Evidence map›Paper›PMID 22815485›Full record

ArticleThe Journal of biological chemistry2012

Structural insights into the anti-methicillin-resistant Staphylococcus aureus (MRSA) activity of ceftobiprole.

Andrew L Lovering, Michael C Gretes, Susan S Safadi, Franck Danel, Liza de Castro, Malcolm G P Page, Natalie C J Strynadka

Abstract read
In one paragraph

Article in The Journal of biological chemistry, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 50 papers.

0numbers the graph read from it
0cells of the map it votes in
50citing papers in PubMed
–field-weighted citation impact
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

50 citing papers in PubMed.

  1. Trial
  2. A phase 3 randomized double-blind comparison of ceftobiprole medocaril versus ceftazidime plus linezolid for the treatment of hospital-acquired pneumonia.Clinical infectious diseases : an official publication of the Infectious Diseases Society of America · 2014
    Trial
  3. Article
  4. Challenges and opportunities in the management of severe pneumonia. Key concepts from the Seventh Annual Meeting of Spanish Experts 2025.Revista espanola de quimioterapia : publicacion oficial de la Sociedad Espanola de Quimioterapia · 2026
    Review
  5. Article
  6. Ceftobiprole activity against multidrug-resistantAntimicrobial agents and chemotherapy · 2025
    Article
  7. Article
  8. Article
  9. Article
  10. Review
  11. The depsidones from marine sponge-derived fungusSaudi pharmaceutical journal : SPJ : the official publication of the Saudi Pharmaceutical Society · 2023
    Article
  12. Article
  13. Article
  14. Ampicillin and Ceftobiprole Combination for the Treatment ofAntibiotics (Basel, Switzerland) · 2023
    Article
  15. Article
  16. Carbazole Derivatives as Potential Antimicrobial Agents.Molecules (Basel, Switzerland) · 2022
    Review
  17. Identification ofAntibiotics (Basel, Switzerland) · 2022
    Article
  18. Article
  19. Phytochemical Investigation ofMolecules (Basel, Switzerland) · 2022
    Article
  20. Methicillin-ResistantInternational journal of microbiology · 2022
    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

7 authors.

Andrew L LoveringDepartment of Biochemistry and Molecular Biology and the Center for Blood Research, University of British Columbia, Vancouver, British Columbia, Canada.
Michael C Gretes
Susan S Safadi
Franck Danel
Liza de Castro
Malcolm G P Page
Natalie C J Strynadka

Funding

Canadian Institutes of Health ResearchHoward Hughes Medical Institute
6 · The paper itself

Abstract

Methicillin-resistant Staphylococcus aureus (MRSA) is an antibiotic-resistant strain of S. aureus afflicting hospitals and communities worldwide. Of greatest concern is its development of resistance to current last-line-of-defense antibiotics; new therapeutics are urgently needed to combat this pathogen. Ceftobiprole is a recently developed, latest generation cephalosporin and has been the first to show activity against MRSA by inhibiting essential peptidoglycan transpeptidases, including the β-lactam resistance determinant PBP2a, from MRSA. Here we present the structure of the complex of ceftobiprole bound to PBP2a. This structure provides the first look at the molecular details of an effective β-lactam-resistant PBP interaction, leading to new insights into the mechanism of ceftobiprole efficacy against MRSA.

Indexed as

Anti-Bacterial Agentsbeta-LactamsCalorimetry, Differential ScanningCatalytic DomainCephalosporinsCrystallography, X-RayEnzyme InhibitorsKineticsMethicillin-Resistant Staphylococcus aureusModels, MolecularMolecular ConformationProtein BindingProtein ConformationStaphylococcal InfectionsStaphylococcus aureusAnti-Bacterial Agentsbeta-LactamsceftobiproleCephalosporinsEnzyme Inhibitors

Identifiers

PMID22815485
PMCPMC3442540

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.