Evidence map›Paper›PMID 40362418›Full record

ArticleInternational journal of molecular sciences2025

Discovery of Boronic Acids-Based β-Lactamase Inhibitors Through In Situ Click Chemistry.

Nicolò Santi, Alessandra Piccirilli, Federico Corsini, Magdalena A Taracila, Mariagrazia Perilli, Robert A Bonomo, Francesco Fini, Fabio Prati, Emilia Caselli

Abstract read
In one paragraph

Article in International journal of molecular sciences, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.

0numbers the graph read from it
0cells of the map it votes in
3citing 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

3 citing papers in PubMed.

  1. Article
  2. Article
  3. Article
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

9 authors.

Nicolò SantiDepartment of Life Sciences, Università degli Studi di Modena e Reggio Emilia (UNIMORE), via Campi 103, 41125 Modena, Italy.ORCID 0000-0001-6361-5457
Alessandra PiccirilliDepartment of Biotechnological and Applied Clinical Sciences, Università degli Studi dell'Aquila, via Vetoio, 67100 L'Aquila, Italy.
Federico CorsiniDepartment of Life Sciences, Università degli Studi di Modena e Reggio Emilia (UNIMORE), via Campi 103, 41125 Modena, Italy.
Magdalena A TaracilaDepartment of Medicine, Case Western Reserve University School of Medicine, Cleveland, OH 44106, USA.
Mariagrazia PerilliDepartment of Biotechnological and Applied Clinical Sciences, Università degli Studi dell'Aquila, via Vetoio, 67100 L'Aquila, Italy.ORCID 0000-0001-7370-1455
Robert A BonomoDepartment of Medicine, Case Western Reserve University School of Medicine, Cleveland, OH 44106, USA.ORCID 0000-0002-3299-894X
Francesco FiniDepartment of Life Sciences, Università degli Studi di Modena e Reggio Emilia (UNIMORE), via Campi 103, 41125 Modena, Italy.ORCID 0000-0003-2555-9313
Fabio PratiDepartment of Life Sciences, Università degli Studi di Modena e Reggio Emilia (UNIMORE), via Campi 103, 41125 Modena, Italy.ORCID 0000-0002-0650-9540
Emilia CaselliDepartment of Life Sciences, Università degli Studi di Modena e Reggio Emilia (UNIMORE), via Campi 103, 41125 Modena, Italy.ORCID 0000-0002-7248-9453

Funding

Understanding B-Lactam Resistance in Acinetobacter baumanniiR01AI072219 · NIAID · CASE WESTERN RESERVE UNIVERSITY · PI ROBERT A. BONOMO, Philip N. Rather · 2007 to 2026
$6.6M
Cleveland Department of Veteran Affair I01BX001974European Union 101068156Ministero dell'Istruzione e del Merito 2022WBPFSCNIH HHS R01 AI072219
6 · The paper itself

Abstract

In this study, we evaluated in situ click chemistry as a platform for discovering boronic acid-based β-lactamase inhibitors (BLIs). Unlike conventional drug discovery approaches requiring multi-step synthesis, protection strategies, and extensive screening, the in situ method can allow for the generation and identification of potent β-lactamase inhibitors in a rapid, economic, and efficient way. Using KPC-2 (class A carbapenemase) and AmpC (class C cephalosporinase) as templates, we demonstrated their ability to catalyse azide-alkyne cycloaddition, facilitating the formation of triazole-based β-lactamase inhibitors. Initial screening of various β-lactamases and boronic warheads identified compound

Indexed as

Anti-Bacterial Agentsbeta-Lactamase Inhibitorsbeta-LactamasesBoronic AcidsClick ChemistryDrug DiscoveryBacterial ProteinsTriazolesAnti-Bacterial AgentsBacterial Proteinsbeta-Lactamase Inhibitorsbeta-LactamasesBoronic AcidsTriazolesantimicrobial resistanceBATSIbeta-lactamase inhibitorsboronic acidin situ click chemistryKTGS

Identifiers

PMID40362418
PMCPMC12071365

What OpenQuestion holds

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LicenceCC BY
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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.