ArticleCommunications chemistry2024
Activity of botulinum neurotoxin X and its structure when shielded by a non-toxic non-hemagglutinin protein.
Article in Communications chemistry, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers, 1 of them a synthesis that pooled it.
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
11 citing papers in PubMed, 1 synthesis or guideline pooled it.
- Current Strategies in the Development of Nanoformulations to Enhance the Stability of Botox: A Systematic Review.AAPS PharmSciTech · 2025Pooled it
- Evolution of botulinum neurotoxin serotype X proteases to induce inflammatory cell death in cancer cells.Nature biotechnology · 2026Article
- Design and Characterization of Recombinant and Chimeric BoNT/A Neurotoxins with Receptor-Binding Domain Grafting.Toxins · 2026Article
- From Gut to Systemic Circulation: Molecular Strategies of Botulinum Neurotoxin Complexes.Toxins · 2026Review
- Identification and characterization of botulinum neurotoxin-like two-component toxins inScience advances · 2025Article
- Structure of the complete 14-subunit botulinum neurotoxin B complex reveals a unique anchoring through the narrow central pore of HA70.Science advances · 2025Article
- A nut-and-bolt assembly of the bimodular large progenitor botulinum neurotoxin complex.Science advances · 2025Article
- Review of Foodborne Botulism in the UK: 2006-2024.Foods (Basel, Switzerland) · 2025Review
- Botulinum Toxin Therapy: A Comprehensive Review on Clinical and Pharmacological Insights.Journal of clinical medicine · 2025Review
- Cryo-EM structure of the botulinum neurotoxin A/SV2B complex and its implications for translocation.Nature communications · 2025Article
- Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
17 authors.
Funding
Abstract
Botulinum neurotoxins (BoNTs) are the most potent toxins known and are used to treat an increasing number of medical disorders. All BoNTs are naturally co-expressed with a protective partner protein (NTNH) with which they form a 300 kDa complex, to resist acidic and proteolytic attack from the digestive tract. We have previously identified a new botulinum neurotoxin serotype, BoNT/X, that has unique and therapeutically attractive properties. We present the cryo-EM structure of the BoNT/X-NTNH/X complex and the crystal structure of the isolated NTNH protein. Unexpectedly, the BoNT/X complex is stable and protease-resistant at both neutral and acidic pH and disassembles only in alkaline conditions. Using the stabilizing effect of NTNH, we isolated BoNT/X and showed that it has very low potency both in vitro and in vivo. Given the high catalytic activity and translocation efficacy of BoNT/X, low activity of the full toxin is likely due to the receptor-binding domain, which presents very weak ganglioside binding and exposed hydrophobic surfaces.
Identifiers
What Socratic 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 Socratic graph.