Evidence map›Paper›PMID 25262664›Full record

ReviewCellular microbiology2014

Bacterial secreted effectors and caspase-3 interactions.

Daniel M Wall, Beth A McCormick

Open access · hybridAbstract readReview
In one paragraph

Review in Cellular microbiology, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 31 papers.

0numbers the graph read from it
0cells of the map it votes in
31citing papers in PubMed
7.0field-weighted citation impact, top 4% 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

31 citing papers in PubMed, 49 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. bioRxiv : the preprint server for biology · 2025
    Article
  5. Article
  6. Article
  7. Article
  8. Review
  9. Article
  10. Article
  11. Article
  12. Heat-KilledMolecules (Basel, Switzerland) · 2020
    Article
  13. Article
  14. Effects ofPathogens (Basel, Switzerland) · 2019
    Article
  15. Article
  16. Article
  17. Article
  18. The Photomodulation Activity of Metformin Against Oral Microbiome.Journal of lasers in medical sciences · 2019
    Review
  19. Article
  20. 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

2 authors at 2 institutions in 2 countries.

Daniel M WallInstitute of Infection, Immunity and Inflammation, University of Glasgow, Glasgow, G12 8QQ, UK.
Beth A McCormick
University of Glasgow · GBUniversity of Massachusetts Chan Medical School · US

Funding

Xenograft and Isograft CoreP01DK033506 · NIDDK · MASSACHUSETTS GENERAL HOSPITAL · PI REINECKER, HANS-CHRISTIAN · 1986 to 2015
$24.2M
INTESTINAL INFLAMMATION ORCHESTRATED BY PATHOGENSR01DK056754 · NIDDK · UNIV OF MASSACHUSETTS MED SCH WORCESTER · PI MCCORMICK, BETH A · 2000 to 2017
$6.5M
Salmonella Pathogenesis and Processing of Secreted Effectors by Caspase-3R56AI107804 · NIAID · UNIV OF MASSACHUSETTS MED SCH WORCESTER · PI MCCORMICK, BETH A · 2013 to 2013
$412k
Biotechnology and Biological Sciences Research Council BB/K008005/1NIAID NIH HHS AI107804NIAID NIH HHS R56 AI107804NIDDK NIH HHS DK33506NIDDK NIH HHS DK56754NIDDK NIH HHS P01 DK033506NIDDK NIH HHS R01 DK056754
6 · The paper itself

Abstract

Apoptosis is a critical process that intrinsically links organism survival to its ability to induce controlled death. Thus, functional apoptosis allows organisms to remove perceived threats to their survival by targeting those cells that it determines pose a direct risk. Central to this process are apoptotic caspases, enzymes that form a signalling cascade, converting danger signals via initiator caspases into activation of the executioner caspase, caspase-3. This enzyme begins disassembly of the cell by activating DNA degrading enzymes and degrading the cellular architecture. Interaction of pathogenic bacteria with caspases, and in particular, caspase-3, can therefore impact both host cell and bacterial survival. With roles outside cell death such as cell differentiation, control of signalling pathways and immunomodulation also being described for caspase-3, bacterial interactions with caspase-3 may be of far more significance in infection than previously recognized. In this review, we highlight the ways in which bacterial pathogens have evolved to subvert caspase-3 both through effector proteins that directly interact with the enzyme or by modulating pathways that influence its activation and activity.

Indexed as

Host-Pathogen InteractionsApoptosisBacteriaBacterial ProteinsCaspase 3Immune EvasionProtein TransportVirulence FactorsBacterial ProteinsCaspase 3Virulence Factors

Identifiers

PMID25262664
PMCPMC4257569
OpenAlexW1541816652

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.