Evidence map›Paper›PMID 30206122›Full record

ArticleThe Journal of biological chemistry2018

Oxidation of cysteine 117 stimulates constitutive activation of the type Iα cGMP-dependent protein kinase.

Jessica L Sheehe, Adrian D Bonev, Anna M Schmoker, Bryan A Ballif, Mark T Nelson, Thomas M Moon, Wolfgang R Dostmann

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.

0numbers the graph read from it
0cells of the map it votes in
12citing papers in PubMed
2.7field-weighted citation impact, top 9% 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

12 citing papers in PubMed, 34 citations in OpenAlex.

  1. Article
  2. Redox Regulation of KAntioxidants & redox signaling · 2024
    Review
  3. Article
  4. Article
  5. Article
  6. Review
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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

7 authors at 2 institutions in 2 countries.

Jessica L SheeheFrom the Department of Pharmacology, Larner College of Medicine, and.
Adrian D BonevFrom the Department of Pharmacology, Larner College of Medicine, and.
Anna M Schmokerthe Department of Biology, University of Vermont, Burlington, Vermont 05405 and.
Bryan A Ballifthe Department of Biology, University of Vermont, Burlington, Vermont 05405 and.
Mark T NelsonFrom the Department of Pharmacology, Larner College of Medicine, and.
Thomas M Moonthe Department of Chemistry and Biochemistry, University of Arizona, Tucson, Arizona 85721 thomasmoon@email.arizona.edu.ORCID 0000-0003-1568-8808
Wolfgang R DostmannFrom the Department of Pharmacology, Larner College of Medicine, and wolfgang.dostmann@uvm.edu.
University of Vermont · USUniversity of Arizona · US

Funding

Vermont INBRE Administrative Supplement 2024 AWD 118P20GM103449 · NIGMS · UNIVERSITY OF VERMONT & ST AGRIC COLLEGE · PI CHRISTOPHER S FRANCKLYN · 2012 to 2026
$58.4M
HEMOSTASIS &THROMBOSIS PROGRAM FOR ACADEMIC TRAINEEST32HL007594 · NHLBI · UNIVERSITY OF VERMONT &ST AGRIC COLLEGE · PI KELM, ROBERT J · 1985 to 2015
$4.6M
Center for Neuroscience ExcellenceP30GM103498 · NIGMS · UNIVERSITY OF VERMONT & ST AGRIC COLLEGE · PI PARSONS, RODNEY L · 2012 to 2015
$4.3M
Regulations of Myoendothelial Function By Signaling Microdomains in HypertensionR01HL121706 · NHLBI · UNIVERSITY OF VERMONT & ST AGRIC COLLEGE · PI NELSON, MARK T · 2014 to 2017
$1.6M
K+ sensing & electrical signaling by Kir channels in brain vasculatureR01HL131181 · NHLBI · UNIVERSITY OF VERMONT & ST AGRIC COLLEGE · PI NELSON, MARK T · 2016 to 2018
$1.4M
CENTER FOR NEUROSCIENCE EXCELLENCEP30RR032135 · NCRR · UNIVERSITY OF VERMONT & ST AGRIC COLLEGE · PI PARSONS, RODNEY L · 2011 to 2011
$1.1M
NCRR NIH HHS P30 RR032135NHLBI NIH HHS R01 HL121706NHLBI NIH HHS R01 HL131181NHLBI NIH HHS T32 HL007594NIGMS NIH HHS P20 GM103449NIGMS NIH HHS P30 GM103498
6 · The paper itself

Abstract

The type I cGMP-dependent protein kinase (PKG I) is an essential regulator of vascular tone. It has been demonstrated that the type Iα isoform can be constitutively activated by oxidizing conditions. However, the amino acid residues implicated in this phenomenon are not fully elucidated. To investigate the molecular basis for this mechanism, we studied the effects of oxidation using recombinant WT, truncated, and mutant constructs of PKG I. Using an

Indexed as

Amino Acid SequenceAnimalsCattleCyclic GMPCyclic GMP-Dependent Protein Kinase Type ICysteineModels, MolecularNitric OxideOxidation-ReductionPhosphorylationProtein ConformationSequence HomologyCyclic GMPCyclic GMP-Dependent Protein Kinase Type ICysteineNitric OxideAGC kinasesallosterycGMP-dependent protein kinaseconstitutive activationcyclic GMP (cGMP)oxidation-reduction (redox)potassium channelprotein kinase G (PKG)signal transduction

Identifiers

PMID30206122
PMCPMC6204908
OpenAlexW2890058925

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.