Evidence map›Paper›PMID 29680579›Full record

ReviewTrends in pharmacological sciences2018

The Continuing Challenge of Metallo-β-Lactamase Inhibition: Mechanism Matters.

Lin-Cheng Ju, Zishuo Cheng, Walter Fast, Robert A Bonomo, Michael W Crowder

Abstract readReview
In one paragraph

Review in Trends in pharmacological sciences, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 73 papers.

0numbers the graph read from it
0cells of the map it votes in
73citing 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

73 citing papers in PubMed.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Review
  6. Article
  7. Reviving Furosemide as a Metallo-β-Lactamase Inhibitor against MDRJournal of microbiology and biotechnology · 2025
    Article
  8. Article
  9. CombattingAntibiotics (Basel, Switzerland) · 2025
    Review
  10. Article
  11. Review
  12. Overcoming beta-lactam resistance inFrontiers in cellular and infection microbiology · 2025
    Article
  13. Review
  14. Approachable Synthetic Methodologies for Second-GenerationPharmaceuticals (Basel, Switzerland) · 2024
    Review
  15. Review
  16. Article
  17. Article
  18. Article
  19. Article
  20. Article

13 more citing papers are in PubMed but not listed here.

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

5 authors.

Lin-Cheng JuDepartment of Urology, Shengjing Hospital of China Medical University, Shenyang, Liaoning 110004, PR China; Department of Chemistry and Biochemistry, Miami University, Oxford, OH 45056, USA. Electronic address: julc@sj-hospital.org.
Zishuo ChengDepartment of Chemistry and Biochemistry, Miami University, Oxford, OH 45056, USA.
Walter FastDivision of Chemical Biology and Medicinal Chemistry, College of Pharmacy, University of Texas, Austin, TX 78712, USA.
Robert A BonomoResearch Services, Louis Stokes Cleveland Department of Veterans Affairs Medical Center, Cleveland, OH 44106, USA; Departments of Medicine, Pharmacology, Molecular Biology and Microbiology, Biochemistry, Proteomics, and Bioinformatics and the CWRU-Cleveland VAMC Center for Antimicrobial Resistance and Epidemiology, Cleveland, OH 44106, USA.
Michael W CrowderDepartment of Chemistry and Biochemistry, Miami University, Oxford, OH 45056, USA.

Funding

Understanding B-Lactam Resistance in Acinetobacter baumanniiR01AI072219 · NIAID · CASE WESTERN RESERVE UNIVERSITY · PI ROBERT A. BONOMO, Philip N. Rather · 2007 to 2026
$6.6M
Understanding ceftazidime resistance in SHV B-LactamasesR01AI063517 · NIAID · CASE WESTERN RESERVE UNIVERSITY · PI BONOMO, ROBERT A. · 2005 to 2023
$4.9M
A Mechanism-Based Approach to Metallo-beta-Lactamase InhibitionR01AI100560 · NIAID · CASE WESTERN RESERVE UNIVERSITY · PI BONOMO, ROBERT A., SPENCER, JAMES · 2012 to 2022
$4.4M
Developing Metallo-Beta-Lactamase InhibitorsR01GM111926 · NIGMS · UNIVERSITY OF TEXAS AT AUSTIN · PI BONOMO, ROBERT A., COHEN, SETH M · 2015 to 2019
$2.3M
NIAID NIH HHS R01 AI063517NIAID NIH HHS R01 AI072219NIAID NIH HHS R01 AI100560NIGMS NIH HHS R01 GM111926
6 · The paper itself

Abstract

Metallo-β-lactamases (MBLs) are a significant clinical problem because they hydrolyze and inactivate nearly all β-lactam-containing antibiotics. These 'lifesaving drugs' constitute >50% of the available contemporary antibiotic arsenal. Despite the global spread of MBLs, MBL inhibitors have not yet appeared in clinical trials. Most MBL inhibitors target active site zinc ions and vary in mechanism from ternary complex formation to metal ion stripping. Importantly, differences in mechanism can impact pharmacology in terms of reversibility, target selectivity, and structure-activity relationship interpretation. This review surveys the mechanisms of MBL inhibitors and describes methods that determine the mechanism of inhibition to guide development of future therapeutics.

Indexed as

AnimalsAnti-Bacterial AgentsBacterial Proteinsbeta-Lactamase Inhibitorsbeta-LactamasesCatalytic DomainDrug Resistance, MicrobialHumansModels, MolecularStructure-Activity RelationshipAnti-Bacterial AgentsBacterial Proteinsbeta-Lactamase Inhibitorsbeta-Lactamasesinhibitormechanismmetallo-β-lactamasespectroscopy

Identifiers

PMID29680579
PMCPMC6005755

What OpenQuestion holds

Textmetadata
LicenceTDM
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.