Evidence map›Paper›PMID 17068076›Full record

ArticleNucleic acids research2006

The molecular basis of the interaction between the proline-rich SH3-binding motif of PNRC and estrogen receptor alpha.

Dujin Zhou, Jing Jing Ye, Yuping Li, Ki Lui, Shiuan Chen

Open access · goldAbstract read
In one paragraph

Article in Nucleic acids research, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.

0numbers the graph read from it
0cells of the map it votes in
14citing papers in PubMed
2.5field-weighted citation impact, top 11% 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

14 citing papers in PubMed, 34 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. Article
  5. Glucocorticoid receptor interacts with PNRC2 in a ligand-dependent manner to recruit UPF1 for rapid mRNA degradation.Proceedings of the National Academy of Sciences of the United States of America · 2015
    Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Article
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

5 authors at 2 institutions in 1 country.

Dujin ZhouDepartment of Surgical Research, Beckman Research Institute of City of Hope, 1450 East Duarte Road, Duarte, CA 91010, USA.
Jing Jing Ye
Yuping Li
Ki Lui
Shiuan Chen
Beckman Research InstituteCity of Hope · US

Funding

Regulatory Roles of PNRC in Breast Epithelial CellsR01DK060560 · NIDDK · CITY OF HOPE/BECKMAN RESEARCH INSTITUTE · PI CHEN, SHIUAN · 2002 to 2005
$1.2M
NIDDK NIH HHS DK60560NIDDK NIH HHS R01 DK060560
6 · The paper itself

Abstract

PNRC and PNRC2 are members of a new family of nuclear receptor coactivators. We systematically determined the molecular basis and the structure/function relationship for the PNRC-ERalpha interaction. PNRC was found to interact with ERalpha mainly through its C-terminus region, amino acids 270-327, and an SH3-binding motif within this region was shown to be essential for PNRC to interact with and function as coactivator of ERalpha. The importance of the flanking sequences of SH3-binding motif in the interaction between PNRC and ERalpha was also investigated. The PNRC-interacting domain(s) on ERalpha was also mapped. PNRC was found to interact with both AF1 and LBD of ERalpha, and to function as a coactivator for both AF1 and AF2 transactivation functions. The interaction of ERalpha mutants, I358R, K362A, V376R, L539R and E542K, with PNRC/PNRC2 was further investigated. ERalpha/HBD/V376R could bind to PNRC or PNRC2, with similar affinity as wild-type ERalpha/HBD, and the transactivation activity of ERalpha/V376R was enhanced 5-fold by PNRC. Since GRIP1, a well-characterized coactivator, was found not to be able to enhance the transactivation function of this mutant, our results indicate that the PNRC-ERalpha interaction interface is not exactly identical to that of GRIP1-ERalpha interaction.

Indexed as

Amino Acid MotifsBinding SitesEstrogen Receptor alphaHeLa CellsHumansMutagenesis, Site-DirectedNuclear ProteinsProlineProtein BindingProtein Structure, TertiaryReceptors, Cytoplasmic and Nuclearsrc Homology DomainsTrans-ActivatorsTranscription FactorsEstrogen Receptor alphaNuclear ProteinsPNRC1 protein, humanPNRC2 protein, humanProlineReceptors, Cytoplasmic and NuclearTrans-ActivatorsTranscription Factors

Identifiers

PMID17068076
PMCPMC1635328
OpenAlexW2036477406

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC
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.