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  2. Matching Content Categories
  3. CMS
  4. Monthly Traffic Estimate
  5. How Does Doi.org Make Money
  6. Keywords
  7. Topics
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We began analyzing https://link.springer.com/article/10.1007/s10495-009-0452-5, but it redirected us to https://link.springer.com/article/10.1007/s10495-009-0452-5. The analysis below is for the second page.

Title[redir]:
Regulation of apoptosis-associated lysosomal membrane permeabilization | Apoptosis
Description:
Lysosomal membrane permeabilization (LMP) occurs in response to a large variety of cell death stimuli causing release of cathepsins from the lysosomal lumen into the cytosol where they participate in apoptosis signaling. In some settings, apoptosis induction is dependent on an early release of cathepsins, while under other circumstances LMP occurs late in the cell death process and contributes to amplification of the death signal. The mechanism underlying LMP is still incompletely understood; however, a growing body of evidence suggests that LMP may be governed by several distinct mechanisms that are likely engaged in a death stimulus- and cell-type-dependent fashion. In this review, factors contributing to permeabilization of the lysosomal membrane including reactive oxygen species, lysosomal membrane lipid composition, proteases, p53, and Bcl-2 family proteins, are described. Potential mechanisms to safeguard lysosomal integrity and confer resistance to lysosome-dependent cell death are also discussed.

Matching Content Categories {📚}

  • Education
  • Science
  • Telecommunications

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 80,486,609 visitors per month in the current month.

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How Does Doi.org Make Money? {💸}

We can't tell how the site generates income.

Not all websites focus on profit; some are designed to educate, connect people, or share useful tools. People create websites for numerous reasons. And this could be one such example. Doi.org has a secret sauce for making money, but we can't detect it yet.

Keywords {🔍}

lysosomal, google, scholar, pubmed, cas, article, membrane, cell, death, apoptosis, lmp, lysosomes, cells, release, proteins, cathepsin, permeabilization, protein, cathepsins, bcl, activation, biol, bax, cytosol, family, destabilization, cancer, human, signaling, induced, pathway, chem, brunk, mechanism, role, mitochondrial, free, iron, tumor, stability, hsp, acid, apoptotic, bid, caspase, zhang, mechanisms, oxidative, necrosis, factor,

Topics {✒️}

guanosine 5′-[gamma-thio]triphosphate-mediated activation c-jun n-terminal kinase raf1-extracellular signal-regulated kinase potentiates β-amyloid-induced disruption tumor necrosis factor-alpha tnf-alpha-mediated lysosomal permeabilization tumor necrosis factor-α staurosporine-induced t-cell apoptosis tnf-α-mediated hepatocyte apoptosis tnf-α-induced cell death ligand-activated transcription factor endoplasmic reticulum stress low-molecular-weight iron 40-kda fitc-dextran molecules 250-kda fitc-dextran molecules selective apoptosis-inducing factor oxidant-induced cell death tumor necrosis factor nmda-mediated calcium influx amyloid beta-protein fibrils article download pdf low steady-state concentration full size image tnf-alpha induced apoptosis stimulating tnf-alpha expression mitigate oxidant-induced lmp cytokine-initiated cathepsin-dependent apoptosis ion-conducting channels produced kinase-dependent signaling events multi-domain family members anti-cancer drug siramesine p53-dependent tumor suppression beta-amyloid-mediated regulation h-ras driven transformation sphingomyelin derivative 3-o-methylsphingomyelin single-membrane bound organelles broad-spectrum antimicrobial function oxidant-mediated lysosomal rupture immuno-electron microscopy showed beta-amyloid-mediated stabilization amyloid beta peptide α-induced lysosomal destabilization amplifying feed-back loop reiners jj jr dna-damaging drugs 5-fluorouracil trail-resistant glioma cells ultra-small gold particles surface-bound iron suffered human cytotoxic t-lymphocytes anti-apoptotic bcl-2 proteins

Questions {❓}

  • Kågedal K, Johansson AC, Johansson U et al (2005) Lysosomal membrane permeabilization during apoptosis-involvement of Bax?
  • Zhao M, Eaton JW, Brunk UT (2000) Protection against oxidant-mediated lysosomal rupture: a new anti-apoptotic activity of Bcl-2?

