ArticleAntimicrobial agents and chemotherapy2011
Structural and biochemical analysis of the pentapeptide repeat protein EfsQnr, a potent DNA gyrase inhibitor.
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 27 papers.
What it found
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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.
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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.
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Who cites it
27 citing papers in PubMed, 44 citations in OpenAlex.
- Novel Qnr Families as Conserved and Intrinsic Quinolone Resistance Determinants inJournal of microbiology and biotechnology · 2024Article
- Friend or Foe: Protein Inhibitors of DNA Gyrase.Biology · 2024Review
- Quinolone Resistance Genes and Their Contribution to Resistance inAntibiotics (Basel, Switzerland) · 2023Article
- The pentapeptide-repeat protein, MfpA, interacts with mycobacterial DNA gyrase as a DNA T-segment mimic.Proceedings of the National Academy of Sciences of the United States of America · 2021Article
- Pentapeptide repeat protein QnrB1 requires ATP hydrolysis to rejuvenate poisoned gyrase complexes.Nucleic acids research · 2021Article
- Overexpression ofInternational journal of microbiology · 2021Article
- Transferable Mechanisms of Quinolone Resistance from 1998 Onward.Clinical microbiology reviews · 2019Review
- The Microbial Toxin Microcin B17: Prospects for the Development of New Antibacterial Agents.Journal of molecular biology · 2019Review
- Interference with KCTD9 inhibits NK cell activation and ameliorates fulminant liver failure in mice.BMC immunology · 2018Article
- Topoisomerases as anticancer targets.The Biochemical journal · 2018Review
- Topoisomerase Inhibitors: Fluoroquinolone Mechanisms of Action and Resistance.Cold Spring Harbor perspectives in medicine · 2016Review
- Mutational Analysis of Quinolone Resistance Protein QnrVC7 Provides Novel Insights into the Structure-Activity Relationship of Qnr Proteins.Antimicrobial agents and chemotherapy · 2016Article
- Characterization of Vibrio fluvialis qnrVC5 Gene in Native and Heterologous Hosts: Synergy of qnrVC5 with other Determinants in Conferring Quinolone Resistance.Frontiers in microbiology · 2016Article
- Mechanisms of drug resistance: quinolone resistance.Annals of the New York Academy of Sciences · 2015Review
- DNA Topoisomerases.EcoSal Plus · 2015Review
- Plasmid-mediated quinolone resistance.Microbiology spectrum · 2014Review
- QnrS1 structure-activity relationships.The Journal of antimicrobial chemotherapy · 2014Article
- Functional verification of computationally predicted qnr genes.Annals of clinical microbiology and antimicrobials · 2013Article
- Dynamic cyanobacterial response to hydration and dehydration in a desert biological soil crust.The ISME journal · 2013Article
- Phylogenetic analysis of chromosomally determined qnr and related proteins.Antimicrobial agents and chemotherapy · 2013Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
5 authors at 2 institutions in 2 countries.
Funding
Abstract
The chromosomally encoded Qnr homolog protein from Enterococcus faecalis (EfsQnr), when expressed, confers to its host a decreased susceptibility to quinolones and consists mainly of tandem repeats, which is consistent with belonging to the pentapeptide repeat family of proteins (PRPs). EfsQnr was cloned with an N-terminal 6× His tag and purified to homogeneity. EfsQnr partially protected DNA gyrase from fluoroquinolone inhibition at concentrations as low as 20 nM. EfsQnr inhibited the ATP-dependent supercoiling activity of DNA gyrase with a 50% inhibitory concentration (IC(50)) of 1.2 μM, while no significant inhibition of ATP-independent relaxation activity was observed. EfsQnr was cytotoxic when overexpressed in Escherichia coli, resulting in the clumping of cells and a loss of viability. The X-ray crystal structure of EfsQnr was determined to 1.6-Å resolution. EfsQnr exhibits the right-handed quadrilateral beta-helical fold typical of PRPs, with features more analogous to MfpA (mycobacterium fluoroquinolone resistance pentapeptide) than to the PRPs commonly found in cyanobacteria.
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Registered trials
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.