Evidence map›Paper›PMID 12682012›Full record

ArticleThe EMBO journal2003

PKA phosphorylates the p75 receptor and regulates its localization to lipid rafts.

Haruhisa Higuchi, Toshihide Yamashita, Hideki Yoshikawa, Masaya Tohyama

Open access · greenAbstract read
In one paragraph

Article in The EMBO journal, 2003. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 41 papers.

0numbers the graph read from it
0cells of the map it votes in
41citing papers in PubMed
4.6field-weighted citation impact, top 4% 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

41 citing papers in PubMed, 114 citations in OpenAlex.

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  3. The Tails of Protein Kinase A.Molecular pharmacology · 2022
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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

4 authors at 1 institution in 1 country.

Haruhisa HiguchiDepartment of Anatomy and Neuroscience, Graduate School of Medicine, Osaka University, 2-2 Yamadaoka, Suita, Osaka 565-087, Japan.
Toshihide Yamashita
Hideki Yoshikawa
Masaya Tohyama
Osaka University · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Although a large number of studies have been carried out on the diverse effects mediated by the common neurotrophin receptor p75(NTR), little is known about the molecular mechanisms by which p75(NTR) initiates intracellular signal transduction. We identified a variant of the beta catalytic subunit of cAMP-dependent protein kinase (PKACbeta) as a p75(NTR)-interacting protein, which phosphorylates p75(NTR) at Ser304. Intracellular cAMP in cerebellar neurons was accumulated transiently by ligand binding to p75(NTR). Activation of cAMP-PKA is required for translocation of p75(NTR) to lipid rafts, and for biochemical and biological activities of p75(NTR), such as inactivation of Rho and the neurite outgrowth. Proper recruitment of activated p75(NTR) to lipid rafts, structures that represent specialized signaling organelles, is of fundamental importance in determining p75(NTR) bioactivity.

Indexed as

Amino Acid SequenceAnimalsBrain-Derived Neurotrophic FactorCells, CulturedCyclic AMPCyclic AMP-Dependent Protein KinasesHumansMembrane MicrodomainsMolecular Sequence DataNerve Growth FactorNeuronsPhosphorylationReceptor, Nerve Growth FactorReceptors, Nerve Growth FactorSignal TransductionTissue DistributionBrain-Derived Neurotrophic FactorCyclic AMPCyclic AMP-Dependent Protein KinasesNerve Growth FactorReceptor, Nerve Growth FactorReceptors, Nerve Growth Factor

Identifiers

PMID12682012
PMCPMC154469
OpenAlexW2060832818

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.