Botulinum toxin as a pain killer: players and actions in antinociception

DW Kim, SK Lee, J Ahnn - Toxins, 2015 - mdpi.com
Botulinum neurotoxins (BoNTs) have been widely used to treat a variety of clinical ailments
associated with pain. The inhibitory action of BoNTs on synaptic vesicle fusion blocks the …

Architecture of the botulinum neurotoxin complex: a molecular machine for protection and delivery

KH Lam, R Jin - Current opinion in structural biology, 2015 - Elsevier
Highlights•Botulinum neurotoxins are highly potent oral toxins.•The large progenitor
complex of BoNT is a bimodular 14-subunit complex.•NTNHA protects BoNT in the acidic …

The long journey of botulinum neurotoxins into the synapse

A Rummel - Toxicon, 2015 - Elsevier
Botulinum neurotoxins (BoNT) cause the disease botulism, a flaccid paralysis of the muscle.
They are also very effective, widely used medicines applied locally in sub-nanogram …

The structure of the tetanus toxin reveals pH‐mediated domain dynamics

G Masuyer, J Conrad, P Stenmark - EMBO reports, 2017 - embopress.org
The tetanus neurotoxin (Te NT) is a highly potent toxin produced by Clostridium tetani that
inhibits neurotransmission of inhibitory interneurons, causing spastic paralysis in the tetanus …

A viral-fusion-peptide-like molecular switch drives membrane insertion of botulinum neurotoxin A1

K Lam, Z Guo, N Krez, T Matsui, K Perry… - Nature …, 2018 - nature.com
Botulinum neurotoxin (BoNT) delivers its protease domain across the vesicle membrane to
enter the neuronal cytosol upon vesicle acidification. This process is mediated by its …

Generation and characterization of six recombinant botulinum neurotoxins as reference material to serve in an international proficiency test

J Weisemann, N Krez, U Fiebig, S Worbs, M Skiba… - Toxins, 2015 - mdpi.com
The detection and identification of botulinum neurotoxins (BoNT) is complex due to the
existence of seven serotypes, derived mosaic toxins and more than 40 subtypes. Expert …

Diverse binding modes, same goal: The receptor recognition mechanism of botulinum neurotoxin

KH Lam, G Yao, R Jin - Progress in biophysics and molecular biology, 2015 - Elsevier
Botulinum neurotoxins (BoNTs) are among the most deadly toxins known. They act rapidly in
a highly specific manner to block neurotransmitter release by cleaving the soluble N …

Dynamic intramolecular regulation of the histone chaperone nucleoplasmin controls histone binding and release

C Warren, T Matsui, JM Karp, T Onikubo… - Nature …, 2017 - nature.com
Nucleoplasmin (Npm) is a highly conserved histone chaperone responsible for the maternal
storage and zygotic release of histones H2A/H2B. Npm contains a pentameric N-terminal …

Protein arginine methyltransferase 8: tetrameric structure and protein substrate specificity

WC Lee, WL Lin, T Matsui, ESW Chen, TYW Wei… - Biochemistry, 2015 - ACS Publications
Type I protein arginine methyltransferases (PRMTs) catalyze asymmetric dimethylation of
various proteins, and their dysregulations often correlate with tumorigenesis or …

The cryo‐EM structure of the BoNT/Wo‐NTNH complex reveals two immunoglobulin‐like domains

S Košenina, J Škerlová, S Zhang, M Dong… - The FEBS …, 2024 - Wiley Online Library
The botulinum neurotoxin‐like toxin from Weissella oryzae (BoNT/Wo) is one of the BoNT‐
like toxins recently identified outside of the Clostridium genus. We show that, like the …