(Q24338580)

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Hetero-oligomerization between beta2- and beta3-adrenergic receptors generates a beta-adrenergic signaling unit with distinct functional properties

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scholarly article

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Hetero-oligomerization between beta2- and beta3-adrenergic receptors generates a beta-adrenergic signaling unit with distinct functional properties (English)

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Adrenoceptor beta 2

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GOA release 2020-03-11

Adrenoceptor beta 3

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GOA release 2020-03-11

norepinephrine binding

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GOA release 2020-03-11

object named as

Michel Bouvier

3

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author name string

Andreas Breit

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Monique Lagacé

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language of work or name

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publication date

2 July 2004

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Journal of Biological Chemistry

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279

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28756-65

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27

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beta-adrenergic modulation of maxi-K channels in vascular smooth muscle via Gi through a membrane-delimited pathway

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Internalization of β-adrenergic receptor binding sites: Involvements of lysosomal enzymes

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Coexistence of three β-adrenoceptor subtypes in white fat cells of various mammalian species

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Transfection of DHFR- and DHFR+ mammalian cells using methotrexate-resistant mutants of mouse dihydrofolate reductase

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Heterodimerization of G-protein-coupled receptors: pharmacology, signaling and trafficking

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Dimerization and domain swapping in G-protein-coupled receptors: a computational study

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Functional significance of oligomerization of G-protein-coupled receptors.

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G-protein-coupled receptor heterodimerization modulates receptor function

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Detection of beta 2-adrenergic receptor dimerization in living cells using bioluminescence resonance energy transfer (BRET)

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A peptide derived from a beta2-adrenergic receptor transmembrane domain inhibits both receptor dimerization and activation.

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10.1074/JBC.M313310200

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