DOI . ORG {}

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

We began analyzing https://link.springer.com/article/10.1007/s12253-015-9946-3, but it redirected us to https://link.springer.com/article/10.1007/s12253-015-9946-3. The analysis below is for the second page.

Title[redir]:
Ferroptosis is Involved in Acetaminophen Induced Cell Death | Pathology & Oncology Research
Description:
The recently described form of programmed cell death, ferroptosis can be induced by agents causing GSH depletion or the inhibition of GPX4. Ferroptosis clearly shows distinct morphologic, biochemical and genetic features from apoptosis, necrosis and autophagy. Since NAPQI the highly reactive metabolite of the widely applied analgesic and antipyretic, acetaminophen induces a cell death which can be characterized by GSH depletion, GPX inhibition and caspase independency the involvement of ferroptosis in acetaminophen induced cell death has been investigated. The specific ferroptosis inhibitor ferrostatin-1 failed to elevate the viability of acetaminophen treated HepG2 cells. It should be noticed that these cells do not form NAPQI due to the lack of phase I enzyme expression therefore GSH depletion cannot be observed. However in the case of acetaminophen treated primary mouse hepatocytes the significant elevation of cell viability could be observed upon ferrostatin-1 treatment. Similar to ferrostatin-1 treatment, the addition of the RIP1 kinase inhibitor necrostatin-1 could also elevate the viability of acetaminophen treated primary hepatocytes. Ferrostatin-1 has no influence on the expression of CYP2E1 or on the cellular GSH level which suggest that the protective effect of ferrostatin-1 in APAP induced cell death is not based on the reduced metabolism of APAP to NAPQI or on altered NAPQI conjugation by cellular GSH. Our results suggest that beyond necroptosis and apoptosis a third programmed cell death, ferroptosis is also involved in acetaminophen induced cell death in primary hepatocytes.

Matching Content Categories {📚}

Education
Telecommunications
Science

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?

🌠 Phenomenal Traffic: 5M - 10M visitors per month

Based on our best estimate, this website will receive around 5,000,019 visitors per month in the current month.
However, some sources were not loaded, we suggest to reload the page to get complete results.

check SE Ranking
check Ahrefs
check Similarweb
check Ubersuggest
check Semrush

How Does Doi.org Make Money? {💸}

We find it hard to spot revenue streams.

Websites don't always need to be profitable; some serve as platforms for education or personal expression. Websites can serve multiple purposes. And this might be one of them. Doi.org could be getting rich in stealth mode, or the way it's monetizing isn't detectable.

Keywords {🔍}

pubmed, article, google, scholar, cas, cell, acetaminophen, death, ferroptosis, research, acetaminopheninduced, liver, toxicol, pharmacol, central, jaeschke, apoptosis, induced, szarka, cells, access, mice, biol, privacy, cookies, content, tamás, jemnitz, gsh, ferrostatin, primary, hepatocytes, cellular, acute, injury, hepatotoxicity, mcgill, appl, human, budapest, publish, search, lőrincz, kardon, mandl, andrás, inhibition, gpx, necrosis, napqi,

Topics {✒️}

apoptosis-inducing factor-mediated necroptosis acetaminophen-induced liver injury month download article/chapter drug-induced liver injury acetaminophen-induced hepatic inflammation impaired thiol-metabolizing enzymes acetaminophen-induced hepatic necrosis full article pdf related subjects acetaminophen-induced apoptosis programmed cell death acetaminophen-induced oxidation privacy choices/manage cookies yang ws article lőrincz liver injury research group nonapoptotic cell death mcgill mr n-acetylcysteine specific cellular target cell death mechanisms mouse primary hepatocytes check access instant access european economic area shows distinct morphologic highly reactive metabolite traditional chinese medicine iron-dependent form cystine transport leading ascorbic acid recycling p450-dependent metabolism ch’en il reactive oxygen species transmembrane electron transfer széchenyi development plan article log tamás lőrincz conditions privacy policy induced hepatotoxicity ordered cellular explosion mouse liver widely applied analgesic protective effect protect hepg2 cells receptor interacting protein article cite clinically relevant model andrás szarka

Questions {❓}

Gujral JS, Knight TR, Farhood A, Bajt ML, Jaeschke H (2002) Mode of cell death after acetaminophen overdose in mice: apoptosis or oncotic necrosis?

