Evidence map›Paper›PMID 19415486›Full record

ReviewNeurochemical research2009

Regulation of CaMKII in vivo: the importance of targeting and the intracellular microenvironment.

Kathryn A Skelding, John A P Rostas

Abstract readReview
PubMed Publisher
In one paragraph

Review in Neurochemical research, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.

0numbers the graph read from it
0cells of the map it votes in
20citing papers in PubMed
2.2field-weighted citation impact, top 14% 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

20 citing papers in PubMed, 39 citations in OpenAlex.

  1. Article
  2. Review
  3. PINK1 and Parkin regulate IPNature communications · 2023
    Article
  4. Article
  5. Calmodulin as CaInternational journal of molecular sciences · 2021
    Article
  6. Review
  7. Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Visualizing CaMKII and CaM activity: a paradigm of compartmentalized signaling.Journal of molecular medicine (Berlin, Germany) · 2013
    Review
  14. Review
  15. αCaMKII is differentially regulated in brain regions that exhibit differing sensitivities to ischemia and excitotoxicity.Journal of cerebral blood flow and metabolism : official journal of the International Society of Cerebral Blood Flow and Metabolism · 2012
    Article
  16. Article
  17. Article
  18. Review
  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

2 authors at 1 institution in 1 country.

Kathryn A SkeldingSchool of Biomedical Sciences and Hunter Medical Research Institute, Faculty of Health, The University of Newcastle, Callaghan, NSW 2308, Australia.
John A P Rostas
Hunter Medical Research Institute · AU

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

CaMKII (calcium/calmodulin-stimulated protein kinase II) is a multifunctional protein kinase that regulates normal neuronal function. CaMKII is regulated by multi-site phosphorylation, which can alter enzyme activity, and targeting to cellular microdomains through interactions with binding proteins. These proteins integrate CaMKII into multiple signalling pathways, which lead to varied functional outcomes following CaMKII phosphorylation, depending on the identity and location of the binding partner. A new phosphorylation site on CaMKII (Thr253) has been identified in vivo. Thr253 phosphorylation controls CaMKII purely by targeting, does not effect enzyme activity, and occurs in response to physiological and pathological stimuli in vivo, but only in CaMKII molecules present in specific cellular locations. This new phosphorylation site offers a potentially novel regulatory mechanism for controlling functional responses elicited by CaMKII that are restricted to specific subcellular locations and/or certain cell types, by controlling interactions with proteins that are expressed in the cell at that location.

Indexed as

AnimalsCalcium-Calmodulin-Dependent Protein Kinase Type 2HumansIntracellular FluidMembrane ProteinsPhosphorylationProtein BindingProtein TransportSignal TransductionThreonineCalcium-Calmodulin-Dependent Protein Kinase Type 2Membrane ProteinsThreonine

Identifiers

PMID19415486
OpenAlexW1976525781

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.