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Phe(303) in TMVI of the alpha(1B)-adrenergic receptor is a key residue coupling TM helical movements to G-protein activation.
Chen S, Lin F, Xu M, Graham RM. Chen S, et al. Biochemistry. 2002 Jan 15;41(2):588-96. doi: 10.1021/bi011868k. Biochemistry. 2002. PMID: 11781098
We showed previously that Phe(303) in transmembrane segment (TM) VI of the alpha(1B)-adrenergic receptor, a highly conserved residue in G-protein-coupled receptors (GPCRs), is critically involved in receptor-activation and G-protein-coupling [Chen, S. H., Lin, F., X …
We showed previously that Phe(303) in transmembrane segment (TM) VI of the alpha(1B)-adrenergic receptor, a highly conserved residue in G-pr …
RACK1 regulates specific functions of Gbetagamma.
Chen S, Dell EJ, Lin F, Sai J, Hamm HE. Chen S, et al. J Biol Chem. 2004 Apr 23;279(17):17861-8. doi: 10.1074/jbc.M313727200. Epub 2004 Feb 12. J Biol Chem. 2004. PMID: 14963031 Free article.
RACK1 binds to a signal transfer region of G betagamma and inhibits phospholipase C beta2 activation.
Chen S, Lin F, Hamm HE. Chen S, et al. J Biol Chem. 2005 Sep 30;280(39):33445-52. doi: 10.1074/jbc.M505422200. Epub 2005 Jul 28. J Biol Chem. 2005. PMID: 16051595 Free article.
Receptor for Activated C Kinase 1 (RACK1), a novel G betagamma-interacting protein, selectively inhibits the activation of a subclass of G betagamma effectors such as phospholipase C beta2 (PLCbeta2) and adenylyl cyclase II by direct binding to G betagamma (Chen, S. …
Receptor for Activated C Kinase 1 (RACK1), a novel G betagamma-interacting protein, selectively inhibits the activation of a subclass of G b …
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