Identification of the binding sites of the SR49059 nonpeptide antagonist into the V1a vasopressin receptor using sulfydryl-reactive ligands and cysteine mutants as chemical sensors (Q28187967)

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scientific article (publication date: 10 October 2003)

Language	Label	Description	Also known as
English	Identification of the binding sites of the SR49059 nonpeptide antagonist into the V1a vasopressin receptor using sulfydryl-reactive ligands and cysteine mutants as chemical sensors	scientific article (publication date: 10 October 2003)

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scholarly article

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Identification of the binding sites of the SR49059 nonpeptide antagonist into the V1a vasopressin receptor using sulfydryl-reactive ligands and cysteine mutants as chemical sensors (English)

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4

object named as

Didier Rognan

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author name string

Chouaïb Tahtaoui

1

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Marie-Noëlle Balestre

2

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Philippe Klotz

3

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Claude Barberis

5

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Bernard Mouillac

6

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Marcel Hibert

7

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language of work or name

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publication date

10 October 2003

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Journal of Biological Chemistry

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278

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41

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40010-9

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Vasopressin as vasopressor

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https://api.crossref.org/works/10.1074%2FJBC.M301128200

21 January 2018

Biochemical and pharmacological properties of SR 49059, a new, potent, nonpeptide antagonist of rat and human vasopressin V1a receptors

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https://api.crossref.org/works/10.1074%2FJBC.M301128200

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The binding site of neuropeptide vasopressin V1a receptor. Evidence for a major localization within transmembrane regions

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Functional architecture of vasopressin/oxytocin receptors

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A single residue (arg46) located within the N-terminus of the V1a vasopressin receptor is critical for binding vasopressin but not peptide or nonpeptide antagonists

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Conserved aromatic residues in the transmembrane region VI of the V1a vasopressin receptor differentiate agonist vs. antagonist ligand binding

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Mapping Peptide-binding Domains of the Human V1a Vasopressin Receptor with a Photoactivatable Linear Peptide Antagonist

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Direct identification of human oxytocin receptor-binding domains using a photoactivatable cyclic peptide antagonist: comparison with the human V1a vasopressin receptor

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Crystal structure of rhodopsin: A G protein-coupled receptor

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Cysteine mutants as chemical sensors for ligand-receptor interactions

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CLUSTAL W: improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice

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Molecular modeling of interactions of the non-peptide antagonist YM087 with the human vasopressin V1a, V2 receptors and with oxytocin receptors.

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Two aromatic residues regulate the response of the human oxytocin receptor to the partial agonist arginine vasopressin

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G protein-coupled receptors. II. Mechanism of agonist activation

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Interaction of non-competitive blockers within the gamma-aminobutyric acid type A chloride channel using chemically reactive probes as chemical sensors for cysteine mutants

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10.1074/JBC.M301128200

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