Evidence map›Paper›PMID 31388008›Full record

ArticleNature communications2019

The antimicrobial peptide thanatin disrupts the bacterial outer membrane and inactivates the NDM-1 metallo-β-lactamase.

Bo Ma, Chao Fang, Linshan Lu, Mingzhi Wang, Xiaoyan Xue, Ying Zhou, Mingkai Li, Yue Hu, Xiaoxing Luo, Zheng Hou

Open access · goldAbstract read
In one paragraph

Article in Nature communications, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 88 papers.

0numbers the graph read from it
0cells of the map it votes in
88citing papers in PubMed
5.5field-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

88 citing papers in PubMed, 172 citations in OpenAlex.

  1. Article
  2. TheInternational journal of molecular sciences · 2026
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  11. Advances of Antimicrobial Peptides in the Treatment of Multidrug-Resistant Bacteria.BioDrugs : clinical immunotherapeutics, biopharmaceuticals and gene therapy · 2025
    Review
  12. Article
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  14. Article
  15. Article
  16. Advances of Peptides for Plant Immunity.Plants (Basel, Switzerland) · 2025
    Review
  17. Article
  18. Article
  19. Rational Design of Natural Xanthones Against Gram-negative Bacteria.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2025
    Article
  20. Review

28 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

10 authors at 1 institution in 1 country.

Bo MaDepartment of Pharmacology, School of Pharmacy, Fourth Military Medical University, Xi'an, 710032, China.
Chao FangDepartment of Pharmacology, School of Pharmacy, Fourth Military Medical University, Xi'an, 710032, China.ORCID http://orcid.org/0000-0003-1011-2113
Linshan LuDepartment of Obstetrics and Gynecology, Tangdu Hospital, Fourth Military Medical University, Xi'an, 710038, China.
Mingzhi WangDepartment of Pharmacology, School of Pharmacy, Fourth Military Medical University, Xi'an, 710032, China.
Xiaoyan XueDepartment of Pharmacology, School of Pharmacy, Fourth Military Medical University, Xi'an, 710032, China.
Ying ZhouDepartment of Pharmacology, School of Pharmacy, Fourth Military Medical University, Xi'an, 710032, China.
Mingkai LiDepartment of Pharmacology, School of Pharmacy, Fourth Military Medical University, Xi'an, 710032, China.
Yue HuDepartment of Pharmacology, School of Pharmacy, Fourth Military Medical University, Xi'an, 710032, China.
Xiaoxing LuoDepartment of Pharmacology, School of Pharmacy, Fourth Military Medical University, Xi'an, 710032, China. xxluo3@fmmu.edu.cn.
Zheng HouDepartment of Pharmacology, School of Pharmacy, Fourth Military Medical University, Xi'an, 710032, China. hzh_0001@163.com.ORCID http://orcid.org/0000-0002-0358-7869
Air Force Medical University · CN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

New Delhi metallo-β-lactamase-1 (NDM-1) is the most prevalent type of metallo-β-lactamase and hydrolyzes almost all clinically used β-lactam antibiotics. Here we show that the antimicrobial peptide thanatin disrupts the outer membrane of NDM-1-producing bacteria by competitively displacing divalent cations on the outer membrane and inducing the release of lipopolysaccharides. In addition, thanatin inhibits the enzymatic activity of NDM-1 by displacing zinc ions from the active site, and reverses carbapenem resistance in NDM-1-producing bacteria in vitro and in vivo. Thus, thanatin's dual mechanism of action may be useful for combating infections caused by NDM-1-producing pathogens.

Indexed as

AnimalsAnti-Bacterial AgentsAntimicrobial Cationic Peptidesbeta-Lactamasesbeta-Lactam ResistanceCarbapenemsCatalytic DomainCell WallDisease Models, AnimalEscherichia coliEscherichia coli InfectionsHumansHuman Umbilical Vein Endothelial CellsInhibitory Concentration 50Klebsiella InfectionsKlebsiella pneumoniaeAnti-Bacterial AgentsAntimicrobial Cationic Peptidesbeta-lactamase NDM-1beta-LactamasesCarbapenemsthanatinZinc

Identifiers

PMID31388008
PMCPMC6684654
OpenAlexW2966130344

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.