Two transmembrane Cys residues are involved in 5-HT4 receptor dimerization
- 1 May 2007
- journal article
- Published by Elsevier in Biochemical and Biophysical Research Communications
- Vol. 356 (3) , 642-647
- https://doi.org/10.1016/j.bbrc.2007.03.030
Abstract
No abstract availableKeywords
This publication has 26 references indexed in Scilit:
- Constitutive dimerization of human serotonin 5‐HT4 receptors in living cellsFEBS Letters, 2005
- Functional studies of the 5′-untranslated region of human 5-HT4 receptor mRNABiochemical Journal, 2005
- Emerging role of homo- and heterodimerization in G-protein-coupled receptor biosynthesis and maturationTrends in Pharmacological Sciences, 2005
- New Insights into Serotonin 5-HT4 Receptors : A Novel Therapeutic Target for Alzheimers Disease?Current Alzheimer Research, 2004
- 5-HT4 ReceptorsCurrent Drug Targets-CNS & Neurological Disorders, 2004
- Heterodimerization of α2A- and β1-Adrenergic ReceptorsJournal of Biological Chemistry, 2003
- The Fourth Transmembrane Segment Forms the Interface of the Dopamine D2 Receptor HomodimerJournal of Biological Chemistry, 2003
- 5-HT4Receptor Ligands: Applications and New ProspectsJournal of Medicinal Chemistry, 2003
- Structural models for dimerization of G‐protein coupled receptors: The opioid receptor homodimersPeptide Science, 2002
- Involvement of the Amino Terminus of the B2 Receptor in Agonist-induced Receptor DimerizationJournal of Biological Chemistry, 1999