Evidence map›Paper›PMID 33563840›Full record

ArticlemBio2021

ApmA Is a Unique Aminoglycoside Antibiotic Acetyltransferase That Inactivates Apramycin.

Emily Bordeleau, Peter J Stogios, Elena Evdokimova, Kalinka Koteva, Alexei Savchenko, Gerard D Wright

Open access · goldAbstract read
In one paragraph

Article in mBio, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.

0numbers the graph read from it
0cells of the map it votes in
20citing papers in PubMed
1.4field-weighted citation impact, top 20% 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

20 citing papers in PubMed, 31 citations in OpenAlex.

  1. Carbapenem and colistin-resistantJAC-antimicrobial resistance · 2026
    Article
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  17. InvasiveFrontiers in cellular and infection microbiology · 2023
    Article
  18. Article
  19. Article
  20. Article
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

6 authors at 2 institutions in 1 country.

Emily BordeleauDavid Braley Centre for Antibiotics Discovery, M.G. DeGroote Institute for Infectious Disease Research, Department of Biochemistry and Biomedical Sciences, McMaster University, Hamilton, Ontario, Canada.
Peter J StogiosDepartment of Chemical Engineering and Applied Chemistry, University of Toronto, Toronto, Ontario, Canada.
Elena EvdokimovaDepartment of Chemical Engineering and Applied Chemistry, University of Toronto, Toronto, Ontario, Canada.
Kalinka KotevaDavid Braley Centre for Antibiotics Discovery, M.G. DeGroote Institute for Infectious Disease Research, Department of Biochemistry and Biomedical Sciences, McMaster University, Hamilton, Ontario, Canada.
Alexei SavchenkoDepartment of Chemical Engineering and Applied Chemistry, University of Toronto, Toronto, Ontario, Canada.ORCID 0000-0002-5256-9237
Gerard D WrightDavid Braley Centre for Antibiotics Discovery, M.G. DeGroote Institute for Infectious Disease Research, Department of Biochemistry and Biomedical Sciences, McMaster University, Hamilton, Ontario, Canada wrightge@mcmaster.ca.ORCID 0000-0002-9129-7131
McMaster University · CAUniversity of Calgary · CA

Funding

CIHR FRN-148463NIAID NIH HHS HHSN272201700060C
6 · The paper itself

Abstract

Apramycin is an aminoglycoside antibiotic with the potential to be developed to combat multidrug-resistant pathogens. Its unique structure evades the clinically widespread mechanisms of aminoglycoside resistance that currently compromise the efficacy of other members in this drug class. Of the aminoglycoside-modifying enzymes that chemically alter these antibiotics, only AAC(3)-IVa has been demonstrated to confer resistance to apramycin through

Indexed as

AcetylationAcetyltransferasesAminoglycosidesAnti-Bacterial AgentsCrystallizationDrug Resistance, BacterialEscherichia coliEscherichia coli ProteinsHumansMicrobial Sensitivity TestsNebramycinAcetyltransferasesAminoglycosidesAnti-Bacterial AgentsapramycinEscherichia coli ProteinsNebramycinaminoglycoside-modifying enzymesantibiotic resistanceapramycin

Identifiers

PMID33563840
PMCPMC7885111
OpenAlexW3128819748

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.