ArticleJournal of molecular biology2014
Structural basis of the pH-dependent assembly of a botulinum neurotoxin complex.
Article in Journal of molecular biology, 2014. 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
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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.
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Who cites it
25 citing papers in PubMed, 32 citations in OpenAlex.
- From Gut to Systemic Circulation: Molecular Strategies of Botulinum Neurotoxin Complexes.Toxins · 2026Review
- Infectious bacteria as biological warfare agents: mechanisms, epidemiological threats, and defense strategies.Frontiers in bioengineering and biotechnology · 2026Review
- Elucidating the activation mechanism of botulinum neurotoxin a: role of α-clostripain and NTNH.Scientific reports · 2025Article
- Complexing Protein-Free Botulinum Neurotoxin A Formulations: Implications of Excipients for Immunogenicity.Toxins · 2024Review
- NTNH protein: more than a bodyguard for botulinum neurotoxins.The FEBS journal · 2024Article
- In Silico Conformational Features of Botulinum Toxins A1 and E1 According to Intraluminal Acidification.Toxins · 2022Article
- Dynamic muscle paralytic effects of a novel botulinum toxin A free of neurotoxin-associated proteins.Pharmacology research & perspectives · 2022Article
- Posttranslational Regulation of Botulinum Neurotoxin Production in Clostridium botulinum Hall A-mSphere · 2021Article
- A viral-fusion-peptide-like molecular switch drives membrane insertion of botulinum neurotoxin A1.Nature communications · 2018Article
- Intrinsic disorder in the regulatory N-terminal domain of diacylglycerol acyltransferase 1 from Brassica napus.Scientific reports · 2018Article
- α-Catenin Structure and Nanoscale Dynamics in Solution and in Complex with F-Actin.Biophysical journal · 2018Article
- The hypothetical protein P47 of Clostridium botulinum E1 strain Beluga has a structural topology similar to bactericidal/permeability-increasing protein.Toxicon : official journal of the International Society on Toxinology · 2018Article
- Purification and Characterization of Recombinant Botulinum Neurotoxin Serotype FA, Also Known as Serotype H.Toxins · 2018Article
- Dynamic intramolecular regulation of the histone chaperone nucleoplasmin controls histone binding and release.Nature communications · 2017Article
- Reversible Association of the Hemagglutinin Subcomplex, HA-33/HA-17 Trimer, with the Botulinum Toxin Complex.The protein journal · 2017Article
- The structure of the tetanus toxin reveals pH-mediated domain dynamics.EMBO reports · 2017Article
- Controllable Activation of Nanoscale Dynamics in a Disordered Protein Alters Binding Kinetics.Journal of molecular biology · 2017Article
- Selective Binding of AIRAPL Tandem UIMs to Lys48-Linked Tri-Ubiquitin Chains.Structure (London, England : 1993) · 2016Article
- Structure of a Bacterial Virus DNA-Injection Protein Complex Reveals a Decameric Assembly with a Constricted Molecular Channel.PloS one · 2016Article
- Protein Arginine Methyltransferase 8: Tetrameric Structure and Protein Substrate Specificity.Biochemistry · 2015Article
Corrections and comments
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Authors and funding
7 authors at 4 institutions in 2 countries.
Funding
Abstract
Botulinum neurotoxins (BoNTs) are among the most poisonous biological substances known. They assemble with non-toxic non-hemagglutinin (NTNHA) protein to form the minimally functional progenitor toxin complexes (M-PTC), which protects BoNT in the gastrointestinal tract and releases it upon entry into the circulation. Here we provide molecular insight into the assembly between BoNT/A and NTNHA-A using small-angle X-ray scattering. We found that the free form BoNT/A maintains a pH-independent conformation with limited domain flexibility. Intriguingly, the free form NTNHA-A adopts pH-dependent conformational changes due to a torsional motion of its C-terminal domain. Once forming a complex at acidic pH, they each adopt a stable conformation that is similar to that observed in the crystal structure of the M-PTC. Our results suggest that assembly of the M-PTC depends on the environmental pH and that the complex form of BoNT/A is induced by interacting with NTNHA-A at acidic pH.
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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.