Design and Operation of the GPS Receiver Onboard the CanX-2 Nanosatellite
NAVIGATION-JOURNAL OF THE INSTITUTE OF NAVIGATION
Authors: Kahr, Erin; O'Keefe, Kyle P. G.; Skone, Susan; Bradbury, Laura
Abstract
Among its payloads, the Canadian Advanced Nanospace eXperiment 2 (CanX-2) nanosatellite is carrying a commercial off-the-shelf GPS receiver, which offers advantages in terms of cost, size and power, and overall continues to perform well more than four years after launch. However, at orbital velocity and with low signal power the receiver is unable to acquire a position fix quickly using its standard acquisition algorithm. In order to effectively collect GPS data over short time intervals, the receiver is manually warm started by pre-assigning channels with PRN and Doppler information. Uploading warm start scripts to the satellite allows for reliable acquisition in an average of 3.5 min compared to a cold start of approximately 20 min, and avoids the need for complex onboard warm start capability. The data collection capability has in turn enabled a variety of scientific results to be obtained. Copyright (C) 2013 Institute of Navigation.
Protein disulfide isomerase chaperone ERP-57 decreases plasma membrane expression of the human GnRH receptor
CELL BIOCHEMISTRY AND FUNCTION
Authors: Yanez, Rodrigo Ayala; Conn, P. Michael
Abstract
Retention of misfolded proteins by the endoplasmic reticulum (ER) is a quality control mechanism involving the participation of endogenous chaperones such as calnexin (CANX). CANX interacts with and restricts plasma membrane expression (PME) of the I gonadotropin releasing hormone receptor (GnRHR), a G protein-coupled receptor. CANX also interacts with ERP-57 a thiol oxidoreductase chaperone present in the ER. CANX along with ERP-57 promotes the formation of disulfide bond bridges in nascent proteins. The human GnRH receptor (hGnRHR) is stabilized by two disulfide bond bridges (C-14-C-200 and C-114-C-196), that, when broken, lead to a decrease in receptor expression at the plasma membrane. To determine if the presence of chaperones CANX and ERP-57 exerts an influence over membrane routing and second messenger activation, we assessed the effect of various mutants including those with broken disulfide bridges (Cys -> Ala) along with the hGnRHR. The effect of chaperones on mutants was insignificant, whereas the over expression of ERP-57 led to an hGnRHR retention. This effect was further enhanced by cotransfection with cDNA for CANX showing receptor retention by ERP-57 augmented by CANX, suggesting utilization of these chaperones for quality control of the GnRHR. Copyright (C) 2009 John Wiley & Sons, Ltd.