ReviewToxins2018
Engineering Botulinum Toxins to Improve and Expand Targeting and SNARE Cleavage Activity.
Review in Toxins, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 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
25 citing papers in PubMed, 40 citations in OpenAlex.
- Characterisation of the SNAP-25 and SNAP-23 cleavage properties of the botulinum neurotoxin-like protein from Enterococcus.Journal of neural transmission (Vienna, Austria : 1996) · 2026Article
- Role of Microbial Toxins in Neurodegenerative Diseases: Insights and Future Perspectives.Biomolecules · 2026Review
- Article
- Probing the properties of PTEN specific botulinum toxin type E mutants.Journal of neural transmission (Vienna, Austria : 1996) · 2025Article
- Botulinum Neurotoxins: History, Mechanism, and Applications. A Narrative Review.Journal of neurochemistry · 2025Review
- Data-driven protease engineering by DNA-recording and epistasis-aware machine learning.Nature communications · 2025Article
- Botulinum Toxin Therapy: A Comprehensive Review on Clinical and Pharmacological Insights.Journal of clinical medicine · 2025Review
- Pioneering pain management with botulinum toxin type A: From anti-inflammation to regenerative therapies.Heliyon · 2025Review
- Embracing the Versatility of Botulinum Neurotoxins in Conventional and New Therapeutic Applications.Toxins · 2024Review
- Article
- Biological and Immunological Characterization of a Functional L-HN Derivative of Botulinum Neurotoxin Serotype F.Toxins · 2023Article
- Split luciferase-based assay to detect botulinum neurotoxins using hiPSC-derived motor neurons.Communications biology · 2023Article
- Review
- Molecular landscape of BoNT/B bound to a membrane-inserted synaptotagmin/ganglioside complex.Cellular and molecular life sciences : CMLS · 2022Article
- Reengineering the specificity of the highly selective Clostridium botulinum protease via directed evolution.Scientific reports · 2022Article
- Botulinum toxin in cancer therapy-current perspectives and limitations.Applied microbiology and biotechnology · 2022Review
- Botulinum Neurotoxins in Central Nervous System: An Overview from Animal Models to Human Therapy.Toxins · 2021Review
- Engineering Botulinum Neurotoxins for Enhanced Therapeutic Applications and Vaccine Development.Toxins · 2020Review
- Article
- Botulinum Toxin in the Treatment of Headache.Toxins · 2020Review
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
5 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Botulinum neurotoxins (BoNTs) are highly successful protein therapeutics. Over 40 naturally occurring BoNTs have been described thus far and, of those, only 2 are commercially available for clinical use. Different members of the BoNT family present different biological properties but share a similar multi-domain structure at the molecular level. In nature, BoNTs are encoded by DNA in producing clostridial bacteria and, as such, are amenable to recombinant production through insertion of the coding DNA into other bacterial species. This, in turn, creates possibilities for protein engineering. Here, we review the production of BoNTs by the natural host and also recombinant production approaches utilised in the field. Applications of recombinant BoNT-production include the generation of BoNT-derived domain fragments, the creation of novel BoNTs with improved performance and enhanced therapeutic potential, as well as the advancement of BoNT vaccines. In this article, we discuss site directed mutagenesis, used to affect the biological properties of BoNTs, including approaches to alter their binding to neurons and to alter the specificity and kinetics of substrate cleavage. We also discuss the target secretion inhibitor (TSI) platform, in which the neuronal binding domain of BoNTs is substituted with an alternative cellular ligand to re-target the toxins to non-neuronal systems. Understanding and harnessing the potential of the biological diversity of natural BoNTs, together with the ability to engineer novel mutations and further changes to the protein structure, will provide the basis for increasing the scope of future BoNT-based therapeutics.
Indexed as
Identifiers
What OpenQuestion holds
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.