Evidence map›Paper›PMID 18924107›Full record

ArticleProteomics2008

PTPepsilon has a critical role in signaling transduction pathways and phosphoprotein network topology in red cells.

Lucia De Franceschi, Andrea Biondani, Franco Carta, Franco Turrini, Carlo Laudanna, Renzo Deana, Anna Maria Brunati, Loris Turretta, Achille Iolascon, Silverio Perrotta and 3 more

Open access · greenAbstract read
In one paragraph

Article in Proteomics, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.

0numbers the graph read from it
0cells of the map it votes in
16citing papers in PubMed
1.7field-weighted citation impact, top 17% 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

16 citing papers in PubMed, 30 citations in OpenAlex.

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  8. Pharmacological inhibition of calpain-1 prevents red cell dehydration and reduces Gardos channel activity in a mouse model of sickle cell disease.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2013
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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

13 authors at 5 institutions in 3 countries.

Lucia De FranceschiDepartment of Clinical and Experimental Medicine, Section of Internal Medicine, University of Verona, Verona, Italy. lucia.defranceschi@univr.it
Andrea Biondani
Franco Carta
Franco Turrini
Carlo Laudanna
Renzo Deana
Anna Maria Brunati
Loris Turretta
Achille Iolascon
Silverio Perrotta
Ari Elson
Cristina Bulato
Carlo Brugnara
University of Padua · ITUniversity of Verona · ITHarvard University · USUniversity of Turin · ITWeizmann Institute of Science · IL

Funding

MAGNESIUM AND SICKLE CELL DISEASER01DK050422 · NIDDK · CHILDREN'S HOSPITAL BOSTON · PI BRUGNARA, CARLO · 1995 to 2005
$1.5M
NIDDK NIH HHS DK50422NIDDK NIH HHS R01 DK050422
6 · The paper itself

Abstract

Protein tyrosine phosphatases (PTPs) are crucial components of cellular signal transduction pathways. Here, we report that red blood cells (RBCs) from mice lacking PTPepsilon (Ptpre(-/-)) exhibit (i) abnormal morphology; (ii) increased Ca(2+)-activated-K(+) channel activity, which was partially blocked by the Src family kinases (SFKs) inhibitor PP1; and (iii) market perturbation of the RBC membrane tyrosine (Tyr-) phosphoproteome, indicating an alteration of RBC signal transduction pathways. Using the signaling network computational analysis of the Tyr-phosphoproteomic data, we identified seven topological clusters. We studied cluster 1 containing Fyn, SFK, and Syk another tyrosine kinase. In Ptpre(-/-)mouse RBCs, the activity of Fyn was increased while Syk kinase activity was decreased compared to wild-type RBCs, validating the network computational analysis, and indicating a novel signaling pathway, which involves Fyn and Syk in regulation of red cell morphology.

Indexed as

Metabolic Networks and PathwaysSignal TransductionAdaptor Proteins, Signal TransducingAlgorithmsAnimalsCalciumCalcium ChannelsClotrimazoleErythrocytesIntracellular Signaling Peptides and ProteinsMiceMice, KnockoutPotassiumProtein-Tyrosine KinasesProteomicsReceptor-Like Protein Tyrosine Phosphatases, Class 4Adaptor Proteins, Signal TransducingCalciumCalcium ChannelsClotrimazoleFyb protein, mouseIntracellular Signaling Peptides and ProteinsPotassiumProtein-Tyrosine KinasesPtpre protein, mouseReceptor-Like Protein Tyrosine Phosphatases, Class 4src-Family KinasesSyk KinaseSyk protein, mouse

Identifiers

PMID18924107
PMCPMC3008556
OpenAlexW1972437720

What OpenQuestion holds

Textmetadata
LicenceTDM
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.