Evidence map›Paper›PMID 9425163›Full record

ArticleThe Journal of cell biology1998

A role for caspases in lens fiber differentiation.

Y Ishizaki, M D Jacobson, M C Raff

Open access · bronzeAbstract read
In one paragraph

Article in The Journal of cell biology, 1998. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 72 papers.

0numbers the graph read from it
0cells of the map it votes in
72citing papers in PubMed
6.0field-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

72 citing papers in PubMed, 291 citations in OpenAlex.

  1. The concealed side of caspases: beyond a killer of cells.Cellular and molecular life sciences : CMLS · 2024
    Review
  2. Article
  3. Article
  4. Article
  5. Article
  6. Review
  7. Review
  8. Article
  9. Making the head: Caspases in life and death.Frontiers in cell and developmental biology · 2022
    Review
  10. Article
  11. Cell Death Related Proteins Beyond Apoptosis in the CNS.Frontiers in cell and developmental biology · 2021
    Review
  12. Article
  13. Article
  14. Review
  15. Article
  16. Review
  17. Caspase-dependent non-apoptotic processes in development.Cell death and differentiation · 2017
    Review
  18. Review
  19. Article
  20. Article

12 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

3 authors at 3 institutions in 2 countries.

Y IshizakiDepartment of Hygiene, Kobe University School of Medicine, Chuo-ku, Kobe 650, Japan.
M D Jacobson
M C Raff
Medical Research Council · GBMRC Laboratory for Molecular Cell Biology · GBUniversity College London · GB

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

There is increasing evidence that programmed cell death (PCD) depends on a novel family of intracellular cysteine proteases, called caspases, that includes the Ced-3 protease in the nematode Caenorhabditis elegans and the interleukin-1beta-converting enzyme (ICE)-like proteases in mammals. Some developing cells, including lens epithelial cells, erythroblasts, and keratinocytes, lose their nucleus and other organelles when they terminally differentiate, but it is not known whether the enzymatic machinery of PCD is involved in any of these normal differentiation events. We show here that at least one CPP32 (caspase-3)-like member of the caspase family becomes activated when rodent lens epithelial cells terminally differentiate into anucleate lens fibers in vivo, and that a peptide inhibitor of these proteases blocks the denucleation process in an in vitro model of lens fiber differentiation. These findings suggest that at least part of the machinery of PCD is involved in lens fiber differentiation.

Indexed as

CaspasesAnimalsApoptosisCaenorhabditis elegansCaspase 3Cell DifferentiationCell NucleusCells, CulturedCysteine EndopeptidasesEpithelial CellsLens, CrystallineOrgan Culture TechniquesPoly (ADP-Ribose) Polymerase-1Poly(ADP-ribose) PolymerasesProteinsRatsCasp3 protein, ratCaspase 3CaspasesCysteine EndopeptidasesParp1 protein, ratPoly (ADP-Ribose) Polymerase-1Poly(ADP-ribose) PolymerasesProteins

Identifiers

PMID9425163
PMCPMC2132591
OpenAlexW2000407232

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-SA
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.