Evidence map›Paper›PMID 31747090›Full record

ReviewProtein science : a publication of the Protein Society2020

Constructing and deconstructing the bacterial cell wall.

Jed F Fisher, Shahriar Mobashery

Open access · bronzeAbstract readReview
In one paragraph

Review in Protein science : a publication of the Protein Society, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 37 papers.

0numbers the graph read from it
0cells of the map it votes in
37citing papers in PubMed
2.0field-weighted citation impact, top 13% 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

37 citing papers in PubMed, 85 citations in OpenAlex.

  1. Review
  2. Article
  3. TheInternational journal of molecular sciences · 2026
    Review
  4. Methicillin-ResistantMicroorganisms · 2026
    Review
  5. Article
  6. Review
  7. Review
  8. Article
  9. Review
  10. Article
  11. Article
  12. Article
  13. Review
  14. Review
  15. Article
  16. Article
  17. Review
  18. Review
  19. Challenges and shortcomings of antibacterial discovery projects.Clinical microbiology and infection : the official publication of the European Society of Clinical Microbiology and Infectious Diseases · 2023
    Article
  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

2 authors at 1 institution in 1 country.

Jed F FisherDepartment of Chemistry and Biochemistry, University of Notre Dame, South Bend, Indiana.
Shahriar MobasheryDepartment of Chemistry and Biochemistry, University of Notre Dame, South Bend, Indiana.ORCID 0000-0002-7695-7883
University of Notre Dame · US

Funding

Inducible Antibiotic Resistance in Methicillin-Resistant Staphylococcus AureusR01AI104987 · NIAID · UNIVERSITY OF NOTRE DAME · PI Shahriar Mobashery · 2013 to 2026
$7.3M
Cell-Wall Recycling and Nexus to Antibiotic ResistanceR35GM131685 · NIGMS · UNIVERSITY OF NOTRE DAME · PI MOBASHERY, SHAHRIAR · 2019 to 2023
$1.9M
NIAID NIH HHS R01 AI104987NIGMS NIH HHS R35 GM131685NIH HHS AI104987NIH HHS GM131685
6 · The paper itself

Abstract

The history of modern medicine cannot be written apart from the history of the antibiotics. Antibiotics are cytotoxic secondary metabolites that are isolated from Nature. The antibacterial antibiotics disproportionately target bacterial protein structure that is distinct from eukaryotic protein structure, notably within the ribosome and within the pathways for bacterial cell-wall biosynthesis (for which there is not a eukaryotic counterpart). This review focuses on a pre-eminent class of antibiotics-the β-lactams, exemplified by the penicillins and cephalosporins-from the perspective of the evolving mechanisms for bacterial resistance. The mechanism of action of the β-lactams is bacterial cell-wall destruction. In the monoderm (single membrane, Gram-positive staining) pathogen Staphylococcus aureus the dominant resistance mechanism is expression of a β-lactam-unreactive transpeptidase enzyme that functions in cell-wall construction. In the diderm (dual membrane, Gram-negative staining) pathogen Pseudomonas aeruginosa a dominant resistance mechanism (among several) is expression of a hydrolytic enzyme that destroys the critical β-lactam ring of the antibiotic. The key sensing mechanism used by P. aeruginosa is monitoring the molecular difference between cell-wall construction and cell-wall deconstruction. In both bacteria, the resistance pathways are manifested only when the bacteria detect the presence of β-lactams. This review summarizes how the β-lactams are sensed and how the resistance mechanisms are manifested, with the expectation that preventing these processes will be critical to future chemotherapeutic control of multidrug resistant bacteria.

Indexed as

Anti-Bacterial Agentsbeta-LactamsCell WallDrug Resistance, BacterialGram-Negative BacteriaGram-Positive BacteriaMicrobial Sensitivity TestsAnti-Bacterial Agentsbeta-LactamsAmpCAmpRlytic transglycosylasesmuropeptidespenicillin-binding proteinspeptidoglycanβ-lactamases

Identifiers

PMID31747090
PMCPMC7021008
OpenAlexW2977866289

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.