Evidence map›Paper›PMID 30388027›Full record

ReviewAnnual review of biochemistry2019

Botulinum and Tetanus Neurotoxins.

Min Dong, Geoffrey Masuyer, Pål Stenmark

Open access · bronzeAbstract readReview
In one paragraph

Review in Annual review of biochemistry, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 137 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
137citing papers in PubMed, 1 pooled it
12.6field-weighted citation impact, top 1% of its field
1 · What the graph read from it

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.

2 · The registry

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.

3 · Its place in the literature

Who cites it

137 citing papers in PubMed, 1 synthesis or guideline pooled it, 230 citations in OpenAlex.

  1. Pooled it
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  12. Gangliosides in molecular interactions and cell regulation.The Journal of biological chemistry · 2026
    Review
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  17. Probing the properties of PTEN specific botulinum toxin type E mutants.Journal of neural transmission (Vienna, Austria : 1996) · 2025
    Article
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77 more citing papers are in PubMed but not listed here.

4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

3 authors at 2 institutions in 2 countries.

Min DongDepartment of Urology, Boston Children's Hospital, Boston, Massachusetts 02115, USA; email: min.dong@childrens.harvard.edu.
Geoffrey MasuyerDepartment of Biochemistry and Biophysics, Stockholm University, 106 91 Stockholm, Sweden; email: stenmark@dbb.su.se.
Pål StenmarkDepartment of Biochemistry and Biophysics, Stockholm University, 106 91 Stockholm, Sweden; email: stenmark@dbb.su.se.
Stockholm University · SEBoston Children's Hospital · US

Funding

STRUCTURE-FUNCTION RELATIONSHIPS IN THE ALIMENTARY TRACTP30DK034854 · NIDDK · HARVARD UNIVERSITY (MEDICAL SCHOOL) · PI JONATHAN C KAGAN · 1986 to 2026
$32.4M
SYNAPTIC MECHANISMS IN HIPPOCAMPAL EPILEPTOGENESISP30HD018655 · NICHD · CHILDREN'S HOSPITAL BOSTON · PI POMEROY, SCOTT LOREN · 1985 to 2015
$26.2M
Long-term effects of botulinum neurotoxins on neuronal viabilityR01NS080833 · NINDS · HARVARD MEDICAL SCHOOL · PI Min Dong · 2013 to 2026
$6.8M
Molecular basis of action and pathogenesis of Clostridium difficile toxin BR01AI132387 · NIAID · BOSTON CHILDREN'S HOSPITAL · PI DONG, MIN · 2017 to 2021
$3.5M
Molecular mechanism for retrograde transport of tetanus neurotoxinR21NS106159 · NINDS · BOSTON CHILDREN'S HOSPITAL · PI DONG, MIN · 2018 to 2019
$487k
NIAID NIH HHS R01 AI132387NICHD NIH HHS P30 HD018655NIDDK NIH HHS P30 DK034854NINDS NIH HHS R01 NS080833NINDS NIH HHS R21 NS106159
6 · The paper itself

Abstract

Botulinum neurotoxins (BoNTs) and tetanus neurotoxin (TeNT) are the most potent toxins known and cause botulism and tetanus, respectively. BoNTs are also widely utilized as therapeutic toxins. They contain three functional domains responsible for receptor-binding, membrane translocation, and proteolytic cleavage of host proteins required for synaptic vesicle exocytosis. These toxins also have distinct features: BoNTs exist within a progenitor toxin complex (PTC), which protects the toxin and facilitates its absorption in the gastrointestinal tract, whereas TeNT is uniquely transported retrogradely within motor neurons. Our increasing knowledge of these toxins has allowed the development of engineered toxins for medical uses. The discovery of new BoNTs and BoNT-like proteins provides additional tools to understand the evolution of the toxins and to engineer toxin-based therapeutics. This review summarizes the progress on our understanding of BoNTs and TeNT, focusing on the PTC, receptor recognition, new BoNT-like toxins, and therapeutic toxin engineering.

Indexed as

AnimalsBotulinum ToxinsHumansMetalloendopeptidasesProtein ConformationProtein EngineeringTetanus ToxinBotulinum ToxinsMetalloendopeptidasestetanospasminTetanus Toxinbacterial toxinbotulinum neurotoxinclostridiumprotein engineeringtetanus neurotoxintoxin

Identifiers

PMID30388027
PMCPMC7539302
OpenAlexW2903612881

What OpenQuestion holds

Textmetadata
LicenceTDM
Read underepoch 390

Registered trials

None linked

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.