Evidence map›Paper›PMID 17906697›Full record

ArticleOncogene2008

Phosphorylation of nm23-H1 by CKI induces its complex formation with h-prune and promotes cell motility.

L Garzia, A D'Angelo, A Amoresano, S K Knauer, C Cirulli, C Campanella, R H Stauber, C Steegborn, A Iolascon, M Zollo

Abstract read
PubMed Publisher
In one paragraph

Article in Oncogene, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 33 papers.

0numbers the graph read from it
0cells of the map it votes in
33citing 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

33 citing papers in PubMed, 51 citations in OpenAlex.

  1. Article
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  7. Article
  8. NME/NM23/NDPK and Histidine Phosphorylation.International journal of molecular sciences · 2020
    Review
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  12. Review
  13. Review
  14. Article
  15. Article
  16. Article
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  18. Article
  19. Regulation of the metastasis suppressor Nm23-H1 by tumor viruses.Naunyn-Schmiedeberg's archives of pharmacology · 2015
    Review
  20. 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

10 authors at 3 institutions in 2 countries.

L GarziaCEINGE, Centro di Ingegneria Genetica e Biotecnologie Avanzate, Naples, Italy.
A D'Angelo
A Amoresano
S K Knauer
C Cirulli
C Campanella
R H Stauber
C Steegborn
A Iolascon
M Zollo
University of Naples Federico II · ITGeorg Speyer Haus · DERuhr University Bochum · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The combination of an increase in the cAMP-phosphodiesterase activity of h-prune and its interaction with nm23-H1 have been shown to be key steps in the induction of cellular motility in breast cancer cells. Here we present the molecular mechanisms of this interaction. The region of the nm23-h-prune interaction lies between S120 and S125 of nm23, where missense mutants show impaired binding; this region has been highly conserved throughout evolution, and can undergo serine phosphorylation by casein kinase I. Thus, the casein kinase I delta-epsilon specific inhibitor IC261 impairs the formation of the nm23-h-prune complex, which translates 'in vitro' into inhibition of cellular motility in a breast cancer cellular model. A competitive permeable peptide containing the region for phosphorylation by casein kinase I impairs cellular motility to the same extent as IC261. The identification of these two modes of inhibition of formation of the nm23-H1-h-prune protein complex pave the way toward new challenges, including translational studies using IC261 or this competitive peptide 'in vivo' to inhibit cellular motility induced by nm23-H1-h-prune complex formation during progression of breast cancer.

Indexed as

Cell MovementAnimalsBinding, CompetitiveBreast NeoplasmsCaenorhabditis elegansCarrier ProteinsCell CommunicationChlorocebus aethiopsCOS CellsCyclin-Dependent Kinase Inhibitor ProteinsDrosophila melanogasterHumansIndolesNM23 Nucleoside Diphosphate KinasesPeptide FragmentsPhloroglucinolCarrier ProteinsCyclin-Dependent Kinase Inhibitor ProteinsIC 261IndolesNM23 Nucleoside Diphosphate KinasesPeptide FragmentsPhloroglucinolPhosphoric Diester HydrolasesPhosphoric Monoester HydrolasesPRUNE1 protein, human

Identifiers

PMID17906697
OpenAlexW2047091025

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.