Schema {🗺️}

WebPage:
      mainEntity:
         headline:Regulation of apoptosis-associated lysosomal membrane permeabilization
         description:Lysosomal membrane permeabilization (LMP) occurs in response to a large variety of cell death stimuli causing release of cathepsins from the lysosomal lumen into the cytosol where they participate in apoptosis signaling. In some settings, apoptosis induction is dependent on an early release of cathepsins, while under other circumstances LMP occurs late in the cell death process and contributes to amplification of the death signal. The mechanism underlying LMP is still incompletely understood; however, a growing body of evidence suggests that LMP may be governed by several distinct mechanisms that are likely engaged in a death stimulus- and cell-type-dependent fashion. In this review, factors contributing to permeabilization of the lysosomal membrane including reactive oxygen species, lysosomal membrane lipid composition, proteases, p53, and Bcl-2 family proteins, are described. Potential mechanisms to safeguard lysosomal integrity and confer resistance to lysosome-dependent cell death are also discussed.
         datePublished:2010-01-14T00:00:00Z
         dateModified:2010-01-14T00:00:00Z
         pageStart:527
         pageEnd:540
         license:https://creativecommons.org/licenses/by-nc/2.0
         sameAs:https://doi.org/10.1007/s10495-009-0452-5
         keywords:
            Lysosome
            Lysosomal release
            Caspases
            Calpains
            Hsp
            LAMP
            Cancer Research
            Cell Biology
            Oncology
            Biochemistry
            general
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ScholarlyArticle:
      headline:Regulation of apoptosis-associated lysosomal membrane permeabilization
      description:Lysosomal membrane permeabilization (LMP) occurs in response to a large variety of cell death stimuli causing release of cathepsins from the lysosomal lumen into the cytosol where they participate in apoptosis signaling. In some settings, apoptosis induction is dependent on an early release of cathepsins, while under other circumstances LMP occurs late in the cell death process and contributes to amplification of the death signal. The mechanism underlying LMP is still incompletely understood; however, a growing body of evidence suggests that LMP may be governed by several distinct mechanisms that are likely engaged in a death stimulus- and cell-type-dependent fashion. In this review, factors contributing to permeabilization of the lysosomal membrane including reactive oxygen species, lysosomal membrane lipid composition, proteases, p53, and Bcl-2 family proteins, are described. Potential mechanisms to safeguard lysosomal integrity and confer resistance to lysosome-dependent cell death are also discussed.
      datePublished:2010-01-14T00:00:00Z
      dateModified:2010-01-14T00:00:00Z
      pageStart:527
      pageEnd:540
      license:https://creativecommons.org/licenses/by-nc/2.0
      sameAs:https://doi.org/10.1007/s10495-009-0452-5
      keywords:
         Lysosome
         Lysosomal release
         Caspases
         Calpains
         Hsp
         LAMP
         Cancer Research
         Cell Biology
         Oncology
         Biochemistry
         general
         Virology
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                     name:Division of Experimental Pathology, Department of Clinical and Experimental Medicine, Linköping University, Linköping, Sweden
                     type:PostalAddress
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            name:Cathrine Nilsson
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                  name:Linköping University Hospital
                  address:
                     name:Division of Otorhinolaryngology, Linköping University Hospital, Linköping, Sweden
                     type:PostalAddress
                  type:Organization
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                  address:
                     name:Division of Experimental Pathology, Department of Clinical and Experimental Medicine, Linköping University, Linköping, Sweden
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                  address:
                     name:Division of Experimental Pathology, Department of Clinical and Experimental Medicine, Linköping University, Linköping, Sweden
                     type:PostalAddress
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            type:Person
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            affiliation:
                  name:Linköping University Hospital
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                     type:PostalAddress
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      address:
         name:Division of Experimental Pathology, Department of Clinical and Experimental Medicine, Linköping University, Linköping, Sweden
         type:PostalAddress
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      address:
         name:Division of Otorhinolaryngology, Linköping University Hospital, Linköping, Sweden
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            address:
               name:Division of Otorhinolaryngology, Linköping University Hospital, Linköping, Sweden
               type:PostalAddress
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      email:[email protected]
      name:Hanna Appelqvist
      affiliation:
            name:Linköping University
            address:
               name:Division of Experimental Pathology, Department of Clinical and Experimental Medicine, Linköping University, Linköping, Sweden
               type:PostalAddress
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      name:Cathrine Nilsson
      affiliation:
            name:Linköping University Hospital
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               name:Division of Otorhinolaryngology, Linköping University Hospital, Linköping, Sweden
               type:PostalAddress
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            name:Linköping University
            address:
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               type:PostalAddress
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      name:Katarina Kågedal
      affiliation:
            name:Linköping University
            address:
               name:Division of Experimental Pathology, Department of Clinical and Experimental Medicine, Linköping University, Linköping, Sweden
               type:PostalAddress
            type:Organization
      name:Karin Roberg
      affiliation:
            name:Linköping University Hospital
            address:
               name:Division of Otorhinolaryngology, Linköping University Hospital, Linköping, Sweden
               type:PostalAddress
            type:Organization
            name:Linköping University
            address:
               name:Division of Otorhinolaryngology, Department of Clinical and Experimental Medicine, Linköping University, Linköping, Sweden
               type:PostalAddress
            type:Organization
      name:Karin Öllinger
      affiliation:
            name:Linköping University
            address:
               name:Division of Experimental Pathology, Department of Clinical and Experimental Medicine, Linköping University, Linköping, Sweden
               type:PostalAddress
            type:Organization
PostalAddress:
      name:Division of Otorhinolaryngology, Linköping University Hospital, Linköping, Sweden
      name:Division of Experimental Pathology, Department of Clinical and Experimental Medicine, Linköping University, Linköping, Sweden
      name:Division of Otorhinolaryngology, Linköping University Hospital, Linköping, Sweden
      name:Division of Experimental Pathology, Department of Clinical and Experimental Medicine, Linköping University, Linköping, Sweden
      name:Division of Experimental Pathology, Department of Clinical and Experimental Medicine, Linköping University, Linköping, Sweden
      name:Division of Otorhinolaryngology, Linköping University Hospital, Linköping, Sweden
      name:Division of Otorhinolaryngology, Department of Clinical and Experimental Medicine, Linköping University, Linköping, Sweden
      name:Division of Experimental Pathology, Department of Clinical and Experimental Medicine, Linköping University, Linköping, Sweden

External Links {🔗}(665)

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