Schema {🗺️}

WebPage:
      mainEntity:
         headline:Ferroptosis is Involved in Acetaminophen Induced Cell Death
         description:The recently described form of programmed cell death, ferroptosis can be induced by agents causing GSH depletion or the inhibition of GPX4. Ferroptosis clearly shows distinct morphologic, biochemical and genetic features from apoptosis, necrosis and autophagy. Since NAPQI the highly reactive metabolite of the widely applied analgesic and antipyretic, acetaminophen induces a cell death which can be characterized by GSH depletion, GPX inhibition and caspase independency the involvement of ferroptosis in acetaminophen induced cell death has been investigated. The specific ferroptosis inhibitor ferrostatin-1 failed to elevate the viability of acetaminophen treated HepG2 cells. It should be noticed that these cells do not form NAPQI due to the lack of phase I enzyme expression therefore GSH depletion cannot be observed. However in the case of acetaminophen treated primary mouse hepatocytes the significant elevation of cell viability could be observed upon ferrostatin-1 treatment. Similar to ferrostatin-1 treatment, the addition of the RIP1 kinase inhibitor necrostatin-1 could also elevate the viability of acetaminophen treated primary hepatocytes. Ferrostatin-1 has no influence on the expression of CYP2E1 or on the cellular GSH level which suggest that the protective effect of ferrostatin-1 in APAP induced cell death is not based on the reduced metabolism of APAP to NAPQI or on altered NAPQI conjugation by cellular GSH. Our results suggest that beyond necroptosis and apoptosis a third programmed cell death, ferroptosis is also involved in acetaminophen induced cell death in primary hepatocytes.
         datePublished:2015-05-12T00:00:00Z
         dateModified:2015-05-12T00:00:00Z
         pageStart:1115
         pageEnd:1121
         sameAs:https://doi.org/10.1007/s12253-015-9946-3
         keywords:
            Acetaminophen
            Hepatotoxicity
            Ferroptosis
            Necroptosis
            Glutathione
            Cancer Research
            Oncology
            Pathology
            Immunology
            Biomedicine
            general
         image:
         isPartOf:
            name:Pathology & Oncology Research
            issn:
               1532-2807
               1219-4956
            volumeNumber:21
            type:
               Periodical
               PublicationVolume
         publisher:
            name:Springer Netherlands
            logo:
               url:https://www.springernature.com/app-sn/public/images/logo-springernature.png
               type:ImageObject
            type:Organization
         author:
               name:Tamás Lőrincz
               affiliation:
                     name:Budapest University of Technology and Economics
                     address:
                        name:Department of Applied Biotechnology and Food Science, Laboratory of Biochemistry and Molecular Biology, Budapest University of Technology and Economics, Budapest, Hungary
                        type:PostalAddress
                     type:Organization
               type:Person
               name:Katalin Jemnitz
               affiliation:
                     name:Hungarian Academy of Sciences
                     address:
                        name:Department of Functional Pharmacology, Institute of Molecular Pharmacology, Research Centre for Natural Sciences, Hungarian Academy of Sciences, Budapest, Hungary
                        type:PostalAddress
                     type:Organization
               type:Person
               name:Tamás Kardon
               affiliation:
                     name:Research Group of Hungarian Academy of Sciences and Semmelweis University
                     address:
                        name:Department of Medical Chemistry, Molecular Biology and Pathobiochemistry Pathobiochemistry, Research Group of Hungarian Academy of Sciences and Semmelweis University, Budapest, , Hungary
                        type:PostalAddress
                     type:Organization
               type:Person
               name:József Mandl
               affiliation:
                     name:Research Group of Hungarian Academy of Sciences and Semmelweis University
                     address:
                        name:Department of Medical Chemistry, Molecular Biology and Pathobiochemistry Pathobiochemistry, Research Group of Hungarian Academy of Sciences and Semmelweis University, Budapest, , Hungary
                        type:PostalAddress
                     type:Organization
               type:Person
               name:András Szarka
               affiliation:
                     name:Budapest University of Technology and Economics
                     address:
                        name:Department of Applied Biotechnology and Food Science, Laboratory of Biochemistry and Molecular Biology, Budapest University of Technology and Economics, Budapest, Hungary
                        type:PostalAddress
                     type:Organization
                     name:Pathobiochemistry Research Group of Hungarian Academy of Sciences and Semmelweis University
                     address:
                        name:Pathobiochemistry Research Group of Hungarian Academy of Sciences and Semmelweis University, Budapest, Hungary
                        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:Ferroptosis is Involved in Acetaminophen Induced Cell Death
