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We began analyzing https://www.nature.com/articles/371346a0, but it redirected us to https://www.nature.com/articles/371346a0. The analysis below is for the second page.

Title[redir]:
Cleavage of poly(ADP-ribose) polymerase by a proteinase with properties like ICE | Nature
Description:
RECENT studies suggest that pro teases of the inter leukin 1-β-con-verting enzyme (ICE)/ced-3 family are involved in initiating the active phase of apoptosis1–3. Here we identify a novel protease resembling ICE (prICE) that is active in a cell-free system that reproduces the morphological and biochemical events of apoptosis4. prICE cleaves the nuclear enzyme poly(ADP-ribose) polymerase (PARP) at a tetrapeptide sequence identical to one of two ICE sites in pro-inter leu kin-l-β. However, prICE does not cleave purified pro-interleukin- 1-β, and purified ICE does not cleave PARP, indicating that the two activities are distinct. Inhibition of prICE abolishes all manifestations of apoptosis in the extracts including morphological changes, cleavage of PARP and production of an oligonucleosomal ladder. These studies suggest that prICE might be pivotal in initiating the active phase of apoptosis in vitro and in intact cells.

Matching Content Categories {📚}

  • Education
  • Social Networks
  • 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?

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


Based on our best estimate, this website will receive around 98,426,998 visitors per month in the current month.

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Keywords {🔍}

article, google, scholar, cas, nature, access, cell, content, cookies, polyadpribose, kaufmann, apoptosis, privacy, journal, polymerase, ice, price, cancer, data, lazebnik, desnoyers, cells, open, usa, department, research, advertising, information, subscribe, september, cleavage, poirier, earnshaw, active, parp, institution, buy, yuan, ads, biol, johns, hopkins, school, medicine, north, wolfe, street, baltimore, maryland, permissions,

Topics {✒️}

nature portfolio pro-inter leu kin-l-β permissions reprints privacy policy advertising subscribe nature nature 356 nature 371 nature social media personal data springerlink instant access data protection permissions studies suggest cell-free system airway epithelial cells privacy explore content subscription content nuclear enzyme poly european economic area tetrapeptide sequence identical institutional subscriptions read autophagy impacts response johns hopkins school hrpa anchors meningococci activates jnk signaling accepting optional cookies journals search log extracts including morphological manage preferences protease resembling ice article lazebnik content article purchase access journal publish laval university article cite essential cookies intact cells cancer res pro teases issue learn optional cookies choices article cookies skip poirier rights

Schema {🗺️}

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         description:RECENT studies suggest that pro teases of the inter leukin 1-β-con-verting enzyme (ICE)/ced-3 family are involved in initiating the active phase of apoptosis1–3. Here we identify a novel protease resembling ICE (prICE) that is active in a cell-free system that reproduces the morphological and biochemical events of apoptosis4. prICE cleaves the nuclear enzyme poly(ADP-ribose) polymerase (PARP) at a tetrapeptide sequence identical to one of two ICE sites in pro-inter leu kin-l-β. However, prICE does not cleave purified pro-interleukin- 1-β, and purified ICE does not cleave PARP, indicating that the two activities are distinct. Inhibition of prICE abolishes all manifestations of apoptosis in the extracts including morphological changes, cleavage of PARP and production of an oligonucleosomal ladder. These studies suggest that prICE might be pivotal in initiating the active phase of apoptosis in vitro and in intact cells.
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      headline:Cleavage of poly(ADP-ribose) polymerase by a proteinase with properties like ICE
      description:RECENT studies suggest that pro teases of the inter leukin 1-β-con-verting enzyme (ICE)/ced-3 family are involved in initiating the active phase of apoptosis1–3. Here we identify a novel protease resembling ICE (prICE) that is active in a cell-free system that reproduces the morphological and biochemical events of apoptosis4. prICE cleaves the nuclear enzyme poly(ADP-ribose) polymerase (PARP) at a tetrapeptide sequence identical to one of two ICE sites in pro-inter leu kin-l-β. However, prICE does not cleave purified pro-interleukin- 1-β, and purified ICE does not cleave PARP, indicating that the two activities are distinct. Inhibition of prICE abolishes all manifestations of apoptosis in the extracts including morphological changes, cleavage of PARP and production of an oligonucleosomal ladder. These studies suggest that prICE might be pivotal in initiating the active phase of apoptosis in vitro and in intact cells.
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