Evidence map›Paper›PMID 38837391›Full record

ReviewmBio2024

Inflammatory caspase substrate specificities.

Patrick M Exconde, Christopher M Bourne, Madhura Kulkarni, Bohdana M Discher, Cornelius Y Taabazuing

Abstract readReview
In one paragraph

Review in mBio, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.

0numbers the graph read from it
0cells of the map it votes in
8citing 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

8 citing papers in PubMed.

  1. Article
  2. Review
  3. Article
  4. Article
  5. Human non-canonical inflammasomes activate CASP3 to limit intracellularbioRxiv : the preprint server for biology · 2025
    Article
  6. Review
  7. Review
  8. Recognition ofJournal of oral microbiology · 2025
    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

5 authors.

Patrick M Exconde *Department of Biochemistry and Biophysics, University of Pennsylvania Perelman School of Medicine, Philadelphia, Pennsylvania, USA.ORCID 0009-0001-7299-8274
Christopher M Bourne *Department of Biochemistry and Biophysics, University of Pennsylvania Perelman School of Medicine, Philadelphia, Pennsylvania, USA.ORCID 0000-0001-9290-4223
Madhura KulkarniDepartment of Biochemistry and Biophysics, University of Pennsylvania Perelman School of Medicine, Philadelphia, Pennsylvania, USA.
Bohdana M DischerDepartment of Biochemistry and Biophysics, University of Pennsylvania Perelman School of Medicine, Philadelphia, Pennsylvania, USA.
Cornelius Y TaabazuingDepartment of Biochemistry and Biophysics, University of Pennsylvania Perelman School of Medicine, Philadelphia, Pennsylvania, USA.ORCID 0000-0003-2361-5457

Funding

Investigating the function of ZU5 domain-containing proteins as amplifiers of caspase activationR00AI148598 · NIAID · UNIVERSITY OF PENNSYLVANIA · PI TAABAZUING, CORNELIUS · 2022 to 2024
$740k
Burroughs Wellcome Fund (BWF) 1054907HHS | NIH | National Institute of Allergy and Infectious Diseases (NIAID) 4R00AI148598-03NIAID NIH HHS R00 AI148598United Negro College Fund (UNCF) EE Just Early Career AwardUniversity of Pennsylvania IIZD Martin and Pamela Winter Infectious Disease Fellowship.University of Pennsylvania Perelman School of Medicine Penn Provost Postdoctoral Fellow
6 · The paper itself

Abstract

Caspases are a family of cysteine proteases that act as molecular scissors to cleave substrates and regulate biological processes such as programmed cell death and inflammation. Extensive efforts have been made to identify caspase substrates and to determine factors that dictate substrate specificity. Thousands of putative substrates have been identified for caspases that regulate an immunologically silent type of cell death known as apoptosis, but less is known about substrates of the inflammatory caspases that regulate an immunostimulatory type of cell death called pyroptosis. Furthermore, much of our understanding of caspase substrate specificities is derived from work done with peptide substrates, which do not often translate to native protein substrates. Our knowledge of inflammatory caspase biology and substrates has recently expanded and here, we discuss the recent advances in our understanding of caspase substrate specificities, with a focus on inflammatory caspases. We highlight new substrates that have been discovered and discuss the factors that engender specificity. Recent evidence suggests that inflammatory caspases likely utilize two binding interfaces to recognize and process substrates, the active site and a conserved exosite.

Indexed as

CaspasesInflammationAnimalsCatalytic DomainHumansPyroptosisSubstrate SpecificityCaspasescaspase-1caspase-11caspase-4caspase-5caspase substratescytokinesIL-18IL-1βinflammasomesinflammatory caspasespyroptosis

Identifiers

PMID38837391
PMCPMC11253702

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.