Evidence map›Paper›PMID 21713383›Full record

ReviewNaunyn-Schmiedeberg's archives of pharmacology2011

Protein-protein interactions: a mechanism regulating the anti-metastatic properties of Nm23-H1.

Natascia Marino, Jean-Claude Marshall, Patricia S Steeg

Open access · greenAbstract readReview
In one paragraph

Review in Naunyn-Schmiedeberg's archives of pharmacology, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 31 papers.

0numbers the graph read from it
0cells of the map it votes in
31citing papers in PubMed
3.3field-weighted citation impact, top 7% 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

31 citing papers in PubMed, 52 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. NME/NM23/NDPK and Histidine Phosphorylation.International journal of molecular sciences · 2020
    Review
  5. Review
  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. The dosage-dependent effect exerted by the NM23-H1/H2 homolog NDK-1 on distal tip cell migration in C. elegans.Laboratory investigation; a journal of technical methods and pathology · 2018
    Review
  10. Regulation of heterotrimeric G-protein signaling by NDPK/NME proteins and caveolins: an update.Laboratory investigation; a journal of technical methods and pathology · 2018
    Review
  11. Metastasis suppressors: functional pathways.Laboratory investigation; a journal of technical methods and pathology · 2018
    Review
  12. Article
  13. Article
  14. Article
  15. Article
  16. Nucleoside diphosphate kinases (NDPKs) in animal development.Cellular and molecular life sciences : CMLS · 2015
    Review
  17. Article
  18. Article
  19. Review
  20. 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.

Natascia MarinoWomen's Cancers Section, Laboratory of Molecular Pharmacology, Center for Cancer Research, National Cancer Institute, Bethesda, MD 20892, USA. Marinon@mail.nih.gov
Jean-Claude Marshall
Patricia S Steeg
National Cancer Institute · US

Funding

Molecular Biology of the Metastatic PhenotypeZIASC000892 · NCI · DIVISION OF CLINICAL SCIENCES - NCI · PI STEEG, PATRICIA SCHRIVER · 2009 to 2023
$8.4M
Molecular OncologyZ01BC010641 · NCI · BASIC SCIENCES · PI STEEG, PATRICIA SCHRIVER · 2005 to 2007
$220k
Intramural NIH HHS Z01 BC010641
6 · The paper itself

Abstract

Nm23-H1, also known as NDPK-A, was the first of a class of metastasis suppressor genes to be identified. Overexpression of Nm23-H1 in metastatic cell lines (melanoma, breast carcinoma, prostate, colon, hepatocellular, and oral squamous cell carcinoma) reduced cell motility in in vitro assays and metastatic potential in xenograft models, without a significant effect on primary tumor size. The mechanism of Nm23-H1 suppression of metastasis, however, is incompletely understood. Nm23-H1 has been reported to bind proteins, including those in small G-protein complexes, transcriptional complexes, the Map kinase, the TGF-β signaling pathways and the cytoskeleton. Evidence supporting these associations is presented together with evidence of resultant biochemical and phenotypic consequences of association. Cumulatively, the data suggest that part of the anti-metastatic function of Nm23-H1 lies in pathways that it interrupts via binding and inactivation of proteins.

Indexed as

Neoplasm MetastasisAnimalsGene Expression Regulation, NeoplasticHumansNM23 Nucleoside Diphosphate KinasesProtein BindingSignal TransductionNM23 Nucleoside Diphosphate Kinases

Identifiers

PMID21713383
PMCPMC6545597
OpenAlexW2023042488

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.