Evidence map›Paper›PMID 26589967›Full record

ReviewBioscience reports2015

Nucleotide-binding mechanisms in pseudokinases.

Henrik M Hammarén, Anniina T Virtanen, Olli Silvennoinen

Abstract readReview
In one paragraph

Review in Bioscience reports, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.

0numbers the graph read from it
0cells of the map it votes in
23citing papers in PubMed
–field-weighted citation impact
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

23 citing papers in PubMed.

  1. Article
  2. Review
  3. Emerging functions of pseudoenzymes.The Biochemical journal · 2023
    Review
  4. Article
  5. Transforming growth factor-β signalling regulates protoscolex formation in theFrontiers in cellular and infection microbiology · 2023
    Article
  6. Article
  7. The EphB6 Receptor: Kinase-Dead but Very Much Alive.International journal of molecular sciences · 2021
    Review
  8. Robustness of plant quantitative disease resistance is provided by a decentralized immune network.Proceedings of the National Academy of Sciences of the United States of America · 2020
    Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. ARGuing for a new kinase class.Nature chemical biology · 2019
    Article
  14. Selective JAKinibs: Prospects in Inflammatory and Autoimmune Diseases.BioDrugs : clinical immunotherapeutics, biopharmaceuticals and gene therapy · 2019
    Review
  15. Article
  16. Article
  17. Article
  18. Review
  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

3 authors.

Henrik M HammarénSchool of Medicine, University of Tampere, Biokatu 8, FI-33014 Tampere, Finland henrik.hammaren@uta.fi olli.silvennoinen@uta.fi.
Anniina T VirtanenSchool of Medicine, University of Tampere, Biokatu 8, FI-33014 Tampere, Finland.
Olli SilvennoinenSchool of Medicine, University of Tampere, Biokatu 8, FI-33014 Tampere, Finland Clinical Hematology, Department of Internal Medicine, Tampere University Hospital, Medisiinarinkatu 3, FI-33520 Tampere, Finland henrik.hammaren@uta.fi olli.silvennoinen@uta.fi.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Pseudokinases are classified by the lack of one or several of the highly conserved motifs involved in nucleotide (nt) binding or catalytic activity of protein kinases (PKs). Pseudokinases represent ∼10% of the human kinome and they are found in all evolutionary classes of kinases. It has become evident that pseudokinases, which were initially considered somewhat peculiar dead kinases, are important components in several signalling cascades. Furthermore, several pseudokinases have been linked to human diseases, particularly cancer, which is raising interest for therapeutic approaches towards these proteins. The ATP-binding pocket is a well-established drug target and elucidation of the mechanism and properties of nt binding in pseudokinases is of significant interest and importance. Recent studies have demonstrated that members of the pseudokinase family are very diverse in structure as well as in their ability and mechanism to bind nts or perform phosphoryl transfer reactions. This diversity also precludes prediction of pseudokinase function, or the importance of nt binding for said function, based on primary sequence alone. Currently available data indicate that ∼40% of pseudokinases are able to bind nts, whereas only few are able to catalyse occasional phosphoryl transfer. Pseudokinases employ diverse mechanisms to bind nts, which usually occurs at low, but physiological, affinity. ATP binding serves often a structural role but in most cases the functional roles are not precisely known. In the present review, we discuss the various mechanisms that pseudokinases employ for nt binding and how this often low-affinity binding can be accurately analysed.

Indexed as

Adenosine TriphosphateAmino Acid MotifsAnimalsBinding SitesHumansPhosphotransferasesProtein Structure, TertiaryAdenosine TriphosphatePhosphotransferasesATPkinase activitykinomenucleotide bindingpseudokinasesignalling

Identifiers

PMID26589967
PMCPMC4718504

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Registered trials

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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.