Function of IRAG2 Is Modulated by NO/cGMP in Murine Platelets.

Open access · goldAbstract read

In one paragraph

Article in International journal of molecular sciences, 2022. 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

0.5field-weighted citation impact, top 34% 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, 3 citations in OpenAlex.

Novel Functional Features of cGMP Substrate Proteins IRAG1 and IRAG2.International journal of molecular sciences · 2023
Review

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.

Sally PrüschenkDepartment of Pharmacology and Toxicology, Institute of Pharmacy, University of Regensburg, 93040 Regensburg, Germany.ORCID 0000-0001-9477-8566

Jens SchlossmannDepartment of Pharmacology and Toxicology, Institute of Pharmacy, University of Regensburg, 93040 Regensburg, Germany.ORCID 0000-0002-2550-6839

University of Regensburg · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Inositol 1,4,5-triphosphate receptor-associated 2 (IRAG2) is a type II membrane protein located at the endoplasmic reticulum. It is a homologue of inositol 1,4,5-triphosphate receptor-associated cGMP kinase substrate 1 (IRAG1), a substrate protein of cGMP-dependent protein kinase I (PKGI), and is among others expressed in platelets. Here, we studied if IRAG2 is also located in platelets and might be a substrate protein of PKGI. IRAG2 was detected in platelets of IRAG2-WT animals but not in those of IRAG2-KO animals. Next, we validated by co-immunoprecipitation studies that IRAG2 is associated with IP

Indexed as

Blood PlateletsThrombinAnimalsCollagenCyclic GMPInositol 1,4,5-Trisphosphate ReceptorsMiceNitric OxidePhosphorylationPlatelet AggregationProtein KinasesCollagenCyclic GMPInositol 1,4,5-Trisphosphate ReceptorsNitric OxideProtein KinasesThrombincGKIcGMPIP3RIRAGIRAG1IRAG2Jaw1LRMPphosphorylationPKGIplatelet aggregationplatelets

Identifiers

PMID35743138

DOI10.3390/ijms23126695

PMCPMC9223716

OpenAlexW4282977220

What OpenQuestion holds

Textmetadata

LicenceCC BY

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.