Evidence map›Paper›PMID 38030964›Full record

ReviewExperimental biology and medicine (Maywood, N.J.)2023

Penicillin-binding protein (PBP) inhibitor development: A 10-year chemical perspective.

Ariane F Bertonha, Caio C L Silva, Karina T Shirakawa, Daniel M Trindade, Andréa Dessen

Open access · greenAbstract readReview
In one paragraph

Review in Experimental biology and medicine (Maywood, N.J.), 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.

0numbers the graph read from it
0cells of the map it votes in
19citing papers in PubMed
3.2field-weighted citation impact, top 6% 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

19 citing papers in PubMed, 33 citations in OpenAlex.

  1. Article
  2. Bioactive Potential of Post-Distillation Residue ofPlants (Basel, Switzerland) · 2026
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  4. Review
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  16. Mechanisms of Antimicrobial Resistance inInfection and drug resistance · 2025
    Review
  17. Article
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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

5 authors at 3 institutions in 2 countries.

Ariane F BertonhaBrazilian Biosciences National Laboratory (LNBio), CNPEM, Campinas 13084-971, Brazil.ORCID 0000-0002-6651-8641
Caio C L SilvaBrazilian Biosciences National Laboratory (LNBio), CNPEM, Campinas 13084-971, Brazil.
Karina T ShirakawaBrazilian Biosciences National Laboratory (LNBio), CNPEM, Campinas 13084-971, Brazil.
Daniel M TrindadeBrazilian Biosciences National Laboratory (LNBio), CNPEM, Campinas 13084-971, Brazil.ORCID 0000-0002-8005-8784
Andréa DessenBrazilian Biosciences National Laboratory (LNBio), CNPEM, Campinas 13084-971, Brazil.ORCID 0000-0001-6487-4020
Brazilian Center for Research in Energy and Materials · BRCentre National de la Recherche Scientifique · FRUniversidade Estadual de Campinas (UNICAMP) · BR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Bacterial cell wall formation is essential for cellular survival and morphogenesis. The peptidoglycan (PG), a heteropolymer that surrounds the bacterial membrane, is a key component of the cell wall, and its multistep biosynthetic process is an attractive antibacterial development target. Penicillin-binding proteins (PBPs) are responsible for cross-linking PG stem peptides, and their central role in bacterial cell wall synthesis has made them the target of successful antibiotics, including β-lactams, that have been used worldwide for decades. Following the discovery of penicillin, several other compounds with antibiotic activity have been discovered and, since then, have saved millions of lives. However, since pathogens inevitably become resistant to antibiotics, the search for new active compounds is continuous. The present review highlights the ongoing development of inhibitors acting mainly in the transpeptidase domain of PBPs with potential therapeutic applications for the development of new antibiotic agents. Both the critical aspects of the strategy, design, and structure-activity relationships (SAR) are discussed, covering the main published articles over the last 10 years. Some of the molecules described display activities against main bacterial pathogens and could open avenues toward the development of new, efficient antibacterial drugs.

Indexed as

Anti-Bacterial Agentsbeta-LactamsBacteriaBacterial ProteinsPenicillin-Binding ProteinsPenicillinsAnti-Bacterial AgentsBacterial Proteinsbeta-LactamsPenicillin-Binding ProteinsPenicillinsinhibitorsnon-β-lactam inhibitorsPenicillin-binding proteinsubstrate analogsβ-lactams

Identifiers

PMID38030964
PMCPMC10723023
OpenAlexW4389180625

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.