ArticleFrontiers in molecular biosciences2021
Evidence for the Rapid and Divergent Evolution of Mycoplasmas: Structural and Phylogenetic Analysis of Enolases.
Article in Frontiers in molecular biosciences, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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Who cites it
8 citing papers in PubMed, 15 citations in OpenAlex.
- mRNA-Encoded antibodies as a next-generation therapeutic paradigm: a rapid and adaptive platform for the prevention and treatment of emerging and re-emerging infectious diseases - A critical review.Immunologic research · 2026Review
- Oleum cinnamomi disruptsFrontiers in microbiology · 2026Article
- A novel quantitative double antigen sandwich ELISA for detecting total antibodies against Candida albicans enolase 1.European journal of clinical microbiology & infectious diseases : official publication of the European Society of Clinical Microbiology · 2024Article
- KAT2A changes the function of endometrial stromal cells via regulating the succinylation of ENO1.Open life sciences · 2024Article
- Host Species and Environment Shape the Gut Microbiota of Cohabiting Marine Bivalves.Microbial ecology · 2023Article
- Transcriptomic Profiling ofJournal of fungi (Basel, Switzerland) · 2023Article
- An alternative vaccine target for bovine Anaplasmosis based on enolase, a moonlighting protein.Frontiers in veterinary science · 2023Article
- Mycoplasmas as Host Pantropic and Specific Pathogens: Clinical Implications, Gene Transfer, Virulence Factors, and Future Perspectives.Frontiers in cellular and infection microbiology · 2022Review
Corrections and comments
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Authors and funding
17 authors at 3 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Mycoplasmas are a group of prokaryotes without cell walls that have evolved through several rounds of degenerative evolution. With a low cell DNA G + C content and definitively long genetic lineages, mycoplasmas are thought to be in a state of rapid evolution. However, little associated evidence has been provided. Enolase is a key enzyme in glycolysis that is widely found in all species from the three domains, and it is evolutionarily conserved. In our previous studies, enolase acted as a virulence factor and participated in cell-surface adhesion in
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