ArticleNucleic acids research2007
Molecular cloning and characterization of the human RNase kappa, an ortholog of Cc RNase.
Article in Nucleic acids research, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.
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Who cites it
14 citing papers in PubMed, 21 citations in OpenAlex.
- RNAseK is vital for epithelial function in Drosophila melanogaster.The Journal of experimental biology · 2026Article
- Article
- RNASEK interacting with PEDV structural proteins facilitates virus entry via clathrin-mediated endocytosis.Journal of virology · 2025Article
- The V-ATPase complex component RNAseK is required for lysosomal hydrolase delivery and autophagosome degradation.Nature communications · 2024Article
- Article
- RNase κ promotes robust piRNA production by generating 2',3'-cyclic phosphate-containing precursors.Nature communications · 2021Article
- Fish Paralog Proteins RNASEK-a and -b Enhance Type I Interferon Secretion and Promote Apoptosis.Frontiers in immunology · 2021Article
- Structure of V-ATPase from the mammalian brain.Science (New York, N.Y.) · 2020Article
- Expressional profiling and clinical relevance of RNase κ in prostate cancer: a novel indicator of favorable progression-free survival.Journal of cancer research and clinical oncology · 2018Article
- Cell fusing agent virus and dengue virus mutually interact in Aedes aegypti cell lines.Scientific reports · 2017Article
- Article
- RNASEK is required for internalization of diverse acid-dependent viruses.Proceedings of the National Academy of Sciences of the United States of America · 2015Article
- A machine learning heuristic to identify biologically relevant and minimal biomarker panels from omics data.BMC genomics · 2015Article
- A subtle alternative splicing event gives rise to a widely expressed human RNase k isoform.PloS one · 2014Article
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
A novel protein family, designated hereafter as RNase kappa (kappa) family, has been recently introduced with the characterization of the specific Cc RNase, isolated from the insect Ceratitis capitata. The human ortholog of this family consists of 98 amino acids and shares > 98% identity with its mammalian counterparts. This RNase is encoded by a single-copy gene found to be expressed in a wide spectrum of normal and cancer tissues. The cDNA of the human ribonuclease has been isolated and subcloned into a variety of prokaryotic expression vectors, but most efforts to express it caused a severe toxic effect. On the other hand, the expression of the human RNase by the use of the methylotrophic yeast Pichia pastoris system resulted in the production of a highly active recombinant enzyme. Using a 30-mer 5'-end-labeled RNA probe as substrate, the purified enzyme seems to preferentially cleave ApU and ApG phosphodiester bonds, while it hydrolyzes UpU bonds at a lower rate. Based on amino acid sequence alignment and substrate specificity data, as well as the complete resistance of the recombinant protein to the placental ribonuclease inhibitor, we concluded that the human RNase kappa is a novel endoribonuclease distinct from other known ribonucleases.
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