Evidence map›Paper›PMID 28475321›Full record

ArticleJournal of the American Chemical Society2017

Metal Ions Effectively Ablate the Action of Botulinum Neurotoxin A.

Paul T Bremer, Sabine Pellett, James P Carolan, William H Tepp, Lisa M Eubanks, Karen N Allen, Eric A Johnson, Kim D Janda

Open access · greenAbstract read
In one paragraph

Article in Journal of the American Chemical Society, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.

0numbers the graph read from it
0cells of the map it votes in
12citing papers in PubMed
1.4field-weighted citation impact, top 19% 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

12 citing papers in PubMed, 19 citations in OpenAlex.

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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

8 authors at 3 institutions in 1 country.

Paul T BremerDepartments of Chemistry and Immunology, The Skaggs Institute for Chemical Biology, Worm Institute of Research and Medicine (WIRM), The Scripps Research Institute , 10550 North Torrey Pines Road, La Jolla, California 92037, United States.ORCID 0000-0002-8357-1743
Sabine PellettDepartment of Bacteriology, University of Wisconsin , 1550 Linden Drive, Madison, Wisconsin 53706, United States.
James P CarolanDepartment of Chemistry, Boston University , 590 Commonwealth Avenue, Boston, Massachusetts 02215, United States.
William H TeppDepartment of Bacteriology, University of Wisconsin , 1550 Linden Drive, Madison, Wisconsin 53706, United States.
Lisa M EubanksDepartments of Chemistry and Immunology, The Skaggs Institute for Chemical Biology, Worm Institute of Research and Medicine (WIRM), The Scripps Research Institute , 10550 North Torrey Pines Road, La Jolla, California 92037, United States.
Karen N AllenDepartment of Chemistry, Boston University , 590 Commonwealth Avenue, Boston, Massachusetts 02215, United States.ORCID 0000-0001-7296-0551
Eric A JohnsonDepartment of Bacteriology, University of Wisconsin , 1550 Linden Drive, Madison, Wisconsin 53706, United States.
Kim D JandaDepartments of Chemistry and Immunology, The Skaggs Institute for Chemical Biology, Worm Institute of Research and Medicine (WIRM), The Scripps Research Institute , 10550 North Torrey Pines Road, La Jolla, California 92037, United States.ORCID 0000-0001-6759-4227
Scripps Research Institute · USUniversity of Wisconsin–Madison · USBoston University · US

Funding

A Multidisciplinary Approach for the Treatment of Botulinum IntoxicationR01AI119564 · NIAID · SCRIPPS RESEARCH INSTITUTE, THE · PI JANDA, KIM · 2016 to 2019
$2.3M
NIAID NIH HHS R01 AI119564
6 · The paper itself

Abstract

Botulinum neurotoxin serotype A (BoNT/A) causes a debilitating and potentially fatal illness known as botulism. The toxin is also a bioterrorism threat, yet no pharmacological antagonist to counteract its effects has reached clinical approval. Existing strategies to negate BoNT/A intoxication have looked to antibodies, peptides, or organic small molecules as potential therapeutics. In this work, a departure from the traditional drug discovery mindset was pursued, in which the enzyme's susceptibility to metal ions was exploited. A screen of a series of metal salts showed marked inhibitory activity of group 11 and 12 metals against the BoNT/A light chain (LC) protease. Enzyme kinetics revealed that copper (I) and (II) cations displayed noncompetitive inhibition of the LC (K

Indexed as

AnimalsBotulinum Toxins, Type ACoordination ComplexesCopperDisease Models, AnimalDose-Response Relationship, DrugHumansInduced Pluripotent Stem CellsKineticsMiceNeuronsProtease InhibitorsStructure-Activity RelationshipThiocarbamatesThiosemicarbazonesBotulinum Toxins, Type ACoordination ComplexesCopperProtease InhibitorsThiocarbamatesThiosemicarbazones

Identifiers

PMID28475321
PMCPMC5612488
OpenAlexW2610769737

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.