ArticleNature communications2022
A unique class of Zn
Article in Nature communications, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.
What it found
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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.
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Who cites it
15 citing papers in PubMed, 27 citations in OpenAlex.
- Article
- Clostridioides difficile pathogenesis and control.Nature reviews. Microbiology · 2026Review
- Molecular dissection of Class A PBP function uncovers novel features of the non-canonical Clostridioides difficile divisome complex.PLoS genetics · 2025Article
- Molecular dissection of Class A PBP function uncovers novel features of the non-canonicalbioRxiv : the preprint server for biology · 2025Article
- The l,d-transpeptidation pathway is inhibited by antibiotics of the β-lactam class iniScience · 2025Article
- Features and rhizosphere colonization strategies ofFrontiers in microbiology · 2025Article
- Virulence factors, antibiotic susceptibility and sequence type distribution of hospital-associated Clostridioides difficile isolates in Israel, 2020-2022.Scientific reports · 2024Article
- Identification of a family of peptidoglycan transpeptidases reveals thatProceedings of the National Academy of Sciences of the United States of America · 2024Article
- Article
- Current and Ongoing Developments in TargetingMicroorganisms · 2024Review
- Review
- Drug Discovery in the Field of β-Lactams: An Academic Perspective.Antibiotics (Basel, Switzerland) · 2024Review
- Clostridioides difficile Sporulation.Advances in experimental medicine and biology · 2024Review
- Diversification of division mechanisms in endospore-forming bacteria revealed by analyses of peptidoglycan synthesis in Clostridioides difficile.Nature communications · 2023Article
- A conserved zinc-binding site inProceedings of the National Academy of Sciences of the United States of America · 2023Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
19 authors at 3 institutions in 1 country.
Funding
Abstract
Treatment with β-lactam antibiotics, particularly cephalosporins, is a major risk factor for Clostridioides difficile infection. These broad-spectrum antibiotics irreversibly inhibit penicillin-binding proteins (PBPs), which are serine-based enzymes that assemble the bacterial cell wall. However, C. difficile has four different PBPs (PBP1-3 and SpoVD) with various roles in growth and spore formation, and their specific links to β-lactam resistance in this pathogen are underexplored. Here, we show that PBP2 (known to be essential for vegetative growth) is the primary bactericidal target for β-lactams in C. difficile. PBP2 is insensitive to cephalosporin inhibition, and this appears to be the main basis for cephalosporin resistance in this organism. We determine crystal structures of C. difficile PBP2, alone and in complex with β-lactams, revealing unique features including ligand-induced conformational changes and an active site Zn
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What 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.