Oligomerization of the alpha 1a- and alpha 1b-adrenergic receptor subtypes. Potential implications in receptor internalization.
about
Nuclear localization drives α1-adrenergic receptor oligomerization and signaling in cardiac myocytesMetabolon disruption: a mechanism that regulates bicarbonate transportHeteromerization of G protein-coupled receptors: relevance to neurological disorders and neurotherapeutics.Allostery at G protein-coupled receptor homo- and heteromers: uncharted pharmacological landscapesThe active metabolite of Clopidogrel disrupts P2Y12 receptor oligomers and partitions them out of lipid raftsFunctional characterization of G-protein-coupled receptors: a bioinformatics approach.Increasingly accurate dynamic molecular models of G-protein coupled receptor oligomers: Panacea or Pandora's box for novel drug discovery?Interrelation of dopamine transporter oligomerization and surface presence as studied with mutant transporter proteins and amphetamine.Cell surface expression of alpha1D-adrenergic receptors is controlled by heterodimerization with alpha1B-adrenergic receptors.Monitoring the formation of dynamic G-protein-coupled receptor-protein complexes in living cells.Chemokine (C-X-C motif) receptor 4 and atypical chemokine receptor 3 regulate vascular α₁-adrenergic receptor function.The G protein-coupled receptor rhodopsin in the native membraneThe α1-adrenergic receptors: diversity of signaling networks and regulationFRET imaging reveals that functional neurokinin-1 receptors are monomeric and reside in membrane microdomains of live cells.Identification of the alpha1L-adrenoceptor in rat cerebral cortex and possible relationship between alpha1L- and alpha1A-adrenoceptorsNuclear alpha1-adrenergic receptors signal activated ERK localization to caveolae in adult cardiac myocytesMuscarinic acetylcholine receptor M3 modulates odorant receptor activity via inhibition of β-arrestin-2 recruitment.Heteromerization of chemokine (C-X-C motif) receptor 4 with α1A/B-adrenergic receptors controls α1-adrenergic receptor function.Computational methods in drug design: modeling G protein-coupled receptor monomers, dimers, and oligomersRoles of G-protein-coupled receptor dimerization.Protein-protein interactions at the adrenergic receptors.Neuron specific alpha-adrenergic receptor expression in human cerebellum: implications for emerging cerebellar roles in neurologic diseaseRecent progress in alpha1-adrenergic receptor research.α₁A-adrenergic receptors regulate cardiac hypertrophy in vivo through interleukin-6 secretion.Cross-desensitization and cointernalization of H1 and H2 histamine receptors reveal new insights into histamine signal integration.GATA4 is a survival factor in adult cardiac myocytes but is not required for alpha1A-adrenergic receptor survival signalingA day in the life of a G protein-coupled receptor: the contribution to function of G protein-coupled receptor dimerization.New Insights into Mechanisms and Functions of Chemokine (C-X-C Motif) Receptor 4 Heteromerization in Vascular Smooth Muscle.Substrates dissociate dopamine transporter oligomers.Characterization of relaxin receptor (RXFP1) desensitization and internalization in primary human decidual cells and RXFP1-transfected HEK293 cellsComplement factor 5a receptor chimeras reveal the importance of lipid-facing residues in transport competence.The alpha 1B/D-adrenoceptor knockout mouse permits isolation of the vascular alpha 1A-adrenoceptor and elucidates its relationship to the other subtypes.Heterodimerisation of G protein-coupled receptors: implications for drug design and ligand screening.Pathophysiology of GPCR Homo- and Heterodimerization: Special Emphasis on Somatostatin ReceptorsCD4 and CCR5 constitutively interact at the plasma membrane of living cells: a confocal fluorescence resonance energy transfer-based approach.Studies on the role of the receptor protein motifs possibly involved in electrostatic interactions on the dopamine D1 and D2 receptor oligomerization.Inhibition of serotonin 5-hydroxytryptamine2c receptor function through heterodimerization: receptor dimers bind two molecules of ligand and one G-protein.Coupling of GABAB receptor GABAB2 subunit to G proteins: evidence from Xenopus oocyte and baby hamster kidney cell expression system.G protein activation by the leukotriene B4 receptor dimer. Evidence for an absence of trans-activation.CD8+ cytotoxic T lymphocyte activation by soluble major histocompatibility complex-peptide dimers.
