Evidence map›Paper›PMID 24961462›Full record

ReviewNaunyn-Schmiedeberg's archives of pharmacology2015

Nucleoside diphosphate kinase as protein histidine kinase.

Paul V Attwood, Thomas Wieland

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 28 papers.

0numbers the graph read from it
0cells of the map it votes in
28citing 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

28 citing papers in PubMed, 56 citations in OpenAlex.

  1. Article
  2. Article
  3. Structure, Folding and Stability of Nucleoside Diphosphate Kinases.International journal of molecular sciences · 2020
    Review
  4. Review
  5. Review
  6. Review
  7. Nonmetabolic functions of metabolic enzymes in cancer development.Cancer communications (London, England) · 2018
    Review
  8. Article
  9. Regulation of KDiabetes · 2018
    Article
  10. Article
  11. Metabolic Kinases Moonlighting as Protein Kinases.Trends in biochemical sciences · 2018
    Review
  12. The actions of NME1/NDPK-A and NME2/NDPK-B as protein kinases.Laboratory investigation; a journal of technical methods and pathology · 2018
    Review
  13. Article
  14. NM23/NDPK proteins in transcription regulatory functions and chromatin modulation: emerging trends.Laboratory investigation; a journal of technical methods and pathology · 2018
    Review
  15. 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
  16. Article
  17. Article
  18. Article
  19. Article
  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

2 authors at 2 institutions in 2 countries.

Paul V AttwoodSchool of Chemistry and Biochemistry, The University of Western Australia (M310), 35 Stirling Highway, Crawley, WA, 6009, Australia, paul.attwood@uwa.edu.au.
Thomas Wieland
Heidelberg University · DEUniversity of Western Australia · AU

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Like phosphorylation of serine, threonine, and tyrosine residues in many organisms, reversible histidine phosphorylation is a well-known regulatory signal in prokaryotes and lower eukaryotes. In vertebrates, phosphohistidine has been mainly described as a phosphorylated intermediate in enzymatic reactions, and it was believed that regulatory histidine phosphorylation is of minor importance. During the last decade, it became evident however, that nucleoside diphosphate kinase (NDPK), an ubiquitously expressed enzyme required for nucleotide homeostasis, can additionally act as a protein histidine kinase. Especially for the isoform NDPK B, at least three defined substrates, the β subunit of heterotrimeric G proteins (Gβ), the intermediate conductance potassium channel KCa3.1, and the Ca(2+)-conducting TRP channel family member, TRPV5, have been identified. In all three proteins, the phosphorylation of a specific histidine residue is of regulatory importance for protein function, and these phosphohistidines are cleaved by a counteracting 14 kDa phosphohistidine phosphatase (PHP). This article will therefore give an overview of our current knowledge on protein histidine phosphorylation in prokaryotes and lower eukaryotes and compare it with the regulatory phosphorylation and dephosphorylation of histidine residues in vertebrates by NDPK and PHP, respectively.

Indexed as

AnimalsHistidineHistidine KinaseHumansNucleoside-Diphosphate KinasePhosphorylationProtein KinasesHistidineHistidine KinaseNucleoside-Diphosphate KinaseProtein Kinases

Identifiers

PMID24961462
OpenAlexW2065714102

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.