Evidence map›Paper›PMID 25366701›Full record

ReviewNaunyn-Schmiedeberg's archives of pharmacology2015

Janus-faces of NME-oncoprotein interactions.

Nikolina Vlatković, Shie-Hong Chang, Mark T Boyd

Abstract readReview
PubMed Publisher
In one paragraph

Review in Naunyn-Schmiedeberg's archives of pharmacology, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.

0numbers the graph read from it
0cells of the map it votes in
10citing papers in PubMed
0.4field-weighted citation impact, top 38% 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

10 citing papers in PubMed, 15 citations in OpenAlex.

  1. Comprehensive analysis of theTranslational cancer research · 2020
    Article
  2. Structure, Folding and Stability of Nucleoside Diphosphate Kinases.International journal of molecular sciences · 2020
    Review
  3. NME/NM23/NDPK and Histidine Phosphorylation.International journal of molecular sciences · 2020
    Review
  4. Article
  5. Expression of nm23-H1, p53, and integrin β1 in endometriosis and their clinical significance.International journal of clinical and experimental pathology · 2020
    Article
  6. Article
  7. Article
  8. Modulation of small GTPase activity by NME proteins.Laboratory investigation; a journal of technical methods and pathology · 2018
    Review
  9. NDPKA is not just a metastasis suppressor - be aware of its metastasis-promoting role in neuroblastoma.Laboratory investigation; a journal of technical methods and pathology · 2018
    Article
  10. 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

3 authors at 1 institution in 1 country.

Nikolina Vlatkovićp53/MDM2 Research Team, Cancer Research Centre, University of Liverpool, 200 London Road, Liverpool, L3 9TA, UK.
Shie-Hong Chang
Mark T Boyd
University of Liverpool · GB

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Since the identification of Nm23 (NME1, NME/NM23 nucleoside diphosphate kinase 1) as the first non-metastatic protein, a great deal of research on members of the NME family of proteins has focused on roles in processes implicated in carcinogenesis and particularly their regulation of cellular motility and the process of metastatic spread. To date, there are ten identified members of this family of genes, and these can be dichotomized into groups both taxonomically and by the presence or absence of their nucleoside diphosphate kinase activity with NMEs 1-4 encoding nucleoside diphosphate kinases (NDPKs) and NMEs 5-9 plus RP2 displaying little if any NDPK activity. NMEs are relatively small proteins that can form hetero-oligomers (typically hexamers), and given the apparent genetic redundancy of some NMEs and the number of different isoforms, it is perhaps not surprising that there remains a great deal of uncertainty regarding their function and even more regarding cellular mechanisms of action. Since residues that contribute to NDPK activity span much of the protein, it seems likely that the consequences of NME expression must be mediated through their NDPK activity, through interactions with other structures in cells including protein-protein interactions or through combinations of these. Our goal in this review is to focus on some of the protein-protein interactions that have been identified and to highlight some of the challenges that face this area of research.

Indexed as

AnimalsCell AdhesionDynaminsHumansIntegrinsNeoplasmsNM23 Nucleoside Diphosphate KinasesOncogene Proteinsras ProteinsTelomeraseTelomereViral ProteinsDynaminsIntegrinsNM23 Nucleoside Diphosphate KinasesOncogene Proteinsras ProteinsTelomeraseViral Proteins

Identifiers

PMID25366701
OpenAlexW1976673187

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.