ArticleProtein science : a publication of the Protein Society2018
Functional and evolutionary analysis of viral proteins containing a Rossmann-like fold.
Article in Protein science : a publication of the Protein Society, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
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Who cites it
13 citing papers in PubMed, 22 citations in OpenAlex.
- Unveiling the structural and functional implications of uncharacterized NSPs and variations in the molecular toolkit across arteriviruses.NAR genomics and bioinformatics · 2025Article
- Ongoing shuffling of protein fragments diversifies core viral functions linked to interactions with bacterial hosts.Nature communications · 2023Article
- Insights into peculiar fungal LPMO family members holding a short C-terminal sequence reminiscent of phosphate binding motifs.Scientific reports · 2023Article
- Insertions and deletions mediated functional divergence of Rossmann fold enzymes.Proceedings of the National Academy of Sciences of the United States of America · 2022Article
- Methyltransferases ofBiomolecules · 2022Article
- Article
- Structure-function analysis of the nsp14 N7-guanine methyltransferase reveals an essential role inProceedings of the National Academy of Sciences of the United States of America · 2021Article
- A Fifth of the Protein World: Rossmann-like Proteins as an Evolutionarily Successful Structural unit.Journal of molecular biology · 2021Article
- Structural bioinformatic analysis of DsbA proteins and their pathogenicity associated substrates.Computational and structural biotechnology journal · 2021Review
- β-Strand-mediated interactions of protein domains.Proteins · 2020Article
- CaComputational and structural biotechnology journal · 2020Article
- Functional analysis of Rossmann-like domains reveals convergent evolution of topology and reaction pathways.PLoS computational biology · 2019Article
- The Urfold: Structural similarity just above the superfold level?Protein science : a publication of the Protein Society · 2019Article
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Authors and funding
3 authors at 2 institutions in 1 country.
Funding
Abstract
Viruses are the most abundant life form and infect practically all organisms. Consequently, these obligate parasites are a major cause of human suffering and economic loss. Rossmann-like fold is the most populated fold among α/β-folds in the Protein Data Bank and proteins containing Rossmann-like fold constitute 22% of all known proteins 3D structures. Thus, analysis of viral proteins containing Rossmann-like domains could provide an understanding of viral biology and evolution as well as could propose possible targets for antiviral therapy. We provide functional and evolutionary analysis of viral proteins containing a Rossmann-like fold found in the evolutionary classification of protein domains (ECOD) database developed in our lab. We identified 81 protein families of bacterial, archeal, and eukaryotic viruses in light of their evolution-based ECOD classification and Pfam taxonomy. We defined their functional significance using enzymatic EC number assignments as well as domain-level family annotations.
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Registered trials
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 Socratic graph.