(Q28215325)

English

Death effector domain-containing proteins DEDD and FLAME-3 form nuclear complexes with the TFIIIC102 subunit of human transcription factor IIIC

scientific article (publication date: April 2002)

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scholarly article

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Death effector domain-containing proteins DEDD and FLAME-3 form nuclear complexes with the TFIIIC102 subunit of human transcription factor IIIC (English)

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author name string

Y Zhan

1

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R Hegde

2

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S M Srinivasula

3

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T Fernandes-Alnemri

4

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E S Alnemri

5

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language of work or name

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publication date

April 2002

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Cell Death & Differentiation

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9

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4

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439-47

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Death receptors: signaling and modulation

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The death domain superfamily: a tale of two interfaces?

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FADD/MORT1 is a common mediator of CD95 (Fas/APO-1) and tumor necrosis factor receptor-induced apoptosis

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Caspase activation: the induced-proximity model

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

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Autoproteolytic activation of pro-caspases by oligomerization.

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Biochemical pathways of caspase activation during apoptosis

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

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The death effector domain of PEA-15 is involved in its regulation of integrin activation

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Death effector domain protein PEA-15 potentiates Ras activation of extracellular signal receptor-activated kinase by an adhesion-independent mechanism

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Regulation of expression of phospholipase D1 and D2 by PEA-15, a novel protein that interacts with them

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PED/PEA-15 gene controls glucose transport and is overexpressed in type 2 diabetes mellitus

1 reference

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DEDD, a novel death effector domain-containing protein, targeted to the nucleolus

1 reference

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Nuclear localization of DEDD leads to caspase-6 activation through its death effector domain and inhibition of RNA polymerase I dependent transcription

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

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

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Activation of NF-kappaB by FADD, Casper, and caspase-8.

1 reference

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Keeping TNF-induced apoptosis under control in astrocytes: PEA-15 as a 'double key' on caspase-dependent and MAP-kinase-dependent pathways.

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DEFT, a novel death effector domain-containing molecule predominantly expressed in testicular germ cells

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Cloning and characterization of two evolutionarily conserved subunits (TFIIIC102 and TFIIIC63) of human TFIIIC and their involvement in functional interactions with TFIIIB and RNA polymerase III

1 reference

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Comparison of the RNA polymerase III transcription machinery in Schizosaccharomyces pombe, Saccharomyces cerevisiae and human

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The RNA polymerase III transcription apparatus

1 reference

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Identification and characterization of DEDD2, a death effector domain-containing protein

1 reference

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Two forms of transcription factor TFIIIC in extracts from HeLa cells

1 reference

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Purification of human transcription factor IIIC and its binding to the gene for ribosomal 5S RNA.

1 reference

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Interaction of BAG-1 with retinoic acid receptor and its inhibition of retinoic acid-induced apoptosis in cancer cells

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FLAME-1, a novel FADD-like anti-apoptotic molecule that regulates Fas/TNFR1-induced apoptosis

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Identification and molecular cloning of two novel receptors for the cytotoxic ligand TRAIL

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CLAP, a novel caspase recruitment domain-containing protein in the tumor necrosis factor receptor pathway, regulates NF-kappaB activation and apoptosis

1 reference

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Molecular determinants of NF-kappaB-inducing kinase action

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Self-association of the Death Domains of the p55 Tumor Necrosis Factor (TNF) Receptor and Fas/APO1 Prompts Signaling for TNF and Fas/APO1 Effects

1 reference

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7 January 2021

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Identifiers

10.1038/SJ.CDD.4401038

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Springer Nature article ID

10.1038/sj.cdd.4401038

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