Evidence map›Paper›PMID 11931644›Full record

ReviewThe Biochemical journal2002

Structure-function of the multifunctional Ca2+/calmodulin-dependent protein kinase II.

Andy Hudmon, Howard Schulman

Abstract readReview
In one paragraph

Review in The Biochemical journal, 2002. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 254 papers.

0numbers the graph read from it
0cells of the map it votes in
254citing 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

254 citing papers in PubMed.

  1. Article
  2. Article
  3. Review
  4. Article
  5. Article
  6. Article
  7. Gene Therapies in Atrial Fibrillation.Journal of cardiovascular translational research · 2025
    Review
  8. Article
  9. Article
  10. Review
  11. Review
  12. Article
  13. Article
  14. Article
  15. Autism spectrum disorder-like behaviors induced by hyper-glutamatergic NMDA receptor signaling through hypo-serotonergic 5-HTNeuropsychopharmacology : official publication of the American College of Neuropsychopharmacology · 2025
    Article
  16. Article
  17. Article
  18. Review
  19. CaCells · 2024
    Review
  20. Article

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

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.

Andy HudmonDepartment of Neurobiology, Fairchild Bldg, D217 299 Campus Drive, Stanford University Medical School, Stanford, CA 94305-5125, USA. ahudman@stanford.edu
Howard Schulman

Funding

REGULATION OF CA++/CALMODULIN KINASE BY NEUROTRANSMITTERR01GM030179 · NIGMS · STANFORD UNIVERSITY · PI MEYER, TOBIAS · 1985 to 2018
$4.9M
REGULATION OF CA++/CALMODULIN KINASE BY NEUROTRANSMITTERR37GM030179 · NIGMS · STANFORD UNIVERSITY · PI MEYER, TOBIAS · 1995 to 2004
$1.7M
MULTIFUNCTIONAL CA++/CALMODULIN-DEPENDENT PROTEIN KINASER01GM040600 · NIGMS · STANFORD UNIVERSITY · PI SCHULMAN, HOWARD · 1988 to 2001
$573k
NIGMS NIH HHS GM30179NIGMS NIH HHS GM40600
6 · The paper itself

Abstract

Ca2+/calmodulin (CaM)-dependent protein kinase (CaMKII) is a ubiquitous mediator of Ca2+-linked signalling that phosphorylates a wide range of substrates to co-ordinate and regulate Ca2+-mediated alterations in cellular function. The transmission of information by the kinase from extracellular stimuli and the intracellular Ca2+ rise is not passive. Rather, its multimeric structure and autoregulation enable this enzyme to participate actively in the sensitivity, timing and location of its action. CaMKII can: (i) be activated in a Ca2+-spike frequency-dependent manner; (ii) become independent of its initial Ca2+/CaM activators; and (iii) undergo a 'molecular switch-like' behaviour, which is crucial for certain forms of learning and memory. CaMKII is derived from a family of four homologous but distinct genes, with over 30 alternatively spliced isoforms described at present. These isoforms possess diverse developmental and anatomical expression patterns, as well as subcellular localization. Six independent catalytic/autoregulatory domains are connected by a narrow stalk-like appendage to each hexameric ring within the dodecameric structure. Ca2+/CaM binding activates the enzyme by disinhibiting the autoregulatory domain; this process initiates an intra-holoenzyme autophosphorylation reaction that induces complex changes in the enzyme's sensitivity to Ca2+/CaM, including the generation of Ca2+/CaM-independent (autonomous) activity and marked increase in affinity for CaM. The role of CaMKII in Ca2+ signal transduction is shaped by its autoregulation, isoenzymic type and subcellular localization. The molecular determinants and mechanisms producing these processes are discussed as they relate to the structure-function of this multifunctional protein kinase.

Indexed as

AnimalsCalcium-Calmodulin-Dependent Protein KinasesCalcium-Calmodulin-Dependent Protein Kinase Type 2Calcium SignalingCell Physiological PhenomenaHomeostasisHumansLearningMemoryPhosphorylationCalcium-Calmodulin-Dependent Protein KinasesCalcium-Calmodulin-Dependent Protein Kinase Type 2

Identifiers

PMID11931644
PMCPMC1222606

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.