Evidence map›Paper›PMID 26060252›Full record

ArticleThe Journal of biological chemistry2015

Evidence That Antibiotics Bind to Human Mitochondrial Ribosomal RNA Has Implications for Aminoglycoside Toxicity.

Seoyeon Hong, Kimberly A Harris, Kathryn D Fanning, Kathryn L Sarachan, Kyla M Frohlich, Paul F Agris

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.

0numbers the graph read from it
0cells of the map it votes in
21citing papers in PubMed
2.3field-weighted citation impact, top 12% 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

21 citing papers in PubMed, 48 citations in OpenAlex.

  1. Review
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  9. Intranasal neomycin evokes broad-spectrum antiviral immunity in the upper respiratory tract.Proceedings of the National Academy of Sciences of the United States of America · 2024
    Article
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  19. Application of antimicrobial drugs in perioperative surgical incision.Annals of clinical microbiology and antimicrobials · 2018
    Review
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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

6 authors at 1 institution in 1 country.

Seoyeon HongFrom The RNA Institute and the Department of Biological Sciences, University at Albany, Albany, New York 12222.
Kimberly A HarrisFrom The RNA Institute and the Department of Biological Sciences, University at Albany, Albany, New York 12222.
Kathryn D FanningFrom The RNA Institute and the Department of Biological Sciences, University at Albany, Albany, New York 12222.
Kathryn L SarachanFrom The RNA Institute and the Department of Biological Sciences, University at Albany, Albany, New York 12222.
Kyla M FrohlichFrom The RNA Institute and the Department of Biological Sciences, University at Albany, Albany, New York 12222.
Paul F AgrisFrom The RNA Institute and the Department of Biological Sciences, University at Albany, Albany, New York 12222 pagris@albany.edu.
University at Albany, State University of New York · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Aminoglycosides are a well known antibiotic family used to treat bacterial infections in humans and animals, but which can be toxic. By binding to the decoding site of helix44 of the small subunit RNA of the bacterial ribosome, the aminoglycoside antibiotics inhibit protein synthesis, cause misreading, or obstruct peptidyl-tRNA translocation. Although aminoglycosides bind helix69 of the bacterial large subunit RNA as well, little is known about their interaction with the homologous human helix69. To probe the role this binding event plays in toxicity, changes to thermal stability, base stacking, and conformation upon aminoglycoside binding to the human cytoplasmic helix69 were compared with those of the human mitochondrial and Escherichia coli helix69. Surprisingly, binding of gentamicin and kanamycin A to the chemically synthesized terminal hairpins of the human cytoplasmic, human mitochondrial, and E. coli helix69 revealed similar dissociation constants (1.3-1.7 and 4.0-5.4 μM, respectively). In addition, aminoglycoside binding enhanced conformational stability of the human mitochondrial helix69 by increasing base stacking. Proton one-dimensional and two-dimensional NMR suggested significant and specific conformational changes of human mitochondrial and E. coli helix69 upon aminoglycoside binding, as compared with human cytoplasmic helix69. The conformational changes and similar aminoglycoside binding affinities observed for human mitochondrial helix69 and E. coli helix69, as well as the increase in structural stability shown for the former, suggest that this binding event is important to understanding aminoglycoside toxicity.

Indexed as

Anti-Bacterial AgentsEscherichia coliGentamicinsHumansInverted Repeat SequencesKanamycinRNARNA, BacterialRNA, MitochondrialRNA, RibosomalRNA StabilityAnti-Bacterial AgentsGentamicinsKanamycinRNARNA, BacterialRNA, MitochondrialRNA, Ribosomalantibiotic actioncircular dichroism (CD)nuclear magnetic resonance (NMR)ribosomal ribonucleic acid (rRNA) (ribosomal RNA)translation

Identifiers

PMID26060252
PMCPMC4521047
OpenAlexW1871843030

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.