Evidence map›Paper›PMID 20975703›Full record

ArticleNature communications2010

Calmodulin methyltransferase is an evolutionarily conserved enzyme that trimethylates Lys-115 in calmodulin.

Roberta Magnani, Lynnette M A Dirk, Raymond C Trievel, Robert L Houtz

Open access · bronzeAbstract read
PubMed Publisher
In one paragraph

Article in Nature communications, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 57 papers, 2 of them syntheses that pooled it.

0numbers the graph read from it
0cells of the map it votes in
57citing papers in PubMed, 2 pooled it
1.9field-weighted citation impact, top 15% 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

57 citing papers in PubMed, 2 syntheses or guidelines pooled it, 77 citations in OpenAlex.

  1. Genome-wide association study of shared liability to anxiety disorders in Army STARRS.American journal of medical genetics. Part B, Neuropsychiatric genetics : the official publication of the International Society of Psychiatric Genetics · 2020
    Pooled it
  2. Pooled it
  3. Review
  4. Article
  5. Article
  6. Review
  7. Article
  8. Article
  9. Calmodulin inMicroorganisms · 2022
    Review
  10. Protein methylation in mitochondria.The Journal of biological chemistry · 2022
    Review
  11. Article
  12. TypiCal but DeliCate CaFrontiers in plant science · 2021
    Review
  13. Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. Review
  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

4 authors at 2 institutions in 1 country.

Roberta MagnaniDepartment of Horticulture, Plant Physiology/Biochemistry/Molecular Biology Program, University of Kentucky, Lexington, Kentucky 40546, USA.
Lynnette M A Dirk
Raymond C Trievel
Robert L Houtz
University of Kentucky · USUniversity of Michigan–Ann Arbor · US

Funding

UNDERSTANDING THE MOLECULAR BASIS OF EPIGENETIC TRANSCRIPTIONAL SILENCINGP20RR020171 · NCRR · UNIVERSITY OF KENTUCKY · PI LOUIS HERSH, LOUIS HERSH LOUIS HERSH · 2004 to 2011
$16.5M
Structure and Function of SET Domain MethyltransferasesR01GM073839 · NIGMS · UNIVERSITY OF MICHIGAN AT ANN ARBOR · PI TRIEVEL, RAYMOND C · 2006 to 2010
$1.4M
NCRR NIH HHS P20 RR020171NIGMS NIH HHS R01 GM073839
6 · The paper itself

Abstract

Calmodulin (CaM) is a key mediator of calcium-dependent signalling and is subject to regulatory post-translational modifications, including trimethylation of Lys-115. In this paper, we identify a class I, non-SET domain protein methyltransferase, calmodulin-lysine N-methyltransferase (EC 2.1.1.60). A polypeptide chosen from a fraction enriched in calmodulin methyltransferase activity was trypsinized and analysed by tandem mass spectrometry. The amino-acid sequence obtained identified conserved, homologous proteins of unknown function across a wide range of species, thus implicating a broad role for lysine methylation in calcium-dependent signalling. Encoded by c2orf34, the human homologue is a component of two related multigene deletion syndromes in humans. Human, rat, frog, insect and plant homologues were cloned and Escherichia coli-recombinant proteins catalysed the formation of a trimethyllysyl residue at position 115 in CaM, as verified by product analyses and mass spectrometry.

Indexed as

Amino Acid SequenceAnimalsCalmodulinChromatography, LiquidChromatography, Thin LayerElectrophoresis, Polyacrylamide GelHumansInsect ProteinsLysineMethylationMethyltransferasesMolecular Sequence DataPlant ProteinsProtein Processing, Post-TranslationalProtein Structure, SecondaryRatsCalmodulincalmodulin methyltransferaseInsect ProteinsLysineMethyltransferasesPlant Proteins

Identifiers

PMID20975703
OpenAlexW1995572023

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.