Evidence map›Paper›PMID 37107012›Full record

ReviewAntibiotics (Basel, Switzerland)2023

Inhibitors of ATP Synthase as New Antibacterial Candidates.

Rawan Mackieh, Nadia Al-Bakkar, Milena Kfoury, Rabih Roufayel, Jean-Marc Sabatier, Ziad Fajloun

Open access · goldAbstract readReview
In one paragraph

Review in Antibiotics (Basel, Switzerland), 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.

0numbers the graph read from it
0cells of the map it votes in
22citing papers in PubMed
5.8field-weighted citation impact, top 3% 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

22 citing papers in PubMed, 38 citations in OpenAlex.

  1. Cryptotanshinone inhibitsVirulence · 2026
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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 4 institutions in 3 countries.

Rawan MackiehFaculty of Sciences 3, Department of Biology, Lebanese University, Campus Michel Slayman Ras Maska, Tripoli 1352, Lebanon.
Nadia Al-BakkarFaculty of Health Sciences, Beirut Arab University, Beirut Campus, Riad El Solh, Beirut 1105, Lebanon.
Milena KfouryFaculty of Sciences 3, Department of Biology, Lebanese University, Campus Michel Slayman Ras Maska, Tripoli 1352, Lebanon.
Rabih RoufayelCollege of Engineering and Technology, American University of the Middle East, Egaila 54200, Kuwait.ORCID 0000-0002-4595-1104
Jean-Marc SabatierCNRS, Institute of Neurophysiopathology, Aix-Marseille Université, 13385 Marseille, France.ORCID 0000-0002-9040-5647
Ziad FajlounFaculty of Sciences 3, Department of Biology, Lebanese University, Campus Michel Slayman Ras Maska, Tripoli 1352, Lebanon.ORCID 0000-0002-6502-3110
Lebanese University · LBAmerican University of the Middle East · KWBeirut Arab University · LBCentre National de la Recherche Scientifique · FR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

ATP, the power of all cellular functions, is constantly used and produced by cells. The enzyme called ATP synthase is the energy factory in all cells, which produces ATP by adding inorganic phosphate (Pi) to ADP. It is found in the inner, thylakoid and plasma membranes of mitochondria, chloroplasts and bacteria, respectively. Bacterial ATP synthases have been the subject of multiple studies for decades, since they can be genetically manipulated. With the emergence of antibiotic resistance, many combinations of antibiotics with other compounds that enhance the effect of these antibiotics have been proposed as approaches to limit the spread of antibiotic-resistant bacteria. ATP synthase inhibitors, such as resveratrol, venturicidin A, bedaquiline, tomatidine, piceatannol, oligomycin A and N,N-dicyclohexylcarbodiimide were the starting point of these combinations. However, each of these inhibitors target ATP synthase differently, and their co-administration with antibiotics increases the susceptibility of pathogenic bacteria. After a brief description of the structure and function of ATP synthase, we aim in this review to highlight therapeutic applications of the major bacterial ATP synthase inhibitors, including animal's venoms, and to emphasize their importance in decreasing the activity of this enzyme and subsequently eradicating resistant bacteria as ATP synthase is their source of energy.

Indexed as

animal venomsATP synthaseATP synthase inhibitorsresistant bacteriatherapeutic application

Identifiers

PMID37107012
PMCPMC10135114
OpenAlexW4361004786

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.