ReviewCurrent pharmaceutical biotechnology2008
Onconase and amphinase, the antitumor ribonucleases from Rana pipiens oocytes.
Review in Current pharmaceutical biotechnology, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 35 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.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
35 citing papers in PubMed, 102 citations in OpenAlex.
- Stalled translation on transcripts cleaved by RNase L activates signaling important for innate immunity.RNA (New York, N.Y.) · 2026Article
- Onconase Induces Apoptosis in Dabrafenib-Resistant Melanoma Cell Lines Through Dysregulation of ROS Homeostasis, Antioxidant Protein Expression, and Mitochondrial Dynamics.International journal of molecular sciences · 2026Article
- Stalled translation on transcripts cleaved by RNase L activates signaling important for innate immunity.bioRxiv : the preprint server for biology · 2025Article
- Engineering Human Pancreatic RNase 1 as an Immunotherapeutic Agent for Cancer Therapy Through Computational and Experimental Studies.The protein journal · 2024Article
- Role of the Ribonuclease ONCONASE in miRNA Biogenesis and tRNA Processing: Focus on Cancer and Viral Infections.International journal of molecular sciences · 2022Review
- Recombinant immunotoxins development for HER2-based targeted cancer therapies.Cancer cell international · 2021Review
- Strengths and Challenges of Secretory Ribonucleases as AntiTumor Agents.Pharmaceutics · 2021Review
- The Cytotoxicity of RNase-Derived Peptides.Biomolecules · 2020Article
- An ancient evolutionary connection between Ribonuclease A and EndoU families.RNA (New York, N.Y.) · 2020Article
- Onconase Restores Cytotoxicity in Dabrafenib-Resistant A375 Human Melanoma Cells and Affects Cell Migration, Invasion and Colony Formation Capability.International journal of molecular sciences · 2019Article
- Biological Activities of Secretory RNases: Focus on Their Oligomerization to Design Antitumor Drugs.Frontiers in immunology · 2019Review
- Evolutionary Trends in RNA Base Selectivity Within the RNase A Superfamily.Frontiers in pharmacology · 2019Article
- The Immunomodulatory and Antimicrobial Properties of the Vertebrate Ribonuclease A Superfamily.Vaccines · 2018Review
- Updates in the Development of ImmunoRNases for the Selective Killing of Tumor Cells.Biomedicines · 2018Review
- Activating transcription factor 3 is crucial for antitumor activity and to strengthen the antiviral properties of Onconase.Oncotarget · 2017Article
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- Site-specific RNase A activity was dramatically reduced in serum from multiple types of cancer patients.PloS one · 2014Article
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- Regulation of cell death by transfer RNA.Antioxidants & redox signaling · 2013Review
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
Rana pipiens oocytes contain two homologues of pancreatic ribonuclease A that are cytostatic and cytotoxic to human cancer cells. Extensively studied Onconase is in advanced Phase IIIb clinical trials against malignant mesothelioma, while Amphinase is a novel enzyme in pre-clinical development. Onconase is the smallest (104 amino acid residues) member of the ribonuclease A superfamily while Amphinase (114 residues) is the largest among amphibian ribonucleases. Both enzymes share the characteristic frog ribonucleases C-terminal disulfide bond but another signature of this group, the N-terminal pyroglutamate, an integral part of Onconase active site is not conserved in Amphinase. Although Onconase and Amphinase are weak catalysts their enzymatic activities are required for cytostatic and cytotoxic activity. While it was postulated that tRNA is the primary substrate of Onconase in vivo there is also extensive indirect evidence that suggests other RNA species, in particular micro RNAs, may actually be the critical target of these ribonucleases. The cytostatic effects of Onconase and Amphinase are manifested as cell arrest in the G(1) cell cycle phase. Apoptosis then follows involving activation of endonucleases(s), caspases, serine proteases and transglutaminase. Onconase was shown to be strongly synergistic when combined with numerous other antitumor modalities. Onconase and Amphinase are highly cationic molecules and their preferential toxicity towards cancer cells (having distinctly higher negative charge compared to normal cells) may depend on increased binding efficiency to the cell surface by electrostatic interactions.
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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.