Tetanus and botulinum neurotoxins: turning bad guys into good by research
Toxicon, ISSN: 0041-0101, Vol: 39, Issue: 1, Page: 27-41
2001
- 154Citations
- 105Captures
- 1Mentions
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Example: if you select the 1-year option for an article published in 2019 and a metric category shows 90%, that means that the article or review is performing better than 90% of the other articles/reviews published in that journal in 2019. If you select the 3-year option for the same article published in 2019 and the metric category shows 90%, that means that the article or review is performing better than 90% of the other articles/reviews published in that journal in 2019, 2018 and 2017.
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Metrics Details
- Citations154
- Citation Indexes153
- 153
- CrossRef128
- Patent Family Citations1
- Patent Families1
- Captures105
- Readers105
- 105
- Mentions1
- References1
- Wikipedia1
Article Description
The neuroparalytic syndromes of tetanus and botulism are caused by neurotoxins produced by bacteria of the genus Clostridium. They are 150 kDa proteins consisting of three-domains, endowed with different functions: neurospecific binding, membrane translocation and specific proteolysis of three key components of the neuroexocytosis apparatus. After binding to the presynaptic membrane of motoneurons, tetanus neurotoxin (TeNT) is internalized and transported retroaxonally to the spinal cord, where it blocks neurotransmitter release from spinal inhibitory interneurons. In contrast, the seven botulinum neurotoxins (BoNT) act at the periphery and inhibit acetylcholine release from peripheral cholinergic nerve terminals. TeNT and BoNT-B, -D, -F and -G cleave specifically at single but different peptide bonds, VAMP/synaptobrevin, a membrane protein of small synaptic vesicles. BoNT types -A, -C and -E cleave SNAP-25 at different sites within the COOH-terminus, whereas BoNT-C also cleaves syntaxin. BoNTs are increasingly used in medicine for the treatment of human diseases characterized by hyperfunction of cholinergic terminals.
Bibliographic Details
http://www.sciencedirect.com/science/article/pii/S004101010000163X; http://dx.doi.org/10.1016/s0041-0101(00)00163-x; http://www.scopus.com/inward/record.url?partnerID=HzOxMe3b&scp=0035239239&origin=inward; http://www.ncbi.nlm.nih.gov/pubmed/10936621; https://linkinghub.elsevier.com/retrieve/pii/S004101010000163X; http://linkinghub.elsevier.com/retrieve/pii/S004101010000163X; http://api.elsevier.com/content/article/PII:S004101010000163X?httpAccept=text/xml; http://api.elsevier.com/content/article/PII:S004101010000163X?httpAccept=text/plain; http://dx.doi.org/10.1016/s0041-0101%2800%2900163-x; https://dx.doi.org/10.1016/s0041-0101%2800%2900163-x
Elsevier BV
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