P2860
Q24298471-7C082A87-D172-49DB-BF73-CAD6D97A67EFQ24306515-8934A395-2203-4330-9C1B-59A4001C90B3Q24630645-774EE320-5DA1-4F5E-B108-C26313E7B335Q24633877-D2EA678E-7317-4E73-8E25-D33A901F4375Q24675155-0B92BE91-49EE-49BE-A9A2-02EB56E86B59Q30009384-4FA138D5-3597-47B5-929F-F68988BCB5C3Q33767121-F36FDA8B-8011-4AAB-AB58-C6F19499DB28Q34020736-590C7A2C-40AF-48CE-8802-75D363532BDEQ34291539-3635F52A-4365-431B-A659-8D1A7D64F3C5Q34361815-DC6BBBC0-D5E0-4CD7-B09D-3246EA3D3111Q34416235-EA85AE45-1817-4C25-AB79-821C7742B586Q34432609-F90D962D-4E9D-4547-8DBB-63BA9376B577Q34476637-8C2528C3-5D71-433B-9865-6B18CB92DEBCQ34478976-95BC0916-4FE9-488E-85CC-EBAE94670E42Q34655702-DB8606E8-88D6-4155-B40D-AF5B0C6CA696Q34831078-819317C1-8AD4-45C3-80DA-865AF636A747Q35214958-A001E457-0965-42F0-AC44-1D75BB45AAF7Q35279688-74829F9C-F7D8-4FA8-B317-773BD61AF57FQ35594835-00A767CC-8512-47A5-932D-C1AA3E4C094DQ35622424-2C0DD5A3-BC10-4416-843B-910D37CE9B47Q35791490-27E468A3-AAB9-47E3-B455-CF68CE42BEB6Q36236288-26D46B5E-1C1A-4C3C-9D5E-4A7725191D0BQ36286458-84E83F11-CA94-443C-9701-0D4894523A88Q36776721-3DCF2A48-42CF-4DC1-B194-E668808D7486Q36776746-A1D86E8F-12ED-412F-8372-2BBDF781E9A6Q36844666-0A75748C-7508-408D-85CC-D79C718B82EAQ36983708-1F240C85-A06F-4966-AC0B-91DA72BE7753Q37050877-5A27E0C1-D57B-4C55-B318-915759E9CBC3Q37051785-DF699206-C5E2-49FD-8780-910F4EB77115Q37165951-BB3C9773-77DC-419C-A4C2-6740417327D6Q37354853-7A670CEA-19DB-4DA4-BA8C-7FD4CD53BCE6Q37481315-E2AE5BBD-7439-4C79-B9DF-07BC8F5326CEQ38028547-6ED500E6-221A-4014-92B7-316BC333126FQ38166623-F5AB46A5-8B17-407C-A4B0-D7385DC94942Q39015489-89D519A9-44F1-47BB-8F53-62DE5A98E148Q39895376-712A8E73-8495-4745-9430-F57B5CECD0B0Q40367280-01D2F31D-83C5-41C3-B582-9282C3BFB0E4Q40381689-9B8DAB34-1257-4786-8DB0-51DD2158385CQ40422401-62E2CFA1-8FC1-47A9-8955-0CCD56172893Q40439959-1389A557-E9D0-4680-85CD-670D18A87FB6
P2860
Oligomerization of the alpha 1a- and alpha 1b-adrenergic receptor subtypes. Potential implications in receptor internalization.
description
2003 nî lūn-bûn
@nan
2003年の論文
@ja
2003年学术文章
@wuu
2003年学术文章
@zh
2003年学术文章
@zh-cn
2003年学术文章
@zh-hans
2003年学术文章
@zh-my
2003年学术文章
@zh-sg
2003年學術文章
@yue
2003年學術文章
@zh-hant
name
Oligomerization of the alpha 1 ...... s in receptor internalization.
@en
Oligomerization of the alpha 1 ...... s in receptor internalization.
@nl
type
label
Oligomerization of the alpha 1 ...... s in receptor internalization.
@en
Oligomerization of the alpha 1 ...... s in receptor internalization.
@nl
prefLabel
Oligomerization of the alpha 1 ...... s in receptor internalization.
@en
Oligomerization of the alpha 1 ...... s in receptor internalization.
@nl
P2093
P2860
P356
P1476
Oligomerization of the alpha 1 ...... s in receptor internalization.
@en
P2093
Horst Vogel
Jean-Baptiste Perez
Laura Stanasila
Susanna Cotecchia
P2860
P304
40239-40251
P356
10.1074/JBC.M306085200
P407
P577
2003-07-29T00:00:00Z