ReviewMicrobial biotechnology2011
Shiga toxin and its use in targeted cancer therapy and imaging.
Review in Microbial biotechnology, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 51 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
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
51 citing papers in PubMed, 116 citations in OpenAlex.
- From molecular mechanisms of glycosphingolipid function to bio-therapeutic applications.Cellular and molecular life sciences : CMLS · 2026Review
- Bacterial small molecule metabolites implicated in gastrointestinal cancer development.Nature reviews. Microbiology · 2025Review
- Shiga Toxin: Emerging Producer Strains, Prophylactic Approaches, and Application in Cancer Therapy.Journal of cancer prevention · 2024Review
- Recent Advances in Biomimetic Nanocarrier-Based Photothermal Therapy for Cancer Treatment.International journal of molecular sciences · 2023Review
- A Shiga Toxin B-Subunit-Based Lectibody Boosts T Cell Cytotoxicity towards Gb3-Positive Cancer Cells.Cells · 2023Article
- AB Toxins as High-Affinity Ligands for Cell Targeting in Cancer Therapy.International journal of molecular sciences · 2023Review
- Expression, purification, characterization, and cytotoxic evaluation of the ML1-STxB fusion protein.Archives of microbiology · 2023Article
- Novel lectin-based chimeric antigen receptors target Gb3-positive tumour cells.Cellular and molecular life sciences : CMLS · 2022Article
- Targeting Nanomaterials to Head and Neck Cancer Cells Using a Fragment of the Shiga Toxin as a Potent Natural Ligand.Cancers · 2021Article
- Shiga Toxins as Antitumor Tools.Toxins · 2021Review
- The Cellular and Chemical Biology of Endocytic Trafficking and Intracellular Delivery-The GL-Lect Hypothesis.Molecules (Basel, Switzerland) · 2021Review
- Review
- Natural and Designed Toxins for Precise Therapy: Modern Approaches in Experimental Oncology.International journal of molecular sciences · 2021Review
- Review
- Cancer trigger or remedy: two faces of the human microbiome.Applied microbiology and biotechnology · 2021Review
- Lectin-Mediated Binding of EngineeredMicroorganisms · 2021Article
- Deciphering the Importance of Glycosphingolipids on Cellular and Molecular Mechanisms Associated with Epithelial-to-Mesenchymal Transition in Cancer.Biomolecules · 2021Review
- Structural Diversities of Lectins Binding to the Glycosphingolipid Gb3.Frontiers in molecular biosciences · 2021Review
- Shiga-Like Toxin Produced by Local Isolates ofBreast cancer : basic and clinical research · 2021Article
- The interaction between flagellin and the glycosphingolipid Gb3 on host cells contributes toVirulence · 2020Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
4 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Shiga and the Shiga-like toxins are related protein toxins produced by Shigella dysenteriae and certain strains of Escherichia coli. These toxins are composed of two non-covalently attached, modular parts: the A moiety (StxA) containing the enzymatically active A1 fragment, and the non-toxic, pentameric binding moiety (StxB). Stx binds specifically to the glycosphingolipid globotriaosylceramide (Gb3) at the surface of target cells and is then internalized by endocytosis. Subsequently, in toxin-sensitive cells, the Stx/Gb3 complex is transported in a retrograde manner via the Golgi apparatus to the endoplasmic reticulum, where the enzymatically active part of Stx is translocated to the cytosol, enabling it to irreversibly inhibit protein synthesis via modification of ribosomal 28S RNA. Whereas Gb3 shows a relatively restricted expression in normal human tissues, it has been reported to be highly expressed in many types of cancers. This review gives a brief introduction to Stx and its intracellular transport. Furthermore, after a description of Gb3 and the methods that are currently used to detect its cellular expression, we provide an updated overview of the published reports on Gb3 overexpression in human cancers. Finally, we discuss the possibility of utilizing Stx or StxB coupled to therapeutic compounds or contrast agents in targeted cancer therapy and imaging.
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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.