Evidence map›Paper›PMID 25000310›Full record

ArticleBioscience reports2014

Endothelial nitric oxide synthase is regulated by ERK phosphorylation at Ser602.

John C Salerno, Dipak K Ghosh, Raj Razdan, Katy A Helms, Christopher C Brown, Jonathan L McMurry, Emily A Rye, Carol A Chrestensen

Open access · goldAbstract read
In one paragraph

Article in Bioscience reports, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.

0numbers the graph read from it
0cells of the map it votes in
9citing papers in PubMed
0.9field-weighted citation impact, top 25% 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

9 citing papers in PubMed, 26 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Impressic Acid, a Lupane-Type Triterpenoid fromInternational journal of molecular sciences · 2019
    Article
  5. Role of GPER in estrogen-dependent nitric oxide formation and vasodilation.The Journal of steroid biochemistry and molecular biology · 2018
    Article
  6. Article
  7. Article
  8. Article
  9. 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

8 authors at 1 institution in 1 country.

John C Salerno*Department of Biology, Kennesaw State University, Kennesaw, GA 30144, U.S.A.
Dipak K Ghosh*Department of Biology, Kennesaw State University, Kennesaw, GA 30144, U.S.A.
Raj Razdan*Department of Biology, Kennesaw State University, Kennesaw, GA 30144, U.S.A.
Katy A Helms†Department of Chemistry and Biochemistry, Kennesaw State University, Kennesaw, GA 30144, U.S.A.
Christopher C Brown†Department of Chemistry and Biochemistry, Kennesaw State University, Kennesaw, GA 30144, U.S.A.
Jonathan L McMurry*Department of Biology, Kennesaw State University, Kennesaw, GA 30144, U.S.A.
Emily A Rye†Department of Chemistry and Biochemistry, Kennesaw State University, Kennesaw, GA 30144, U.S.A.
Carol A Chrestensen†Department of Chemistry and Biochemistry, Kennesaw State University, Kennesaw, GA 30144, U.S.A.
Kennesaw State University · US

Funding

Purification of a Modified Flagellar Export ApparatusR15GM080701 · NIGMS · KENNESAW STATE UNIVERSITY · PI MCMURRY, JONATHAN L · 2007 to 2012
$652k
NIGMS NIH HHS R15 GM080701
6 · The paper itself

Abstract

eNOS (endothelial nitric oxide synthase) contains a MAPK (mitogen-activated protein kinase)-binding site associated with a major eNOS control element. Purified ERK (extracellular-signal-regulated kinase) phosphorylates eNOS with a stoichiometry of 2-3 phosphates per eNOS monomer. Phosphorylation decreases NO synthesis and cytochrome c reductase activity. Three sites of phosphorylation were detected by MS. All sites matched the SP and TP MAPK (mitogen-activated protein kinase) phosphorylation motif. Ser602 lies at the N-terminal edge of the 42-residue eNOS AI (autoinhibitory) element. The pentabasic MAPK-binding site lies at the opposite end of the AI, and other critical regulatory features are between them. Thr46 and Ser58 are located in a flexible region associated with the N terminus of the oxygenase domain. In contrast with PKC (protein kinase C), phosphorylation by ERK did not significantly interfere with CaM (calmodulin) binding as analysed by optical biosensing. Instead, ERK phosphorylation favours a state in which FMN and FAD are in close association and prevents conformational changes that expose reduced FMN to acceptors. The close associations between control sites in a few regions of the molecule suggest that control of signal generation is modulated by multiple inputs interacting directly on the surface of eNOS via overlapping binding domains and tightly grouped targets.

Indexed as

AnimalsBinding SitesCalmodulinCattleCells, CulturedExtracellular Signal-Regulated MAP KinasesFlavin-Adenine DinucleotideFlavin MononucleotideNitric Oxide Synthase Type IIIPhosphorylationProtein Kinase CCalmodulinExtracellular Signal-Regulated MAP KinasesFlavin-Adenine DinucleotideFlavin MononucleotideNitric Oxide Synthase Type IIIProtein Kinase C

Identifiers

PMID25000310
PMCPMC4166121
OpenAlexW2335327709

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.