Evidence map›Paper›PMID 22717267›Full record

ReviewTrends in neurosciences2012

CaMKII regulation in information processing and storage.

Steven J Coultrap, K Ulrich Bayer

Abstract readReview
In one paragraph

Review in Trends in neurosciences, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 186 papers.

0numbers the graph read from it
0cells of the map it votes in
186citing papers in PubMed
11.2field-weighted citation impact, top 1% 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

186 citing papers in PubMed, 313 citations in OpenAlex.

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126 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 at 1 institution in 1 country.

Steven J CoultrapDepartment of Pharmacology, University of Colorado Denver School of Medicine, Aurora, CO 80045, USA.
K Ulrich Bayer
University of Colorado Denver · US

Funding

Structural and Catalytic Functions of CaMKII in NeuronsR01NS052644 · NINDS · UNIVERSITY OF COLORADO DENVER · PI BAYER, K. ULRICH · 2007 to 2011
$1.7M
NINDS NIH HHS R01 NS052644
6 · The paper itself

Abstract

The Ca(2+)/Calmodulin(CaM)-dependent protein kinase II (CaMKII) is activated by Ca(2+)/CaM, but becomes partially autonomous (Ca(2+)-independent) upon autophosphorylation at T286. This hallmark feature of CaMKII regulation provides a form of molecular memory and is indeed important in long-term potentiation (LTP) of excitatory synapse strength and memory formation. However, emerging evidence supports a direct role in information processing, while storage of synaptic information may instead be mediated by regulated interaction of CaMKII with the NMDA receptor (NMDAR) complex. These and other CaMKII regulation mechanisms are discussed here in the context of the kinase structure and their impact on postsynaptic functions. Recent findings also implicate CaMKII in long-term depression (LTD), as well as functional roles at inhibitory synapses, lending renewed emphasis on better understanding the spatiotemporal control of CaMKII regulation.

Indexed as

AnimalsCalcium-Calmodulin-Dependent Protein Kinase Type 2Gene Expression Regulation, EnzymologicHippocampusHumansIsoenzymesLong-Term PotentiationLong-Term Synaptic DepressionMemoryNeural InhibitionPhosphorylationProtein ConformationReceptors, N-Methyl-D-AspartateSynapsesSynaptic TransmissionCalcium-Calmodulin-Dependent Protein Kinase Type 2IsoenzymesReceptors, N-Methyl-D-Aspartate

Identifiers

PMID22717267
PMCPMC3461103
OpenAlexW2140944550

What OpenQuestion holds

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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.