Detailed Information

Cited 4 time in webofscience Cited 3 time in scopus
Metadata Downloads

Molecular basis of dimerization of initiator caspase was revealed by crystal structure of caspase-8 pro-domain

Authors
Park, H.H.
Issue Date
Jul-2019
Publisher
Nature Publishing Group
Citation
Cell Death and Differentiation, v.26, no.7, pp 1213 - 1220
Pages
8
Journal Title
Cell Death and Differentiation
Volume
26
Number
7
Start Page
1213
End Page
1220
URI
https://scholarworks.bwise.kr/cau/handle/2019.sw.cau/3328
DOI
10.1038/s41418-018-0200-x
ISSN
1350-9047
1476-5403
Abstract
The assembly of death-inducing signaling complex (DISC) for activation of initiator caspase is a key step for the receptor-mediated apoptosis signaling. Many death effector domain (DED)-containing proteins are involved in DISC assembly and controlling. One of the main DISC component, caspase-8, contains DED and DED-mediated dimerization and oligomerization in the DISC is critical for the activation of this initiator caspase. There have been intensive studies to understand DED-mediated dimerization and oligomerization for the DISC assembly but no clear answer has been provided and there are many controversial arguments. Here, we suggested novel dimerization process of tandem DED of caspase-8 with crystallographic study. © 2018, ADMC Associazione Differenziamento e Morte Cellulare.
Files in This Item
There are no files associated with this item.
Appears in
Collections
Graduate School > ETC > 1. Journal Articles

qrcode

Items in ScholarWorks are protected by copyright, with all rights reserved, unless otherwise indicated.

Related Researcher

Researcher Park, Hyun Ho photo

Park, Hyun Ho
대학원 (글로벌혁신신약학과)
Read more

Altmetrics

Total Views & Downloads

BROWSE