DOI . ORG {}

Analyzed Page
Matching Content Categories
CMS
Monthly Traffic Estimate
How Does Doi.org Make Money
Keywords
Topics
Schema
Social Networks
External Links
Analytics And Tracking
Libraries
Hosting Providers

We began analyzing https://www.nature.com/articles/1208901, but it redirected us to https://www.nature.com/articles/1208901. The analysis below is for the second page.

Title[redir]:
JunD activates transcription of the human ferritin H gene through an antioxidant response element during oxidative stress | Oncogene
Description:
Ferritin is the major intracellular iron storage protein that sequesters excess free iron to minimize generation of iron-catalysed reactive oxygen species. We previously demonstrated that expression of ferritin heavy chain (ferritin H) was induced by pro-oxidants, which is a part of cellular antioxidant response to protect cells from oxidative damage. In this study, we have identified that the antioxidant/electrophile response element (ARE) located 4.5 kb upstream to the human ferritin H transcription initiation site is responsible for the oxidant response. The human ferritin H ARE comprises two copies of bidirectional AP1 motifs. Mutations in each AP1 motif significantly impaired protein binding and the function of the ARE, indicating that both of the AP1 motifs are required for pro-oxidant-mediated activation of the ferritin H gene. We identified that JunD, an AP1 family basic-leucine zipper (bZip) transcription factor, is one of the ferritin H ARE binding proteins and activates ferritin H transcription in HepG2 hepatocarcinoma cells. Gel retardation assay demonstrated that H2O2 (hydrogen peroxide) or t-BHQ (tert-butylhydroquinone) treatment increased total protein binding as well as JunD binding to the ferritin H ARE. Chromatin immunoprecipitation assay showed that H2O2 treatment induced JunD binding to the ferritin H ARE. Both H2O2 and t-BHQ induced phosphorylation of JunD at Ser-100, an activated form of JunD. Furthermore, overexpression of JunD induced endogenous ferritin H protein synthesis. Since JunD has recently been demonstrated to protect cells from several stress stimuli including oxidative stress, these results suggest that, in addition to NFE2-related factor 2 (Nrf2) as a major ARE regulatory protein, JunD is another ARE regulatory protein for transcriptional activation of the human ferritin H gene and probably other antioxidant genes containing the conserved ARE sequences by which JunD may confer cytoprotection during oxidative stress.

Matching Content Categories {📚}

Non-Profit & Charity
Telecommunications
Health & Fitness

Content Management System {📝}

What CMS is doi.org built with?

Custom-built

No common CMS systems were detected on Doi.org, and no known web development framework was identified.

Traffic Estimate {📈}

What is the average monthly size of doi.org audience?

🏙️ Massive Traffic: 50M - 100M visitors per month

Based on our best estimate, this website will receive around 96,105,781 visitors per month in the current month.

check SE Ranking
check Ahrefs
check Similarweb
check Ubersuggest
check Semrush

How Does Doi.org Make Money? {💸}

We can't see how the site brings in money.

Not every website is profit-driven; some are created to spread information or serve as an online presence. Websites can be made for many reasons. This could be one of them. Doi.org might have a hidden revenue stream, but it's not something we can detect.

Keywords {🔍}

biol, torti, chem, ferritin, nature, tsuji, jund, biochem, access, article, mol, cell, content, oncogene, oxidative, protein, arosio, sci, usa, cookies, human, stress, levi, proc, natl, acad, miller, privacy, transcription, gene, response, iron, binding, open, beaumont, jaiswal, pickett, research, data, antioxidant, induced, cells, med, cozzi, santambrogio, albertini, biophys, pharmacol, advertising, information,

Topics {✒️}

nature portfolio permissions reprints privacy policy nature advertising social media author information authors author correspondence 2025 genome-wide meta-analysis t-bhq induced phosphorylation springerlink instant access personal data antioxidant/electrophile response element pro-oxidant-mediated activation data protection permissions nfe2l2/ap-1 targets expression iron status biomarkers privacy ferritin heavy chain issue learn bidirectional ap1 motifs recombinant protein ferritin explore content subscription content antioxidant response element european economic area cellular antioxidant response institutional subscriptions read dinkova-kostova archives accepting optional cookies article purchase journals search log nfe2-related factor 2 dr kazushi inoue article tsuji access hepg2 hepatocarcinoma cells article cite jund activates transcription manage preferences choi h https basal conditions oxidative stress transcription initiation site human ferritin content journal publish hydrogen peroxide

