Fluorescence resonance energy transfer analysis of secretin docking to its receptor: mapping distances between residues distributed throughout the ligand pharmacophore and distinct receptor residues.

Fluorescence resonance energy transfer analysis of secretin docking to its receptor: mapping distances between residues distributed throughout the ligand pharmacophore and distinct receptor residues.

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http://www.wikidata.org/entity/Q51794822
Fluorescent approaches for understanding interactions of ligands with G protein coupled receptorsSecretin occupies a single protomer of the homodimeric secretin receptor complex: insights from photoaffinity labeling studies using dual sites of covalent attachment.Molecular basis of secretin docking to its intact receptor using multiple photolabile probes distributed throughout the pharmacophoreCalcitonin and calcitonin receptor-like receptors: common themes with family B GPCRs?Mapping spatial approximations between the amino terminus of secretin and each of the extracellular loops of its receptor using cysteine trapping.Use of Cysteine Trapping to Map Spatial Approximations between Residues Contributing to the Helix N-capping Motif of Secretin and Distinct Residues within Each of the Extracellular Loops of Its Receptor.Insights into the structural basis of endogenous agonist activation of family B G protein-coupled receptorsUse of multidimensional fluorescence resonance energy transfer to establish the orientation of cholecystokinin docked at the type A cholecystokinin receptor.Effects of pH and temperature on photoaffinity labeling of Family B G protein-coupled receptors.Exploration of the endogenous agonist mechanism for activation of secretin and VPAC1 receptors using synthetic glycosylated peptidesSpatial approximation between secretin residue five and the third extracellular loop of its receptor provides new insight into the molecular basis of natural agonist binding.Homology modelling and spectroscopy, a never-ending love story.The orthosteric agonist-binding pocket in the prototypic class B G-protein-coupled secretin receptor.Spirohexene-Tetrazine Ligation Enables Bioorthogonal Labeling of Class B G Protein-Coupled Receptors in Live Cells.Structure and Modeling of GPCRs: Implications for Drug Discovery
P2860

Fluorescence resonance energy transfer analysis of secretin docking to its receptor: mapping distances between residues distributed throughout the ligand pharmacophore and distinct receptor residues.

Item
http://www.wikidata.org/entity/Q51794822
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2007 nî lūn-bûn
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2007年の論文
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2007年学术文章
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name
Fluorescence resonance energy ...... nd distinct receptor residues.
@en
Fluorescence resonance energy ...... nd distinct receptor residues.
@nl
type
label
Fluorescence resonance energy ...... nd distinct receptor residues.
@en
Fluorescence resonance energy ...... nd distinct receptor residues.
@nl
prefLabel
Fluorescence resonance energy ...... nd distinct receptor residues.
@en
Fluorescence resonance energy ...... nd distinct receptor residues.
@nl
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P1476
P2093
P2860
P304
P31
P356
P407
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P50
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Fluorescence resonance energy ...... nd distinct receptor residues.
@en
P2093
P2860
P304
P31
P356
P407
P433
P478
P50
P577
P698