Evidence map›Paper›PMID 25866265›Full record

ReviewAnnals of the New York Academy of Sciences2015

External guide sequence technology: a path to development of novel antimicrobial therapeutics.

Carol Davies-Sala, Alfonso Soler-Bistué, Robert A Bonomo, Angeles Zorreguieta, Marcelo E Tolmasky

Open access · hybridAbstract readReview
In one paragraph

Review in Annals of the New York Academy of Sciences, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.

0numbers the graph read from it
0cells of the map it votes in
19citing papers in PubMed
1.7field-weighted citation impact, top 17% 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

19 citing papers in PubMed, 35 citations in OpenAlex.

  1. Article
  2. Article
  3. Trans-splicing for gene regulation.Nature chemical biology · 2025
    Article
  4. Review
  5. Article
  6. Review
  7. Review
  8. Article
  9. Bridged Nucleic Acids Reloaded.Molecules (Basel, Switzerland) · 2019
    Review
  10. Article
  11. Article
  12. Article
  13. Review
  14. Article
  15. Advances in therapeutic bacterial antisense biotechnology.Applied microbiology and biotechnology · 2018
    Review
  16. Identification of theFrontiers in microbiology · 2018
    Article
  17. Amikacin: Uses, Resistance, and Prospects for Inhibition.Molecules (Basel, Switzerland) · 2017
    Review
  18. Article
  19. Article
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

5 authors at 4 institutions in 2 countries.

Carol Davies-SalaFundación Instituto Leloir, IIBBA-CONICET, and FCEyN, University of Buenos Aires, Argentina.
Alfonso Soler-BistuéFundación Instituto Leloir, IIBBA-CONICET, and FCEyN, University of Buenos Aires, Argentina.
Robert A BonomoDepartment of Medicine, Case Western Reserve University School of Medicine, Cleveland, Ohio.
Angeles ZorreguietaFundación Instituto Leloir, IIBBA-CONICET, and FCEyN, University of Buenos Aires, Argentina.
Marcelo E TolmaskyCenter for Applied Biotechnology Studies, College of Natural Sciences and Mathematics, California State University Fullerton, Fullerton, California.
Consejo Nacional de Investigaciones Científicas y Técnicas · ARCalifornia State University, Fullerton · USCase Western Reserve University · USFundación Instituto Leloir · AR

Funding

Minority Health and Health Disparities International Research Training ProgramT37MD001368 · NIMHD · CALIFORNIA STATE UNIVERSITY FULLERTON · PI TOLMASKY, MARCELO E · 2005 to 2024
$3.9M
DEALING WITH ANTIBIOTIC RESISTANCE--ANTISENSE TECHNOLOGYR15AI047115 · NIAID · CALIFORNIA STATE UNIVERSITY FULLERTON · PI TOLMASKY, MARCELO E · 2000 to 2022
$1.8M
The Continuing Challenge of Carbapenemases in K. pneumoniae: KPC-2 & NDM-1I01BX001974 · VA · LOUIS STOKES CLEVELAND VA MEDICAL CENTER · PI BONOMO, ROBERT A. · 2013 to 2024
–
BLRD VA I01 BX001974NIAID NIH HHS 2R15AI047115NIAID NIH HHS R15 AI047115NIMHD NIH HHS T37 MD001368
6 · The paper itself

Abstract

RNase P is a ribozyme originally identified for its role in maturation of tRNAs by cleavage of precursor tRNAs (pre-tRNAs) at the 5'-end termini. RNase P is a ribonucleoprotein consisting of a catalytic RNA molecule and, depending on the organism, one or more cofactor proteins. The site of cleavage of a pre-tRNA is identified by its tertiary structure; and any RNA molecule can be cleaved by RNase P as long as the RNA forms a duplex that resembles the regional structure in the pre-tRNA. When the antisense sequence that forms the duplex with the strand that is subsequently cleaved by RNase P is in a separate molecule, it is called an external guide sequence (EGS). These fundamental observations are the basis for EGS technology, which consists of inhibiting gene expression by utilizing an EGS that elicits RNase P-mediated cleavage of a target mRNA molecule. EGS technology has been used to inhibit expression of a wide variety of genes, and may help development of novel treatments of diseases, including multidrug-resistant bacterial and viral infections.

Indexed as

Anti-Bacterial AgentsBacteriaBacterial InfectionsHumansModels, GeneticNucleic Acid ConformationOligoribonucleotides, AntisenseRibonuclease PRNA, BacterialRNA, CatalyticAnti-Bacterial AgentsOligoribonucleotides, AntisenseRibonuclease PRNA, BacterialRNA, Catalyticantimicrobialsantisensedrug designexternal guide sequenceRNase P

Identifiers

PMID25866265
PMCPMC4600001
OpenAlexW1579015871

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.