Schema {🗺️}

WebPage:
      mainEntity:
         headline:JunD activates transcription of the human ferritin H gene through an antioxidant response element during oxidative stress
         description:Ferritin is the major intracellular iron storage protein that sequesters excess free iron to minimize generation of iron-catalysed reactive oxygen species. We previously demonstrated that expression of ferritin heavy chain (ferritin H) was induced by pro-oxidants, which is a part of cellular antioxidant response to protect cells from oxidative damage. In this study, we have identified that the antioxidant/electrophile response element (ARE) located 4.5âkb upstream to the human ferritin H transcription initiation site is responsible for the oxidant response. The human ferritin H ARE comprises two copies of bidirectional AP1 motifs. Mutations in each AP1 motif significantly impaired protein binding and the function of the ARE, indicating that both of the AP1 motifs are required for pro-oxidant-mediated activation of the ferritin H gene. We identified that JunD, an AP1 family basic-leucine zipper (bZip) transcription factor, is one of the ferritin H ARE binding proteins and activates ferritin H transcription in HepG2 hepatocarcinoma cells. Gel retardation assay demonstrated that H2O2 (hydrogen peroxide) or t-BHQ (tert-butylhydroquinone) treatment increased total protein binding as well as JunD binding to the ferritin H ARE. Chromatin immunoprecipitation assay showed that H2O2 treatment induced JunD binding to the ferritin H ARE. Both H2O2 and t-BHQ induced phosphorylation of JunD at Ser-100, an activated form of JunD. Furthermore, overexpression of JunD induced endogenous ferritin H protein synthesis. Since JunD has recently been demonstrated to protect cells from several stress stimuli including oxidative stress, these results suggest that, in addition to NFE2-related factor 2 (Nrf2) as a major ARE regulatory protein, JunD is another ARE regulatory protein for transcriptional activation of the human ferritin H gene and probably other antioxidant genes containing the conserved ARE sequences by which JunD may confer cytoprotection during oxidative stress.
         datePublished:2005-07-11T00:00:00Z
         dateModified:2005-07-11T00:00:00Z
         pageStart:7567
         pageEnd:7578
         sameAs:https://doi.org/10.1038/sj.onc.1208901
         keywords:
            ferritin
            oxidative stress
            JunD
            AP1
            ARE
            iron
            Medicine/Public Health
            general
            Internal Medicine
            Cell Biology
            Human Genetics
            Oncology
            Apoptosis
         image:
            https://media.springernature.com/lw1200/springer-static/image/art%3A10.1038%2Fsj.onc.1208901/MediaObjects/41388_2005_Article_BF1208901_Fig1_HTML.jpg
            https://media.springernature.com/lw1200/springer-static/image/art%3A10.1038%2Fsj.onc.1208901/MediaObjects/41388_2005_Article_BF1208901_Fig2_HTML.jpg
            https://media.springernature.com/lw1200/springer-static/image/art%3A10.1038%2Fsj.onc.1208901/MediaObjects/41388_2005_Article_BF1208901_Fig3_HTML.jpg
            https://media.springernature.com/lw1200/springer-static/image/art%3A10.1038%2Fsj.onc.1208901/MediaObjects/41388_2005_Article_BF1208901_Fig4_HTML.jpg
            https://media.springernature.com/lw1200/springer-static/image/art%3A10.1038%2Fsj.onc.1208901/MediaObjects/41388_2005_Article_BF1208901_Fig5_HTML.jpg
            https://media.springernature.com/lw1200/springer-static/image/art%3A10.1038%2Fsj.onc.1208901/MediaObjects/41388_2005_Article_BF1208901_Fig6_HTML.jpg
            https://media.springernature.com/lw1200/springer-static/image/art%3A10.1038%2Fsj.onc.1208901/MediaObjects/41388_2005_Article_BF1208901_Fig7_HTML.jpg
         isPartOf:
            name:Oncogene
            issn:
               1476-5594
               0950-9232
            volumeNumber:24
            type:
               Periodical
               PublicationVolume
         publisher:
            name:Nature Publishing Group UK
            logo:
               url:https://www.springernature.com/app-sn/public/images/logo-springernature.png
               type:ImageObject
            type:Organization
         author:
               name:Yoshiaki Tsuji
               affiliation:
                     name:North Carolina State University
                     address:
                        name:Department of Environmental and Molecular Toxicology, North Carolina State University, Raleigh, USA
                        type:PostalAddress
                     type:Organization
               email:[email protected]
               type:Person
         isAccessibleForFree:
         hasPart:
            isAccessibleForFree:
            cssSelector:.main-content
            type:WebPageElement
         type:ScholarlyArticle
      context:https://schema.org
ScholarlyArticle:
      headline:JunD activates transcription of the human ferritin H gene through an antioxidant response element during oxidative stress
