ArticleNucleic acids research2003
Human RNase 7: a new cationic ribonuclease of the RNase A superfamily.
Article in Nucleic acids research, 2003. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 46 papers.
What it found
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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
46 citing papers in PubMed, 94 citations in OpenAlex.
- The howler monkey genome provides new insights into the distinctive howling and folivorous adaptations of New World monkeys.Genome biology · 2026Article
- Engineering human RNase 7 with an eosinophil RNase segment reveals determinants of cytotoxic and antimicrobial activity.The Journal of biological chemistry · 2026Article
- Pharmacophores of Influenza Virus PA Endonuclease Inhibitors.Advances in experimental medicine and biology · 2026Review
- The Contribution of Human Antimicrobial Peptides to Fungi.International journal of molecular sciences · 2025Review
- The making and breaking of tRNAs by ribonucleases.Trends in genetics : TIG · 2024Review
- Functional Insight into hTRIR.Current molecular medicine · 2024Article
- Review
- Antimicrobial Peptide Expression at the Ocular Surface and Their Therapeutic Use in the Treatment of Microbial Keratitis.Frontiers in microbiology · 2022Review
- Expression and function of human ribonuclease 4 in the kidney and urinary tract.American journal of physiology. Renal physiology · 2021Article
- Magnetite Nanoparticles Functionalized with RNases against Intracellular Infection ofPharmaceutics · 2020Article
- Functional roles of the human ribonuclease A superfamily in RNA metabolism and membrane receptor biology.Molecular aspects of medicine · 2019Review
- The Antimicrobial and Immunomodulatory Function of RNase 7 in Skin.Frontiers in immunology · 2019Review
- The Immunomodulatory and Antimicrobial Properties of the Vertebrate Ribonuclease A Superfamily.Vaccines · 2018Review
- A novel ligand-receptor relationship between families of ribonucleases and receptor tyrosine kinases.Journal of biomedical science · 2018Review
- Host Antimicrobial Peptides: The Promise of New Treatment Strategies against Tuberculosis.Frontiers in immunology · 2017Review
- Endogenous Antimicrobial Peptide Expression in Response to Bacterial Epidermal Colonization.Frontiers in immunology · 2017Review
- RNase 7 in Cutaneous Defense.International journal of molecular sciences · 2016Review
- A Review of Ribonuclease 7's Structure, Regulation, and Contributions to Host Defense.International journal of molecular sciences · 2016Review
- The role of antimicrobial peptides in chronic inflammatory skin diseases.Postepy dermatologii i alergologii · 2016Review
- Eosinophil-associated ribonuclease 11 is a macrophage chemoattractant.The Journal of biological chemistry · 2015Article
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
Here we report on the expression and function of RNase 7, one of the final RNase A superfamily ribonucleases identified in the human genome sequence. The human RNase 7 gene is expressed in various somatic tissues including the liver, kidney, skeletal muscle and heart. Recombinant RNase 7 is ribonucleolytically active against yeast tRNA, as expected from the presence of eight conserved cysteines and the catalytic histidine-lysine- histidine triad which are signature motifs of this superfamily. The protein is atypically cationic with an isoelectric point (pI) of 10.5. Expression of recombinant RNase 7 in Escherichia coli completely inhibits the growth of the host bacteria, similar to what has been observed for the cationic RNase, eosinophil cationic protein (ECP/RNase 3, pI 11.4). An in vitro assay demonstrates dose-dependent cytotoxicity of RNase 7 against bacteria E.coli, Pseudomonas aeruginosa and Staphylococcus aureus. While RNase 7 and ECP/RNase 3 are both cationic and share this particular aspect of functional similarity, their protein sequence identity is only 40%. Of particular interest, ECP/RNase 3's cationicity is based on an (over)abundance of arginine residues, whereas RNase 7 includes an excess of lysine. This difference, in conjunction with the independent origins and different expression patterns, suggests that RNase 7 and ECP/RNase 3 may have been recruited to target different pathogens in vivo, if their physiological functions are indeed host defenses.
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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 OpenQuestion graph.