The N-terminal parts of VIP and antagonist PG97-269 physically interact with different regions of the human VPAC1 receptor. (Q46505277)

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10 January 2020

title

The N-terminal parts of VIP and antagonist PG97-269 physically interact with different regions of the human VPAC1 receptor (English)

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4

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author name string

Emilie Ceraudo

1

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10 January 2020

Yossan-Var Tan

2

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Pascal Nicole

3

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Marc Laburthe

5

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publication date

3 July 2008

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Journal of Molecular Neuroscience

10 January 2020

published in

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volume

36

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issue

1-3

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page(s)

245-248

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https://scigraph.springernature.com/pub.10.1007/s12031-008-9073-7

10 January 2020

exact match

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cites work

Peptide agonist docking in the N-terminal ectodomain of a class II G protein-coupled receptor, the VPAC1 receptor. Photoaffinity, NMR, and molecular modeling

1 reference

12 December 2020

Photoaffinity labeling demonstrates physical contact between vasoactive intestinal peptide and the N-terminal ectodomain of the human VPAC1 receptor

1 reference

12 December 2020

Pharmaceutical VIP: prospects and problems

1 reference

12 December 2020

The origin and function of the pituitary adenylate cyclase-activating polypeptide (PACAP)/glucagon superfamily

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12 December 2020

In vitro properties of a high affinity selective antagonist of the VIP1 receptor

1 reference

12 December 2020

Constitutive activation of the human vasoactive intestinal peptide 1 receptor, a member of the new class II family of G protein-coupled receptors

1 reference

12 December 2020

The vasoactive intestinal peptide (VIP) alpha-Helix up to C terminus interacts with the N-terminal ectodomain of the human VIP/Pituitary adenylate cyclase-activating peptide 1 receptor: photoaffinity, molecular modeling, and dynamics

1 reference

12 December 2020

Diffuse pharmacophoric domains of vasoactive intestinal peptide (VIP) and further insights into the interaction of VIP with the N-terminal ectodomain of human VPAC1 receptor by photoaffinity labeling with [Bpa6]-VIP.

1 reference

12 December 2020

Identification of key residues for interaction of vasoactive intestinal peptide with human VPAC1 and VPAC2 receptors and development of a highly selective VPAC1 receptor agonist. Alanine scanning and molecular modeling of the peptide

1 reference

12 December 2020

Spatial approximation between the amino terminus of a peptide agonist and the top of the sixth transmembrane segment of the secretin receptor.

1 reference

12 December 2020

Class II G protein-coupled receptors for VIP and PACAP: structure, models of activation and pharmacology.

1 reference

12 December 2020

10.1007/S12031-008-9073-7

Identifiers

DOI

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