Literature DB >> 14634625

The death effector domain protein family.

Bryan C Barnhart1, Justine C Lee, Elizabeth C Alappat, Marcus E Peter.   

Abstract

Apoptosis signaling is regulated and executed by specialized proteins that often carry protein/protein interaction domains. One of these domains is the death effector domain (DED) that is predominantly found in components of the death-inducing signaling complex, which forms at the members of the death receptor family following their ligation. Both proapoptotic- and antiapoptotic-DED-containing proteins have been identified, which makes these proteins exquisitely suited to the regulation of apoptosis. Aside from their pivotal role in the control of the apoptotic program, DED-containing proteins have recently been demonstrated to exert their influence on other cellular processes as well, including cell proliferation. These data highlight the multiple roles for the members of this family, suggesting that they are suited to control both life and death decisions of cells. Additionally, because they can act proapoptotically, antiapoptotically, or in the regulation of the cell cycle, this family of proteins may be excellent candidates for cancer therapy targets. Oncogene (2003) 22, 8634-8644. doi:10.1038/sj.onc.1207103

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Year:  2003        PMID: 14634625     DOI: 10.1038/sj.onc.1207103

Source DB:  PubMed          Journal:  Oncogene        ISSN: 0950-9232            Impact factor:   9.867


  27 in total

1.  The death effector domain protein PEA-15 negatively regulates T-cell receptor signaling.

Authors:  Sandra Pastorino; Hemamalini Renganathan; Maisel J Caliva; Erin L Filbert; John Opoku-Ansah; Florian J Sulzmaier; Joanna E Gawecka; Guy Werlen; Andrey S Shaw; Joe W Ramos
Journal:  FASEB J       Date:  2010-03-30       Impact factor: 5.191

2.  The MC160 protein expressed by the dermatotropic poxvirus molluscum contagiosum virus prevents tumor necrosis factor alpha-induced NF-kappaB activation via inhibition of I kappa kinase complex formation.

Authors:  Daniel Brian Nichols; Joanna L Shisler
Journal:  J Virol       Date:  2006-01       Impact factor: 5.103

3.  Crystal structure at 2.8 A of Huntingtin-interacting protein 1 (HIP1) coiled-coil domain reveals a charged surface suitable for HIP1 protein interactor (HIPPI).

Authors:  Qian Niu; Joel A Ybe
Journal:  J Mol Biol       Date:  2007-11-22       Impact factor: 5.469

Review 4.  Regulation of cell survival and death during Flavivirus infections.

Authors:  Sounak Ghosh Roy; Beata Sadigh; Emmanuel Datan; Richard A Lockshin; Zahra Zakeri
Journal:  World J Biol Chem       Date:  2014-05-26

5.  Identification and characterization of DEDDL, a human-specific isoform of DEDD.

Authors:  Xin Huang; Minghui Zhang; Hua Tang; Chunfang Ruo; Xuetao Cao
Journal:  Gene Expr       Date:  2006

6.  Cloning, expression, purification, crystallization and preliminary crystallographic analysis of pseudo death-effector domain of HIPPI, a molecular partner of Huntingtin-interacting protein HIP-1.

Authors:  Manisha Banerjee; Pritha Majumder; Nitai P Bhattacharyya; Jiban K Dattagupta; Udayaditya Sen
Journal:  Acta Crystallogr Sect F Struct Biol Cryst Commun       Date:  2006-11-30

Review 7.  Polygenic susceptibility to breast cancer: current state-of-the-art.

Authors:  Maya Ghoussaini; Paul D P Pharoah
Journal:  Future Oncol       Date:  2009-06       Impact factor: 3.404

8.  Evasion of apoptosis as a cellular stress response in cancer.

Authors:  Simone Fulda
Journal:  Int J Cell Biol       Date:  2010-02-18

9.  Paclitaxel promotes a caspase 8-mediated apoptosis through death effector domain association with microtubules.

Authors:  A Mielgo; V A Torres; K Clair; S Barbero; D G Stupack
Journal:  Oncogene       Date:  2009-08-10       Impact factor: 9.867

10.  Differential regulation of the TRAIL death receptors DR4 and DR5 by the signal recognition particle.

Authors:  Yan-Guo Ren; Klaus W Wagner; Deborah A Knee; Pedro Aza-Blanc; Marc Nasoff; Quinn L Deveraux
Journal:  Mol Biol Cell       Date:  2004-09-08       Impact factor: 4.138

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