Evidence map›Paper›PMID 33481230›Full record

ArticleMethods in molecular biology (Clifton, N.J.)2021

Profiling of Phosphoinositide Molecular Species in Resting or Activated Human or Mouse Platelets by a LC-MS Method.

Gaëtan Chicanne, Justine Bertrand-Michel, Julien Viaud, Karim Hnia, Jonathan Clark, Bernard Payrastre

Abstract read
PubMed Publisher
In one paragraph

Article in Methods in molecular biology (Clifton, N.J.), 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.

0numbers the graph read from it
0cells of the map it votes in
1citing papers in PubMed
3.3field-weighted citation impact, top 10% 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

1 citing paper in PubMed, 2 citations in OpenAlex.

  1. 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

6 authors at 5 institutions in 2 countries.

Gaëtan ChicanneInstitut des Maladies Métaboliques et Cardiovasculaires, Inserm U1048, Université Toulouse III, Toulouse, France.
Justine Bertrand-MichelInstitut des Maladies Métaboliques et Cardiovasculaires, Inserm U1048, Université Toulouse III, Toulouse, France.
Julien ViaudInstitut des Maladies Métaboliques et Cardiovasculaires, Inserm U1048, Université Toulouse III, Toulouse, France.
Karim HniaInstitut des Maladies Métaboliques et Cardiovasculaires, Inserm U1048, Université Toulouse III, Toulouse, France.
Jonathan ClarkSignalling Programme, Babraham Institute, Cambridge, UK.
Bernard PayrastreInstitut des Maladies Métaboliques et Cardiovasculaires, Inserm U1048, Université Toulouse III, Toulouse, France. bernard.payrastre@inserm.fr.
Inserm · FRBabraham Institute · GBCentre Hospitalier Universitaire de Toulouse · FRInstitut des Maladies Métaboliques et Cardiovasculaires · FRUniversité Toulouse III - Paul Sabatier · FR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Our knowledge of the role and biology of the different phosphoinositides has greatly expanded over recent years. Reversible phosphorylation by specific kinases and phosphatases of positions 3, 4, and 5 on the inositol ring is a highly dynamic process playing a critical role in the regulation of the spatiotemporal recruitment and binding of effector proteins. The specific phosphoinositide kinases and phosphatases are key players in the control of many cellular functions, including proliferation, survival, intracellular trafficking, or cytoskeleton reorganization. Several of these enzymes are mutated in human diseases. The impact of the fatty acid composition of phosphoinositides in their function is much less understood. There is an important molecular diversity in the fatty acid side chains of PI. While stearic and arachidonic fatty acids are the major acyl species in PIP, PIP

Indexed as

1-Phosphatidylinositol 4-KinaseAnimalsBiochemical PhenomenaBlood PlateletsCell LineCells, CulturedChromatography, LiquidFatty AcidsInositolMicePhosphatidylinositol 3-KinasesPhosphatidylinositol PhosphatesPhosphatidylinositolsPhosphoric Monoester HydrolasesSignal TransductionTandem Mass Spectrometry1-Phosphatidylinositol 4-KinaseFatty AcidsInositolPhosphatidylinositol 3-KinasesPhosphatidylinositol PhosphatesPhosphatidylinositolsPhosphoric Monoester HydrolasesFatty acyl chainsLC-MSMolecular speciesPhosphoinositidesPlatelets

Identifiers

PMID33481230
OpenAlexW3121271874

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.