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DOI . ORG {}

  1. Analyzed Page
  2. Matching Content Categories
  3. CMS
  4. Monthly Traffic Estimate
  5. How Does Doi.org Make Money
  6. Keywords
  7. Topics
  8. Questions
  9. Schema
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We began analyzing https://link.springer.com/article/10.1007/s00018-016-2205-2, but it redirected us to https://link.springer.com/article/10.1007/s00018-016-2205-2. The analysis below is for the second page.

Title[redir]:
The intersection of cell death and inflammasome activation | Cellular and Molecular Life Sciences
Description:
Inflammasomes sense cellular danger to activate the cysteine-aspartic protease caspase-1, which processes precursor interleukin-1β (IL-1β) and IL-18 into their mature bioactive fragments. In addition, activated caspase-1 or the related inflammatory caspase, caspase-11, can cleave gasdermin D to induce a lytic cell death, termed pyroptosis. The intertwining of IL-1β activation and cell death is further highlighted by research showing that the extrinsic apoptotic caspase, caspase-8, may, like caspase-1, directly process IL-1β, activate the NLRP3 inflammasome itself, or bind to inflammasome complexes to induce apoptotic cell death. Similarly, RIPK3- and MLKL-dependent necroptotic signaling can activate the NLRP3 inflammasome to drive IL-1β inflammatory responses in vivo. Here, we review the mechanisms by which cell death signaling activates inflammasomes to initiate IL-1β-driven inflammation, and highlight the clinical relevance of these findings to heritable autoinflammatory diseases. We also discuss whether the act of cell death can be separated from IL-1β secretion and evaluate studies suggesting that several cell death regulatory proteins can directly interact with, and modulate the function of, inflammasome and IL-1β containing protein complexes.

Matching Content Categories {📚}

  • Education
  • Telecommunications
  • Business & Finance

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.

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How Does Doi.org Make Money? {💸}

We find it hard to spot revenue streams.

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 could be secretly minting cash, but we can't detect the process.

Keywords {🔍}

pubmed, google, scholar, article, cas, central, inflammasome, cell, activation, caspase, nlrp, immunol, death, nature, nat, apoptosis, doinature, doijimmunol, silke, ilbeta, vince, fitzgerald, chen, signaling, zhang, immunity, sci, wang, inflammasomes, huang, usa, inflammation, secretion, doini, proc, natl, acad, yang, protein, mice, rep, kaiser, mocarski, doipnas, processing, inflammatory, pyroptosis, immune, role, doijcell,

Topics {✒️}

pro-interleukin-1beta protein complexes initiate il-1β-driven inflammation month download article/chapter inflammasome-independent il-1beta production rip1-rip3-drp1 signaling pathway real-time single-cell imaging mavs-induced membrane permeabilization tnf-induced keratinocyte apoptosis mlkl-dependent necroptotic signaling rh domain-interacting protein multi-system autoinflammatory disorder nf-kappab signalling tnf-r1 signaling complex mediates noncanonical il-1beta francisella-infected caspase-1-deficient macrophages rip3-mediated macrophage necrosis calcium-sensing receptor regulates metabolite-sensing receptor gpr43 processes precursor interleukin-1β produce mature il-1beta modulate il-1beta production metabolite-sensing receptors gpr43 microbiota-modulated metabolites shape rip3-dependent cell death pro-interleukin-1beta regulates immune signalling vince & john silke tnf-mediated gene induction cysteine-aspartic protease caspase-1 directly process il-1β full article pdf caspase-1-dependent mitochondrial damage autophagy-mediated secretion il-1beta production shigella-induced apoptosis caspase-1-deficient mice infected cytoplasmic lps recognition interleukin-1beta secretion innate immune receptors caspase-1-dependent pore formation caspase-8-induced il-1 innate immune defense promotes inflammasome activation tlr4-independent endotoxic shock toxin-induced necroptosis il-1beta secretion nf-kappab skin inflammation independently innate immune response adaptor asc acts

Questions {❓}

  • Lawlor KE, Vince JE (2014) Ambiguities in NLRP3 inflammasome regulation: is there a role for mitochondria?

Schema {🗺️}

WebPage:
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         headline:The intersection of cell death and inflammasome activation
         description:Inflammasomes sense cellular danger to activate the cysteine-aspartic protease caspase-1, which processes precursor interleukin-1β (IL-1β) and IL-18 into their mature bioactive fragments. In addition, activated caspase-1 or the related inflammatory caspase, caspase-11, can cleave gasdermin D to induce a lytic cell death, termed pyroptosis. The intertwining of IL-1β activation and cell death is further highlighted by research showing that the extrinsic apoptotic caspase, caspase-8, may, like caspase-1, directly process IL-1β, activate the NLRP3 inflammasome itself, or bind to inflammasome complexes to induce apoptotic cell death. Similarly, RIPK3- and MLKL-dependent necroptotic signaling can activate the NLRP3 inflammasome to drive IL-1β inflammatory responses in vivo. Here, we review the mechanisms by which cell death signaling activates inflammasomes to initiate IL-1β-driven inflammation, and highlight the clinical relevance of these findings to heritable autoinflammatory diseases. We also discuss whether the act of cell death can be separated from IL-1β secretion and evaluate studies suggesting that several cell death regulatory proteins can directly interact with, and modulate the function of, inflammasome and IL-1β containing protein complexes.
         datePublished:2016-04-11T00:00:00Z
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      description:Inflammasomes sense cellular danger to activate the cysteine-aspartic protease caspase-1, which processes precursor interleukin-1β (IL-1β) and IL-18 into their mature bioactive fragments. In addition, activated caspase-1 or the related inflammatory caspase, caspase-11, can cleave gasdermin D to induce a lytic cell death, termed pyroptosis. The intertwining of IL-1β activation and cell death is further highlighted by research showing that the extrinsic apoptotic caspase, caspase-8, may, like caspase-1, directly process IL-1β, activate the NLRP3 inflammasome itself, or bind to inflammasome complexes to induce apoptotic cell death. Similarly, RIPK3- and MLKL-dependent necroptotic signaling can activate the NLRP3 inflammasome to drive IL-1β inflammatory responses in vivo. Here, we review the mechanisms by which cell death signaling activates inflammasomes to initiate IL-1β-driven inflammation, and highlight the clinical relevance of these findings to heritable autoinflammatory diseases. We also discuss whether the act of cell death can be separated from IL-1β secretion and evaluate studies suggesting that several cell death regulatory proteins can directly interact with, and modulate the function of, inflammasome and IL-1β containing protein complexes.
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         Biochemistry
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External Links {🔗}(619)

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