Evidence map›Paper›PMID 22208312›Full record

ReviewACS chemical biology2012

The chemistry of peptidyltransferase center-targeted antibiotics: enzymatic resistance and approaches to countering resistance.

Kevin P McCusker, Danica Galonić Fujimori

Abstract readReview
In one paragraph

Review in ACS chemical biology, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.

0numbers the graph read from it
0cells of the map it votes in
15citing papers in PubMed
–field-weighted citation impact
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

15 citing papers in PubMed.

  1. Article
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  4. Review
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  8. Review
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  11. Article
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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.

Kevin P McCuskerDepartment of Cellular and Molecular Pharmacology, University of California, San Francisco, 94158, United States.
Danica Galonić Fujimori

Funding

Radical SAM MethytransferasesR01AI095393 · NIAID · UNIVERSITY OF CALIFORNIA, SAN FRANCISCO · PI FUJIMORI, DANICA GALONIC · 2011 to 2015
$1.7M
NIAID NIH HHS R01 AI095393NIAID NIH HHS R01AI095393-01
6 · The paper itself

Abstract

The continued ability to treat bacterial infections requires effective antibiotics. The development of new therapeutics is guided by knowledge of the mechanisms of action of and resistance to these antibiotics. Continued efforts to understand and counteract antibiotic resistance mechanisms at a molecular level have the potential to direct development of new therapeutic strategies in addition to providing insight into the underlying biochemical functions impacted by antibiotics. The interaction of antibiotics with the peptidyltransferase center and adjacent exit tunnel within the bacterial ribosome is the predominant mechanism by which antibiotics impede translation, thus stalling growth. Resistance enzymes catalyze the chemical modification of the RNA that composes these functional regions, leading to diminished binding of antibiotics. This review discusses recent advances in the elucidation of chemical mechanisms underlying resistance and driving the development of new antibiotics.

Indexed as

AcetamidesAnti-Bacterial AgentsBacteriaBacterial InfectionsBinding SitesDrug Resistance, Multiple, BacterialErythromycinHumansLinezolidMethylationOxazolidinonesPeptidyl TransferasesProtein BiosynthesisRibosomesRNA, Ribosomal, 23STetrazolesAcetamidesAnti-Bacterial AgentsErythromycinLinezolidOxazolidinonesPeptidyl TransferasesRNA, Ribosomal, 23StedizolidTetrazoles

Identifiers

PMID22208312
PMCPMC3499096

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.