Evidence map›Paper›PMID 35561079›Full record

ArticleBioFactors (Oxford, England)2022

Selective inhibition of phosphodiesterase 4D increases tau phosphorylation at Ser214 residue.

Viviana Villa, Giulia Montalto, Francesca Caudano, Ernesto Fedele, Roberta Ricciarelli

Open access · hybridAbstract read
In one paragraph

Article in BioFactors (Oxford, England), 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.

0numbers the graph read from it
0cells of the map it votes in
3citing papers in PubMed
0.4field-weighted citation impact, top 42% 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

3 citing papers in PubMed, 5 citations in OpenAlex.

  1. Review
  2. Article
  3. A New Bistable Switch Model of Alzheimer's Disease Pathogenesis.International journal of molecular sciences · 2022
    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

5 authors at 2 institutions in 1 country.

Viviana VillaDepartment of Experimental Medicine, Section of General Pathology, School of Medical and Pharmaceutical Sciences, University of Genoa, Genoa, Italy.
Giulia MontaltoDepartment of Experimental Medicine, Section of General Pathology, School of Medical and Pharmaceutical Sciences, University of Genoa, Genoa, Italy.
Francesca CaudanoDepartment of Experimental Medicine, Section of General Pathology, School of Medical and Pharmaceutical Sciences, University of Genoa, Genoa, Italy.
Ernesto FedeleDepartment of Pharmacy, Section of Pharmacology and Toxicology, School of Medical and Pharmaceutical Sciences, University of Genoa, Genoa, Italy.ORCID https://orcid.org/0000-0002-0386-0925
Roberta RicciarelliDepartment of Experimental Medicine, Section of General Pathology, School of Medical and Pharmaceutical Sciences, University of Genoa, Genoa, Italy.ORCID https://orcid.org/0000-0002-2053-2501
University of Genoa · ITOspedale Policlinico San Martino · IT

Funding

Università degli Studi di Genova
6 · The paper itself

Abstract

Tau is a protein that normally participates in the assembly and stability of microtubules. However, it can form intraneuronal hyperphosphorylated aggregates that are hallmarks of Alzheimer's disease and other neurodegenerative disorders known as tauopathies. Tau can be phosphorylated by multiple kinases at several sites. Among such kinases, the cAMP-dependent protein kinase A (PKA) phosphorylates tau at Ser214 (pTAU-S214), an event that was shown to reduce the pathological assembly of the protein. Given that the neuronal cAMP/PKA-activated cascade is involved in synaptic plasticity and memory, and that cAMP-enhancing strategies demonstrated promising therapeutic potential for the treatment of cognitive deficits, we investigated the impact of cAMP on pTAU-S214 in N2a cells and rat hippocampal slices. Our results confirm that the activation of adenylyl cyclase increases pTAU-S214 in both model systems and, more interestingly, this effect is mimicked by GEBR-7b, a phosphodiesterase 4D inhibitor with proven pro-cognitive efficacy in rodents.

Indexed as

Alzheimer DiseaseCyclic Nucleotide Phosphodiesterases, Type 4Adenylyl CyclasesAnimalsCyclic AMP-Dependent Protein KinasesPhosphorylationRatsAdenylyl CyclasesCyclic AMP-Dependent Protein KinasesCyclic Nucleotide Phosphodiesterases, Type 4cyclic adenosine monophosphateGEBR-7bphosphodiesterase inhibitorstau protein

Identifiers

PMID35561079
PMCPMC9790528
OpenAlexW4280551348

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-ND
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.