Evidence map›Paper›PMID 42159406›Full record

ArticlemBio2026

MAP4Ks drive cell death in response to

Mitchell A Pallett, Romina Tocci, Andrea Majstorovic, Elena Everatt, Ioanna Panagi, Ines Diaz-Del-Olmo, Camilla Godlee, Teresa L M Thurston, David W Holden

Abstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in mBio, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

0numbers the graph read from it
0cells of the map it votes in
0citing papers in PubMed
–field-weighted citation impact
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

0 citing papers in PubMed.

No citing paper in PubMed yet.

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

9 authors.

Mitchell A PallettCentre for Bacterial Resistance Biology, Department of Infectious Disease, Faculty of Medicine, Imperial College London, London, United Kingdom.ORCID 0000-0002-4194-3190
Romina TocciCentre for Bacterial Resistance Biology, Department of Infectious Disease, Faculty of Medicine, Imperial College London, London, United Kingdom.
Andrea MajstorovicCentre for Bacterial Resistance Biology, Department of Infectious Disease, Faculty of Medicine, Imperial College London, London, United Kingdom.
Elena EverattCentre for Bacterial Resistance Biology, Department of Infectious Disease, Faculty of Medicine, Imperial College London, London, United Kingdom.
Ioanna PanagiCentre for Bacterial Resistance Biology, Department of Infectious Disease, Faculty of Medicine, Imperial College London, London, United Kingdom.
Ines Diaz-Del-OlmoSir William Dunn School of Pathology, University of Oxford, Oxford, United Kingdom.
Camilla GodleeDepartment of Biochemistry, Cambridge University, Cambridge, United Kingdom.
Teresa L M ThurstonSir William Dunn School of Pathology, University of Oxford, Oxford, United Kingdom.
David W HoldenCentre for Bacterial Resistance Biology, Department of Infectious Disease, Faculty of Medicine, Imperial College London, London, United Kingdom.

Funding

Biotechnology and Biological Sciences Research Council BB/R011834/1Engineering and Physical Sciences Research Council EP/X02377X/2Medical Research Council MR/V031058/2Wellcome Trust 209411/Z/17/Z
6 · The paper itself

Abstract

Many pathogens target the host actin cytoskeleton through the delivery of actin depolymerizing toxins, including mono-ADP-ribosyltransferases (mART), ultimately triggering host cell death. Despite the importance of mARTs in pathogen virulence, it remains unclear whether actin ribosylation is required for mART-dependent cell death, and how actin depolymerization leads to cell death. Using the non-typhoidal IMPORTANCE: Host cell death plays a critical role as an intrinsic defense mechanism against infection and disease. However, many pathogens subvert cell death signaling to enhance their replication and survival. Here, we show that the mono-ADP ribosyl transferase family of toxins encoded by pathogens of global importance, including

Indexed as

ActinsADP Ribose TransferasesBacterial ProteinsCell DeathHost-Pathogen InteractionsProtein Serine-Threonine KinasesSalmonella typhimuriumAnimalsBacterial ToxinsHeLa CellsHumansSignal TransductionVirulence FactorsActinsADP Ribose TransferasesBacterial ProteinsBacterial ToxinsProtein Serine-Threonine KinasesspvB protein, Salmonella enterica virulence plasmidVirulence Factorsactincell deathhost–pathogen interactionspathogenesis

Identifiers

PMID42159406
PMCPMC13251412

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.