      description:The recently described form of programmed cell death, ferroptosis can be induced by agents causing GSH depletion or the inhibition of GPX4. Ferroptosis clearly shows distinct morphologic, biochemical and genetic features from apoptosis, necrosis and autophagy. Since NAPQI the highly reactive metabolite of the widely applied analgesic and antipyretic, acetaminophen induces a cell death which can be characterized by GSH depletion, GPX inhibition and caspase independency the involvement of ferroptosis in acetaminophen induced cell death has been investigated. The specific ferroptosis inhibitor ferrostatin-1 failed to elevate the viability of acetaminophen treated HepG2 cells. It should be noticed that these cells do not form NAPQI due to the lack of phase I enzyme expression therefore GSH depletion cannot be observed. However in the case of acetaminophen treated primary mouse hepatocytes the significant elevation of cell viability could be observed upon ferrostatin-1 treatment. Similar to ferrostatin-1 treatment, the addition of the RIP1 kinase inhibitor necrostatin-1 could also elevate the viability of acetaminophen treated primary hepatocytes. Ferrostatin-1 has no influence on the expression of CYP2E1 or on the cellular GSH level which suggest that the protective effect of ferrostatin-1 in APAP induced cell death is not based on the reduced metabolism of APAP to NAPQI or on altered NAPQI conjugation by cellular GSH. Our results suggest that beyond necroptosis and apoptosis a third programmed cell death, ferroptosis is also involved in acetaminophen induced cell death in primary hepatocytes.
      datePublished:2015-05-12T00:00:00Z
      dateModified:2015-05-12T00:00:00Z
      pageStart:1115
      pageEnd:1121
      sameAs:https://doi.org/10.1007/s12253-015-9946-3
      keywords:
         Acetaminophen
         Hepatotoxicity
         Ferroptosis
         Necroptosis
         Glutathione
         Cancer Research
         Oncology
         Pathology
         Immunology
         Biomedicine
         general
      image:
      isPartOf:
         name:Pathology & Oncology Research
         issn:
            1532-2807
            1219-4956
         volumeNumber:21
         type:
            Periodical
            PublicationVolume
      publisher:
         name:Springer Netherlands
         logo:
            url:https://www.springernature.com/app-sn/public/images/logo-springernature.png
            type:ImageObject
         type:Organization
      author:
            name:Tamás Lőrincz
            affiliation:
                  name:Budapest University of Technology and Economics
                  address:
                     name:Department of Applied Biotechnology and Food Science, Laboratory of Biochemistry and Molecular Biology, Budapest University of Technology and Economics, Budapest, Hungary
                     type:PostalAddress
                  type:Organization
            type:Person
            name:Katalin Jemnitz
            affiliation:
                  name:Hungarian Academy of Sciences
                  address:
                     name:Department of Functional Pharmacology, Institute of Molecular Pharmacology, Research Centre for Natural Sciences, Hungarian Academy of Sciences, Budapest, Hungary
                     type:PostalAddress
                  type:Organization
            type:Person
            name:Tamás Kardon
            affiliation:
                  name:Research Group of Hungarian Academy of Sciences and Semmelweis University
                  address:
                     name:Department of Medical Chemistry, Molecular Biology and Pathobiochemistry Pathobiochemistry, Research Group of Hungarian Academy of Sciences and Semmelweis University, Budapest, , Hungary
                     type:PostalAddress
                  type:Organization
            type:Person
            name:József Mandl
            affiliation:
                  name:Research Group of Hungarian Academy of Sciences and Semmelweis University
                  address:
                     name:Department of Medical Chemistry, Molecular Biology and Pathobiochemistry Pathobiochemistry, Research Group of Hungarian Academy of Sciences and Semmelweis University, Budapest, , Hungary
                     type:PostalAddress
                  type:Organization
            type:Person
            name:András Szarka
            affiliation:
                  name:Budapest University of Technology and Economics
                  address:
                     name:Department of Applied Biotechnology and Food Science, Laboratory of Biochemistry and Molecular Biology, Budapest University of Technology and Economics, Budapest, Hungary
                     type:PostalAddress
                  type:Organization
                  name:Pathobiochemistry Research Group of Hungarian Academy of Sciences and Semmelweis University
                  address:
                     name:Pathobiochemistry Research Group of Hungarian Academy of Sciences and Semmelweis University, Budapest, Hungary
                     type:PostalAddress
                  type:Organization
            email:[email protected]
            type:Person
      isAccessibleForFree:
      hasPart:
         isAccessibleForFree:
         cssSelector:.main-content
         type:WebPageElement
["Periodical","PublicationVolume"]:
      name:Pathology & Oncology Research
      issn:
         1532-2807
         1219-4956
      volumeNumber:21
Organization:
      name:Springer Netherlands
      logo:
         url:https://www.springernature.com/app-sn/public/images/logo-springernature.png
