Literature DB >> 21207148

Structural analyses of death domains and their interactions.

Hyun Ho Park1.   

Abstract

The death domain (DD), which is a versatile protein interaction module, is the prime mediator of the interactions necessary for apoptosis, innate immunity and the necrosis signaling pathway. Because DD mediated signaling events are associated with critical human diseases, studies in these areas are of great biological importance. Accordingly, many biochemical and structural studies of DD have been conducted in the past decade to investigate apoptotic and innate immune signaling. Evaluation of the molecular structure of DD and their interactions with partners have shown the underlying molecular basis for the assembly of DD mediated complexes and for the regulation of apoptosis and innate immunity. This review summarizes the structure and function of various DDs and DD:DD complexes involved in those signaling pathways.

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Year:  2011        PMID: 21207148     DOI: 10.1007/s10495-010-0571-z

Source DB:  PubMed          Journal:  Apoptosis        ISSN: 1360-8185            Impact factor:   4.677


  35 in total

1.  Crystallization and preliminary X-ray crystallographic studies of the PYD domain of human NALP3.

Authors:  Ju Young Bae; Hyun Ho Park
Journal:  Acta Crystallogr Sect F Struct Biol Cryst Commun       Date:  2011-10-27

2.  The emerging role of matrix metalloproteases of the ADAM family in male germ cell apoptosis.

Authors:  Ricardo D Moreno; Paulina Urriola-Muñoz; Raúl Lagos-Cabré
Journal:  Spermatogenesis       Date:  2011-07-01

3.  Expression, crystallization and preliminary X-ray crystallographic studies of SCP3 coiled-coil domain.

Authors:  Eun Kyoung Seo; Tae Woo Kim; Hyun Ho Park
Journal:  Acta Crystallogr Sect F Struct Biol Cryst Commun       Date:  2013-10-30

4.  Crystal structure of NALP3 protein pyrin domain (PYD) and its implications in inflammasome assembly.

Authors:  Ju Young Bae; Hyun Ho Park
Journal:  J Biol Chem       Date:  2011-08-31       Impact factor: 5.157

5.  Crystallization and preliminary X-ray crystallographic analysis of the CARD domain of apoptosis repressor with CARD (ARC).

Authors:  Seong Hyun Kim; Hyun Ho Park
Journal:  Acta Crystallogr F Struct Biol Commun       Date:  2015-01-01       Impact factor: 1.056

6.  Identification and analysis of dominant negative mutants of RIP1 DD that disrupt RIPoptosome core formation.

Authors:  Hyun Ji Ha; Hyun Ho Park
Journal:  Mol Biol Rep       Date:  2018-08-23       Impact factor: 2.316

7.  Crystallization and preliminary X-ray crystallographic studies of cPOP1.

Authors:  Kyung Hoon Do; Hyun Ho Park
Journal:  Acta Crystallogr Sect F Struct Biol Cryst Commun       Date:  2013-02-23

8.  Purification, crystallization and preliminary X-ray crystallographic studies of Drep2 CIDE domain.

Authors:  Seung Mi Lee; Hyun Ho Park
Journal:  Acta Crystallogr F Struct Biol Commun       Date:  2014-09-25       Impact factor: 1.056

9.  Insulin-like growth factor binding protein-3 (IGFBP-3): Novel ligands mediate unexpected functions.

Authors:  Robert C Baxter
Journal:  J Cell Commun Signal       Date:  2013-08       Impact factor: 5.782

10.  Crystallization and preliminary X-ray crystallographic studies of the CIDE-N domain of CIDE-3.

Authors:  Seung Mi Lee; Hyun Ho Park
Journal:  Acta Crystallogr Sect F Struct Biol Cryst Commun       Date:  2013-10-30
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