ReviewToxicon : official journal of the International Society on Toxinology2013
Targeting ricin to the ribosome.
Review in Toxicon : official journal of the International Society on Toxinology, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 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
22 citing papers in PubMed.
- Ricin as a Biothreat Agent: From Molecular Mechanisms to Clinical Toxicology, Forensic Aspects, and Risk Mitigation.BioMed research international · 2026Review
- Legume lectin phytohemagglutinin reduces transepithelial electrical resistance by counteracting the chaperone function of heat shock protein-70.Journal of nutritional science · 2025Article
- Improving the cytotoxicity of immunotoxins by reducing the affinity of the antibody in acidic pH.Journal of translational medicine · 2023Article
- Bacterial Toxin-Antitoxin Systems' Cross-Interactions-Implications for Practical Use in Medicine and Biotechnology.Toxins · 2023Review
- Thermochemical and Quantum Descriptor Calculations for Gaining Insight into Ricin Toxin A (RTA) Inhibitors.ACS omega · 2021Article
- The role of enzymatic activities of antiviral proteins from plants for action against plant pathogens.3 Biotech · 2020Review
- Structural basis for the interaction of Shiga toxin 2a with a C-terminal peptide of ribosomal P stalk proteins.The Journal of biological chemistry · 2020Article
- Mayahuelin, a Type I Ribosome Inactivating Protein: Characterization, Evolution, and Utilization in Phylogenetic Analyses ofFrontiers in plant science · 2020Article
- Leucine 232 and hydrophobic residues at the ribosomal P stalk binding site are critical for biological activity of ricin.Bioscience reports · 2019Article
- Amino acid-linked platinum(II) compounds: non-canonical nucleoside preferences and influence on glycosidic bond stabilities.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2019Article
- Multiple metabolic pathways are predictive of ricin intoxication in a rat model.Metabolomics : Official journal of the Metabolomic Society · 2019Article
- Review
- Inhibition of ricin A-chain (RTA) catalytic activity by a viral genome-linked protein (VPg).Biochimica et biophysica acta. Proteins and proteomics · 2019Article
- Article
- Biological Toxins as the Potential Tools for Bioterrorism.International journal of molecular sciences · 2019Review
- Article
- Structures and Ribosomal Interaction of Ribosome-Inactivating Proteins.Molecules (Basel, Switzerland) · 2016Review
- Modeling of toxin-antibody interaction and toxin transport toward the endoplasmic reticulum.Journal of biological physics · 2016Article
- Do the A subunits contribute to the differences in the toxicity of Shiga toxin 1 and Shiga toxin 2?Toxins · 2015Review
- Review
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.
Funding
Abstract
The plant toxin ricin is highly toxic for mammalian cells and is of concern for bioterrorism. Ricin belongs to a family of functionally related toxins, collectively referred to as ribosome inactivating proteins (RIPs), which disable ribosomes and halt protein synthesis. Currently there are no specific antidotes against ricin or related RIPs. The catalytic subunit of ricin is an N-glycosidase that depurinates a universally conserved adenine residue within the sarcin/ricin loop (SRL) of the 28S rRNA. This depurination activity inhibits translation and its biochemistry has been intensively studied. Yet, recent developments paint a more complex picture of toxicity, with ribosomal proteins and cellular signaling pathways contributing to the potency of ricin. In particular, several studies have now established the importance of the ribosomal stalk structure in facilitating the depurination activity and ribosome specificity of ricin and other RIPs. This review highlights recent developments defining toxin-ribosome interactions and examines the significance of these interactions for toxicity and therapeutic intervention.
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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.