Evidence map›Paper›PMID 23485681›Full record

ArticleBiochimie2013

Domain dissection and characterization of the aminoglycoside resistance enzyme ANT(3″)-Ii/AAC(6')-IId from Serratia marcescens.

Keith D Green, Sylvie Garneau-Tsodikova

Open access · greenAbstract read
In one paragraph

Article in Biochimie, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.

0numbers the graph read from it
0cells of the map it votes in
10citing papers in PubMed
0.6field-weighted citation impact, top 41% 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

10 citing papers in PubMed, 13 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

2 authors at 1 institution in 1 country.

Keith D GreenLife Sciences Institute, 210 Washtenaw Ave, University of Michigan, Ann Arbor, MI 48109-2216, USA.
Sylvie Garneau-Tsodikova
Washtenaw Community College · US

Funding

Novel aminoglycoside adjuvants and stand-alone agents to combat tuberculosisR01AI090048 · NIAID · UNIVERSITY OF MICHIGAN AT ANN ARBOR · PI GARNEAU-TSODIKOVA, SYLVIE · 2011 to 2021
$4.4M
NIAID NIH HHS AI090048NIAID NIH HHS R01 AI090048
6 · The paper itself

Abstract

Aminoglycosides (AGs) are broad-spectrum antibiotics whose constant use and presence in growth environments has led bacteria to develop resistance mechanisms to aid in their survival. A common mechanism of resistance to AGs is their chemical modification (nucleotidylation, phosphorylation, or acetylation) by AG-modifying enzymes (AMEs). Through evolution, fusion of two AME-encoding genes has resulted in bifunctional enzymes with broader spectrum of activity. Serratia marcescens, a human enteropathogen, contains such a bifunctional enzyme, ANT(3″)-Ii/AAC(6')-IId. To gain insight into the role, effect, and importance of the union of ANT(3″)-Ii and AAC(6')-IId in this bifunctional enzyme, we separated the two domains and compared their activity to that of the full-length enzyme. We performed a thorough comparison of the substrate and cosubstrate profiles as well as kinetic characterization of the bifunctional ANT(3″)-Ii/AAC(6')-IId and its individually expressed components.

Indexed as

AminoglycosidesAcetyltransferasesBacterial ProteinsDrug Resistance, MicrobialMass SpectrometryPolymerase Chain ReactionSerratia marcescensAcetyltransferasesAminoglycosidesBacterial Proteins

Identifiers

PMID23485681
PMCPMC3646955
OpenAlexW2017140509

What OpenQuestion holds

Textmetadata
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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.