Evidence map›Paper›PMID 19343785›Full record

ArticleJournal of cellular biochemistry2009

Evidence for phosphatase activity of p27SJ and its impact on the cell cycle.

Nune Darbinian, Marta Czernik, Armine Darbinyan, Mikael Elias, Eric Chabriere, Surekha Bonasu, Kamel Khalili, Shohreh Amini

Erratum issuedOpen access · greenAbstract read
In one paragraph

Article in Journal of cellular biochemistry, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 18 papers.

0numbers the graph read from it
0cells of the map it votes in
18citing papers in PubMed
1.2field-weighted citation impact, top 22% 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, 25 citations in OpenAlex.

  1. Article
  2. DING Proteins Extend to the Extremophilic World.International journal of molecular sciences · 2021
    Review
  3. Article
  4. Article
  5. Article
  6. Article
  7. DING proteins: numerous functions, elusive genes, a potential for health.Cellular and molecular life sciences : CMLS · 2013
    Review
  8. Article
  9. Crystallization and preliminary X-ray diffraction analysis of a DING protein from Pseudomonas aeruginosa PA14.Acta crystallographica. Section F, Structural biology and crystallization communications · 2013
    Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Article
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

8 authors at 2 institutions in 2 countries.

Nune DarbinianDepartment of Neuroscience, Center for Neurovirology, Temple University School of Medicine, Philadelphia, Pennsylvania 19122, USA.
Marta Czernik
Armine Darbinyan
Mikael Elias
Eric Chabriere
Surekha Bonasu
Kamel Khalili
Shohreh Amini
Temple University · USArchitecture et Fonction des Macromolécules Biologiques · FR

Funding

Suppression of HIV-1 in CNS by a novel protein from ST John's WortR01MH074392 · NIMH · TEMPLE UNIV OF THE COMMONWEALTH · PI AMINI, SHOHREH · 2006 to 2010
$1.6M
NIMH NIH HHS 1R01 MH074392NIMH NIH HHS R01 MH074392
6 · The paper itself

Abstract

p27SJ, a novel protein isolated from St John's wort (Hypericum perforatum), belongs to an emerging family of DING proteins that are related to a prokaryotic phosphate-binding protein superfamily. Here we demonstrate that p27SJ exhibits phosphatase activity and that its expression in cells decreases the level of phosphorylated Erk1/2, a key protein of several signaling pathways. Treatment of p27SJ-expressing cells with phosphatase inhibitors including okadaic acid, maintained Erk1/2 in its phosphorylated form, suggesting that dephosphorylation of Erk1/2 is mediated by p27SJ. Further, expression of p27SJ affects Erk1/2 downstream regulatory targets such as STAT3 and CREB. Moreover, the level of expression of cyclin A that associates with active ERK1/2 and is regulated by CREB, was modestly reduced in p27SJ-expressing cells. Accordingly, results from in vitro kinase assays revealed a noticeable decrease in the activity of cyclin A in cells expressing p27SJ. Cell cycle analysis demonstrated dysregulation at S and G2/M phases in cells expressing p27SJ, supporting the notion that a decline in cyclin A activity by p27SJ has a biological impact on cell growth. These observations provide evidence that p27SJ alters the state of Erk1/2 phosphorylation, and impacts several biological events associated with cell growth and function.

Indexed as

Cell CycleCell Line, TumorDNA-Binding ProteinsHumansHypericumMitogen-Activated Protein Kinase 1Models, BiologicalPhosphoprotein PhosphatasesPhosphorylationPlant ProteinsProtein ConformationDNA-Binding ProteinsMitogen-Activated Protein Kinase 1Phosphoprotein PhosphatasesPlant Proteins

Identifiers

PMID19343785
PMCPMC2769080
OpenAlexW2036917332

What OpenQuestion holds

Textmetadata
LicenceTDM
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.