Evidence map›Paper›PMID 9889191›Full record

ArticleThe EMBO journal1999

Neisserial porin (PorB) causes rapid calcium influx in target cells and induces apoptosis by the activation of cysteine proteases.

A Müller, D Günther, F Düx, M Naumann, T F Meyer, T Rudel

Open access · bronzeAbstract read
In one paragraph

Article in The EMBO journal, 1999. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 77 papers.

0numbers the graph read from it
0cells of the map it votes in
77citing papers in PubMed
6.2field-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

77 citing papers in PubMed, 195 citations in OpenAlex.

  1. Pathogens (Basel, Switzerland) · 2026
    Article
  2. Review
  3. Review
  4. Article
  5. Infection and immunity · 2024
    Article
  6. Article
  7. Mechanisms of host manipulation byFrontiers in microbiology · 2023
    Review
  8. Antimicrobial Susceptibility Testing Patterns ofTropical medicine and infectious disease · 2022
    Article
  9. Article
  10. Frontiers in cellular and infection microbiology · 2022
    Article
  11. Virulence Mechanisms ofFrontiers in microbiology · 2022
    Review
  12. Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Properly folded and functional PorB fromThe Journal of biological chemistry · 2018
    Article
  18. Lipid binding attenuates channel closure of the outer membrane protein OmpF.Proceedings of the National Academy of Sciences of the United States of America · 2018
    Article
  19. Article
  20. Gonorrhea - an evolving disease of the new millennium.Microbial cell (Graz, Austria) · 2016
    Review

17 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

6 authors at 1 institution in 1 country.

A MüllerMax-Planck-Institut für Infektionsbiologie, Abteilung Molekulare Biologie, Monbijoustrasse 2, 10117 Berlin, Germany.
D Günther
F Düx
M Naumann
T F Meyer
T Rudel
Max Planck Institute for Infection Biology · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The porin (PorB) of Neisseria gonorrhoeae is an intriguing bacterial factor owing to its ability to translocate from the outer bacterial membrane into host cell membranes where it modulates the infection process. Here we report on the induction of programmed cell death after prolonged infection of epithelial cells with pathogenic Neisseria species. The underlying mechanism we propose includes translocation of the porin, a transient increase in cytosolic Ca2+ and subsequent activation of the Ca2+ dependent protease calpain as well as proteases of the caspase family. Blocking the porin channel by ATP eliminates the Ca2+ signal and also abolishes its pro-apoptotic function. The neisserial porins share structural and functional homologies with the mitochondrial voltage-dependent anion channels (VDAC). The neisserial porin may be an analogue or precursor of the ancient permeability transition pore, the putative central regulator of apoptosis.

Indexed as

Adenosine TriphosphateAmino Acid Chloromethyl KetonesApoptosisBacterial Outer Membrane ProteinsCalciumCalpainCell LineCysteine EndopeptidasesCysteine Proteinase InhibitorsEnzyme ActivationHeLa CellsHumansIon TransportMutationNeisseria gonorrhoeaePorinsAdenosine TriphosphateAmino Acid Chloromethyl KetonesBacterial Outer Membrane Proteinsbenzyloxycarbonylvalyl-alanyl-aspartyl fluoromethyl ketoneCalciumCalpainCysteine EndopeptidasesCysteine Proteinase Inhibitorsporin protein, NeisseriaPorins

Identifiers

PMID9889191
PMCPMC1171129
OpenAlexW1977644290

What OpenQuestion holds

Textmetadata
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.