ArticleNaunyn-Schmiedeberg's archives of pharmacology2026
Quercetin as a promising HIS-C inhibitor and novel therapeutic against antibacterial drug-resistant Acinetobacter baumannii: in vitro and in silico insights.
Article in Naunyn-Schmiedeberg's archives of pharmacology, 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
Acinetobacter baumannii (A. baumannii), a common hospital-associated pathogen, is known for its rapid ability to develop antibacterial drug resistance. The HIS-C enzyme in this pathogen is essential for histidine biosynthesis, making this a prominent drug target for antimicrobial therapy. This experimental investigation analyzes the inhibitory function of quercetin, a well-known antibacterial flavonoid, on HIS-C enzyme through the in vitro and in silico approaches. The binding affinity between quercetin and HIS-C was further examined through in vitro assays. Further, the surface plasmon resonance (SPR) experiments confirmed the strong binding affinity, with a dissociation constant (KD) of 3.3 × 10
Indexed as
Identifiers
41263994What 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.