Evidence map›Paper›PMID 19060202›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2008

A dimer-specific function of the transcription factor NFATp.

James V Falvo, Charles H Lin, Alla V Tsytsykova, Peter K Hwang, Dimitris Thanos, Anne E Goldfeld, Tom Maniatis

Open access · greenAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.

0numbers the graph read from it
0cells of the map it votes in
18citing papers in PubMed
1.1field-weighted citation impact, top 23% 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

18 citing papers in PubMed, 27 citations in OpenAlex.

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  18. Transcriptional control of the TNF gene.Current directions in autoimmunity · 2010
    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

7 authors at 3 institutions in 2 countries.

James V FalvoImmune Disease Institute and Harvard Medical School, 800 Huntington Avenue, Boston, MA 02115, USA.
Charles H Lin
Alla V Tsytsykova
Peter K Hwang
Dimitris Thanos
Anne E Goldfeld
Tom Maniatis
Harvard University · USColumbia University · USUniversity of California, San Francisco · US

Funding

UCSF PROSTATE CANCER SPOREP50CA089520 · NCI · UNIVERSITY OF CALIFORNIA, SAN FRANCISCO · PI CARROLL, PETER R · 2000 to 2008
$13.9M
Innate Immunity: Signal Transduction and Interferon Gene RegulationR01AI020642 · NIAID · HARVARD UNIVERSITY · PI MANIATIS, THOMAS P · 1985 to 2010
$5.3M
IMMUNOLOGICAL ACTIVATION OF TNF ALPHA GENE EXPRESSIONR01GM056492 · NIGMS · IMMUNE DISEASE INSTITUTE, INC. · PI GOLDFELD, ANNE · 1999 to 2003
$1.1M
HIGH MOBILITY GROUP PROTEIN IN GENE TRANSCRIPTIONR01GM054605 · NIGMS · COLUMBIA UNIVERSITY HEALTH SCIENCES · PI THANOS, DIMITRIS · 1996 to 2002
$885k
HUMAN B-INTERFERON GENE REGULATIONR37AI020642 · NIAID · HARVARD UNIVERSITY · PI MANIATIS, THOMAS P · 1987 to 1996
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NCI NIH HHS P50 CA089520NCI NIH HHS P50 CA89520NIAID NIH HHS AI-20642NIAID NIH HHS R01 AI020642NIGMS NIH HHS GM-54605NIGMS NIH HHS GM-56492NIGMS NIH HHS R01 GM054605NIGMS NIH HHS R01 GM056492
6 · The paper itself

Abstract

The transcription factor NFATp integrates multiple signal transduction pathways through coordinate binding with basic-region leucine zipper (bZIP) proteins and other transcription factors. The NFATp monomer, even in the absence of its activation domains, recruits bZIP proteins to canonical NFAT-bZIP composite DNA elements. By contrast, the NFATp dimer and its bZIP partner bind noncooperatively to the NFAT-bZIP element of the tumor necrosis factor (TNF) gene promoter. This observation raises the possibility that the function of the activation domains of NFATp is dimer-specific. Here, we determine the consensus DNA binding site of the NFATp dimer, describe monomer- and dimer-specific NFATp-DNA contact patterns, and demonstrate that NFATp dimerization and dimer-specific activation subdomains are required for transcriptional activation from the TNF NFAT-bZIP element. We also show that these NFATp subdomains interact with the coactivator CBP (CREB-binding protein), which is required for NFATp-dependent TNF gene transcription. Thus, the context-specific function of the activation domains of NFAT can be potentiated by DNA-directed dimerization.

Indexed as

Base SequenceBasic-Leucine Zipper Transcription FactorsConsensus SequenceCREB-Binding ProteinDimerizationDNAElectrophoretic Mobility Shift AssayNFATC Transcription FactorsPromoter Regions, GeneticProtein Structure, TertiaryTranscription, GeneticTumor Necrosis Factor-alphaBasic-Leucine Zipper Transcription FactorsCREB-Binding ProteinDNANFATC Transcription FactorsTumor Necrosis Factor-alpha

Identifiers

PMID19060202
PMCPMC2604938
OpenAlexW2063513426

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.