Literature DB >> 23100161

PYRIN domains and their interactions in the apoptosis and inflammation signaling pathway.

Hyun Ho Park1.   

Abstract

The PYRIN domain (PYD) is a well known protein interaction module and a prime mediator of the protein interactions necessary for apoptosis, inflammation and innate immune signaling pathway. Because PYD-mediated apoptosis, inflammation and innate immune processes are associated with many human diseases, studies in these areas are of great biological importance. Intensive biochemical and structural studies of PYD have been conducted in the past decade to elucidate PYD-mediated signaling events, and evaluations of the molecular structure of PYDs have shown the underlying molecular basis for the assembly of PYD-mediated complexes and for the regulation of inflammation and innate immunity. This review summarizes the structure and function of various PYDs and proposes a PYD:PYD interaction for assembly of the complexes involved in those signaling pathways.

Entities:  

Mesh:

Substances:

Year:  2012        PMID: 23100161     DOI: 10.1007/s10495-012-0775-5

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


  15 in total

1.  ASC Pyrin Domain Self-associates and Binds NLRP3 Protein Using Equivalent Binding Interfaces.

Authors:  Javier Oroz; Susana Barrera-Vilarmau; Carlos Alfonso; Germán Rivas; Eva de Alba
Journal:  J Biol Chem       Date:  2016-07-18       Impact factor: 5.157

2.  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

3.  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

4.  Structural mechanism of DNA recognition by the p202 HINa domain: insights into the inhibition of Aim2-mediated inflammatory signalling.

Authors:  He Li; Jue Wang; Jie Wang; Lu-Sha Cao; Zhi-Xin Wang; Jia-Wei Wu
Journal:  Acta Crystallogr F Struct Biol Commun       Date:  2013-12-24       Impact factor: 1.056

Review 5.  Immune sensing of DNA.

Authors:  Søren R Paludan; Andrew G Bowie
Journal:  Immunity       Date:  2013-05-23       Impact factor: 31.745

6.  Crystal structure of caspase recruiting domain (CARD) of apoptosis repressor with CARD (ARC) and its implication in inhibition of apoptosis.

Authors:  Tae-ho Jang; Seong Hyun Kim; Jae-Hee Jeong; Sunghwan Kim; Yeon-Gil Kim; Yeun Gil Kim; Hyun Ho Park
Journal:  Sci Rep       Date:  2015-06-03       Impact factor: 4.379

7.  Structural study of the RIPoptosome core reveals a helical assembly for kinase recruitment.

Authors:  Tae-ho Jang; Chao Zheng; Jixi Li; Claire Richards; Yu-Shan Hsiao; Thomas Walz; Hao Wu; Hyun Ho Park
Journal:  Biochemistry       Date:  2014-08-13       Impact factor: 3.162

Review 8.  On the Quest of Cellular Functions of PEA-15 and the Therapeutic Opportunities.

Authors:  Yufeng Wei
Journal:  Pharmaceuticals (Basel)       Date:  2015-07-31

9.  Structures of the NLRP14 pyrin domain reveal a conformational switch mechanism regulating its molecular interactions.

Authors:  Clarissa Eibl; Manuel Hessenberger; Julia Wenger; Hans Brandstetter
Journal:  Acta Crystallogr D Biol Crystallogr       Date:  2014-06-29

10.  PIDD mediates and stabilizes the interaction between RAIDD and caspase-2 for the PIDDosome assembly.

Authors:  Tae-ho Jang; Hyun Ho Park
Journal:  BMB Rep       Date:  2013-09       Impact factor: 4.778

View more

北京卡尤迪生物科技股份有限公司 © 2022-2023.