Evidence map›Paper›PMID 30355734›Full record

ArticleThe Journal of biological chemistry2018

The structures of penicillin-binding protein 4 (PBP4) and PBP5 from

Thomas M Moon, Éverton D D'Andréa, Christopher W Lee, Alexei Soares, Jean Jakoncic, Charlene Desbonnet, Monica Garcia-Solache, Lou B Rice, Rebecca Page, Wolfgang Peti

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 39 papers.

0numbers the graph read from it
0cells of the map it votes in
39citing papers in PubMed
1.8field-weighted citation impact, top 16% 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

39 citing papers in PubMed, 75 citations in OpenAlex.

  1. Observational
  2. Article
  3. Microbiology (Reading, England) · 2026
    Article
  4. Article
  5. Article
  6. Review
  7. Review
  8. Article
  9. Article
  10. Review
  11. Article
  12. Article
  13. Article
  14. Potential Antibacterial of Leaf Sirih Merah AgainstCombinatorial chemistry & high throughput screening · 2025
    Article
  15. Article
  16. Conjugation of Polycationic Peptides Extends the Efficacy Spectrum of β-Lactam Antibiotics.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2024
    Article
  17. Article
  18. The Genetic Landscape of Antimicrobial Resistance Genes inAntibiotics (Basel, Switzerland) · 2024
    Article
  19. Review
  20. 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

10 authors at 3 institutions in 1 country.

Thomas M MoonFrom the Department of Chemistry and Biochemistry, College of Medicine, University of Arizona, Tucson, Arizona 85721.ORCID 0000-0003-1568-8808
Éverton D D'AndréaFrom the Department of Chemistry and Biochemistry, College of Medicine, University of Arizona, Tucson, Arizona 85721.
Christopher W Leethe Department of Molecular Pharmacology, Physiology, and Biotechnology, Brown University, Providence, Rhode Island 02912.
Alexei SoaresPhoton Sciences, Brookhaven National Laboratory, Upton, New York 11973, and.
Jean JakoncicPhoton Sciences, Brookhaven National Laboratory, Upton, New York 11973, and.
Charlene Desbonnetthe Departments of Medicine and Microbiology and Immunology, Warren Alpert School of Medicine of Brown University, Providence, Rhode Island 02903.
Monica Garcia-Solachethe Departments of Medicine and Microbiology and Immunology, Warren Alpert School of Medicine of Brown University, Providence, Rhode Island 02903.
Lou B Ricethe Departments of Medicine and Microbiology and Immunology, Warren Alpert School of Medicine of Brown University, Providence, Rhode Island 02903.
Rebecca PageFrom the Department of Chemistry and Biochemistry, College of Medicine, University of Arizona, Tucson, Arizona 85721.
Wolfgang PetiFrom the Department of Chemistry and Biochemistry, College of Medicine, University of Arizona, Tucson, Arizona 85721, wolfgangpeti@email.arizona.edu.
Brown University · USUniversity of Arizona · USBrookhaven National Laboratory · US

Funding

X-ray Absorption Spectroscopy (XAS) pp.711-759P41GM103393 · NIGMS · STANFORD UNIVERSITY · PI HODGSON, KEITH O · 2012 to 2019
$30.6M
Mechanism and activity of beta-lactam resistant enzymes in E. faecium and E. faecalisR01AI141522 · NIAID · RHODE ISLAND HOSPITAL · PI Wolfgang Peti, Louis B. Rice · 2019 to 2026
$5.1M
Cell wall synthesis enzymes and beta-lactam resistance in Enterococcus faeciumR56AI045626 · NIAID · RHODE ISLAND HOSPITAL · PI RICE, LOUIS B. · 2016 to 2016
$609k
NIAID NIH HHS R01 AI141522NIAID NIH HHS R56 AI045626NIGMS NIH HHS P41 GM103393
6 · The paper itself

Abstract

The final steps of cell-wall biosynthesis in bacteria are carried out by penicillin-binding proteins (PBPs), whose transpeptidase domains form the cross-links in peptidoglycan chains that define the bacterial cell wall. These enzymes are the targets of β-lactam antibiotics, as their inhibition reduces the structural integrity of the cell wall. Bacterial resistance to antibiotics is a rapidly growing concern; however, the structural underpinnings of PBP-derived antibiotic resistance are poorly understood. PBP4 and PBP5 are low-affinity, class B transpeptidases that confer antibiotic resistance to

Indexed as

beta-Lactam ResistanceAcylationBacterial ProteinsCarbapenemsCatalytic DomainCephalosporinsEnterococcus faecalisEnterococcus faeciumMicrobial Sensitivity TestsPenicillin-Binding ProteinsPenicillinsProtein ConformationProtein DomainsProtein IsoformsBacterial ProteinsCarbapenemsCephalosporinsPenicillin-Binding ProteinsPenicillinsProtein Isoformsantibiotic actionantibiotic resistancecrystal structureEnterococcusenzyme structureESKAPE pathogenpenicillin-binding proteinstranspeptidaseβ-lactam

Identifiers

PMID30355734
PMCPMC6290140
OpenAlexW2898356850

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.