Evidence map›Paper›PMID 17483456›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2007

Cryopyrin/NALP3 binds ATP/dATP, is an ATPase, and requires ATP binding to mediate inflammatory signaling.

Joseph A Duncan, Daniel T Bergstralh, Yanhong Wang, Stephen B Willingham, Zhengmao Ye, Albert G Zimmermann, Jenny Pan-Yun Ting

Open access · greenAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 273 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
273citing papers in PubMed, 1 pooled it
8.3field-weighted citation impact, top 2% 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

273 citing papers in PubMed, 1 synthesis or guideline pooled it, 482 citations in OpenAlex.

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213 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

7 authors at 4 institutions in 2 countries.

Joseph A DuncanDepartment of Medicine, Division of Infectious Diseases, University of North Carolina, Chapel Hill, NC 27599-7295, USA.
Daniel T Bergstralh
Yanhong Wang
Stephen B Willingham
Zhengmao Ye
Albert G Zimmermann
Jenny Pan-Yun Ting
Institut thématique Génétique, génomique et bioinformatique · FROffice of Infectious Diseases · USUNC Lineberger Comprehensive Cancer CenterUniversity of North Carolina at Chapel Hill · US

Funding

Yessinia autotransporters (Yaps): Structure, function, and host responseU54AI057157 · NIAID · UNIV OF NORTH CAROLINA CHAPEL HILL · PI SEMPOWSKI, GREGORY D · 2003 to 2013
$91.4M
Multidisciplinary Clinical Research Career Develop(RMI)K12RR023248 · NCRR · UNIV OF NORTH CAROLINA CHAPEL HILL · PI ORRINGER, EUGENE P · 2005 to 2007
$6.3M
INFECTIOUS DISEASE PATHOGENESIS TRAININGT32AI007151 · NIAID · UNIV OF NORTH CAROLINA CHAPEL HILL · PI JULIANO, JONATHAN J · 1985 to 2024
$5.5M
Innate Immune Response Genes and P. GingivalisR01DE016326 · NIDCR · UNIV OF NORTH CAROLINA CHAPEL HILL · PI TING, JENNY P · 2005 to 2009
$2.0M
M Tuberculosis and Host-Defense MechanismsR01AI063031 · NIAID · UNIV OF NORTH CAROLINA CHAPEL HILL · PI TING, JENNY P · 2005 to 2009
$1.7M
NCRR NIH HHS K12 RR023248NCRR NIH HHS K12RR023248NIAID NIH HHS R01AI057157NIAID NIH HHS R01 AI063031NIAID NIH HHS R01AI063031NIAID NIH HHS T32 AI007151NIAID NIH HHS T32AI007151NIAID NIH HHS U54 AI057157NIDCR NIH HHS R01 DE016326NIDCR NIH HHS R01DE16326
6 · The paper itself

Abstract

The CATERPILLER (CLR/NLR) gene family encodes a family of putative nucleotide-binding proteins important for host defense. Although nucleotide binding is thought to be central to this family, this aspect is largely unstudied. The CATERPILLER protein cryopyrin/NALP3 regulates IL-1beta processing by assembling the multimeric inflammasome complex. Mutations within the exon encoding the nucleotide-binding domain are associated with hereditary periodic fevers characterized by constitutive IL-1beta production. We demonstrate that purified cryopyrin binds ATP, dATP, and ATP-agarose, but not CTP, GTP, or UTP, and exhibits ATPase activity. Mutation of the nucleotide-binding domain reduces ATP binding, caspase-1 activation, IL-1beta production, cell death, macromolecular complex formation, self-association, and association with the inflammasome component ASC. Disruption of nucleotide binding abolishes the constitutive activation of disease-associated mutants, identifying nucleotide binding by cryopyrin as a potential target for antiinflammatory pharmacologic intervention.

Indexed as

Signal TransductionAdenosine TriphosphatasesAdenosine TriphosphateAmino Acid SequenceBinding SitesCarrier ProteinsCells, CulturedChromatography, AffinityHumansInflammationInterleukin-1betaMolecular Sequence DataNLR Family, Pyrin Domain-Containing 3 ProteinRecombinant ProteinsAdenosine TriphosphatasesAdenosine TriphosphateCarrier ProteinsInterleukin-1betaNLR Family, Pyrin Domain-Containing 3 ProteinNLRP3 protein, humanRecombinant Proteins

Identifiers

PMID17483456
PMCPMC1876568
OpenAlexW2028519649

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.