Evidence map›Paper›PMID 28498362›Full record

ReviewCell death and differentiation2017

Caspases and their substrates.

Olivier Julien, James A Wells

Open access · bronzeAbstract readReview
In one paragraph

Review in Cell death and differentiation, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 418 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
418citing papers in PubMed, 1 pooled it
25.2field-weighted citation impact, top 1% 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

418 citing papers in PubMed, 1 synthesis or guideline pooled it, 792 citations in OpenAlex.

  1. Pooled it
  2. Article
  3. Review
  4. Review
  5. Review
  6. Article
  7. Article
  8. Caspase-mediated cleavage events hidden by secondary proteolysis during apoptosis.Protein science : a publication of the Protein Society · 2026
    Article
  9. Potential Host-Directed Mechanisms ofVeterinary sciences · 2026
    Article
  10. Achieving protease substrate-specific inhibition by mAb dual functional selections.Protein science : a publication of the Protein Society · 2026
    Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Processing and release of endogenous immunogenic peptide signals.The Plant journal : for cell and molecular biology · 2026
    Review
  16. Journal of agricultural and food chemistry · 2026
    Article
  17. Article
  18. Article
  19. Article
  20. Article

358 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

2 authors at 1 institution in 1 country.

Olivier JulienDepartment of Pharmaceutical Chemistry and Cellular &Molecular Pharmacology, University of California, San Francisco, CA, USA.ORCID 0000-0001-7068-7299
James A WellsDepartment of Pharmaceutical Chemistry and Cellular &Molecular Pharmacology, University of California, San Francisco, CA, USA.
University of California, San Francisco · US

Funding

Global Analysis of Proteolysis in ApoptosisR01GM081051 · NIGMS · UNIVERSITY OF CALIFORNIA, SAN FRANCISCO · PI WELLS, JAMES A · 2007 to 2015
$2.8M
NIGMS NIH HHS R01 GM081051
6 · The paper itself

Abstract

Protease biology is intimately linked to the functional consequences of substrate cleavage events. Human caspases are a family of 12 fate-determining cysteine proteases that are best known for driving cell death, either apoptosis or pyroptosis. More recently, caspases have been shown to be involved in other cellular remodeling events as well including stem cell fate determination, spermatogenesis, and erythroid differentiation. Recent global proteomics methods enable characterization of the substrates that caspases cleave in live cells and cell extracts. The number of substrate targets identified for individual caspases can vary widely ranging from only a (few) dozen targets for caspases-4, -5, -9, and -14 to hundreds of targets for caspases-1, -2, -3, -6, -7, and -8. Proteomic studies characterizing the rates of target cleavage show that each caspase has a preferred substrate cohort that sometimes overlaps between caspases, but whose rates of cleavage vary over 500-fold within each group. Determining the functional consequences of discrete proteolytic events within the global substrate pool is a major challenge for the field. From the handful of individual targets that have been studied in detail, there are only a few so far that whose single cleavage event is capable of sparking apoptosis alone, such as cleavage of caspase-3/-7 and BIM

Indexed as

Gene Expression RegulationAnimalsBcl-2-Like Protein 11CaspasesCell DifferentiationEukaryotic CellsGasderminsHumansIntracellular Signaling Peptides and ProteinsKineticsNeoplasm ProteinsPhosphate-Binding ProteinsProteolysisPyroptosisSignal TransductionSubstrate SpecificityBCL2L11 protein, humanBcl-2-Like Protein 11CaspasesGasderminsGSDMD protein, humanIntracellular Signaling Peptides and ProteinsNeoplasm ProteinsPhosphate-Binding Proteins

Identifiers

PMID28498362
PMCPMC5520456
OpenAlexW2613163105

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.