Human beta 2-adrenergic receptors expressed in Escherichia coli membranes retain their pharmacological properties.
about
Large-scale production and protein engineering of G protein-coupled receptors for structural studiesMembrane topology of the DrrB protein of the doxorubicin transporter of Streptomyces peucetiusNonselective coupling of the human mu-opioid receptor to multiple inhibitory G-protein isoformsTuning microbial hosts for membrane protein production.Selective binding of ligands to beta 1, beta 2 or chimeric beta 1/beta 2-adrenergic receptors involves multiple subsites.Mutational analysis of ligand binding activity of beta 2 adrenergic receptor expressed in Escherichia coliMapping of a functional autoimmune epitope on the beta 1-adrenergic receptor in patients with idiopathic dilated cardiomyopathyCloning the mRNA encoding 1-aminocyclopropane-1-carboxylate synthase, the key enzyme for ethylene biosynthesis in plantsTopological analysis of the human beta 2-adrenergic receptor expressed in Escherichia coliAlkaline phosphatase fusions: sensors of subcellular locationSignificance of the carbohydrate moiety of the rat ovarian luteinizing-hormone/chorionic-gonadotropin receptor for ligand-binding specificity and signal transduction.Expression and functional characterization of membrane-integrated mammalian corticotropin releasing factor receptors 1 and 2 in Escherichia coli.High level functional expression of human beta 1-adrenergic receptor in baculovirus-infected cells screened by a rapid in situ procedure.Choice of cellular protein expression system.Membrane targeting and determination of transmembrane topology of the human vasopressin V2 receptor.
P2860
Q26866010-3DDFBE15-1D83-49DE-95A7-B9B790352C63Q28256996-6F77C757-BE9B-4D1C-B256-18FC8A67E123Q28640362-D7C0948E-5D17-4396-912F-BC2A9239A412Q33596003-B73B801E-3B20-4738-8C17-5CF87B83B5E4Q33919600-911EECDB-F515-4BC7-B329-4755ECB465D4Q33921259-519FDBAF-BB38-4EC0-B226-C457674AC94FQ34263678-6B26E2F6-1460-47BD-B7C3-FA5500341077Q34300859-C0634307-0AFB-42A1-AEAC-1309CBB8E1A8Q35860176-12D1CB89-7D50-4986-B5C6-71D95B61BC54Q36157660-0BB2BD1C-B904-463A-9F12-125ED1DC7D77Q38318383-F263126C-212B-43E2-ADF4-8425C2D94758Q41877624-CDBF2554-E000-403F-8423-3E62F2419BE7Q42070602-ADFB484A-2A28-4E79-BCC2-D3D09B66B694Q45966460-BC31B99F-EB9E-41C4-A6ED-39FFD180299DQ54577139-6328D002-B11C-4FA1-81DE-F52CC1C2F032
P2860
Human beta 2-adrenergic receptors expressed in Escherichia coli membranes retain their pharmacological properties.
description
1988 nî lūn-bûn
@nan
1988 թուականի Հոկտեմբերին հրատարակուած գիտական յօդուած
@hyw
1988 թվականի հոտեմբերին հրատարակված գիտական հոդված
@hy
1988年の論文
@ja
1988年学术文章
@wuu
1988年学术文章
@zh-cn
1988年学术文章
@zh-hans
1988年学术文章
@zh-my
1988年学术文章
@zh-sg
1988年學術文章
@yue
name
Human beta 2-adrenergic recept ...... ir pharmacological properties.
@ast
Human beta 2-adrenergic recept ...... ir pharmacological properties.
@en
type
label
Human beta 2-adrenergic recept ...... ir pharmacological properties.
@ast
Human beta 2-adrenergic recept ...... ir pharmacological properties.
@en
prefLabel
Human beta 2-adrenergic recept ...... ir pharmacological properties.
@ast
Human beta 2-adrenergic recept ...... ir pharmacological properties.
@en
P2093
P2860
P356
P1476
Human beta 2-adrenergic recept ...... eir pharmacological properties
@en
P2093
A D Strosberg
C Delavier-Klutchko
P2860
P304
P356
10.1073/PNAS.85.20.7551
P407
P577
1988-10-01T00:00:00Z