Evidence map›Paper›PMID 29400699›Full record

ArticleLaboratory investigation; a journal of technical methods and pathology2018

Characterization of a group I Nme protein of Capsaspora owczarzaki-a close unicellular relative of animals.

Helena Ćetković, Maja Herak Bosnar, Drago Perina, Andreja Mikoč, Martina Deželjin, Robert Belužić, Helena Bilandžija, Iñaki Ruiz-Trillo, Matija Harcet

Open access · bronzeAbstract read
PubMed Publisher
In one paragraph

Article in Laboratory investigation; a journal of technical methods and pathology, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.

0numbers the graph read from it
0cells of the map it votes in
4citing papers in PubMed
0.3field-weighted citation impact, top 44% 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

4 citing papers in PubMed, 7 citations in OpenAlex.

  1. Article
  2. Article
  3. Long-chain fatty acyl coenzyme A inhibits NME1/2 and regulates cancer metastasis.Proceedings of the National Academy of Sciences of the United States of America · 2022
    Article
  4. The NDPK/NME superfamily: state of the art.Laboratory investigation; a journal of technical methods and pathology · 2018
    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

9 authors at 3 institutions in 2 countries.

Helena ĆetkovićLaboratory of Molecular Genetics, Division of Molecular Biology, Ruđer Bošković Institute, Zagreb, Croatia.
Maja Herak BosnarLaboratory of Molecular Oncology, Division of Molecular Medicine, Ruđer Bošković Institute, Zagreb, Croatia.
Drago PerinaLaboratory of Molecular Genetics, Division of Molecular Biology, Ruđer Bošković Institute, Zagreb, Croatia.
Andreja MikočLaboratory of Molecular Genetics, Division of Molecular Biology, Ruđer Bošković Institute, Zagreb, Croatia.
Martina DeželjinLaboratory of Molecular Oncology, Division of Molecular Medicine, Ruđer Bošković Institute, Zagreb, Croatia.
Robert BelužićLaboratory of Molecular Oncology, Division of Molecular Medicine, Ruđer Bošković Institute, Zagreb, Croatia.
Helena BilandžijaLaboratory of Molecular Genetics, Division of Molecular Biology, Ruđer Bošković Institute, Zagreb, Croatia.
Iñaki Ruiz-TrilloInstitut de Biologia Evolutiva (CSIC-Universitat Pompeu Fabra), Institut de Biologia Evolutiva (CSIC-Universitat Pompeu Fabra), Passeig Marítim de la Barceloneta, Barcelona, Spain.
Matija HarcetLaboratory of Molecular Genetics, Division of Molecular Biology, Ruđer Bošković Institute, Zagreb, Croatia.
Ruđer Bošković Institute · HRInstitució Catalana de Recerca i Estudis Avançats · ESUniversitat Pompeu Fabra · ES

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Nucleoside diphosphate kinases are enzymes present in all domains of life. In animals, they are called Nme or Nm23 proteins, and are divided into group I and II. Human Nme1 was the first protein identified as a metastasis suppressor. Because of its medical importance, it has been extensively studied. In spite of the large research effort, the exact mechanism of metastasis suppression remains unclear. It is unknown which of the biochemical properties or biological functions are responsible for the antimetastatic role of the mammalian Nme1. Furthermore, it is not clear at which point in the evolution of life group I Nme proteins acquired the potential to suppress metastasis, a process that is usually associated with complex animals. In this study we performed a series of tests and assays on a group I Nme protein from filasterean Capsaspora owczarzaki, a close unicellular relative of animals. The aim was to compare the protein to the well-known human Nme1 and Nme2 homologs, as well as with the homolog from a simple animal-sponge (Porifera), in order to see how the proteins changed with the transition to multicellularity, and subsequently in the evolution of complex animals. We found that premetazoan-type protein is highly similar to the homologs from sponge and human, in terms of biochemical characteristics and potential biological functions. Like the human Nme1 and Nme2, it is able to diminish the migratory potential of human cancer cells in culture.

Indexed as

Cell MovementAmino Acid SequenceCell Migration AssaysEukaryotaEvolution, MolecularHeLa CellsHumansNM23 Nucleoside Diphosphate KinasesNM23 Nucleoside Diphosphate Kinases

Identifiers

PMID29400699
OpenAlexW2786301534

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.