Articlenpj antimicrobials and resistance2026
Molecular mechanism of transition-state inhibitors of bacterial antibiotic efflux pumps.
Article in npj antimicrobials and resistance, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.
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.
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.
Who cites it
0 citing papers in PubMed.
No citing paper in PubMed yet.
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
13 authors.
Funding
Abstract
In many Gram-negative bacteria such as Escherichia coli and Klebsiella pneumoniae, the AcrAB-TolC efflux pump is central to multidrug resistance. We report the development of BDM91531, a nanomolar pyridylpiperazine inhibitor that potentiates the activity of several antibiotics. Structural analyses by X-ray crystallography and cryo-EM revealed that the divalent cationic BDM91531 binds AcrB through electrostatic interactions with a central role for residues D408 and E947, trapping protomers in an O to L transitional state and blocking the conformational cycling of the trimer. Differential scanning fluorimetry and susceptibility tests confirmed this inhibitory mechanism. Negative charges at the cytoplasmic rim are essential for inhibitor uptake as electrostatic attraction from rim carboxylates, including E947 and D951, facilitates entry. Loss of D951 abolished inhibitor sensitivity, whereas introducing alternative negative charges restored activity. These findings establish BDM91531 as a potent AcrB efflux pump inhibitor and highlight structural determinants for inhibitor access and binding.
Identifiers
What OpenQuestion holds
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.