Cargando…
Internalization Dissociates β(2)-Adrenergic Receptors
G protein-coupled receptors (GPCRs) self-associate as dimers or higher-order oligomers in living cells. The stability of associated GPCRs has not been extensively studied, but it is generally thought that these receptors move between the plasma membrane and intracellular compartments as intact dimer...
Autores principales: | Lan, Tien-Hung, Kuravi, Sudhakiranmayi, Lambert, Nevin A. |
---|---|
Formato: | Texto |
Lenguaje: | English |
Publicado: |
Public Library of Science
2011
|
Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3043075/ https://www.ncbi.nlm.nih.gov/pubmed/21364942 http://dx.doi.org/10.1371/journal.pone.0017361 |
Ejemplares similares
-
BRET evidence that β2 adrenergic receptors do not oligomerize in cells
por: Lan, Tien-Hung, et al.
Publicado: (2015) -
Molecular Basis of Ligand Dissociation in β-Adrenergic Receptors
por: González, Angel, et al.
Publicado: (2011) -
Agonist binding by the β(2)-adrenergic receptor: an effect of receptor conformation on ligand association–dissociation characteristics
por: Plazinska, Anita, et al.
Publicado: (2015) -
Cardiac β(2)-Adrenergic Receptor Phosphorylation at Ser(355/356) Regulates Receptor Internalization and Functional Resensitization
por: Fan, Xiaofang, et al.
Publicado: (2016) -
Muscle Plasticity and
β(2)-Adrenergic
Receptors: Adaptive Responses of
β(2)-Adrenergic
Receptor Expression to Muscle Hypertrophy and
Atrophy
por: Sato, Shogo, et al.
Publicado: (2011)