N-glycosylation and disulfide bonding affects GPRC6A receptor expression, function, and dimerization-Reference-Cited by-同舟云学术

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N-glycosylation and disulfide bonding affects GPRC6A receptor expression, function, and dimerization

Published:2015-01-21 Issue:5 Volume:589 Page:588-597
ISSN:0014-5793
Container-title:FEBS Letters
language:en
Short-container-title:

Author:

Nørskov-Lauritsen Lenea,Jørgensen Stine,Bräuner-Osborne Hans

Funder

Danish Council for Independent Research

Medical Sciences and the Lundbeck Foundation

Publisher

Wiley

Subject

Cell Biology,Genetics,Molecular Biology,Biochemistry,Structural Biology,Biophysics

Link

http://onlinelibrary.wiley.com/wol1/doi/10.1016/j.febslet.2015.01.019/fullpdf

Reference58 articles.

1. Involvement of the amino terminus of the B(2) receptor in agonist-induced receptor dimerization;AbdAlla;J. Biol. Chem.,1999

2. On the frequency of protein glycosylation, as deduced from analysis of the SWISS-PROT database;Apweiler;Biochim. Biophys. Acta,1999

3. Dimerization of the extracellular calcium-sensing receptor (CaR) on the cell surface of CaR-transfected HEK293 cells;Bai;J. Biol. Chem.,1998

4. Venus fly trap domain of mGluR1 functions as a dominant negative against group I mGluR signaling;Beqollari;J. Neurophysiol.,2010

5. Pharmacological characterization of mouse GPRC6A, an l-alpha-amino-acid receptor modulated by divalent cations;Christiansen;Br. J. Pharmacol.,2007

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