Evidence map›Paper›PMID 19609660›Full record

ArticleJournal of computational neuroscience2009

Dissecting cooperative calmodulin binding to CaM kinase II: a detailed stochastic model.

Michael J Byrne, John A Putkey, M Neal Waxham, Yoshihisa Kubota

Open access · greenAbstract read
In one paragraph

Article in Journal of computational neuroscience, 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
3.2field-weighted citation impact, top 9% 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, 23 citations in OpenAlex.

  1. Article
  2. Article
  3. Astrocyte Intracellular CaNeurotoxicity research · 2021
    Article
  4. Article
  5. Bilobal architecture is a requirement for calmodulin signaling to CaProceedings of the National Academy of Sciences of the United States of America · 2018
    Article
  6. Article
  7. Conformational frustration in calmodulin-target recognition.Journal of molecular recognition : JMR · 2015
    Article
  8. Article
  9. The delicate bistability of CaMKII.Biophysical journal · 2013
    Article
  10. Article
  11. Article
  12. Mechanisms of CaMKII action in long-term potentiation.Nature reviews. Neuroscience · 2012
    Review
  13. Ca(2+) sensor proteins in dendritic spines: a race for Ca(2+).Frontiers in molecular neuroscience · 2012
    Article
  14. Article
  15. Article
  16. Sequestration of CaMKII in dendritic spines in silico.Journal of computational neuroscience · 2011
    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

4 authors at 1 institution in 1 country.

Michael J ByrneDepartment of Neurobiology and Anatomy, University of Texas Medical School, Houston, TX 77030, USA.
John A Putkey
M Neal Waxham
Yoshihisa Kubota
The University of Texas Health Science Center at Houston · US

Funding

Neural Models of Plasticity: Molecules to NetworksP01NS038310 · NINDS · UNIVERSITY OF TEXAS HLTH SCI CTR HOUSTON · PI BYRNE, JOHN H · 1999 to 2009
$9.3M
STRUCTURE/FUNCTION OF CAM-KINASE IIR01NS026086 · NINDS · UNIVERSITY OF TEXAS HLTH SCI CTR HOUSTON · PI WAXHAM, M. NEAL · 1988 to 2012
$4.2M
Calcium-Dependent Protein RegulationR01GM069611 · NIGMS · UNIVERSITY OF TEXAS HLTH SCI CTR HOUSTON · PI PUTKEY, JOHN ANTHONY · 2005 to 2008
$1.1M
Training in NeuroplasticityT32NS041226 · NINDS · UNIVERSITY OF TEXAS HLTH SCI CTR HOUSTON · PI WAXHAM, M. NEAL · 2001 to 2005
$748k
Structure and Function of CaM-Kinase IIR56NS026086 · NINDS · UNIVERSITY OF TEXAS HLTH SCI CTR HOUSTON · PI WAXHAM, M. NEAL · 2008 to 2008
$375k
NIGMS NIH HHS GM069611NIGMS NIH HHS R01 GM069611NINDS NIH HHS NS038310NINDS NIH HHS NS 041226NINDS NIH HHS NS26086NINDS NIH HHS P01 NS038310NINDS NIH HHS R01 NS026086NINDS NIH HHS R56 NS026086NINDS NIH HHS T32 NS041226
6 · The paper itself

Abstract

Calmodulin (CaM) is a major Ca(2+) binding protein involved in two opposing processes of synaptic plasticity of CA1 pyramidal neurons: long-term potentiation (LTP) and depression (LTD). The N- and C-terminal lobes of CaM bind to its target separately but cooperatively and introduce complex dynamics that cannot be well understood by experimental measurement. Using a detailed stochastic model constructed upon experimental data, we have studied the interaction between CaM and Ca(2+)-CaM-dependent protein kinase II (CaMKII), a key enzyme underlying LTP. The model suggests that the accelerated binding of one lobe of CaM to CaMKII, when the opposing lobe is already bound to CaMKII, is a critical determinant of the cooperative interaction between Ca(2+), CaM, and CaMKII. The model indicates that the target-bound Ca(2+) free N-lobe has an extended lifetime and may regulate the Ca(2+) response of CaMKII during LTP induction. The model also reveals multiple kinetic pathways which have not been previously predicted for CaM-dissociation from CaMKII.

Indexed as

Models, BiologicalStochastic ProcessesAlgorithmsAnimalsBinding SitesCalciumCalcium-Calmodulin-Dependent Protein KinasesCalcium SignalingCalmodulinDose-Response Relationship, DrugLong-Term PotentiationTime FactorsCalciumCalcium-Calmodulin-Dependent Protein KinasesCalmodulin

Identifiers

PMID19609660
PMCPMC3617043
OpenAlexW1990999093

What OpenQuestion holds

Textmetadata
LicenceTDM
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.