Evidence map›Paper›PMID 15131267›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2004

Selective inhibition of calcineurin-NFAT signaling by blocking protein-protein interaction with small organic molecules.

Michael H A Roehrl, Sunghyun Kang, José Aramburu, Gerhard Wagner, Anjana Rao, Patrick G Hogan

Open access · bronzeAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 80 papers.

0numbers the graph read from it
0cells of the map it votes in
80citing papers in PubMed
3.7field-weighted citation impact, top 6% 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

80 citing papers in PubMed, 182 citations in OpenAlex.

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  10. NADProceedings of the National Academy of Sciences of the United States of America · 2022
    Article
  11. Article
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  14. A Review of Calcineurin Biophysics with Implications for Cardiac Physiology.International journal of molecular sciences · 2021
    Review
  15. Article
  16. Article
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  20. Article

20 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

6 authors at 2 institutions in 2 countries.

Michael H A RoehrlDepartment of Biological Chemistry, Harvard Medical School, Boston, MA 02115, USA.
Sunghyun Kang
José Aramburu
Gerhard Wagner
Anjana Rao
Patrick G Hogan
Harvard University · USPompeu Fabra University · ES

Funding

SIGNAL TRANSDUCTION AND GENE INDUCTION IN T LYMPHOCYTESR01AI040127 · NIAID · LA JOLLA INSTITUTE FOR IMMUNOLOGY · PI HOGAN, PATRICK, RAO, ANJANA · 1996 to 2025
$13.3M
BZIP PROTEINS AND LYMPHOCYTE GENE INDUCTIONR37CA042471 · NCI · IMMUNE DISEASE INSTITUTE, INC. · PI RAO, ANJANA · 1999 to 2006
$3.6M
ROLE OF THE FOS ONCOGENE IN LYMPHOCYTE GROWTHR01CA042471 · NCI · LA JOLLA INSTITUTE FOR IMMUNOLOGY · PI RAO, ANJANA · 1986 to 2012
$3.1M
NMR STUDIES OF PROTEIN-TARGET INTERACTIONSR01GM038608 · NIGMS · UNIVERSITY OF MICHIGAN AT ANN ARBOR · PI WAGNER, GERHARD · 1988 to 2002
$591k
PEPTIDE INHIBITORS OF NFAT ACTIVATION BY CALCINEURINR43AI043726 · NIAID · CBR LABORATORIES, INC. · PI HOGAN, PATRICK G · 1998 to 1998
–
NCI NIH HHS CA42471NCI NIH HHS R01 CA042471NCI NIH HHS R37 CA042471NIAID NIH HHS AI40127NIAID NIH HHS AI43726NIAID NIH HHS R01 AI040127NIGMS NIH HHS GM038608NIGMS NIH HHS R01 GM038608
6 · The paper itself

Abstract

Transient or reversible protein-protein interactions are commonly used to ensure efficient targeting of signaling enzymes to their cellular substrates. These interactions include direct binding to substrate, interaction with an accessory or scaffold protein, and positioning at subcellular locations in proximity to substrates. The existence of specialized targeting mechanisms raises the possibility of designing inhibitors that do not block enzyme activity per se, but rather interfere with targeting of the enzyme to one or more of its substrates within the cell. Here, we identify small organic molecules that specifically block targeting of the protein phosphatase calcineurin to its substrate nuclear factor of activated T cells (NFAT, also termed NFATc) and show that they are effective inhibitors of calcineurin-NFAT signaling.

Indexed as

Nuclear ProteinsCalcineurinCalcineurin InhibitorsDNA-Binding ProteinsNFATC Transcription FactorsOligopeptidesProtein BindingSignal TransductionTranscription FactorsCalcineurinCalcineurin InhibitorsDNA-Binding ProteinsNFATC Transcription FactorsNuclear ProteinsOligopeptidesTranscription FactorsVIVIT peptide

Identifiers

PMID15131267
PMCPMC419644
OpenAlexW2089988801

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.