Evidence map›Paper›PMID 32383764›Full record

ArticleNucleic acids research2020

AWSEM-Suite: a protein structure prediction server based on template-guided, coevolutionary-enhanced optimized folding landscapes.

Shikai Jin, Vinicius G Contessoto, Mingchen Chen, Nicholas P Schafer, Wei Lu, Xun Chen, Carlos Bueno, Arya Hajitaheri, Brian J Sirovetz, Aram Davtyan and 3 more

Abstract read
In one paragraph

Article in Nucleic acids research, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.

0numbers the graph read from it
0cells of the map it votes in
12citing 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

12 citing papers in PubMed.

  1. State-of-the-Art and Future Directions in Structural Proteomics.Molecular & cellular proteomics : MCP · 2025
    Review
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  7. Computationally exploring the mechanism of bacteriophage T7 gp4 helicase translocating along ssDNA.Proceedings of the National Academy of Sciences of the United States of America · 2022
    Article
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  9. Review
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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

13 authors.

Shikai JinDepartment of Biosciences, Rice University, 6100 Main St, Houston, TX 77005, USA.
Vinicius G ContessotoCenter for Theoretical Biological Physics, Rice University, 6100 Main St, Houston, TX 77005, USA.
Mingchen ChenCenter for Theoretical Biological Physics, Rice University, 6100 Main St, Houston, TX 77005, USA.
Nicholas P SchaferCenter for Theoretical Biological Physics, Rice University, 6100 Main St, Houston, TX 77005, USA.
Wei LuCenter for Theoretical Biological Physics, Rice University, 6100 Main St, Houston, TX 77005, USA.
Xun ChenCenter for Theoretical Biological Physics, Rice University, 6100 Main St, Houston, TX 77005, USA.
Carlos BuenoCenter for Theoretical Biological Physics, Rice University, 6100 Main St, Houston, TX 77005, USA.
Arya HajitaheriDepartment of Computer Science, University of Houston, 4800 Calhoun Rd, Houston, TX 77004, USA.
Brian J SirovetzCenter for Theoretical Biological Physics, Rice University, 6100 Main St, Houston, TX 77005, USA.
Aram DavtyanCenter for Theoretical Biological Physics, Rice University, 6100 Main St, Houston, TX 77005, USA.
Garegin A PapoianDepartment of Chemistry, University of Maryland, College Park, MD 20742, USA.
Min-Yeh TsaiDepartment of Chemistry, Tamkang University, 151 Yingzhuan Road, New Taipei City 25137, Taiwan.
Peter G WolynesDepartment of Biosciences, Rice University, 6100 Main St, Houston, TX 77005, USA.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The accurate and reliable prediction of the 3D structures of proteins and their assemblies remains difficult even though the number of solved structures soars and prediction techniques improve. In this study, a free and open access web server, AWSEM-Suite, whose goal is to predict monomeric protein tertiary structures from sequence is described. The model underlying the server's predictions is a coarse-grained protein force field which has its roots in neural network ideas that has been optimized using energy landscape theory. Employing physically motivated potentials and knowledge-based local structure biasing terms, the addition of homologous template and co-evolutionary restraints to AWSEM-Suite greatly improves the predictive power of pure AWSEM structure prediction. From the independent evaluation metrics released in the CASP13 experiment, AWSEM-Suite proves to be a reasonably accurate algorithm for free modeling, standing at the eighth position in the free modeling category of CASP13. The AWSEM-Suite server also features a front end with a user-friendly interface. The AWSEM-Suite server is a powerful tool for predicting monomeric protein tertiary structures that is most useful when a suitable structure template is not available. The AWSEM-Suite server is freely available at: https://awsem.rice.edu.

Indexed as

Protein Structure, TertiarySoftwareAlgorithmsEvolution, MolecularProtein FoldingSequence Analysis, ProteinStructural Homology, Protein

Identifiers

PMID32383764
PMCPMC7319565

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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.