Evidence map›Paper›PMID 36788654›Full record

ReviewBiomolecules & therapeutics2023

Structural Insights for β-Lactam Antibiotics.

Dogyeoung Kim, Sumin Kim, Yongdae Kwon, Yeseul Kim, Hyunjae Park, Kiwoong Kwak, Hyeonmin Lee, Jung Hun Lee, Kyung-Min Jang, Donghak Kim and 2 more

Open access · hybridAbstract readReview
In one paragraph

Review in Biomolecules & therapeutics, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.

0numbers the graph read from it
0cells of the map it votes in
27citing papers in PubMed
5.0field-weighted citation impact, top 3% 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

27 citing papers in PubMed, 52 citations in OpenAlex.

  1. Article
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  4. Article
  5. Review
  6. Review
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  8. Review
  9. Review
  10. Article
  11. Article
  12. Review
  13. Review
  14. Development andRSC advances · 2025
    Article
  15. Phenotypic and Genotypic Characterization of ESBL andAntibiotics (Basel, Switzerland) · 2025
    Article
  16. Article
  17. CombattingAntibiotics (Basel, Switzerland) · 2025
    Review
  18. Article
  19. 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

12 authors at 2 institutions in 1 country.

Dogyeoung KimDepartment of Biological Sciences, Konkuk University, Seoul 05029, Republic of Korea.
Sumin KimDepartment of Biological Sciences, Konkuk University, Seoul 05029, Republic of Korea.
Yongdae KwonDepartment of Biological Sciences, Konkuk University, Seoul 05029, Republic of Korea.
Yeseul KimDepartment of Biological Sciences, Konkuk University, Seoul 05029, Republic of Korea.
Hyunjae ParkDepartment of Biological Sciences, Konkuk University, Seoul 05029, Republic of Korea.
Kiwoong KwakDepartment of Biological Sciences, Konkuk University, Seoul 05029, Republic of Korea.
Hyeonmin LeeDepartment of Biological Sciences, Konkuk University, Seoul 05029, Republic of Korea.
Jung Hun LeeNational Leading Research Laboratory of Drug Resistance Proteomics, Department of Biological Sciences, Myongji University, Yongin 17058, Republic of Korea.
Kyung-Min JangNational Leading Research Laboratory of Drug Resistance Proteomics, Department of Biological Sciences, Myongji University, Yongin 17058, Republic of Korea.
Donghak KimDepartment of Biological Sciences, Konkuk University, Seoul 05029, Republic of Korea.
Sang Hee LeeNational Leading Research Laboratory of Drug Resistance Proteomics, Department of Biological Sciences, Myongji University, Yongin 17058, Republic of Korea.
Lin-Woo KangDepartment of Biological Sciences, Konkuk University, Seoul 05029, Republic of Korea.
Konkuk University · KRMyongji University · KR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Antibiotic resistance has emerged as a global threat to modern healthcare systems and has nullified many commonly used antibiotics. β-Lactam antibiotics are among the most successful and occupy approximately two-thirds of the prescription antibiotic market. They inhibit the synthesis of the peptidoglycan layer in the bacterial cell wall by mimicking the D-Ala-D-Ala in the pentapeptide crosslinking neighboring glycan chains. To date, various β-lactam antibiotics have been developed to increase the spectrum of activity and evade drug resistance. This review emphasizes the three-dimensional structural characteristics of β-lactam antibiotics regarding the overall scaffold, working mechanism, chemical diversity, and hydrolysis mechanism by β-lactamases. The structural insight into various β-lactams will provide an in-depth understanding of the antibacterial efficacy and susceptibility to drug resistance in multidrug-resistant bacteria and help to develop better β-lactam antibiotics and inhibitors.

Indexed as

Antibiotic resistanceAntibioticsMetallo-β-lactamasesPeptidoglycanSerine β-lactamasesβ-Lactams

Identifiers

PMID36788654
PMCPMC9970833
OpenAlexW4320857705

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC
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.