ArticleParasites & vectors2014
Bioinformatic analysis of beta carbonic anhydrase sequences from protozoans and metazoans.
Article in Parasites & vectors, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.
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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.
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Who cites it
17 citing papers in PubMed, 41 citations in OpenAlex.
- Cloning, expression, and purification of an α-carbonic anhydrase fromJournal of enzyme inhibition and medicinal chemistry · 2024Article
- Biomimetic COEnvironmental science & technology · 2024Article
- Advances in the Development of Carbonic Anhydrase Inhibitors as New Antiprotozoal Agents.Current medicinal chemistry · 2024Review
- Potential Novel Role of Membrane-Associated Carbonic Anhydrases in the Kidney.International journal of molecular sciences · 2023Review
- Cloning, purification, kinetic and anion inhibition studies of a recombinant β-carbonic anhydrase from the Atlantic salmon parasite platyhelminthJournal of enzyme inhibition and medicinal chemistry · 2022Article
- A reverse vaccinology approach on transmembrane carbonic anhydrases from Plasmodium species as vaccine candidates for malaria prevention.Malaria journal · 2022Article
- Roles of Carbonic Anhydrases and Carbonic Anhydrase Related Proteins in Zebrafish.International journal of molecular sciences · 2022Review
- Emerging trends in environmental and industrial applications of marine carbonic anhydrase: a review.Bioprocess and biosystems engineering · 2022Review
- Application of beta and gamma carbonic anhydrase sequences as tools for identification of bacterial contamination in the whole genome sequence of inbred Wuzhishan minipig (Sus scrofa) annotated in databases.Database : the journal of biological databases and curation · 2021Article
- Phytochemicals as Modulators of Long Non-Coding RNAs and Inhibitors of Cancer-Related Carbonic Anhydrases.International journal of molecular sciences · 2019Review
- Involvement of β-Carbonic Anhydrase Genes in Bacterial Genomic Islands and Their Horizontal Transfer to Protists.Applied and environmental microbiology · 2018Article
- Horizontal transfer of β-carbonic anhydrase genes from prokaryotes to protozoans, insects, and nematodes.Parasites & vectors · 2016Article
- Innovative molecular diagnosis of Trichinella species based on β-carbonic anhydrase genomic sequence.Microbial biotechnology · 2016Article
- Carbonic Anhydrases in Cnidarians: Novel Perspectives from the Octocorallian Corallium rubrum.PloS one · 2016Article
- Ascaris lumbricoides β carbonic anhydrase: a potential target enzyme for treatment of ascariasis.Parasites & vectors · 2015Article
- β carbonic anhydrase is required for female fertility in Drosophila melanogaster.Frontiers in zoology · 2015Article
- Beta carbonic anhydrases: novel targets for pesticides and anti-parasitic agents in agriculture and livestock husbandry.Parasites & vectors · 2014Article
Corrections and comments
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Authors and funding
5 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
backgroundDespite the high prevalence of parasitic infections, and their impact on global health and economy, the number of drugs available to treat them is extremely limited. As a result, the potential consequences of large-scale resistance to any existing drugs are a major concern. A number of recent investigations have focused on the effects of potential chemical inhibitors on bacterial and fungal carbonic anhydrases. Among the five classes of carbonic anhydrases (alpha, beta, gamma, delta and zeta), beta carbonic anhydrases have been reported in most species of bacteria, yeasts, algae, plants, and particular invertebrates (nematodes and insects). To date, there has been a lack of knowledge on the expression and molecular structure of beta carbonic anhydrases in metazoan (nematodes and arthropods) and protozoan species.
methodsHere, the identification of novel beta carbonic anhydrases was based on the presence of the highly-conserved amino acid sequence patterns of the active site. A phylogenetic tree was constructed based on codon-aligned DNA sequences. Subcellular localization prediction for each identified invertebrate beta carbonic anhydrase was performed using the TargetP webserver.
resultsWe verified a total of 75 beta carbonic anhydrase sequences in metazoan and protozoan species by proteome-wide searches and multiple sequence alignment. Of these, 52 were novel, and contained highly conserved amino acid residues, which are inferred to form the active site in beta carbonic anhydrases. Mitochondrial targeting peptide analysis revealed that 31 enzymes are predicted with mitochondrial localization; one was predicted to be a secretory enzyme, and the other 43 were predicted to have other undefined cellular localizations.
conclusionsThese investigations identified 75 beta carbonic anhydrases in metazoan and protozoan species, and among them there were 52 novel sequences that were not previously annotated as beta carbonic anhydrases. Our results will not only change the current information in proteomics and genomics databases, but will also suggest novel targets for drugs against parasites.
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