Cellular FLICE-inhibitory protein splice variants inhibit different steps of caspase-8 activation at the CD95 death-inducing signaling complex (Q28209029)

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scientific article (publication date: 8 June 2001)

Language	Label	Description	Also known as
English	Cellular FLICE-inhibitory protein splice variants inhibit different steps of caspase-8 activation at the CD95 death-inducing signaling complex	scientific article (publication date: 8 June 2001)

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scholarly article

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Cellular FLICE-inhibitory protein splice variants inhibit different steps of caspase-8 activation at the CD95 death-inducing signaling complex (English)

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author name string

A Krueger

1

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I Schmitz

2

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S Baumann

3

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P H Krammer

4

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S Kirchhoff

5

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language of work or name

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publication date

8 June 2001

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Journal of Biological Chemistry

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276

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23

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20633-40

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CD95's deadly mission in the immune system

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A novel protein that interacts with the death domain of Fas/APO1 contains a sequence motif related to the death domain

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FADD, a novel death domain-containing protein, interacts with the death domain of Fas and initiates apoptosis

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FLICE, a novel FADD-homologous ICE/CED-3-like protease, is recruited to the CD95 (Fas/APO-1) death--inducing signaling complex

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FLICE is activated by association with the CD95 death-inducing signaling complex (DISC).

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Fas- and tumor necrosis factor-induced apoptosis is inhibited by the poxvirus crmA gene product

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Requirement of an ICE/CED-3 protease for Fas/APO-1-mediated apoptosis

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Involvement of an ICE-like protease in Fas-mediated apoptosis

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Inhibition of the Caenorhabditis elegans cell-death protease CED-3 by a CED-3 cleavage site in baculovirus p35 protein

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Two CD95 (APO-1/Fas) signaling pathways

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Viral FLICE-inhibitory proteins (FLIPs) prevent apoptosis induced by death receptors

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Inhibition of death receptor signals by cellular FLIP

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I-FLICE, a Novel Inhibitor of Tumor Necrosis Factor Receptor-1- and CD-95-induced Apoptosis

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Casper is a FADD- and caspase-related inducer of apoptosis

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CASH, a novel caspase homologue with death effector domains

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MRIT, a novel death-effector domain-containing protein, interacts with caspases and BclXL and initiates cell death

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CLARP, a death effector domain-containing protein interacts with caspase-8 and regulates apoptosis

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The role of c-FLIP in modulation of CD95-induced apoptosis

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Requirement for Casper (c-FLIP) in regulation of death receptor-induced apoptosis and embryonic development

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Immune escape of tumors in vivo by expression of cellular FLICE-inhibitory protein

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The inhibitor of death receptor signaling, FLICE-inhibitory protein defines a new class of tumor progression factors

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Biochemical mechanisms of IL-2-regulated Fas-mediated T cell apoptosis

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Autoimmunity as a consequence of retrovirus-mediated expression of C-FLIP in lymphocytes

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Up-regulation of c-FLIPshort and reduction of activation-induced cell death in CD28-costimulated human T cells.

1 reference

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FLICE is predominantly expressed as two functionally active isoforms, caspase-8/a and caspase-8/b.

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Monoclonal antibody-mediated tumor regression by induction of apoptosis.

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Tumoricidal activity of tumor necrosis factor-related apoptosis-inducing ligand in vivo.

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Regulation of death receptor-mediated apoptosis pathways

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An induced proximity model for caspase-8 activation.

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Activation of the NF-kappaB pathway by caspase 8 and its homologs

1 reference

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Modulation of the NF-kappa B pathway by virally encoded death effector domains-containing proteins

1 reference

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The caspase-8 inhibitor FLIP promotes activation of NF-kappaB and Erk signaling pathways

1 reference

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Inhibition of death receptor-mediated gene induction by a cycloheximide-sensitive factor occurs at the level of or upstream of Fas-associated death domain protein (FADD)

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Identifiers

10.1074/JBC.M101780200

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Consolidated OpenCitations Corpus – April 2017

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OpenCitations bibliographic resource ID

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Consolidated OpenCitations Corpus – April 2017

OpenCitations bibliographic resource ID

PubMed publication ID

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Consolidated OpenCitations Corpus – April 2017

OpenCitations bibliographic resource ID

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