Evidence map›Paper›PMID 25228390›Full record

ArticleCirculation research2014

Phosphorylation of Nox1 regulates association with NoxA1 activation domain.

Jennifer Streeter, Brandon M Schickling, Shuxia Jiang, Bojana Stanic, William H Thiel, Lokesh Gakhar, Jon C D Houtman, Francis J Miller

Open access · bronzeAbstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Circulation research, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.

0numbers the graph read from it
0cells of the map it votes in
22citing papers in PubMed
1.3field-weighted citation impact, top 20% 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

22 citing papers in PubMed, 38 citations in OpenAlex.

  1. Review
  2. Article
  3. Review
  4. Review
  5. Review
  6. AhR and STAT3: A Dangerous Duo in Chemical Carcinogenesis.International journal of molecular sciences · 2025
    Review
  7. Article
  8. Article
  9. Review
  10. Article
  11. Review
  12. Review
  13. Article
  14. Review
  15. Article
  16. Review
  17. Review
  18. Review
  19. Review
  20. Article
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

8 authors at 1 institution in 1 country.

Jennifer StreeterFrom the Departments of Internal Medicine (B.M.S., S.J., B.S., W.H.T., F.J.M.), Microbiology (J.C.D.H.), Anatomy and Cell Biology (J.S.), Biochemistry (L.G.), and Protein Crystallography Facility (L.G.), University of Iowa, Iowa City; and Veterans Affair Medical Center, Iowa City, IA (F.J.M.).
Brandon M SchicklingFrom the Departments of Internal Medicine (B.M.S., S.J., B.S., W.H.T., F.J.M.), Microbiology (J.C.D.H.), Anatomy and Cell Biology (J.S.), Biochemistry (L.G.), and Protein Crystallography Facility (L.G.), University of Iowa, Iowa City; and Veterans Affair Medical Center, Iowa City, IA (F.J.M.).
Shuxia JiangFrom the Departments of Internal Medicine (B.M.S., S.J., B.S., W.H.T., F.J.M.), Microbiology (J.C.D.H.), Anatomy and Cell Biology (J.S.), Biochemistry (L.G.), and Protein Crystallography Facility (L.G.), University of Iowa, Iowa City; and Veterans Affair Medical Center, Iowa City, IA (F.J.M.).
Bojana StanicFrom the Departments of Internal Medicine (B.M.S., S.J., B.S., W.H.T., F.J.M.), Microbiology (J.C.D.H.), Anatomy and Cell Biology (J.S.), Biochemistry (L.G.), and Protein Crystallography Facility (L.G.), University of Iowa, Iowa City; and Veterans Affair Medical Center, Iowa City, IA (F.J.M.).
William H ThielFrom the Departments of Internal Medicine (B.M.S., S.J., B.S., W.H.T., F.J.M.), Microbiology (J.C.D.H.), Anatomy and Cell Biology (J.S.), Biochemistry (L.G.), and Protein Crystallography Facility (L.G.), University of Iowa, Iowa City; and Veterans Affair Medical Center, Iowa City, IA (F.J.M.).
Lokesh GakharFrom the Departments of Internal Medicine (B.M.S., S.J., B.S., W.H.T., F.J.M.), Microbiology (J.C.D.H.), Anatomy and Cell Biology (J.S.), Biochemistry (L.G.), and Protein Crystallography Facility (L.G.), University of Iowa, Iowa City; and Veterans Affair Medical Center, Iowa City, IA (F.J.M.).
Jon C D HoutmanFrom the Departments of Internal Medicine (B.M.S., S.J., B.S., W.H.T., F.J.M.), Microbiology (J.C.D.H.), Anatomy and Cell Biology (J.S.), Biochemistry (L.G.), and Protein Crystallography Facility (L.G.), University of Iowa, Iowa City; and Veterans Affair Medical Center, Iowa City, IA (F.J.M.).
Francis J MillerFrom the Departments of Internal Medicine (B.M.S., S.J., B.S., W.H.T., F.J.M.), Microbiology (J.C.D.H.), Anatomy and Cell Biology (J.S.), Biochemistry (L.G.), and Protein Crystallography Facility (L.G.), University of Iowa, Iowa City; and Veterans Affair Medical Center, Iowa City, IA (F.J.M.). francis-miller@uiowa.edu.
University of Iowa · US

Funding

MEDICAL SCIENTIST TRAINING PROGRAMT32GM007337 · NIGMS · UNIVERSITY OF IOWA · PI GEYER, PAMELA K., LENTZ, STEVEN R · 1985 to 2020
$15.9M
Glutathione Peroxidase &Redox State in AtherosclerosisR01HL081750 · NHLBI · UNIVERSITY OF IOWA · PI MILLER, FRANCIS J · 2005 to 2009
$2.0M
Cooperative SH2 and SH3 domain-mediated interactions at the adaptor protein Grb2R01CA136729 · NCI · UNIVERSITY OF IOWA · PI HOUTMAN, JON C.D. · 2010 to 2014
$1.6M
Regulation of the Nox1 NADPH Oxidase in Vascular Smooth Muscle CellsI01BX001729 · VA · IOWA CITY VA MEDICAL CENTER · PI MILLER, FRANCIS J · 2012 to 2020
–
BLRD VA I01 BX001729NCI NIH HHS CA136729NCI NIH HHS R01 CA136729NHLBI NIH HHS HL081750NHLBI NIH HHS R01 HL081750NIGMS NIH HHS T32 GM007337
6 · The paper itself

Abstract

rationaleActivation of Nox1 initiates redox-dependent signaling events crucial in the pathogenesis of vascular disease. Selective targeting of Nox1 is an attractive potential therapy, but requires a better understanding of the molecular modifications controlling its activation.

objectiveTo determine whether posttranslational modifications of Nox1 regulate its activity in vascular cells. METHODS AND

resultsWe first found evidence that Nox1 is phosphorylated in multiple models of vascular disease. Next, studies using mass spectroscopy and a pharmacological inhibitor demonstrated that protein kinase C-beta1 mediates phosphorylation of Nox1 in response to tumor necrosis factor-α. siRNA-mediated silencing of protein kinase C-beta1 abolished tumor necrosis factor-α-mediated reactive oxygen species production and vascular smooth muscle cell migration. Site-directed mutagenesis and isothermal titration calorimetry indicated that protein kinase C-beta1 phosphorylates Nox1 at threonine 429. Moreover, Nox1 threonine 429 phosphorylation facilitated the association of Nox1 with the NoxA1 activation domain and was necessary for NADPH oxidase complex assembly, reactive oxygen species production, and vascular smooth muscle cell migration.

conclusionsWe conclude that protein kinase C-beta1 phosphorylation of threonine 429 regulates activation of Nox1 NADPH oxidase.

Indexed as

Adaptor Proteins, Signal TransducingAmino Acid SequenceAnimalsAortaBinding SitesCell MovementCells, CulturedMiceMice, Inbred C57BLMolecular Sequence DataMuscle, Smooth, VascularMutationMyocytes, Smooth MuscleNADH, NADPH OxidoreductasesNADPH Oxidase 1PhosphorylationAdaptor Proteins, Signal TransducingNADH, NADPH OxidoreductasesNADPH Oxidase 1NOX1 protein, mouseNoxa1 protein, mouseProtein Kinase C betaProteinsReactive Oxygen SpeciesTumor Necrosis Factor-alphaatherosclerosisNADPH oxidaseneointimaPKCβTNF-αvascular smooth muscle cells

Identifiers

PMID25228390
PMCPMC5025877
OpenAlexW2113202066

What OpenQuestion holds

Textmetadata
LicenceTDM
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.