ArticleThe Journal of biological chemistry2014
Structural insights into the lipoprotein outer membrane regulator of penicillin-binding protein 1B.
Article in The Journal of biological chemistry, 2014. 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
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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.
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.
- SanA Plays a Role in Peptidoglycan Integrity in Escherichia coli.Molecular microbiology · 2026Article
- Clinical characteristics, specific resistance patterns, and molecular mechanisms of carbapenem-resistantFrontiers in cellular and infection microbiology · 2025Article
- Structural diversity, bioactivity, and biosynthesis of phosphoglycolipid family antibiotics: Recent advances.BBA advances · 2022Article
- CryoEM structure of the antibacterial target PBP1b at 3.3 Å resolution.Nature communications · 2021Article
- Review
- Structure of the Peptidoglycan Synthase Activator LpoP in Pseudomonas aeruginosa.Structure (London, England : 1993) · 2020Article
- Cell-Wall Recycling of the Gram-Negative Bacteria and the Nexus to Antibiotic Resistance.Chemical reviews · 2018Review
- Conserved mechanism of cell-wall synthase regulation revealed by the identification of a new PBP activator inProceedings of the National Academy of Sciences of the United States of America · 2018Article
- Structural analyses of theThe Journal of biological chemistry · 2017Article
- Structural Insights into Inhibition of Escherichia coli Penicillin-binding Protein 1B.The Journal of biological chemistry · 2017Article
- Biochemical and Structural Analysis of a Novel Esterase from Caulobacter crescentus related to Penicillin-Binding Protein (PBP).Scientific reports · 2016Article
- Cofactor bypass variants reveal a conformational control mechanism governing cell wall polymerase activity.Proceedings of the National Academy of Sciences of the United States of America · 2016Article
- Activities and regulation of peptidoglycan synthases.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2015Review
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.
Funding
Abstract
In bacteria, the synthesis of the protective peptidoglycan sacculus is a dynamic process that is tightly regulated at multiple levels. Recently, the lipoprotein co-factor LpoB has been found essential for the in vivo function of the major peptidoglycan synthase PBP1b in Enterobacteriaceae. Here, we reveal the crystal structures of Salmonella enterica and Escherichia coli LpoB. The LpoB protein can be modeled as a ball and tether, consisting of a disordered N-terminal region followed by a compact globular C-terminal domain. Taken together, our structural data allow us to propose new insights into LpoB-mediated regulation of peptidoglycan synthesis.
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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.