Evidence map›Paper›PMID 21537023›Full record

ArticleAntimicrobial agents and chemotherapy2011

Effects of altering aminoglycoside structures on bacterial resistance enzyme activities.

Keith D Green, Wenjing Chen, Sylvie Garneau-Tsodikova

Abstract read
In one paragraph

Article in Antimicrobial agents and chemotherapy, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 29 papers.

0numbers the graph read from it
0cells of the map it votes in
29citing papers in PubMed
1.4field-weighted citation impact, top 21% 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

29 citing papers in PubMed, 37 citations in OpenAlex.

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  15. Tobramycin Variants with Enhanced Ribosome-Targeting Activity.Chembiochem : a European journal of chemical biology · 2015
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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

3 authors at 1 institution in 1 country.

Keith D GreenDepartment of Medicinal Chemistry, Life Sciences Institute, Michigan 48109-2216, USA.
Wenjing Chen
Sylvie Garneau-Tsodikova
Washtenaw Community College · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Aminoglycoside-modifying enzymes (AMEs) constitute the most prevalent mechanism of resistance to aminoglycosides by bacteria. We show that aminoglycosides can be doubly modified by the sequential actions of AMEs, with the activity of the second AME in most cases unaffected, decreased, or completely abolished. We demonstrate that the bifunctional enzyme AAC(3)-Ib/AAC(6')-Ib' can diacetylate gentamicin. Since single acetylation does not always inactivate the parent drugs completely, two modifications likely provide more-robust inactivation in vivo.

Indexed as

AminoglycosidesAnti-Bacterial AgentsBacterial ProteinsChromatography, Thin LayerGentamicinsMass SpectrometryMicrobial Sensitivity TestsAminoglycosidesAnti-Bacterial AgentsBacterial ProteinsGentamicins

Identifiers

PMID21537023
PMCPMC3122451
OpenAlexW2137189301

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.