Evidence map›Paper›PMID 17584123›Full record

ReviewCurrent protein & peptide science2007

The PYRIN domain in signal transduction.

Christian Stehlik

Abstract readReview
In one paragraph

Review in Current protein & peptide science, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.

0numbers the graph read from it
0cells of the map it votes in
17citing 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

17 citing papers in PubMed.

  1. Article
  2. Review
  3. Article
  4. Article
  5. Review
  6. Review
  7. Article
  8. COPs and POPs Patrol Inflammasome Activation.Journal of molecular biology · 2018
    Review
  9. Article
  10. Review
  11. Article
  12. Review
  13. Article
  14. Article
  15. Article
  16. Article
  17. COPs and POPs: modulators of inflammasome activity.Journal of immunology (Baltimore, Md. : 1950) · 2007
    Review
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.

Christian StehlikMary Babb Randolph Cancer Center and Department of Microbiology, Immunology and Cell Biology, West Virginia University, Morgantown, WV 26506-9300, USA. cstehlik@hsc.wvu.edu

Funding

THE ROLE OF HEF1 PROTEIN IN INVASION OF METASTATIC BREAST CANCERP20RR016440 · NCRR · WEST VIRGINIA UNIVERSITY · PI CUFF, CHRISTOPHER F · 2001 to 2010
$22.8M
PYRIN PROTEINS AS REGULATORS OF INNATE IMMUNE PATHWAYSR01GM071723 · NIGMS · WEST VIRGINIA UNIVERSITY · PI STEHLIK, CHRISTIAN · 2007 to 2011
$1.7M
Viral PYRIN-only proteins as suppressors of the host immune responseR21AI067680 · NIAID · WEST VIRGINIA UNIVERSITY · PI STEHLIK, CHRISTIAN · 2006 to 2007
$361k
Novel Functions of PYRIN proteinsR03AI067806 · NIAID · WEST VIRGINIA UNIVERSITY · PI STEHLIK, CHRISTIAN · 2006 to 2007
$144k
NCRR NIH HHS 5P20RR016440NCRR NIH HHS P20 RR016440NIAID NIH HHS 1R03AI067806NIAID NIH HHS 1R21AI067680NIAID NIH HHS R03 AI067806NIAID NIH HHS R21 AI067680NIGMS NIH HHS 1R01GM071723
6 · The paper itself

Abstract

The Death Domain Fold superfamily of evolutionarily conserved protein-protein interaction domains consists of 4 subfamilies: the death domain, the death effector domain, the caspase recruitment domain, and the PYRIN domain. Interaction of Death Domain Fold containing proteins modulates the activity of several downstream effectors, such as caspases and transcription factors. Recent studies provide evidence for not only homotypic-, but also heterotypic interactions among different sub-families, and even unconventional non-death domain fold interactions. As the number of potential protein associations among Death Domain Fold containing proteins expands and their influence on cellular responses increases, a challenging field for new investigations opens up. This review will focus on PYRIN domain-containing proteins and discuss the recent advances that provide strong evidence that PYRIN domain-mediated signal transduction has broad implications on cellular functions, including innate immunity, inflammation, differentiation, apoptosis, and cancer.

Indexed as

Amino Acid SequenceAnimalsApoptosisBinding SitesChromosome MappingConserved SequenceEvolution, MolecularHumansImmunityInflammationModels, MolecularMolecular Sequence DataProtein ConformationReceptors, Death DomainSequence AlignmentSequence Homology, Amino AcidReceptors, Death Domain

Identifiers

PMID17584123
PMCPMC4259900

What OpenQuestion holds

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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.