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Zoology and wildlife conservation

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Abstracts » Zoology and wildlife conservation

Searching for FLASH domains

Article Abstract:

It is possible to raise doubts about research indicating that a protein named FLASH, required during programmed apoptosis to regulate the proteolytic cascade that leads to the death of the cell, is a functional analogue of mammalian Apaf-1 and its nematode homologue CED-4. Subsequent research was not able to identify any sequence similarity between FLASH and the Apaf-1/CED-4 or death-effector domain domains. Those responsible for the original research defend their work, but acknowledge that they may have overestimated the structural homology of FLASH with CED-4, even though these proteins are functionally homologous.

Author: Koonin, Eugene V., Aravind, L., Imai, Yuzuru, Tschopp, Jurg, Dixit, Vishva M., Hofmann, Kay, Kimura, Takaharu, Yonehara, Shin
Publisher: Macmillan Publishing Ltd.
Publication Name: Nature
Subject: Zoology and wildlife conservation
ISSN: 0028-0836
Year: 1999

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Cardif is an adaptor protein in the RIG-I antiviral pathway and is targeted by hepatitis C virus

Article Abstract:

Cardif is a new caspase recruitment domains (CARD)-containing adaptor protein that interacts with RIG-I and recruits IKKbeta and IKKepsilon kinases by means of its C-terminal region, leading to the activation of NF(sub -kappaB) and IRF3. Cardif is targeted and inactivated by NS3-4A, a serine protease from hepatitis C virus, functioning as an adaptor, linking the cytoplasmic dsRNA receptor RIG-I to the initiation of antiviral programmes.

Author: Moradpour, Darius, Tschopp, Jurg, Meylan, Etienne, Curran, Joseph, Binder, Marco, Bartenschlager, Ralf, Hofmann, Kay
Publisher: Macmillan Publishing Ltd.
Publication Name: Nature
Subject: Zoology and wildlife conservation
ISSN: 0028-0836
Year: 2005
United States, Science & research, Hepatitis C, Antiviral agents, Protein research

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Inhibition of death receptor signals by cellular FLIP

Article Abstract:

Scientists have identified a FLICE-inhibitory protein (FLIP) contained within muscle and lymphoid tissue which inhibits apoptosis. The short-form protein contains identical genetic sequences to viral FLIP inhibitors and has two death effector domains. The long-form protein has a caspase-like domain with an active-centre tyrosine residue. The research indicates that FLIP has a key role in tissue homeostatis and apoptosis regulation.

Author: Schneider, Pascal, Tschopp, Jurg, Hofmann, Kay, Mattmann, Chantal, Burns, Kim, Bodmer, Jean-Luc, Schroter, Michael, Irmler, Martin, Thome, Margot, Hahne, Michael, Steiner, Veronique, Rimoldi, Donata, French, Lars E.
Publisher: Macmillan Publishing Ltd.
Publication Name: Nature
Subject: Zoology and wildlife conservation
ISSN: 0028-0836
Year: 1997
Cell proliferation, Homeostasis

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Subjects list: Research, Cell death
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