Evidence map›Paper›PMID 35008622›Full record

ReviewInternational journal of molecular sciences2021

Enzyme Inhibitors: The Best Strategy to Tackle Superbug NDM-1 and Its Variants.

Xiaoting Li, Dongmei Zhao, Weina Li, Jichao Sun, Xiuying Zhang

Open access · goldAbstract readReview
In one paragraph

Review in International journal of molecular sciences, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.

0numbers the graph read from it
0cells of the map it votes in
14citing papers in PubMed
1.2field-weighted citation impact, top 23% 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

14 citing papers in PubMed, 30 citations in OpenAlex.

  1. Genetic and Phenotypic Characterization of aAntibiotics (Basel, Switzerland) · 2026
    Article
  2. Review
  3. Article
  4. Review
  5. Article
  6. ACS omega · 2025
    Article
  7. Review
  8. Article
  9. Article
  10. Review
  11. Article
  12. The First Report ofInfection and drug resistance · 2023
    Article
  13. Emergence of aFrontiers in cellular and infection microbiology · 2022
    Article
  14. Review
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 at 1 institution in 1 country.

Xiaoting LiHeilongjiang Key Laboratory for Animal Disease Control and Pharmaceutical Development, Northeast Agricultural University, Harbin 150036, China.
Dongmei ZhaoHeilongjiang Key Laboratory for Animal Disease Control and Pharmaceutical Development, Northeast Agricultural University, Harbin 150036, China.
Weina LiHeilongjiang Key Laboratory for Animal Disease Control and Pharmaceutical Development, Northeast Agricultural University, Harbin 150036, China.
Jichao SunHeilongjiang Key Laboratory for Animal Disease Control and Pharmaceutical Development, Northeast Agricultural University, Harbin 150036, China.
Xiuying ZhangHeilongjiang Key Laboratory for Animal Disease Control and Pharmaceutical Development, Northeast Agricultural University, Harbin 150036, China.
Northeast Agricultural University · CN

Funding

the National 13th Five-Year Key R&D Program Special 2018YFD0500306
6 · The paper itself

Abstract

Multidrug bacterial resistance endangers clinically effective antimicrobial therapy and continues to cause major public health problems, which have been upgraded to unprecedented levels in recent years, worldwide. β-Lactam antibiotics have become an important weapon to fight against pathogen infections due to their broad spectrum. Unfortunately, the emergence of antibiotic resistance genes (ARGs) has severely astricted the application of β-lactam antibiotics. Of these, New Delhi metallo-β-lactamase-1 (NDM-1) represents the most disturbing development due to its substrate promiscuity, the appearance of variants, and transferability. Given the clinical correlation of β-lactam antibiotics and NDM-1-mediated resistance, the discovery, and development of combination drugs, including NDM-1 inhibitors, for NDM-1 bacterial infections, seems particularly attractive and urgent. This review summarizes the research related to the development and optimization of effective NDM-1 inhibitors. The detailed generalization of crystal structure, enzyme activity center and catalytic mechanism, variants and global distribution, mechanism of action of existing inhibitors, and the development of scaffolds provides a reference for finding potential clinically effective NDM-1 inhibitors against drug-resistant bacteria.

Indexed as

Amino Acid Sequencebeta-LactamasesCatalytic DomainChelating AgentsEnzyme InhibitorsHydrolysisMutationbeta-lactamase NDM-1beta-LactamasesChelating AgentsEnzyme Inhibitorsbiological activityenzyme inhibitorsmultidrug resistanceNDM-1pharmacophorevariants

Identifiers

PMID35008622
PMCPMC8745225
OpenAlexW4200535411

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.