Evidence map›Paper›PMID 9887450›Full record

ReviewMolecular neurobiology1998

Regulation of neuronal plasticity in the central nervous system by phosphorylation and dephosphorylation.

M Tokuda, O Hatase

Abstract readReview
PubMed Publisher
In one paragraph

Review in Molecular neurobiology, 1998. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.

0numbers the graph read from it
0cells of the map it votes in
7citing papers in PubMed
2.8field-weighted citation impact, top 8% 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

7 citing papers in PubMed, 59 citations in OpenAlex.

  1. Review
  2. Review
  3. Phosphorylation-dependent low-frequency depression at phasic synapses of a crayfish motoneuron.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2005
    Article
  4. Strong calcium entry activates mitochondrial superoxide generation, upregulating kinase signaling in hippocampal neurons.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2004
    Article
  5. Developmental regulation and specific brain distribution of phosphorabphilin.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2001
    Article
  6. Hypoxia-induced silencing of NMDA receptors in turtle neurons.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2000
    Article
  7. Protein phosphatase-1 regulation in the induction of long-term potentiation: heterogeneous molecular mechanisms.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2000
    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.

M TokudaDepartment of Physiology, Kagawa Medical University, Japan.
O Hatase
Kagawa University · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Neuronal plasticity can be defined as adaptive changes in structure and function of the nervous system, an obvious example of which is the capacity to remember and learn. Long-term potentiation and long-term depression are the experimental models of memory in the central nervous system (CNS), and have been frequently utilized for the analysis of the molecular mechanisms of memory formation. Extensive studies have demonstrated that various kinases and phosphatases regulate neuronal plasticity by phosphorylating and dephosphorylating proteins essential to the basic processes of adaptive changes in the CNS. These proteins include receptors, ion channels, synaptic vesicle proteins, and nuclear proteins. Multifunctional kinases (cAMP-dependent protein kinase, Ca2+/phospholipid-dependent protein kinase, and Ca2+/calmodulin-dependent protein kinases) and phosphatases (calcineurin, protein phosphatases 1, and 2A) that specifically modulate the phosphorylation status of neuronal-signaling proteins have been shown to be required for neuronal plasticity. In general, kinases are involved in upregulation of the activity of target substrates, and phosphatases downregulate them. Although this rule is applicable in most of the cases studied, there are also a number of exceptions. A variety of regulation mechanisms via phosphorylation and dephosphorylation mediated by multiple kinases and phosphatases are discussed.

Indexed as

AnimalsBrainGTP-Binding ProteinsHomeostasisHumansLong-Term PotentiationNeuronal PlasticityPhosphoprotein PhosphatasesPhosphorylationProtein KinasesReceptors, Cell SurfaceSpinal CordGTP-Binding ProteinsPhosphoprotein PhosphatasesProtein KinasesReceptors, Cell Surface

Identifiers

PMID9887450
OpenAlexW2026286058

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.