Evidence map›Paper›PMID 8385278›Full record

ReviewNeurochemical research1993

Multifunctional Ca2+/calmodulin-dependent protein kinase.

H Schulman, P I Hanson

Abstract readReview
PubMed Publisher
In one paragraph

Review in Neurochemical research, 1993. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.

0numbers the graph read from it
0cells of the map it votes in
24citing papers in PubMed
7.5field-weighted citation impact, top 2% 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

24 citing papers in PubMed, 135 citations in OpenAlex.

  1. Article
  2. Review
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  4. Article
  5. Physiological and Pathological Roles of CaMKII-PP1 Signaling in the Brain.International journal of molecular sciences · 2017
    Review
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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.

H SchulmanDepartment of Pharmacology, Stanford University School of Medicine, California 94305-5332.
P I Hanson
Stanford University · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Multifunctional Ca2+/calmodulin-dependent protein kinase (CaM kinase) is a prominent mediator of neurotransmitters which elevate Ca2+. It coordinates cellular responses to external stimuli by phosphorylating proteins involved in neurotransmitter synthesis, neurotransmitter release, carbohydrate metabolism, ion flux and neuronal plasticity. Structure/function studies of CaM kinase have provided insights into how it decodes Ca2+ signals. The kinase is kept relatively inactive in its basal state by the presence of an autoinhibitory domain. Binding of Ca2+/calmodulin eliminates this inhibitory constraint and allows the kinase to phosphorylate its substrates, as well as itself. This autophosphorylation significantly slows dissociation of calmodulin, thereby trapping calmodulin even when Ca2+ levels are subthreshold. The kinase may respond particularly well to multiple Ca2+ spikes since trapping may enable a spike frequency-dependent recruitment of calmodulin with each successive Ca2+ spike leading to increased activation of the kinase. Once calmodulin dissociates, CaM kinase remains partially active until it is dephosphorylated, providing for an additional period in which its response to brief Ca2+ transients is potentiated.

Indexed as

Protein KinasesAnimalsBinding SitesCalciumCalcium-Calmodulin-Dependent Protein KinasesHomeostasisPhosphorylationStructure-Activity RelationshipCalciumCalcium-Calmodulin-Dependent Protein KinasesProtein Kinases

Identifiers

PMID8385278
OpenAlexW2045632212

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.