The G protein-coupled receptor proteolytic site (GPS) autoproteolysis in EGF-TM7 receptors is modulated by N-glycosylation
碩士 === 長庚大學 === 基礎醫學研究所 === 95 === The LNB-TM7 molecules belong to a subfamily of class B G protein-coupled receptor (GPCR) and are characterized by a novel hybrid structure that contains a long N-terminal extracellular domain connected to a 7TM domain by a mucin-like spacer. Based upon their unique...
Main Authors: | Cheng-Chih Hsiao, 蕭丞志 |
---|---|
Other Authors: | Hsi-Hsien Lin |
Format: | Others |
Language: | en_US |
Published: |
2007
|
Online Access: | http://ndltd.ncl.edu.tw/handle/47977631878230498867 |
Similar Items
-
Structural Analysis of GPS autoproteolysis of LNB-TM7 receptors – Characterization of the interaction between the extracellular α-subunit and the 7TM β-subunit
by: Yi-Shu Huang, et al.
Published: (2007) -
Functional characteristics of EGF-TM7 receptors
by: Davies, John Q.
Published: (2005) -
Epidermal growth factor seven transmembrane (EGF-TM7) receptors in myleloid biology
by: Siu, Willie Omar
Published: (2009) -
The physiological role of autoproteolysis of the Adhesion GPCR Latrophilin/dCIRL
by: Nieberler, Matthias
Published: (2019) -
The heparin-binding domain of HB-EGF mediates localization to sites of cell-cell contact and prevents HB-EGF proteolytic release
by: Prince, Robin N., et al.
Published: (2012)