         type:ImageObject
      name:Budapest University of Technology and Economics
      address:
         name:Department of Applied Biotechnology and Food Science, Laboratory of Biochemistry and Molecular Biology, Budapest University of Technology and Economics, Budapest, Hungary
         type:PostalAddress
      name:Hungarian Academy of Sciences
      address:
         name:Department of Functional Pharmacology, Institute of Molecular Pharmacology, Research Centre for Natural Sciences, Hungarian Academy of Sciences, Budapest, Hungary
         type:PostalAddress
      name:Research Group of Hungarian Academy of Sciences and Semmelweis University
      address:
         name:Department of Medical Chemistry, Molecular Biology and Pathobiochemistry Pathobiochemistry, Research Group of Hungarian Academy of Sciences and Semmelweis University, Budapest, , Hungary
         type:PostalAddress
      name:Research Group of Hungarian Academy of Sciences and Semmelweis University
      address:
         name:Department of Medical Chemistry, Molecular Biology and Pathobiochemistry Pathobiochemistry, Research Group of Hungarian Academy of Sciences and Semmelweis University, Budapest, , Hungary
         type:PostalAddress
      name:Budapest University of Technology and Economics
      address:
         name:Department of Applied Biotechnology and Food Science, Laboratory of Biochemistry and Molecular Biology, Budapest University of Technology and Economics, Budapest, Hungary
         type:PostalAddress
      name:Pathobiochemistry Research Group of Hungarian Academy of Sciences and Semmelweis University
      address:
         name:Pathobiochemistry Research Group of Hungarian Academy of Sciences and Semmelweis University, Budapest, Hungary
         type:PostalAddress
ImageObject:
      url:https://www.springernature.com/app-sn/public/images/logo-springernature.png
Person:
      name:Tamás Lőrincz
      affiliation:
            name:Budapest University of Technology and Economics
            address:
               name:Department of Applied Biotechnology and Food Science, Laboratory of Biochemistry and Molecular Biology, Budapest University of Technology and Economics, Budapest, Hungary
               type:PostalAddress
            type:Organization
      name:Katalin Jemnitz
      affiliation:
            name:Hungarian Academy of Sciences
            address:
               name:Department of Functional Pharmacology, Institute of Molecular Pharmacology, Research Centre for Natural Sciences, Hungarian Academy of Sciences, Budapest, Hungary
               type:PostalAddress
            type:Organization
      name:Tamás Kardon
      affiliation:
            name:Research Group of Hungarian Academy of Sciences and Semmelweis University
            address:
               name:Department of Medical Chemistry, Molecular Biology and Pathobiochemistry Pathobiochemistry, Research Group of Hungarian Academy of Sciences and Semmelweis University, Budapest, , Hungary
               type:PostalAddress
            type:Organization
      name:József Mandl
      affiliation:
            name:Research Group of Hungarian Academy of Sciences and Semmelweis University
            address:
               name:Department of Medical Chemistry, Molecular Biology and Pathobiochemistry Pathobiochemistry, Research Group of Hungarian Academy of Sciences and Semmelweis University, Budapest, , Hungary
               type:PostalAddress
            type:Organization
      name:András Szarka
      affiliation:
            name:Budapest University of Technology and Economics
            address:
               name:Department of Applied Biotechnology and Food Science, Laboratory of Biochemistry and Molecular Biology, Budapest University of Technology and Economics, Budapest, Hungary
               type:PostalAddress
            type:Organization
            name:Pathobiochemistry Research Group of Hungarian Academy of Sciences and Semmelweis University
            address:
               name:Pathobiochemistry Research Group of Hungarian Academy of Sciences and Semmelweis University, Budapest, Hungary
               type:PostalAddress
            type:Organization
      email:[email protected]
PostalAddress:
      name:Department of Applied Biotechnology and Food Science, Laboratory of Biochemistry and Molecular Biology, Budapest University of Technology and Economics, Budapest, Hungary
      name:Department of Functional Pharmacology, Institute of Molecular Pharmacology, Research Centre for Natural Sciences, Hungarian Academy of Sciences, Budapest, Hungary
      name:Department of Medical Chemistry, Molecular Biology and Pathobiochemistry Pathobiochemistry, Research Group of Hungarian Academy of Sciences and Semmelweis University, Budapest, , Hungary
      name:Department of Medical Chemistry, Molecular Biology and Pathobiochemistry Pathobiochemistry, Research Group of Hungarian Academy of Sciences and Semmelweis University, Budapest, , Hungary
      name:Department of Applied Biotechnology and Food Science, Laboratory of Biochemistry and Molecular Biology, Budapest University of Technology and Economics, Budapest, Hungary
      name:Pathobiochemistry Research Group of Hungarian Academy of Sciences and Semmelweis University, Budapest, Hungary
WebPageElement:
      isAccessibleForFree:
      cssSelector:.main-content

External Links {🔗}(176)

Analytics and Tracking {📊}

Google Tag Manager

Libraries {📚}

Clipboard.js
Prism.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

CDN Services {📦}

Crossref

4.85s.