Evidence map›Paper›PMID 31431523›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2019

Gangliosides interact with synaptotagmin to form the high-affinity receptor complex for botulinum neurotoxin B.

Alessandra Flores, Jorge Ramirez-Franco, Richard Desplantes, Kévin Debreux, Géraldine Ferracci, Florian Wernert, Marie-Pierre Blanchard, Yves Maulet, Fahamoe Youssouf, Marion Sangiardi and 6 more

Open access · bronzeAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 33 papers.

0numbers the graph read from it
0cells of the map it votes in
33citing papers in PubMed
4.5field-weighted citation impact, top 5% 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

33 citing papers in PubMed, 57 citations in OpenAlex.

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  11. A novel RRGW derived peptide is a promising inhibitor of BoNT/A.Journal of enzyme inhibition and medicinal chemistry · 2023
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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

16 authors at 3 institutions in 1 country.

Alessandra FloresUnité de Neurobiologie des Canaux Ioniques et de la Synapse, INSERM UMR_S 1072, 13015 Marseille, France.
Jorge Ramirez-FrancoUnité de Neurobiologie des Canaux Ioniques et de la Synapse, INSERM UMR_S 1072, 13015 Marseille, France.
Richard DesplantesUnité de Neurobiologie des Canaux Ioniques et de la Synapse, INSERM UMR_S 1072, 13015 Marseille, France.
Kévin DebreuxUnité de Neurobiologie des Canaux Ioniques et de la Synapse, INSERM UMR_S 1072, 13015 Marseille, France.
Géraldine FerracciAix-Marseille Université, 13015 Marseille, France.
Florian WernertUnité de Neurobiologie des Canaux Ioniques et de la Synapse, INSERM UMR_S 1072, 13015 Marseille, France.
Marie-Pierre BlanchardAix-Marseille Université, 13015 Marseille, France.
Yves MauletUnité de Neurobiologie des Canaux Ioniques et de la Synapse, INSERM UMR_S 1072, 13015 Marseille, France.
Fahamoe YoussoufUnité de Neurobiologie des Canaux Ioniques et de la Synapse, INSERM UMR_S 1072, 13015 Marseille, France.
Marion SangiardiUnité de Neurobiologie des Canaux Ioniques et de la Synapse, INSERM UMR_S 1072, 13015 Marseille, France.
Cécile IborraUnité de Neurobiologie des Canaux Ioniques et de la Synapse, INSERM UMR_S 1072, 13015 Marseille, France.
Michel Robert PopoffBacterial Toxins, Équipe de Recherche Labellisée 6002, Institut Pasteur, 75015 Paris, France.
Michael SeagarUnité de Neurobiologie des Canaux Ioniques et de la Synapse, INSERM UMR_S 1072, 13015 Marseille, France.
Jacques FantiniUnité de Neurobiologie des Canaux Ioniques et de la Synapse, INSERM UMR_S 1072, 13015 Marseille, France.
Christian LévêqueUnité de Neurobiologie des Canaux Ioniques et de la Synapse, INSERM UMR_S 1072, 13015 Marseille, France.
Oussama El FarUnité de Neurobiologie des Canaux Ioniques et de la Synapse, INSERM UMR_S 1072, 13015 Marseille, France; oussama.el-far@inserm.fr.ORCID 0000-0002-7473-8345
Inserm · FRCentre National de la Recherche Scientifique · FRInstitut Pasteur · FR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Botulinum neurotoxin type B (BoNT/B) recognizes nerve terminals by binding to 2 receptor components: a polysialoganglioside, predominantly GT1b, and synaptotagmin 1/2. It is widely thought that BoNT/B initially binds to GT1b then diffuses in the plane of the membrane to interact with synaptotagmin. We have addressed the hypothesis that a GT1b-synaptotagmin

Indexed as

Botulinum Toxins, Type AGangliosidesSynaptotagmin IAnimalsBinding SitesProtein Conformation, alpha-HelicalProtein DomainsRatsSynaptotagmin IIBotulinum Toxins, Type AGangliosidesrimabotulinumtoxinBSynaptotagmin ISynaptotagmin IISyt1 protein, ratSyt2 protein, rattrisialoganglioside GT1botulinum neurotoxin B receptorgangliosidessynaptotagmin

Identifiers

PMID31431523
PMCPMC6731659
OpenAlexW2969420263

What OpenQuestion holds

Textmetadata
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.