Evidence map›Paper›PMID 33672408›Full record

ArticlePharmaceuticals (Basel, Switzerland)2021

Discovery of Substituted (2-Aminooxazol-4-yl)Isoxazole-3-carboxylic Acids as Inhibitors of Bacterial Serine Acetyltransferase in the Quest for Novel Potential Antibacterial Adjuvants.

Joana Magalhães, Nina Franko, Samanta Raboni, Giannamaria Annunziato, Päivi Tammela, Agostino Bruno, Stefano Bettati, Stefano Armao, Costanza Spadini, Clotilde Silvia Cabassi and 4 more

Open access · goldAbstract read
In one paragraph

Article in Pharmaceuticals (Basel, Switzerland), 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.

0numbers the graph read from it
0cells of the map it votes in
7citing papers in PubMed
0.7field-weighted citation impact, top 32% 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

7 citing papers in PubMed, 13 citations in OpenAlex.

  1. Serine Acetyltransferase fromInternational journal of molecular sciences · 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

14 authors at 2 institutions in 3 countries.

Joana MagalhãesP4T Group, Department of Food and Drug, University of Parma, 43124 Parma, Italy.
Nina FrankoLaboratory of Biochemistry and Molecular Biology, Department of Food and Drug, University of Parma, 43124 Parma, Italy.
Samanta RaboniLaboratory of Biochemistry and Molecular Biology, Department of Food and Drug, University of Parma, 43124 Parma, Italy.
Giannamaria AnnunziatoP4T Group, Department of Food and Drug, University of Parma, 43124 Parma, Italy.ORCID 0000-0001-9629-6966
Päivi TammelaDrug Research Program, Division of Pharmaceutical Biosciences, Faculty of Pharmacy, University of Helsinki, P.O. Box 56 (Viikinkaari 5 E), FI-00014 Helsinki, Finland.ORCID 0000-0003-4697-8066
Agostino BrunoP4T Group, Department of Food and Drug, University of Parma, 43124 Parma, Italy.
Stefano BettatiInstitute of Biophysics, CNR, 56124 Pisa, Italy.ORCID 0000-0001-6787-0594
Stefano ArmaoLaboratory of Biochemistry and Molecular Biology, Department of Food and Drug, University of Parma, 43124 Parma, Italy.
Costanza SpadiniOperative Unit of Animals Infectious Diseases, Department of Veterinary Science, University of Parma, Via del Taglio 10, 43126 Parma, Italy.
Clotilde Silvia CabassiOperative Unit of Animals Infectious Diseases, Department of Veterinary Science, University of Parma, Via del Taglio 10, 43126 Parma, Italy.ORCID 0000-0002-1936-9858
Andrea MozzarelliLaboratory of Biochemistry and Molecular Biology, Department of Food and Drug, University of Parma, 43124 Parma, Italy.ORCID 0000-0003-3762-0062
Marco PieroniP4T Group, Department of Food and Drug, University of Parma, 43124 Parma, Italy.ORCID 0000-0001-9190-3712
Barbara CampaniniLaboratory of Biochemistry and Molecular Biology, Department of Food and Drug, University of Parma, 43124 Parma, Italy.ORCID 0000-0003-0359-0627
Gabriele CostantinoP4T Group, Department of Food and Drug, University of Parma, 43124 Parma, Italy.
University of Parma · ITUniversity of Helsinki · FI

Funding

Academy of Finland 277001
6 · The paper itself

Abstract

Many bacteria and actinomycetales use L-cysteine biosynthesis to increase their tolerance to antibacterial treatment and establish a long-lasting infection. In turn, this might lead to the onset of antimicrobial resistance that currently represents one of the most menacing threats to public health worldwide. The biosynthetic machinery required to synthesise L-cysteine is absent in mammals; therefore, its exploitation as a drug target is particularly promising. In this article, we report a series of inhibitors of

Indexed as

adjuvant therapiesantimicrobial resistancecysteine biosynthesisnon-essential targetsserine acetyltransferase

Identifiers

PMID33672408
PMCPMC7931047
OpenAlexW3132692482

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.