Evidence map›Paper›PMID 36918581›Full record

ArticleScientific data2023

SARS-CoV-2 receptor-binding domain deep mutational AlphaFold2 structures.

Oz Kilim, Anikó Mentes, Balázs Pál, István Csabai, Ákos Gellért

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In one paragraph

Article in Scientific data, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.

0numbers the graph read from it
0cells of the map it votes in
6citing 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

6 citing papers in PubMed.

  1. Review
  2. Article
  3. Review
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  6. Review
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

5 authors.

Oz KilimDepartment of Physics of Complex Systems, Eötvös Loránd University, Budapest, Hungary.ORCID 0000-0003-3457-2739
Anikó MentesDepartment of Physics of Complex Systems, Eötvös Loránd University, Budapest, Hungary.ORCID 0000-0001-9559-374X
Balázs PálDepartment of Physics of Complex Systems, Eötvös Loránd University, Budapest, Hungary.ORCID 0000-0001-9399-390X
István CsabaiDepartment of Physics of Complex Systems, Eötvös Loránd University, Budapest, Hungary.ORCID 0000-0001-9232-9898
Ákos GellértDepartment of Physics of Complex Systems, Eötvös Loránd University, Budapest, Hungary. gellert.akos@gmail.com.ORCID 0000-0002-1455-8879

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Leveraging recent advances in computational modeling of proteins with AlphaFold2 (AF2) we provide a complete curated data set of all single mutations from each of the 7 main SARS-CoV-2 lineages spike protein receptor binding domain (RBD) resulting in 3819X7 = 26733 PDB structures. We visualize the generated structures and show that AF2 pLDDT values are correlated with state-of-the-art disorder approximations, implying some internal protein dynamics are also captured by the model. Joint increasing mutational coverage of both structural and phenotype data coupled with advances in machine learning can be leveraged to accelerate virology research, specifically future variant prediction. We hope this data release can offer assistance into further understanding of the local and global mutational landscape of SARS-CoV-2 as well as provide insight into the biological understanding that 3D structure acts as a bridge between protein genotype and phenotype.

Indexed as

COVID-19SARS-CoV-2Computer SimulationFurylfuramideHumansMutationFurylfuramide

Identifiers

PMID36918581
PMCPMC10013278

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Registered trials

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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.