Evidence map›Paper›PMID 9630889›Full record

ReviewNature biotechnology1996

ICE/CED3-like proteases as therapeutic targets for the control of inappropriate apoptosis.

D W Nicholson

Abstract readReview
PubMed Publisher
In one paragraph

Review in Nature biotechnology, 1996. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 46 papers.

0numbers the graph read from it
0cells of the map it votes in
46citing papers in PubMed
20.9field-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

46 citing papers in PubMed, 268 citations in OpenAlex.

  1. Advances in the application of logic gates in nanozymes.Analytical and bioanalytical chemistry · 2024
    Review
  2. Frontiers in nutrition · 2021
    Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. Noninvasive imaging of apoptosis and its application in cancer therapeutics.Clinical cancer research : an official journal of the American Association for Cancer Research · 2008
    Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Mechanisms of apoptosis.The American journal of pathology · 2000
    Article
  14. Article
  15. HIV-1 envelope induces activation of caspase-3 and cleavage of focal adhesion kinase in primary human CD4(+) T cells.Proceedings of the National Academy of Sciences of the United States of America · 2000
    Article
  16. The baculovirus antiapoptotic p35 gene also functions via an oxidant-dependent pathway.Proceedings of the National Academy of Sciences of the United States of America · 1999
    Article
  17. Oligodendrocyte apoptosis mediated by caspase activation.The Journal of neuroscience : the official journal of the Society for Neuroscience · 1999
    Article
  18. Article
  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

1 author at 1 institution in 1 country.

D W NicholsonDepartment of Biochemistry and Molecular Biology, Merck Frosst Centre for Therapeutic Research, Pointe Claire-Dorval, Quebec, Canada. donald_nicholson@merck.com
Merck Canada Inc. (Canada) · CA

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Excessive or failed apoptosis is a prominent morphological feature of several human diseases. Many of the key biochemical players that contribute to the highly ordered process of apoptotic cell death have recently been identified. These include members of the emerging family of cysteine proteases related to mammalian interleukin-1 beta converting enzyme (ICE) and to CED-3, the product of a gene that is necessary for programmed cell death in the nematode C. elegans. Among a growing number of potential molecular targets for the control of human diseases where inappropriate apoptosis is prominent, ICE/CED-3-like proteases may be an attractive and tangible point for therapeutic intervention.

Indexed as

CaspasesAmino Acid SequenceAnimalsApoptosisBiotechnologyCaenorhabditis elegansCaenorhabditis elegans ProteinsCatalysisCysteine EndopeptidasesCysteine Proteinase InhibitorsDrug DesignHumansOligopeptidesProtein ConformationCaenorhabditis elegans ProteinsCaspasesced-3 protein, C elegansCysteine EndopeptidasesCysteine Proteinase InhibitorsOligopeptides

Identifiers

PMID9630889
OpenAlexW1973190361

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.