C5a receptor activation. Genetic identification of critical residues in four transmembrane helices.
about
A microdomain formed by the extracellular ends of the transmembrane domains promotes activation of the G protein-coupled alpha-factor receptorFunction, structure and therapeutic potential of complement C5a receptorsSynthetic biology: lessons from engineering yeast MAPK signalling pathwaysThe use of evolutionary patterns in protein annotationIdentification of determinants of ligand binding affinity and selectivity in the prostaglandin D2 receptor CRTH2Cell wall trapping of autocrine peptides for human G-protein-coupled receptors on the yeast cell surfaceSingle amino acid substitutions and deletions that alter the G protein coupling properties of the V2 vasopressin receptor identified in yeast by receptor random mutagenesis.Functional expression of heteromeric calcitonin gene-related peptide and adrenomedullin receptors in yeast.Signaling of human frizzled receptors to the mating pathway in yeast.Identification of allosteric peptide agonists of CXCR4.Systematic identification of mutations that constitutively activate the angiotensin II type 1A receptor by screening a randomly mutated cDNA library with an original pharmacological bioassayGenetic mapping of the human C5a receptor. Identification of transmembrane amino acids critical for receptor function.Constitutive activation of CCR5 and CCR2 induced by conformational changes in the conserved TXP motif in transmembrane helix 2.Random mutagenesis of the M3 muscarinic acetylcholine receptor expressed in yeast: identification of second-site mutations that restore function to a coupling-deficient mutant M3 receptor.A small molecule antagonist of chemokine receptors CCR1 and CCR3. Potent inhibition of eosinophil function and CCR3-mediated HIV-1 entry.An activation switch in the ligand binding pocket of the C5a receptor.Disulfide trapping to localize small-molecule agonists and antagonists for a G protein-coupled receptor.Random mutagenesis of the complement factor 5a (C5a) receptor N terminus provides a structural constraint for C5a docking.E2F8 is a nonreceptor activator of heterotrimeric G proteins.Structure of the complement factor 5a receptor-ligand complex studied by disulfide trapping and molecular modeling.Naturally occurring mutations of the luteinizing-hormone receptor: lessons learned about reproductive physiology and G protein-coupled receptors.An angiotensin II type 1 receptor activation switch patch revealed through evolutionary trace analysis.Neurotensin induces mating in Saccharomyces cerevisiae cells that express human neurotensin receptor type 1 in place of the endogenous pheromone receptor.GPCR-I-TASSER: A Hybrid Approach to G Protein-Coupled Receptor Structure Modeling and the Application to the Human Genome.Prediction and redesign of protein-protein interactionsThe role of the anaphylatoxins in health and disease.The melanocortin-4 receptor: physiology, pharmacology, and pathophysiology.Constitutive activity of muscarinic acetylcholine receptors.Frizzled receptors signal through G proteins.Differential dynamics in the G protein-coupled receptor rhodopsin revealed by solution NMR.Constitutive activation of G protein-coupled receptors and diseases: insights into mechanisms of activation and therapeutics.A cannabinoid receptor 1 mutation proximal to the DRY motif results in constitutive activity and reveals intramolecular interactions involved in receptor activation.Complement factor 5a receptor chimeras reveal the importance of lipid-facing residues in transport competence.Three "hotspots" important for adenosine A(2B) receptor activation: a mutational analysis of transmembrane domains 4 and 5 and the second extracellular loopPheVI:09 (Phe6.44) as a sliding microswitch in seven-transmembrane (7TM) G protein-coupled receptor activation.A conserved Asn in transmembrane helix 7 is an on/off switch in the activation of the thyrotropin receptor.Molecular characterization of the gerbil C5a receptor and identification of a transmembrane domain V amino acid that is crucial for small molecule antagonist interaction.Simplified modeling approach suggests structural mechanisms for constitutive activation of the C5a receptor.Light activation of rhodopsin: insights from molecular dynamics simulations guided by solid-state NMR distance restraints.Control of conformational equilibria in the human B2 bradykinin receptor. Modeling of nonpeptidic ligand action and comparison to the rhodopsin structure.
P2860
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P2860
C5a receptor activation. Genetic identification of critical residues in four transmembrane helices.
description
1999 nî lūn-bûn
@nan
1999 թուականի Մայիսին հրատարակուած գիտական յօդուած
@hyw
1999 թվականի մայիսին հրատարակված գիտական հոդված
@hy
1999年の論文
@ja
1999年論文
@yue
1999年論文
@zh-hant
1999年論文
@zh-hk
1999年論文
@zh-mo
1999年論文
@zh-tw
1999年论文
@wuu
name
C5a receptor activation. Genet ...... in four transmembrane helices.
@ast
C5a receptor activation. Genet ...... in four transmembrane helices.
@en
type
label
C5a receptor activation. Genet ...... in four transmembrane helices.
@ast
C5a receptor activation. Genet ...... in four transmembrane helices.
@en
prefLabel
C5a receptor activation. Genet ...... in four transmembrane helices.
@ast
C5a receptor activation. Genet ...... in four transmembrane helices.
@en
P2093
P2860
P356
P1476
C5a receptor activation. Genet ...... in four transmembrane helices.
@en
P2093
Baranski TJ
Herzmark P
Lichtarge O
Trueheart J
P2860
P304
15757-15765
P356
10.1074/JBC.274.22.15757
P407
P577
1999-05-01T00:00:00Z