Identification of a ligand-dependent switch within a muscarinic receptor.
about
Flexible modulation of agonist efficacy at the human A3 adenosine receptor by the imidazoquinoline allosteric enhancer LUF6000Molecular bases of defective signal transduction in the platelet P2Y12 receptor of a patient with congenital bleedingStructure and topology of a peptide segment of the 6th transmembrane domain of the Saccharomyces cerevisae alpha-factor receptor in phospholipid bilayersC5a receptor activation. Genetic identification of critical residues in four transmembrane helices.Leu128(3.43) (l128) and Val247(6.40) (V247) of CXCR1 are critical amino acid residues for g protein coupling and receptor activation.Identification of orthosteric and allosteric site mutations in M2 muscarinic acetylcholine receptors that contribute to ligand-selective signaling biasThe muscarinic M(5) receptor: a silent or emerging subtype?Molecular basis of ligand dissociation in β-adrenergic receptorsFRET-based detection of M1 muscarinic acetylcholine receptor activation by orthosteric and allosteric agonists.The cytoplasmic end of transmembrane domain 3 regulates the activity of the Saccharomyces cerevisiae G-protein-coupled alpha-factor receptorConstitutive activity of muscarinic acetylcholine receptors.Activation and dynamic network of the M2 muscarinic receptor.Conserved Mechanism of Conformational Stability and Dynamics in G-Protein-Coupled Receptors.Molecular determinants of allosteric modulation at the M1 muscarinic acetylcholine receptor.On the discovery and development of pimavanserin: a novel drug candidate for Parkinson's psychosis.Gating function of isoleucine-116 in TM-3 (position III:16/3.40) for the activity state of the CC-chemokine receptor 5 (CCR5).Activation of constitutive 5-hydroxytryptamine(1B) receptor by a series of mutations in the BBXXB motif: positioning of the third intracellular loop distal junction and its G(o)alpha protein interactionsMembrane environment imposes unique selection pressures on transmembrane domains of G protein-coupled receptorsPheVI:09 (Phe6.44) as a sliding microswitch in seven-transmembrane (7TM) G protein-coupled receptor activation.Functional importance of the Ala(116)-Pro(136) region in the calcium-sensing receptor. Constitutive activity and inverse agonism in a family C G-protein-coupled receptor.A conserved Asn in transmembrane helix 7 is an on/off switch in the activation of the thyrotropin receptor.Simplified modeling approach suggests structural mechanisms for constitutive activation of the C5a receptor.Evidence for a model of agonist-induced activation of 5-hydroxytryptamine 2A serotonin receptors that involves the disruption of a strong ionic interaction between helices 3 and 6.Transmembrane domains 4 and 7 of the M(1) muscarinic acetylcholine receptor are critical for ligand binding and the receptor activation switch.Activation of muscarinic receptors induces protein synthesis-dependent long-lasting depression in the perirhinal cortex.Control of conformational equilibria in the human B2 bradykinin receptor. Modeling of nonpeptidic ligand action and comparison to the rhodopsin structure.Receptors coupling to G proteins: is there a signal behind the sequence?Mutations remote from the human gonadotropin-releasing hormone (GnRH) receptor-binding sites specifically increase binding affinity for GnRH II but not GnRH I: evidence for ligand-selective, receptor-active conformations.
P2860
Q21262008-543CEB32-8D80-4EAA-9593-FD1188C67F69Q24294523-1EAF998C-AD33-454D-9370-F5D32F9C845BQ24631459-57BB3585-330E-4C6D-88EC-7D614583C676Q30636240-014DA7FD-6CE1-4EF5-BBCB-DA3388913259Q31088115-82AF0F8E-8130-490C-90D9-9DA3D7206D68Q33748133-8213F1E0-C46A-4539-98B4-35412368FA1EQ33898782-BC7DEA96-D670-46F5-A422-BE6FC5BC0EB8Q34018861-F2C18DDB-CB30-4471-A878-F236E9749FE0Q34137423-BE965AC6-A8AE-4640-9F8A-D35D5122BF13Q34614352-CE8DA2AF-B96D-471A-BF25-A2D14A12BBB9Q36440733-51DA5D68-2BA6-4150-94B3-E3C670ECA61AQ36990877-D6028B86-E457-4AD6-8FAD-E601EB117CC5Q37490747-9A6F4B85-001D-44A8-9617-E9B2C7191E2EQ37608542-A8F03F6D-4C2A-4547-985E-91144DD60E62Q38200546-4B7158C1-E96F-41B7-9480-9F62EF0FD52EQ38274861-5E87965A-9F76-4F24-9C37-559AAC898A15Q42035013-A8BCD97E-98A0-43D8-926C-E9863CBB2D5CQ42146149-37F8EC3B-73D3-4454-9F15-42167D74D63DQ42425022-E6EBC02F-8FA2-49C9-A507-77249E9CD9F1Q42488693-76959E4A-DF0D-4516-AB88-9550AA731163Q42503124-63D2503B-364A-4354-A559-41B8BCE0F1FEQ42712396-1FC1785D-0432-4FCC-9F69-E7D654065342Q42819583-4DDC641A-F52B-499A-ADAA-EDC49956EF54Q43664677-A1DF793B-58A0-48AD-9079-DFCD3941FCFCQ43698145-C000B75B-F1E0-4631-894D-8DADEE809ED9Q43701636-6DE7C557-0AAB-41EF-88C0-5DFEB70F0D3FQ52072064-AA07B804-8D85-4EC4-B072-B7AAC7F78C50Q52564801-AF1425FD-73CA-4AD3-A750-6454D95D024B
P2860
Identification of a ligand-dependent switch within a muscarinic receptor.
description
1998 nî lūn-bûn
@nan
1998年の論文
@ja
1998年論文
@yue
1998年論文
@zh-hant
1998年論文
@zh-hk
1998年論文
@zh-mo
1998年論文
@zh-tw
1998年论文
@wuu
1998年论文
@zh
1998年论文
@zh-cn
name
Identification of a ligand-dependent switch within a muscarinic receptor.
@en
Identification of a ligand-dependent switch within a muscarinic receptor.
@nl
type
label
Identification of a ligand-dependent switch within a muscarinic receptor.
@en
Identification of a ligand-dependent switch within a muscarinic receptor.
@nl
prefLabel
Identification of a ligand-dependent switch within a muscarinic receptor.
@en
Identification of a ligand-dependent switch within a muscarinic receptor.
@nl
P2093
P2860
P356
P1476
Identification of a ligand-dependent switch within a muscarinic receptor.
@en
P2093
Burstein ES
Henderson SC
Spalding TA
P2860
P304
21563-21568
P356
10.1074/JBC.273.34.21563
P407
P577
1998-08-01T00:00:00Z