Evidence map›Paper›PMID 18571832›Full record

ReviewMolecular and cellular endocrinology2008

PELP1--a novel estrogen receptor-interacting protein.

Darrell W Brann, Quan-Guang Zhang, Rui-Min Wang, Virendra B Mahesh, Ratna K Vadlamudi

Open access · greenAbstract readReview
In one paragraph

Review in Molecular and cellular endocrinology, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.

0numbers the graph read from it
0cells of the map it votes in
23citing papers in PubMed
2.3field-weighted citation impact, top 12% 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

23 citing papers in PubMed, 49 citations in OpenAlex.

  1. Article
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  4. Review
  5. Review
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  8. Proline-, glutamic acid-, and leucine-rich protein 1 mediates estrogen rapid signaling and neuroprotection in the brain.Proceedings of the National Academy of Sciences of the United States of America · 2015
    Article
  9. Article
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  12. Article
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  15. Article
  16. Review
  17. Review
  18. Article
  19. Article
  20. Estrogen and its role in gastrointestinal health and disease.International journal of colorectal disease · 2009
    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

5 authors at 3 institutions in 2 countries.

Darrell W BrannInstitute of Molecular Medicine and Genetics, Department of Neurology, Medical College of Georgia, 1120 15th Street, Augusta, GA 30912, USA. dbrann@mcg.edu
Quan-Guang Zhang
Rui-Min Wang
Virendra B Mahesh
Ratna K Vadlamudi
Augusta University · USNorth China University of Science and Technology · CNThe University of Texas Health Science Center at San Antonio · US

Funding

Neuroprotective and Neurogenic Actions of E2 and SERMsR01NS050730 · NINDS · MEDICAL COLLEGE OF GEORGIA (MCG) · PI BRANN, DARRELL W, VADLAMUDI, RATNA K · 2005 to 2014
$3.2M
PELP1, a Novel Regulator of Estrogen ReceptorR01CA095681 · NCI · UNIVERSITY OF TEXAS MD ANDERSON CAN CTR · PI VADLAMUDI, RATNA K · 2003 to 2013
$2.5M
NCI NIH HHS R01 CA095681NINDS NIH HHS R01 NS050730
6 · The paper itself

Abstract

PELP1 (proline-, glutamic acid-, and leucine-rich protein-1) is a novel estrogen receptor (ER)-interacting protein that has been implicated to be important for mediation of both the genomic and nongenomic signaling of 17beta-estradiol (E2). PELP1 contains ten nuclear receptor-interacting boxes (LXXLL motifs), which allow it to interact with ER and other nuclear hormone receptors, a zinc finger, a glutamic acid-rich domain, and two proline-rich domains. The proline-rich regions contain several consensus PXXP motifs, which allow PELP1 to couple the ER with SH3 domain-containing kinase signaling proteins, such as Src and PI3K P85 regulatory subunit. PELP1 is expressed in many different brain regions, including the hippocampus, hypothalamus, and cerebral cortex. Further work has demonstrated that PELP1 is colocalized with ER-alpha in neurons in various brain regions. PELP1 is primarily expressed in neurons, with some expression also observed in glia. Subcellular localization studies revealed that PELP1 is highly localized in the cell nucleus of neurons, with some cytoplasm localization as well, and PELP1 is also localized at synaptic sites. Work in other tissues has demonstrated that PELP1 is critical for nongenomic and genomic signaling by E2, as PELP1 knockdown studies significantly attenuates E2-induced activation of ERK and Akt signaling pathways, and inhibits E2 genomic transcriptional effects on gene expression in breast cancer cells. Preliminary studies in the brain, suggests that similar roles may exist for PELP1 in the brain, but this remains to be established, and further work to characterize the precise roles and functions of PELP1 in the brain are needed.

Indexed as

AnimalsHumansProtein BindingProtein Processing, Post-TranslationalProtein Structure, TertiaryReceptors, EstrogenTrans-ActivatorsReceptors, EstrogenTrans-Activators

Identifiers

PMID18571832
PMCPMC2578818
OpenAlexW1987387393

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.