Evidence map›Paper›PMID 29200201›Full record

ReviewLaboratory investigation; a journal of technical methods and pathology2018

The actions of NME1/NDPK-A and NME2/NDPK-B as protein kinases.

Paul V Attwood, Richmond Muimo

Open access · bronzeAbstract readReview
PubMed Publisher
In one paragraph

Review 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 26 papers.

0numbers the graph read from it
0cells of the map it votes in
26citing papers in PubMed
2.1field-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

26 citing papers in PubMed, 52 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. Review
  8. Review
  9. Article
  10. Review
  11. Article
  12. Revisiting trypanosomatid nucleoside diphosphate kinases.Memorias do Instituto Oswaldo Cruz · 2022
    Review
  13. [Roles of Histidine Kinases and Histidine Phosphatases in Cancer].Zhongguo fei ai za zhi = Chinese journal of lung cancer · 2021
    Review
  14. Article
  15. Article
  16. Review
  17. Review
  18. NME/NM23/NDPK and Histidine Phosphorylation.International journal of molecular sciences · 2020
    Review
  19. Article
  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

2 authors at 2 institutions in 2 countries.

Paul V AttwoodSchool of Molecular Sciences, The University of Western Australia (M310), Crawley, WA, Australia.
Richmond MuimoDepartment of Infection, Immunity and Cardiovascular Disease, The Medical School, University of Sheffield, Sheffield, UK.
The University of Western Australia · AUUniversity of Sheffield · GB

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Nucleoside diphosphate kinases (NDPKs) are multifunctional proteins encoded by the nme (non-metastatic cells) genes, also called NM23. NDPKs catalyze the transfer of γ-phosphate from nucleoside triphosphates to nucleoside diphosphates by a ping-pong mechanism involving the formation of a high-energy phosphohistidine intermediate. Growing evidence shows that NDPKs, particularly NDPK-B, can additionally act as a protein histidine kinase. Protein kinases and phosphatases that regulate reversible O-phosphorylation of serine, threonine, and tyrosine residues have been studied extensively in many organisms. Interestingly, other phosphoamino acids histidine, lysine, arginine, aspartate, glutamate, and cysteine exist in abundance but remain understudied due to the paucity of suitable methods and antibodies. The N-phosphorylation of histidine by histidine kinases via the two- or multi-component signaling systems is an important mediator in cellular responses in prokaryotes and lower eukaryotes, like yeast, fungi, and plants. However, in vertebrates knowledge of phosphohistidine signaling has lagged far behind and the identity of the protein kinases and protein phosphatases involved is not well established. This article will therefore provide an overview of our current knowledge on protein histidine phosphorylation particularly the role of nm 23 gene products as protein histidine kinases.

Indexed as

AnimalsCalcium ChannelsCystic Fibrosis Transmembrane Conductance RegulatorGTP-Binding ProteinsHistidine KinaseHumansNeoplasm MetastasisNM23 Nucleoside Diphosphate KinasesPhosphorylationPotassium Channels, Calcium-ActivatedCalcium ChannelsCystic Fibrosis Transmembrane Conductance RegulatorGTP-Binding ProteinsHistidine KinaseNM23 Nucleoside Diphosphate KinasesPotassium Channels, Calcium-Activated

Identifiers

PMID29200201
OpenAlexW2772158603

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.