Constitutive dimerization of human serotonin 5-HT4 receptors in living cells (Q33292564)

25 July 2017

title

Constitutive dimerization of human serotonin 5-HT4 receptors in living cells (English)

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25 July 2017

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Rodolphe Fischmeister

6

Rodolphe Fischmeister

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Frank Lezoualc'h

9

Frank Lezoualc'h

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Isabelle Berque-Bestel

7

Isabelle Berque-Bestel

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Magali Berthouze

1

Magali Berthouze

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Sames Sicsic

5

Sames Sicsic

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Charlotte Olivier

3

Olivier Russo

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Lucie Rivail

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Ralf Jockers

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Mohammed Ayoub

2

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25 July 2017

language of work or name

English

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publication date

1 June 2005

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25 July 2017

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25 July 2017

volume

579

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25 July 2017

issue

14

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page(s)

2973-2980

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Molecular, pharmacological and functional diversity of 5-HT receptors

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cites work

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Serotonin receptors represent highly favorable molecular targets for cognitive enhancement in schizophrenia and other disorders

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Structure of the human serotonin 5-HT4 receptor gene and cloning of a novel 5-HT4 splice variant

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Isolation of the serotoninergic 5-HT4(e) receptor from human heart and comparative analysis of its pharmacological profile in C6-glial and CHO cell lines

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Pharmacological characterization of the human 5-HT(4(d)) receptor splice variant stably expressed in Chinese hamster ovary cells

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Characterization of human 5-HT4(d) receptor desensitization in CHO cells

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Differences in signal transduction of two 5-HT4 receptor splice variants: compound specificity and dual coupling with Galphas- and Galphai/o-proteins

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Roles of G-protein-coupled receptor dimerization

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G-protein-coupled receptor heterodimerization modulates receptor function

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GABA(B) receptors function as a heteromeric assembly of the subunits GABA(B)R1 and GABA(B)R2.

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Cloning, expression, and pharmacology of four human 5-hydroxytryptamine 4 receptor isoforms produced by alternative splicing in the carboxyl terminus

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Quantitative mRNA analysis of five C-terminal splice variants of the human 5-HT4 receptor in the central nervous system by TaqMan real time RT-PCR.

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Monitoring of ligand-independent dimerization and ligand-induced conformational changes of melatonin receptors in living cells by bioluminescence resonance energy transfer

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A bioluminescence resonance energy transfer (BRET) system: application to interacting circadian clock proteins

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Activation of the Leptin Receptor by a Ligand-induced Conformational Change of Constitutive Receptor Dimers

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New sorting nexin (SNX27) and NHERF specifically interact with the 5-HT4a receptor splice variant: roles in receptor targeting

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The fourth transmembrane segment forms the interface of the dopamine D2 receptor homodimer.

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C5a receptor oligomerization. I. Disulfide trapping reveals oligomers and potential contact surfaces in a G protein-coupled receptor

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G-protein-coupled receptor dimerization: modulation of receptor function.

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SL65.0155, a novel 5-hydroxytryptamine(4) receptor partial agonist with potent cognition-enhancing properties

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Identifiers

DOI

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25 July 2017

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