article
  18. Article
  19. Article
  20. FLI1 and GATA1 governHaematologica · 2025
    Article

57 more citing papers are in PubMed but not listed here.

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

8 authors.

Ning ZhangCenter for Systems Biology, Department of Bioinformatics, School of Biology and Basic Medical Sciences, Soochow University, Suzhou 215123, China.
Yuting ChenCenter for Systems Biology, Department of Bioinformatics, School of Biology and Basic Medical Sciences, Soochow University, Suzhou 215123, China.
Haoyu LuCenter for Systems Biology, Department of Bioinformatics, School of Biology and Basic Medical Sciences, Soochow University, Suzhou 215123, China.
Feiyang ZhaoCenter for Systems Biology, Department of Bioinformatics, School of Biology and Basic Medical Sciences, Soochow University, Suzhou 215123, China.
Roberto Vera AlvarezNational Center for Biotechnology Information, National Institutes of Health, Bethesda, MD 20894, USA.
Alexander GoncearencoNational Center for Biotechnology Information, National Institutes of Health, Bethesda, MD 20894, USA.
Anna R PanchenkoNational Center for Biotechnology Information, National Institutes of Health, Bethesda, MD 20894, USA. Electronic address: panch@ncbi.nlm.nih.gov.
Minghui LiCenter for Systems Biology, Department of Bioinformatics, School of Biology and Basic Medical Sciences, Soochow University, Suzhou 215123, China. Electronic address: minghui.li@suda.edu.cn.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Missense mutations may affect proteostasis by destabilizing or over-stabilizing protein complexes and changing the pathway flux. Predicting the effects of stabilizing mutations on protein-protein interactions is notoriously difficult because existing experimental sets are skewed toward mutations reducing protein-protein binding affinity and many computational methods fail to correctly evaluate their effects. To address this issue, we developed a method MutaBind2, which estimates the impacts of single as well as multiple mutations on protein-protein interactions. MutaBind2 employs only seven features, and the most important of them describe interactions of proteins with the solvent, evolutionary conservation of the site, and thermodynamic stability of the complex and each monomer. This approach shows a distinct improvement especially in evaluating the effects of mutations increasing binding affinity. MutaBind2 can be used for finding disease driver mutations, designing stable protein complexes, and discovering new protein-protein interaction inhibitors.

Indexed as

3D Reconstruction of ProteinBioinformaticsProtein Folding

Identifiers

PMID32169820
PMCPMC7068639

What OpenQuestion holds

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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.