Evidence map›Paper›PMID 24180383›Full record

ReviewCurrent pharmaceutical design2014

Regulation of endothelial nitric oxide synthase activity by protein-protein interaction.

Yunchao Su

Open access · greenAbstract readReview
In one paragraph

Review in Current pharmaceutical design, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.

0numbers the graph read from it
0cells of the map it votes in
27citing papers in PubMed
2.3field-weighted citation impact, top 12% 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

27 citing papers in PubMed, 47 citations in OpenAlex.

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  20. CCL28-induced CCR10/eNOS interaction in angiogenesis and skin wound healing.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2020
    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

1 author at 1 institution in 1 country.

Yunchao SuDepartment of Pharmacology and Toxicology, Medical College of Georgia, Georgia Regents University, 1120 15th Street, Augusta, GA 30912. ysu@gru.edu.
Augusta University · US

Funding

eNOS-actin Interaction and Oxygen in Lung EndotheliumR01HL088261 · NHLBI · UNIVERSITY OF FLORIDA · PI SU, YUNCHAO · 2008 to 2012
$1.8M
NHLBI NIH HHS R01 HL088261
6 · The paper itself

Abstract

Endothelial nitric oxide synthase (eNOS) is expressed in vascular endothelial cells and plays an important role in the regulation of vascular tone, platelet aggregation and angiogenesis. Protein-protein interactions represent an important posttranslational mechanism for eNOS regulation. eNOS has been shown to interact with a variety of regulatory and structural proteins which provide fine tuneup of eNOS activity and eNOS protein trafficking between plasma membrane and intracellular membranes in a number of physiological and pathophysiological processes. eNOS interacts with calmodulin, heat shock protein 90 (Hsp90), dynamin-2, β-actin, tubulin, porin, high-density lipoprotein (HDL) and apolipoprotein AI (ApoAI), resulting in increases in eNOS activity. The negative eNOS interacting proteins include caveolin, G protein-coupled receptors (GPCR), nitric oxide synthase-interacting protein (NOSIP), and nitric oxide synthase trafficking inducer (NOSTRIN). Dynamin-2, NOSIP, NOSTRIN, and cytoskeleton are also involved in eNOS trafficking in endothelial cells. In addition, eNOS associations with cationic amino acid transporter-1 (CAT-1), argininosuccinate synthase (ASS), argininosuccinate lyase (ASL), and soluble guanylate cyclase (sGC) facilitate directed delivery of substrate (L-arginine) to eNOS and optimizing NO production and NO action on its target. Regulation of eNOS by protein-protein interactions would provide potential targets for pharmacological interventions in NO-compromised cardiovascular diseases.

Indexed as

ActinsApolipoprotein A-ICalmodulinDynamin IIHSP90 Heat-Shock ProteinsHumansLipoproteins, HDLNitric OxideNitric Oxide Synthase Type IIIPorinsProtein BindingTubulinActinsApolipoprotein A-ICalmodulinDynamin IIHSP90 Heat-Shock ProteinsLipoproteins, HDLNitric OxideNitric Oxide Synthase Type IIIPorinsTubulin

Identifiers

PMID24180383
PMCPMC7039309
OpenAlexW2094110089

What OpenQuestion holds

Textmetadata
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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.