Evidence map›Paper›PMID 38180572›Full record

ReviewCancer metastasis reviews2024

PRUNE1 and NME/NDPK family proteins influence energy metabolism and signaling in cancer metastases.

Veronica Ferrucci, Santosh Lomada, Thomas Wieland, Massimo Zollo

Open access · hybridAbstract readReview
In one paragraph

Review in Cancer metastasis reviews, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.

0numbers the graph read from it
0cells of the map it votes in
9citing papers in PubMed
2.3field-weighted citation impact, top 12% 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

9 citing papers in PubMed, 10 citations in OpenAlex.

  1. Article
  2. Article
  3. Review
  4. Article
  5. Article
  6. Article
  7. Schmiedeberg Medal for Thomas Wieland: an artist of G-protein signaling.Naunyn-Schmiedeberg's archives of pharmacology · 2025
    Article
  8. Article
  9. 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

4 authors at 3 institutions in 2 countries.

Veronica Ferrucci *Department of Molecular Medicine and Medical Biotechnology, DMMBM, University of Naples, Federico II, Via Pansini 5, 80131, Naples, Italy.
Santosh Lomada *Experimental Pharmacology Mannheim, European Center for Angioscience, Medical Faculty Mannheim, Heidelberg University, 68167, Mannheim, Germany.
Thomas WielandExperimental Pharmacology Mannheim, European Center for Angioscience, Medical Faculty Mannheim, Heidelberg University, 68167, Mannheim, Germany. thomas.wieland@medma.uni-heidelberg.de.
Massimo ZolloDepartment of Molecular Medicine and Medical Biotechnology, DMMBM, University of Naples, Federico II, Via Pansini 5, 80131, Naples, Italy. massimo.zollo@unina.it.
Ceinge Biotecnologie Avanzate (Italy) · ITGerman Centre for Cardiovascular Research · DEHeidelberg University · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

We describe here the molecular basis of the complex formation of PRUNE1 with the tumor metastasis suppressors NME1 and NME2, two isoforms appertaining to the nucleoside diphosphate kinase (NDPK) enzyme family, and how this complex regulates signaling the immune system and energy metabolism, thereby shaping the tumor microenvironment (TME). Disrupting the interaction between NME1/2 and PRUNE1, as suggested, holds the potential to be an excellent therapeutic target for the treatment of cancer and the inhibition of metastasis dissemination. Furthermore, we postulate an interaction and regulation of the other Class I NME proteins, NME3 and NME4 proteins, with PRUNE1 and discuss potential functions. Class I NME1-4 proteins are NTP/NDP transphosphorylases required for balancing the intracellular pools of nucleotide diphosphates and triphosphates. They regulate different cellular functions by interacting with a large variety of other proteins, and in cancer and metastasis processes, they can exert pro- and anti-oncogenic properties depending on the cellular context. In this review, we therefore additionally discuss general aspects of class1 NME and PRUNE1 molecular structures as well as their posttranslational modifications and subcellular localization. The current knowledge on the contributions of PRUNE1 as well as NME proteins to signaling cascades is summarized with a special regard to cancer and metastasis.

Indexed as

Energy MetabolismNeoplasm MetastasisNeoplasmsNM23 Nucleoside Diphosphate KinasesSignal TransductionAcid Anhydride HydrolasesAnimalsHumansNucleoside-Diphosphate KinasePhosphoric Monoester HydrolasesTumor MicroenvironmentAcid Anhydride HydrolasesNM23 Nucleoside Diphosphate KinasesNME1 protein, humanNucleoside-Diphosphate KinasePhosphoric Monoester HydrolasesPRUNE1 protein, humanEnergy metabolismExopolyphosphataseImmune systemNME familyNMR structuresNucleoside diphosphate kinase NDPKPRUNE1Tumor microenvironment

Identifiers

PMID38180572
PMCPMC11156750
OpenAlexW4390614929

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.