Evidence map›Paper›PMID 21074407›Full record

ReviewCurrent opinion in structural biology2010

Pseudokinases-remnants of evolution or key allosteric regulators?

Elton Zeqiraj, Daan M F van Aalten

Abstract readReview
In one paragraph

Review in Current opinion in structural biology, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 84 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
84citing papers in PubMed, 1 pooled it
–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

84 citing papers in PubMed, 1 synthesis or guideline pooled it.

  1. Pooled it
  2. Article
  3. Modulating pseudokinase conformation from the ATP-binding site.Structure (London, England : 1993) · 2026
    Article
  4. Review
  5. Review
  6. Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Illumination of understudied ciliary kinases.Frontiers in molecular biosciences · 2024
    Review
  13. Article
  14. A PAX6-regulated receptor tyrosine kinase pairs with a pseudokinase to activate immune defense upon oomycete recognition inProceedings of the National Academy of Sciences of the United States of America · 2023
    Article
  15. Emerging functions of pseudoenzymes.The Biochemical journal · 2023
    Review
  16. Article
  17. Review
  18. Article
  19. ULK4 in Neurodevelopmental and Neuropsychiatric Disorders.Frontiers in cell and developmental biology · 2022
    Review
  20. The EphB6 Receptor: Kinase-Dead but Very Much Alive.International journal of molecular sciences · 2021
    Review

24 more citing papers are in PubMed but not listed here.

4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

2 authors.

Elton ZeqirajSamuel Lunenfeld Research Institute, Mount Sinai Hospital, 600 University Avenue, Room 1090, Toronto, Ontario M5G 1X5, Canada. zeqiraj@lunenfeld.ca
Daan M F van Aalten

Funding

Cancer Research UK A10969Cancer Research UK C33794/A10969aMedical Research Council G0900138Wellcome Trust 087590Wellcome Trust 092381
6 · The paper itself

Abstract

Protein kinases provide a platform for the integration of signal transduction networks. A key feature of transmitting these cellular signals is the ability of protein kinases to activate one another by phosphorylation. A number of kinases are predicted by sequence homology to be incapable of phosphoryl group transfer due to degradation of their catalytic motifs. These are termed pseudokinases and because of the assumed lack of phosphoryltransfer activity their biological role in cellular transduction has been mysterious. Recent structure-function studies have uncovered the molecular determinants for protein kinase inactivity and have shed light to the biological functions and evolution of this enigmatic subset of the human kinome. Pseudokinases act as signal transducers by bringing together components of signalling networks, as well as allosteric activators of active protein kinases.

Indexed as

Evolution, MolecularAllosteric RegulationAmino Acid SequenceAnimalsHumansMolecular Sequence DataNucleotidesProtein KinasesPseudogenesNucleotidesProtein Kinases

Identifiers

PMID21074407
PMCPMC3014569

What OpenQuestion holds

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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.