Evidence map›Paper›PMID 38488135›Full record

ReviewJournal of enzyme inhibition and medicinal chemistry2024

Elucidation of critical chemical moieties of metallo-β-lactamase inhibitors and prioritisation of target metallo-β-lactamases.

Jung Hun Lee, Sang-Gyu Kim, Kyung-Min Jang, Kyoungmin Shin, Hyeonku Jin, Dae-Wi Kim, Byeong Chul Jeong, Sang Hee Lee

Abstract readReview
In one paragraph

Review in Journal of enzyme inhibition and medicinal chemistry, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.

0numbers the graph read from it
0cells of the map it votes in
1citing 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

1 citing paper in PubMed.

  1. 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

8 authors.

Jung Hun LeeNational Leading Research Laboratory of Drug Resistance Proteomics, Department of Biological Sciences, Myongji University, Yongin, Republic of Korea.ORCID 0000-0001-5504-4033
Sang-Gyu KimDivision of Life Sciences, Jeonbuk National University, Jeonju, Republic of Korea.ORCID 0000-0001-9503-8412
Kyung-Min JangNational Leading Research Laboratory of Drug Resistance Proteomics, Department of Biological Sciences, Myongji University, Yongin, Republic of Korea.ORCID 0009-0009-3778-5116
Kyoungmin ShinNational Leading Research Laboratory of Drug Resistance Proteomics, Department of Biological Sciences, Myongji University, Yongin, Republic of Korea.ORCID 0009-0004-4298-3161
Hyeonku JinNational Leading Research Laboratory of Drug Resistance Proteomics, Department of Biological Sciences, Myongji University, Yongin, Republic of Korea.ORCID 0009-0003-0855-9458
Dae-Wi KimDivision of Life Sciences, Jeonbuk National University, Jeonju, Republic of Korea.ORCID 0000-0002-5208-300X
Byeong Chul JeongNational Leading Research Laboratory of Drug Resistance Proteomics, Department of Biological Sciences, Myongji University, Yongin, Republic of Korea.ORCID 0009-0004-0628-1752
Sang Hee LeeNational Leading Research Laboratory of Drug Resistance Proteomics, Department of Biological Sciences, Myongji University, Yongin, Republic of Korea.ORCID 0000-0002-5660-7122

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The urgent demand for effective countermeasures against metallo-β-lactamases (MBLs) necessitates development of novel metallo-β-lactamase inhibitors (MBLIs). This study is dedicated to identifying critical chemical moieties within previously developed MBLIs, and critical MBLs should serve as the target in MBLI evaluations. Using the Preferred Reporting Items for Systematic Reviews and Meta-Analyses (PRISMA), a systematic literature analysis was conducted, and the NCBI RefSeq genome database was exploited to access the abundance profile and taxonomic distribution of MBLs and their variant types. Through the implementation of two distinct systematic approaches, we elucidated critical chemical moieties of MBLIs, providing pivotal information for rational drug design. We also prioritised MBLs and their variant types, highlighting the imperative need for comprehensive testing to ensure the potency and efficacy of the newly developed MBLIs. This approach contributes valuable information to advance the field of antimicrobial drug discovery.

Indexed as

beta-Lactamase Inhibitorsbeta-LactamasesAnti-Bacterial AgentsDrug DesignAnti-Bacterial Agentsbeta-Lactamase Inhibitorsbeta-Lactamaseschemical moietyMetallo-β-lactamase inhibitormetallo-β-lactamase variant type

Identifiers

PMID38488135
PMCPMC10946278

What OpenQuestion holds

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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.