ArticlemBio2021
The Penicillin-Binding Protein PbpP Is a Sensor of β-Lactams and Is Required for Activation of the Extracytoplasmic Function σ Factor σ
Article in mBio, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
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.
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.
Who cites it
13 citing papers in PubMed, 14 citations in OpenAlex.
- Differences in β-lactamase activity and carbapenem resistance among theAntimicrobial agents and chemotherapy · 2026Article
- The Dual Role of RsiP in Regulating Virulence and Host Adaptation inPathogens (Basel, Switzerland) · 2026Article
- The Quantum Paradox in Pharmaceutical Science: Understanding Without Comprehending-A Centennial Reflection.International journal of molecular sciences · 2025Review
- Unseen Enemy: Mechanisms of Multidrug Antimicrobial Resistance in Gram-Negative ESKAPE Pathogens.Antibiotics (Basel, Switzerland) · 2025Review
- Polyphenolic compounds in combating MDR periodontal pathogens: current research and future directions.Frontiers in pharmacology · 2025Review
- Molecular detection ofIn silico pharmacology · 2025Article
- The Bee Gut Microbiota: Bridging Infective Agents Potential in the One Health Context.International journal of molecular sciences · 2024Article
- Biological Function of Prophage-Related Gene Cluster ΔInternational journal of molecular sciences · 2024Article
- Antimicrobial Resistance: Is There a 'Light' at the End of the Tunnel?Antibiotics (Basel, Switzerland) · 2023Review
- The role of site-2-proteases in bacteria: a review on physiology, virulence, and therapeutic potential.microLife · 2023Review
- The two-component system ChvGI maintains cell envelope homeostasis in Caulobacter crescentus.PLoS genetics · 2022Article
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Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
β-Lactams are a class of antibiotics that target the synthesis of peptidoglycan, an essential component of the cell wall. β-Lactams inhibit the function of penicillin-binding proteins (PBPs), which form the cross-links between strands of peptidoglycan. Resistance to β-lactams complicates the treatment of bacterial infections. In recent years, the spread of β-lactam resistance has increased with growing intensity. Resistance is often conferred by β-lactamases, which inactivate β-lactams, or the expression of alternative β-lactam-resistant PBPs. σ
Indexed as
Identifiers
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.