Evidence map›Paper›PMID 39161148›Full record

ArticleInfectious disorders drug targets2025

Screening and Identification of Natural Compounds as Potential Inhibitors of Glutamate Racemase, an Emerging Drug Target of Food Pathogen

Rajnish Kumar, Samarth Gupta, Sujata Adhana, Anoushka Khanna, Sibasis Sahoo, Muniba Faiza, Renu Baweja, Archna Pandey, Avneesh Mittal, Uma Chaudhry

Abstract read
PubMed Publisher
In one paragraph

Article in Infectious disorders drug targets, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

0numbers the graph read from it
0cells of the map it votes in
0citing papers in PubMed
–field-weighted citation impact
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

0 citing papers in PubMed.

No citing paper in PubMed yet.

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

10 authors.

Rajnish KumarDepartment of Biomedical Science, Bhaskaracharya College of Applied Sciences, University of Delhi, Sector-2, Phase-I, Dwarka, New Delhi, 110075, India.ORCID 0000-0001-5330-5703
Samarth GuptaDepartment of Biomedical Science, Bhaskaracharya College of Applied Sciences, University of Delhi, Sector-2, Phase-I, Dwarka, New Delhi, 110075, India.ORCID 0000-0003-0734-0123
Sujata AdhanaDepartment of Biomedical Science, Bhaskaracharya College of Applied Sciences, University of Delhi, Sector-2, Phase-I, Dwarka, New Delhi, 110075, India.ORCID 0000-0003-4866-0115
Anoushka KhannaDepartment of Biomedical Science, Bhaskaracharya College of Applied Sciences, University of Delhi, Sector-2, Phase-I, Dwarka, New Delhi, 110075, India.ORCID 0000-0001-6601-8762
Sibasis SahooDepartment of Biomedical Science, Bhaskaracharya College of Applied Sciences, University of Delhi, Sector-2, Phase-I, Dwarka, New Delhi, 110075, India.ORCID 0000-0002-6998-0911
Muniba FaizaDepartment of Biology, Nazarbayev University, Qabanbay Batyr Avenue, Nur-Sultan, Kazakhstan.ORCID 0000-0003-4711-4075
Renu BawejaDepartment of Biochemistry, Shivaji College, University of Delhi, Mahatma Gandhi Rd, Shivaji Enclave, Raja Garden, Delhi, 110027, India.ORCID 0000-0001-9868-2449
Archna PandeyDepartment of Biomedical Science, Acharya Narendra Dev College, University of Delhi, Govindpuri, KalkaJi, New Delhi, 110019, India.ORCID 0000-0003-1323-9574
Avneesh MittalDepartment of Electronics, Bhaskaracharya College of Applied Sciences, University of Delhi, Sector- 2, Phase-I, Dwarka, 110075, New Delhi, India.ORCID 0000-0002-5819-4392
Uma ChaudhryDepartment of Biomedical Science, Bhaskaracharya College of Applied Sciences, University of Delhi, Sector-2, Phase-I, Dwarka, New Delhi, 110075, India.ORCID 0000-0002-0897-2926

Funding

Department of Science and Technology (DST), Delhi, India CO/A/FP/G62/2019-GIndian Council of Medical Research (ICMR), India 2021-6434
6 · The paper itself

Abstract

backgroundShiga Toxin-Producing Escherichia coli (

objectiveThis study aims to evaluate Glutamate Racemase (MurI protein) of the food-pathogenic

methodsUsing computational tools, the study identified inhibitor binding sites on EC MurI and identified relevant inhibitors capable of binding to these sites. Molecular docking techniques were employed to assess potential hits, and selected compounds were further analyzed for their structural activity and binding affinity to the protein.

resultsThe results of the study revealed that Frigocyclinone and Deslanoside, exhibited the best binding affinity with EC-MurI. Subsequent molecular dynamic (MD) simulations of the selected complexes indicated that both compounds were stable. This suggests that Frigocyclinone and Deslanoside have the potential to serve as potent inhibitors of EC-MurI.

conclusionIn summary, this study highlights the urgent need for alternative therapies against food-pathogenic

Indexed as

Amino Acid IsomerasesAnti-Bacterial AgentsEscherichia coli O157Molecular Docking SimulationBinding SitesBiological ProductsComputer SimulationDrug Resistance, BacterialEnzyme InhibitorsEscherichia coli InfectionsEscherichia coli ProteinsFoodborne DiseasesFood MicrobiologyHumansMolecular Dynamics SimulationAmino Acid IsomerasesAnti-Bacterial AgentsBiological ProductsEnzyme InhibitorsEscherichia coli Proteinsglutamate racemaseantibiotic resistance.dockingEC-MurIglutamate racemaseinhibitorspeptidoglycanShiga toxin-producing E.coli

Identifiers

PMID39161148

What OpenQuestion holds

Textmetadata
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.