Light Chain of Botulinum A Neurotoxin Expressed as an Inclusion Body from a Synthetic Gene Is Catalytically and Functionally Active
- 1 August 2000
- journal article
- Published by Springer Nature in Protein Journal
- Vol. 19 (6) , 475-487
- https://doi.org/10.1023/a:1026549431380
Abstract
Botulinum neurotoxins, the most potent of all toxins, induce lethal neuromuscular paralysis by inhibiting exocytosis at the neuromuscular junction. The light chains (LC) of these dichain neurotoxins...Keywords
This publication has 37 references indexed in Scilit:
- Sequence homology and structural analysis of the clostridial neurotoxinsJournal of Molecular Biology, 1999
- Enhancement of the Endopeptidase Activity of Botulinum Neurotoxin by Its Associated Proteins and DithiothreitolBiochemistry, 1999
- Expression and Purification of the Light Chain of Botulinum Neurotoxin A: A Single Mutation Abolishes Its Cleavage of SNAP-25 and Neurotoxicity after Reconstitution with the Heavy ChainBiochemistry, 1995
- Proteolysis of synthetic peptides by type A botulinum neurotoxinProtein Journal, 1995
- SNARE motif and neurotoxinsNature, 1994
- A Single Mutation in the Recombinant Light Chain of Tetanus Toxin Abolishes Its Proteolytic Activity and Removes the Toxicity Seen after Reconstitution with Native Heavy ChainBiochemistry, 1994
- Cell Membrane Resealing by a Vesicular Mechanism Similar to Neurotransmitter ReleaseScience, 1994
- Identification of an ion channel‐forming motif in the primary structure of tetanus and botulinum neurotoxinsFEBS Letters, 1992
- Botulinum neurotoxin type A: sequence of amino acids at the N-terminus and around the nicking siteBiochimie, 1990
- Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4Nature, 1970