Evidence map›Paper›PMID 20795673›Full record

ArticleBiochemistry2010

Activation and specificity of human caspase-10.

Katherine Wachmann, Cristina Pop, Bram J van Raam, Marcin Drag, Peter D Mace, Scott J Snipas, Christian Zmasek, Robert Schwarzenbacher, Guy S Salvesen, Stefan J Riedl

Abstract readComparative Study
In one paragraph

Article in Biochemistry, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 47 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
47citing papers in PubMed, 1 pooled it
2.3field-weighted citation impact, top 12% 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

47 citing papers in PubMed, 1 synthesis or guideline pooled it, 76 citations in OpenAlex.

  1. Pooled it
  2. Article
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  5. Article
  6. Article
  7. Review
  8. Article
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  10. Review
  11. Cells · 2023
    Review
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  14. Article
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  16. Article
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  18. Induction of apoptosis on ovarian adenocarcinoma cells, A2780 by tricyclohexylphosphanegold (I) mercaptobenzoate derivatives via intrinsic and extrinsic pathways.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2021
    Article
  19. The intricate biophysical puzzle of caspase-1 activation.Archives of biochemistry and biophysics · 2021
    Review
  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

10 authors at 2 institutions in 3 countries.

Katherine WachmannProgram in Apoptosis and Cell Death Research, Sanford-BurnhamMedical Research Institute, 10901 North Torrey Pines Road, La Jolla, California 92037, USA.
Cristina Pop
Bram J van Raam
Marcin Drag
Peter D Mace
Scott J Snipas
Christian Zmasek
Robert Schwarzenbacher
Guy S Salvesen
Stefan J Riedl
Toxicologie, Pharmacologie et Signalisation Cellulaire · FRUniversity of Salzburg · AT

Funding

SPHINGOMYELIN SIGNALING PATHWAY IN FAS-INDUCED APOPTOSISP01CA069381 · NCI · SANFORD BURNHAM PREBYS MEDICAL DISCOVERY INSTITUTE · PI WARE, CARL F · 1996 to 2009
$16.8M
The Mechanism of DISC FormationR01AA017238 · NIAAA · SANFORD BURNHAM PREBYS MEDICAL DISCOVERY INSTITUTE · PI RIEDL, STEFAN J · 2008 to 2012
$2.1M
NCI NIH HHS CA69381NCI NIH HHS P01 CA069381NIAAA NIH HHS R01 AA017238NIAAA NIH HHS R01AA017238
6 · The paper itself

Abstract

Two apical caspases, caspase-8 and -10, are involved in the extrinsic death receptor pathway in humans, but it is mainly caspase-8 in its apoptotic and nonapoptotic functions that has been an intense research focus. In this study we concentrate on caspase-10, its mechanism of activation, and the role of the intersubunit cleavage. Our data obtained through in vitro dimerization assays strongly suggest that caspase-10 follows the proximity-induced dimerization model for apical caspases. Furthermore, we compare the specificity and activity of the wild-type protease with a mutant incapable of autoprocessing by using positional scanning substrate analysis and cleavage of natural protein substrates. These experiments reveal a striking difference between the wild type and the mutant, leading us to hypothesize that the single chain enzyme has restricted activity on most proteins but high activity on the proapoptotic protein Bid, potentially supporting a prodeath role for both cleaved and uncleaved caspase-10.

Indexed as

BH3 Interacting Domain Death Agonist ProteinCaspase 10DimerizationEndopeptidasesEnzyme ActivationHumansSubstrate SpecificityBH3 Interacting Domain Death Agonist ProteinCASP10 protein, humanCaspase 10Endopeptidases

Identifiers

PMID20795673
PMCPMC2943529
OpenAlexW1978695791

What OpenQuestion holds

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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.