Structural analyses of death domains and their interactions

Title
Structural analyses of death domains and their interactions
Author(s)
박현호
Keywords
NF-KAPPA-B; 1-ASSOCIATED PROTEIN TRADD; FADD-DEPENDENT APOPTOSIS; INDUCED-PROXIMITY MODEL; TRAIL RECEPTORS 1; TNF RECEPTOR; SIGNAL-TRANSDUCTION; CELL-DEATH; CRYSTAL-STRUCTURE; ADAPTER MOLECULE
Issue Date
201103
Publisher
SPRINGER
Citation
APOPTOSIS, v.16, no.3, pp.209 - 220
Abstract
The death domain (DD), which is a versatle 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.
URI
http://hdl.handle.net/YU.REPOSITORY/25561http://dx.doi.org/10.1007/s10495-010-0571-z
ISSN
1360-8185
Appears in Collections:
이과대학 > 화학생화학부 > Articles
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