      description:Ferritin is the major intracellular iron storage protein that sequesters excess free iron to minimize generation of iron-catalysed reactive oxygen species. We previously demonstrated that expression of ferritin heavy chain (ferritin H) was induced by pro-oxidants, which is a part of cellular antioxidant response to protect cells from oxidative damage. In this study, we have identified that the antioxidant/electrophile response element (ARE) located 4.5âkb upstream to the human ferritin H transcription initiation site is responsible for the oxidant response. The human ferritin H ARE comprises two copies of bidirectional AP1 motifs. Mutations in each AP1 motif significantly impaired protein binding and the function of the ARE, indicating that both of the AP1 motifs are required for pro-oxidant-mediated activation of the ferritin H gene. We identified that JunD, an AP1 family basic-leucine zipper (bZip) transcription factor, is one of the ferritin H ARE binding proteins and activates ferritin H transcription in HepG2 hepatocarcinoma cells. Gel retardation assay demonstrated that H2O2 (hydrogen peroxide) or t-BHQ (tert-butylhydroquinone) treatment increased total protein binding as well as JunD binding to the ferritin H ARE. Chromatin immunoprecipitation assay showed that H2O2 treatment induced JunD binding to the ferritin H ARE. Both H2O2 and t-BHQ induced phosphorylation of JunD at Ser-100, an activated form of JunD. Furthermore, overexpression of JunD induced endogenous ferritin H protein synthesis. Since JunD has recently been demonstrated to protect cells from several stress stimuli including oxidative stress, these results suggest that, in addition to NFE2-related factor 2 (Nrf2) as a major ARE regulatory protein, JunD is another ARE regulatory protein for transcriptional activation of the human ferritin H gene and probably other antioxidant genes containing the conserved ARE sequences by which JunD may confer cytoprotection during oxidative stress.
      datePublished:2005-07-11T00:00:00Z
      dateModified:2005-07-11T00:00:00Z
      pageStart:7567
      pageEnd:7578
      sameAs:https://doi.org/10.1038/sj.onc.1208901
      keywords:
         ferritin
         oxidative stress
         JunD
         AP1
         ARE
         iron
         Medicine/Public Health
         general
         Internal Medicine
         Cell Biology
         Human Genetics
         Oncology
         Apoptosis
      image:
         https://media.springernature.com/lw1200/springer-static/image/art%3A10.1038%2Fsj.onc.1208901/MediaObjects/41388_2005_Article_BF1208901_Fig1_HTML.jpg
         https://media.springernature.com/lw1200/springer-static/image/art%3A10.1038%2Fsj.onc.1208901/MediaObjects/41388_2005_Article_BF1208901_Fig2_HTML.jpg
         https://media.springernature.com/lw1200/springer-static/image/art%3A10.1038%2Fsj.onc.1208901/MediaObjects/41388_2005_Article_BF1208901_Fig3_HTML.jpg
         https://media.springernature.com/lw1200/springer-static/image/art%3A10.1038%2Fsj.onc.1208901/MediaObjects/41388_2005_Article_BF1208901_Fig4_HTML.jpg
         https://media.springernature.com/lw1200/springer-static/image/art%3A10.1038%2Fsj.onc.1208901/MediaObjects/41388_2005_Article_BF1208901_Fig5_HTML.jpg
         https://media.springernature.com/lw1200/springer-static/image/art%3A10.1038%2Fsj.onc.1208901/MediaObjects/41388_2005_Article_BF1208901_Fig6_HTML.jpg
         https://media.springernature.com/lw1200/springer-static/image/art%3A10.1038%2Fsj.onc.1208901/MediaObjects/41388_2005_Article_BF1208901_Fig7_HTML.jpg
      isPartOf:
         name:Oncogene
         issn:
            1476-5594
            0950-9232
         volumeNumber:24
         type:
            Periodical
            PublicationVolume
      publisher:
         name:Nature Publishing Group UK
         logo:
            url:https://www.springernature.com/app-sn/public/images/logo-springernature.png
            type:ImageObject
         type:Organization
      author:
            name:Yoshiaki Tsuji
            affiliation:
                  name:North Carolina State University
                  address:
                     name:Department of Environmental and Molecular Toxicology, North Carolina State University, Raleigh, USA
                     type:PostalAddress
                  type:Organization
            email:[email protected]
            type:Person
      isAccessibleForFree:
      hasPart:
         isAccessibleForFree:
         cssSelector:.main-content
         type:WebPageElement
["Periodical","PublicationVolume"]:
      name:Oncogene
      issn:
         1476-5594
         0950-9232
      volumeNumber:24
Organization:
      name:Nature Publishing Group UK
      logo:
         url:https://www.springernature.com/app-sn/public/images/logo-springernature.png
         type:ImageObject
      name:North Carolina State University
      address:
         name:Department of Environmental and Molecular Toxicology, North Carolina State University, Raleigh, USA
         type:PostalAddress
ImageObject:
      url:https://www.springernature.com/app-sn/public/images/logo-springernature.png
Person:
      name:Yoshiaki Tsuji
      affiliation:
            name:North Carolina State University
            address:
               name:Department of Environmental and Molecular Toxicology, North Carolina State University, Raleigh, USA
               type:PostalAddress
            type:Organization
      email:[email protected]
PostalAddress:
      name:Department of Environmental and Molecular Toxicology, North Carolina State University, Raleigh, USA
WebPageElement:
      isAccessibleForFree:
      cssSelector:.main-content

Social Networks {👍}(1)

https://twitter.com/oncogenejournal

External Links {🔗}(97)

Analytics and Tracking {📊}

Google Tag Manager

Libraries {📚}

Prism.js
Zoom.js

Emails and Hosting {✉️}

Mail Servers:

mx.zoho.eu
mx2.zoho.eu
mx3.zoho.eu

Name Servers:

josh.ns.cloudflare.com
zita.ns.cloudflare.com

4.7s.