Evidence map›Paper›PMID 11451368›Full record

ArticleMolecular and cellular biochemistry2001

The SMRT corepressor is a target of phosphorylation by protein kinase CK2 (casein kinase II).

Y Zhou, W Gross, S H Hong, M L Privalsky

Open access · greenAbstract read
In one paragraph

Article in Molecular and cellular biochemistry, 2001. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.

0numbers the graph read from it
0cells of the map it votes in
20citing papers in PubMed
1.5field-weighted citation impact, top 19% 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

20 citing papers in PubMed, 52 citations in OpenAlex.

  1. Article
  2. Review
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  8. Article
  9. Nuclear hormone receptor co-repressors: structure and function.Molecular and cellular endocrinology · 2012
    Review
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  11. Article
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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

4 authors at 1 institution in 1 country.

Y ZhouDivision of Biological Sciences, University of California at Davis, 95616, USA.
W Gross
S H Hong
M L Privalsky
University of California, Davis · US

Funding

MECHANISM OF ACTION OF THE VERB A ONCOGENE OF AEVR37CA053394 · NCI · UNIVERSITY OF CALIFORNIA DAVIS · PI PRIVALSKY, MARTIN L. · 1994 to 2012
$3.4M
Role of cofactors in nuclear hormone receptor function.R01DK053528 · NIDDK · UNIVERSITY OF CALIFORNIA DAVIS · PI PRIVALSKY, MARTIN L. · 1998 to 2012
$2.9M
NCI NIH HHS R37 CA053394NCI NIH HHS R37 CA-53394NIDDK NIH HHS R01 DK053528NIDDK NIH HHS R01 DK-53528
6 · The paper itself

Abstract

The Silencing-Mediator for Retinoid/Thyroid hormone receptors (SMRT) interacts with, and mediates transcriptional repression by, a variety of eukaryotic transcription factors, including the nuclear hormone receptors. The ability of SMRT to function as a transcriptional 'corepressor' is regulated by a variety of signal transduction pathways. We report here that SMRT is a phosphoprotein in vivo, and is also phosphorylated in vitro by unfractionated cell extracts. A major site of phosphorylation of SMRT is a protein kinase CK2 motif centered on serine 1492, and located within a C-terminal SMRT domain that mediates interaction of the corepressor with the nuclear hormone receptors. Phosphorylation of SMRT by CK2 stabilizes the ability of the SMRT protein to interact with nuclear hormone receptors. Our results indicate that SMRT is a member of an expanding family of transcriptional regulators that are modified, and potentially regulated, in response to protein kinase CK2.

Indexed as

Amino Acid SequenceAnimalsCasein Kinase IICell LineDNA-Binding ProteinsDose-Response Relationship, DrugFibroblastsGene Expression Regulation, EnzymologicHaplorhiniMicroscopy, ConfocalMolecular Sequence DataNuclear Receptor Co-Repressor 2PhosphorylationPlasmidsProtein BindingProtein Serine-Threonine KinasesCasein Kinase IIDNA-Binding ProteinsNuclear Receptor Co-Repressor 2Protein Serine-Threonine KinasesReceptors, Thyroid HormoneRecombinant ProteinsRepressor Proteins

Identifiers

PMID11451368
PMCPMC2655343
OpenAlexW1945152805

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.