Evidence map›Paper›PMID 32272725›Full record

ArticleInternational journal of molecular sciences2020

SAAMBE-3D: Predicting Effect of Mutations on Protein-Protein Interactions.

Swagata Pahari, Gen Li, Adithya Krishna Murthy, Siqi Liang, Robert Fragoza, Haiyuan Yu, Emil Alexov

Open access · goldAbstract read
In one paragraph

Article in International journal of molecular sciences, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 61 papers.

0numbers the graph read from it
0cells of the map it votes in
61citing papers in PubMed
6.0field-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

61 citing papers in PubMed, 124 citations in OpenAlex.

  1. Article
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  9. Mapping the interaction surface between CaNature communications · 2025
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  11. Review
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  19. MuToN Quantifies Binding Affinity Changes upon Protein Mutations by Geometric Deep Learning.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2024
    Article
  20. Article

1 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

7 authors at 2 institutions in 1 country.

Swagata PahariDepartment of Physics and Astronomy, Clemson University, Clemson, SC 29634, USA.
Gen LiDepartment of Physics and Astronomy, Clemson University, Clemson, SC 29634, USA.ORCID 0000-0002-6862-5547
Adithya Krishna MurthyDepartment of Physics and Astronomy, Clemson University, Clemson, SC 29634, USA.
Siqi LiangDepartment of Computational Biology, Cornell University, Ithaca, NY 14850, USA.ORCID 0000-0002-6433-5964
Robert FragozaDepartment of Computational Biology, Cornell University, Ithaca, NY 14850, USA.
Haiyuan YuDepartment of Computational Biology, Cornell University, Ithaca, NY 14850, USA.
Emil AlexovDepartment of Physics and Astronomy, Clemson University, Clemson, SC 29634, USA.ORCID 0000-0001-5346-0156
Clemson University · USCornell University · US

Funding

Tissue Structural and Neural Remodeling in Human Sacroiliac JointP20GM121342 · NIGMS · CLEMSON UNIVERSITY · PI Hai Yao · 2018 to 2026
$24.7M
New Generation DelPhi: large systems and beyond electrostaticsR01GM093937 · NIGMS · CLEMSON UNIVERSITY · PI ALEXOV, EMIL GEORGIEV · 2010 to 2023
$4.3M
Quantifying molecular consequences of human missense variants with large-scale interactome perturbation studiesR01GM125639 · NIGMS · CORNELL UNIVERSITY · PI ALEXOV, EMIL GEORGIEV, CLARK, ANDREW G · 2018 to 2021
$2.6M
NIGMS NIH HHS P20 GM121342NIGMS NIH HHS R01 GM093937NIGMS NIH HHS R01 GM125639NIH HHS P20GM121342NIH HHS R01GM093937NIH HHS R01GM125639
6 · The paper itself

Abstract

Maintaining wild type protein-protein interactions is essential for the normal function of cell and any mutation that alter their characteristics can cause disease. Therefore, the ability to correctly and quickly predict the effect of amino acid mutations is crucial for understanding disease effects and to be able to carry out genome-wide studies. Here, we report a new development of the SAAMBE method, SAAMBE-3D, which is a machine learning-based approach, resulting in accurate predictions and is extremely fast. It achieves the Pearson correlation coefficient ranging from 0.78 to 0.82 depending on the training protocol in benchmarking five-fold validation test against the SKEMPI v2.0 database and outperforms currently existing algorithms on various blind-tests. Furthermore, optimized and tested via five-fold cross-validation on the Cornell University dataset, the SAAMBE-3D achieves AUC of 1.0 and 0.96 on a homo and hereto-dimer test datasets. Another important feature of SAAMBE-3D is that it is very fast, it takes less than a fraction of a second to complete a prediction. SAAMBE-3D is available as a web server and as well as a stand-alone code, the last one being another important feature allowing other researchers to directly download the code and run it on their local computer. Combined all together, SAAMBE-3D is an accurate and fast software applicable for genome-wide studies to assess the effect of amino acid mutations on protein-protein interactions. The webserver and the stand-alone codes (SAAMBE-3D for predicting the change of binding free energy and SAAMBE-3D-DN for predicting if the mutation is disruptive or non-disruptive) are available.

Indexed as

AlgorithmsAmino AcidsGenome-Wide Association StudyHumansMachine LearningMutationProtein BindingProtein Interaction MapsProteinsSoftwareAmino AcidsProteinsdisruptive and non-disruptive mutationmachine learningprotein–protein bindingstabilizing and destabilizing mutation

Identifiers

PMID32272725
PMCPMC7177817
OpenAlexW3015602557

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.