Evidence map›Paper›PMID 30191728›Full record

ArticleJournal of enzyme inhibition and medicinal chemistry2018

Coptisine-induced inhibition of Helicobacter pylori: elucidation of specific mechanisms by probing urease active site and its maturation process.

Cailan Li, Ping Huang, Kambo Wong, Yifei Xu, Lihua Tan, Hanbin Chen, Qiang Lu, Chaodan Luo, Chunlai Tam, Lixiang Zhu and 2 more

Open access · goldAbstract read
In one paragraph

Article in Journal of enzyme inhibition and medicinal chemistry, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 30 papers.

0numbers the graph read from it
0cells of the map it votes in
30citing papers in PubMed
3.8field-weighted citation impact, top 7% 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

30 citing papers in PubMed, 70 citations in OpenAlex.

  1. Trial
  2. Article
  3. Review
  4. Review
  5. Article
  6. Research Status and Prospects ofGastroenterology research and practice · 2026
    Review
  7. Article
  8. Towards EffectiveInternational journal of molecular sciences · 2025
    Review
  9. Article
  10. Review
  11. Article
  12. Article
  13. Review
  14. Article
  15. Component characterization ofFrontiers in cellular and infection microbiology · 2025
    Article
  16. New Directions inInfection and drug resistance · 2025
    Review
  17. Article
  18. Loureirin A is a narrow-spectrum antimicrobial agent againstAntimicrobial agents and chemotherapy · 2024
    Article
  19. Article
  20. Review of Phytochemical Potency as a Natural Anti-Molecules (Basel, Switzerland) · 2023
    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

12 authors at 3 institutions in 2 countries.

Cailan Lia Guangdong Provincial Key Laboratory of New Drug Development and Research of Chinese Medicine, Mathematical Engineering Academy of Chinese Medicine , Guangzhou University of Chinese Medicine , Guangzhou , P. R. China.
Ping Huangb School of Pharmaceutical Sciences , Guangzhou University of Chinese Medicine , Guangzhou , P. R. China.
Kambo Wongc School of Life Sciences , Center for Protein Science and Crystallography, The Chinese University of Hong Kong , P. R. China.
Yifei Xub School of Pharmaceutical Sciences , Guangzhou University of Chinese Medicine , Guangzhou , P. R. China.
Lihua Tana Guangdong Provincial Key Laboratory of New Drug Development and Research of Chinese Medicine, Mathematical Engineering Academy of Chinese Medicine , Guangzhou University of Chinese Medicine , Guangzhou , P. R. China.
Hanbin Chend The First Affiliated Hospital of Chinese Medicine, Guangzhou University of Chinese Medicine , Guangzhou , P. R. China.ORCID http://orcid.org/0000-0003-2271-7769
Qiang Lue Key Laboratory of Chinese Medicinal Resource from Lingnan, Ministry of Education and Research Center of Chinese Herbal Resource Science and Engineering , Guangzhou University of Chinese Medicine , Guangzhou , P. R. China.
Chaodan Luoa Guangdong Provincial Key Laboratory of New Drug Development and Research of Chinese Medicine, Mathematical Engineering Academy of Chinese Medicine , Guangzhou University of Chinese Medicine , Guangzhou , P. R. China.
Chunlai Tamc School of Life Sciences , Center for Protein Science and Crystallography, The Chinese University of Hong Kong , P. R. China.
Lixiang Zhub School of Pharmaceutical Sciences , Guangzhou University of Chinese Medicine , Guangzhou , P. R. China.
Ziren Sua Guangdong Provincial Key Laboratory of New Drug Development and Research of Chinese Medicine, Mathematical Engineering Academy of Chinese Medicine , Guangzhou University of Chinese Medicine , Guangzhou , P. R. China.
Jianhui Xief Guangdong Provincial Key Laboratory of Clinical Research on Traditional Chinese Medicine Syndrome , The Second Affiliated Hospital, Guangzhou University of Chinese Medicine , Guangzhou , P. R. China.
Guangzhou University of Chinese Medicine · CNChinese University of Hong Kong · HKFirst Affiliated Hospital of Guangzhou University of Chinese Medicine · CN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

In this study, we examined the anti-Helicobactor pylori effects of the main protoberberine-type alkaloids in Rhizoma Coptidis. Coptisine exerted varying antibacterial and bactericidal effects against three standard H. pylori strains and eleven clinical isolates, including four drug-resistant strains, with minimum inhibitory concentrations ranging from 25 to 50 μg/mL and minimal bactericidal concentrations ranging from 37.5 to 125 μg/mL. Coptisine's anti-H. pylori effects derived from specific inhibition of urease in vivo. In vitro, coptisine inactivated urease in a concentration-dependent manner through slow-binding inhibition and involved binding to the urease active site sulfhydryl group. Coptisine inhibition of H. pylori urease (HPU) was mixed type, while inhibition of jack bean urease was non-competitive. Importantly, coptisine also inhibited HPU by binding to its nickel metallocentre. Besides, coptisine interfered with urease maturation by inhibiting activity of prototypical urease accessory protein UreG and formation of UreG dimers and by promoting dissociation of nickel from UreG dimers. These findings demonstrate that coptisine inhibits urease activity by targeting its active site and inhibiting its maturation, thereby effectively inhibiting H. pylori. Coptisine may thus be an effective anti-H. pylori agent.

Indexed as

Anti-Bacterial AgentsBerberineCatalytic DomainDose-Response Relationship, DrugEnzyme InhibitorsHelicobacter pyloriHydrogen-Ion ConcentrationMolecular Docking SimulationMolecular StructureStructure-Activity RelationshipUreaseAnti-Bacterial AgentsBerberinecoptisineEnzyme InhibitorsUreasecoptisineHelicobacter pylori ureasenickel ionsulfhydryl groupUreG

Identifiers

PMID30191728
PMCPMC6136390
OpenAlexW2890134799

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.