ReviewToxins2010
Clostridial neurotoxins: mechanism of SNARE cleavage and outlook on potential substrate specificity reengineering.
Review in Toxins, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 35 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
35 citing papers in PubMed, 65 citations in OpenAlex.
- Design and Characterization of Recombinant and Chimeric BoNT/A Neurotoxins with Receptor-Binding Domain Grafting.Toxins · 2026Article
- Review
- Pioneering pain management with botulinum toxin type A: From anti-inflammation to regenerative therapies.Heliyon · 2025Review
- Cleavage of VAMP2/3 Affects Oligodendrocyte Lineage Development in the Developing Mouse Spinal Cord.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2023Article
- Botulinum neurotoxins: Future innovations.Medicine · 2023Article
- Article
- How Botulinum Neurotoxin Light Chain A1 Maintains Stable Association with the Intracellular Neuronal Plasma Membrane.Toxins · 2022Article
- Article
- Ability of human SNAP-23 to generate high molecular weight SDS-resistant ternary SNARE complexes is influenced by C-terminal coil content.Biochemistry and biophysics reports · 2021Article
- Therapeutic efficacy of new botulinum toxin identified in CCUG 7968 strain.Applied microbiology and biotechnology · 2021Article
- Resolution of Two Steps in Botulinum Neurotoxin Serotype A1 Light Chain Localization to the Intracellular Plasma Membrane.International journal of molecular sciences · 2021Article
- The MAL Protein, an Integral Component of Specialized Membranes, in Normal Cells and Cancer.Cells · 2021Review
- Comparative Pharmacodynamics Study of 3 Different Botulinum Toxin Type A Preparations in Mice.Dermatologic surgery : official publication for American Society for Dermatologic Surgery [et al.] · 2020Article
- KRAS regulation by small non-coding RNAs and SNARE proteins.Nature communications · 2019Article
- Bioinformatic discovery of a toxin family in Chryseobacterium piperi with sequence similarity to botulinum neurotoxins.Scientific reports · 2019Article
- Engineering Botulinum Toxins to Improve and Expand Targeting and SNARE Cleavage Activity.Toxins · 2018Review
- Review
- Structural and biochemical characterization of the protease domain of the mosaic botulinum neurotoxin type HA.Pathogens and disease · 2018Article
- Purification and Characterization of Recombinant Botulinum Neurotoxin Serotype FA, Also Known as Serotype H.Toxins · 2018Article
- VAMP2 is implicated in the secretion of antibodies by human plasma cells and can be replaced by other synaptobrevins.Cellular & molecular immunology · 2018Article
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 at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The clostridial neurotoxin family consists of tetanus neurotoxin and seven distinct botulinum neurotoxins which cause the diseases tetanus and botulism. The extreme potency of these toxins primarily relies not only on their ability to specifically enter motoneurons but also on the activity their catalytic domains display inside presynaptic motoneuronal terminals. Subsequent to neurotoxin binding and endocytosis the catalytic domains become translocated across endosomal membranes and proteolyze unique peptide bonds of one of three soluble N-ethylmaleimide-sensitive fusion protein attachment receptors (SNAREs), vesicle associated membrane protein/synaptobrevin, synaptosome associated protein of 25 kDa, or syntaxin. As these substrate proteins are core components of the vesicular membrane fusion apparatus, cleavage of any of the substrate molecules results in the blockade of neurotransmitter release. This review summarizes the present knowledge about the molecular basis of the specific substrate recognition and cleavage mechanism and assesses the feasibility of reengineering catalytic domains to hydrolyze non-substrate members of the three SNARE families in order to expand the therapeutic application of botulinum neurotoxins.
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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.