ArticleThe Biochemical journal1997
Metal substitution of tetanus neurotoxin.
Article in The Biochemical journal, 1997. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 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.
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
4 citing papers in PubMed, 28 citations in OpenAlex.
- The Molecular Basis of Toxins' Interactions with Intracellular Signaling via Discrete Portals.Toxins · 2017Review
- The blockade of the neurotransmitter release apparatus by botulinum neurotoxins.Cellular and molecular life sciences : CMLS · 2014Review
- Article
- Tetanus and botulinum neurotoxins: mechanism of action and therapeutic uses.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 1999Review
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
Abstract
Tetanus neurotoxin was depleted of its catalytic Zn2+ ion, and the apotoxin was reconstituted with different transition metal ions. The Mn2+- and Co2+-tetanus neurotoxins are highly active in the proteolysis of vesicle-associated membrane protein/synaptobrevin, the natural substrate of this toxin, whereas Cu2+ and Fe2+ minimally supported proteolytic activity. The visible absorbance spectrum of Co2+-tetanus neurotoxin shows a maximum at 538 nm with a molar absorption coefficient of 82 M(-1) x cm(-1). These results indicate that the Zn2+ environment at the active site of tetanus neurotoxin is different from those of known Zn2+-endopeptidases and provide a structural basis for the definition of tetanus neurotoxin, and the related clostridial neurotoxins, as an independent family of metalloproteases.
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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.