Vasoactive intestinal peptide (VIP)1 receptor. Three nonadjacent amino acids are responsible for species selectivity with respect to recognition of peptide histidine isoleucineamide. (Q41197334)

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scientific article published on May 1996

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English	Vasoactive intestinal peptide (VIP)1 receptor. Three nonadjacent amino acids are responsible for species selectivity with respect to recognition of peptide histidine isoleucineamide.	scientific article published on May 1996

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16 October 2019

Vasoactive intestinal peptide (VIP)1 receptor. Three nonadjacent amino acids are responsible for species selectivity with respect to recognition of peptide histidine isoleucineamide (English)

1 reference

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16 October 2019

Alain Couvineau

1

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16 October 2019

author name string

C Rouyer-Fessard

2

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16 October 2019

J J Maoret

3

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16 October 2019

P Gaudin

4

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16 October 2019

P Nicole

5

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16 October 2019

M Laburthe

6

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1 May 1996

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16 October 2019

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6

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Journal of Biological Chemistry

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16 October 2019

271

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16 October 2019

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12795-12800

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16 October 2019

Molecular analysis of vasoactive intestinal peptide receptors. A comparison with receptors for VIP-related peptides

1 reference

https://api.crossref.org/works/10.1074%2FJBC.271.22.12795

21 January 2018

Functional expression and tissue distribution of a novel receptor for vasoactive intestinal polypeptide

1 reference

https://api.crossref.org/works/10.1074%2FJBC.271.22.12795

21 January 2018

The VIP2 receptor: molecular characterisation of a cDNA encoding a novel receptor for vasoactive intestinal peptide

1 reference

https://api.crossref.org/works/10.1074%2FJBC.271.22.12795

21 January 2018

Human intestinal VIP receptor: cloning and functional expression of two cDNA encoding proteins with different N-terminal domains

1 reference

https://api.crossref.org/works/10.1074%2FJBC.271.22.12795

21 January 2018

Molecular cloning and functional characterization of a human VIP receptor from SUP-T1 lymphoblasts

1 reference

https://api.crossref.org/works/10.1074%2FJBC.271.22.12795

21 January 2018

Structure, expression, and chromosomal localization of the type I human vasoactive intestinal peptide receptor gene

1 reference

https://api.crossref.org/works/10.1074%2FJBC.271.22.12795

21 January 2018

Receptors for secretin, calcitonin, parathyroid hormone (PTH)/PTH-related peptide, vasoactive intestinal peptide, glucagonlike peptide 1, growth hormone-releasing hormone, and glucagon belong to a newly discovered G-protein-linked receptor family

1 reference

https://api.crossref.org/works/10.1074%2FJBC.271.22.12795

21 January 2018

Highly conserved aspartate 68, tryptophane 73 and glycine 109 in the N-terminal extracellular domain of the human VIP receptor are essential for its ability to bind VIP.

1 reference

https://api.crossref.org/works/10.1074%2FJBC.271.22.12795

21 January 2018

Mutational analysis of cysteine residues within the extracellular domains of the human vasoactive intestinal peptide (VIP) 1 receptor identifies seven mutants that are defective in VIP binding.

1 reference

https://api.crossref.org/works/10.1074%2FJBC.271.22.12795

21 January 2018

Mutagenesis of N-glycosylation sites in the human vasoactive intestinal peptide 1 receptor. Evidence that asparagine 58 or 69 is crucial for correct delivery of the receptor to plasma membrane

1 reference

https://api.crossref.org/works/10.1074%2FJBC.271.22.12795

21 January 2018

Critical contributions of amino-terminal extracellular domains in agonist binding and activation of secretin and vasoactive intestinal polypeptide receptors. Studies of chimeric receptors

1 reference

https://api.crossref.org/works/10.1074%2FJBC.271.22.12795

21 January 2018

Properties of chimeric secretin and VIP receptor proteins indicate the importance of the N-terminal domain for ligand discrimination

1 reference

https://api.crossref.org/works/10.1074%2FJBC.271.22.12795

21 January 2018

Interaction of PHM, PHI and 24-glutamine PHI with human VIP receptors from colonic epithelium: comparison with rat intestinal receptors.

1 reference

https://api.crossref.org/works/10.1074%2FJBC.271.22.12795

21 January 2018

LIGAND: A versatile computerized approach for characterization of ligand-binding systems

1 reference

https://api.crossref.org/works/10.1074%2FJBC.271.22.12795

21 January 2018

G alpha i RNA antisense expression demonstrates the exclusive coupling of peptide YY receptors to G(i)2 proteins in renal proximal tubule cells

1 reference

https://api.crossref.org/works/10.1074%2FJBC.271.22.12795

21 January 2018

The amino-terminal fragment of the adenylate cyclase activating polypeptide (PACAP) receptor functions as a high affinity PACAP binding domain.

1 reference

https://api.crossref.org/works/10.1074%2FJBC.271.22.12795

21 January 2018

Molecular cloning and tissue distribution of a receptor for pituitary adenylate cyclase-activating polypeptide.

1 reference

https://api.crossref.org/works/10.1074%2FJBC.271.22.12795

21 January 2018

Interaction of GRF with VIP receptors and stimulation of adenylate cyclase in rat and human intestinal epithelial membranes. Comparison with PHI and secretin

1 reference

https://api.crossref.org/works/10.1074%2FJBC.271.22.12795

21 January 2018

Porcine peptide having N-terminal histidine and C-terminal isoleucine amide (PHI): vasoactive intestinal peptide (VIP) and secretin-like effects in different tissues from the rat

1 reference

https://api.crossref.org/works/10.1074%2FJBC.271.22.12795

21 January 2018

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10.1074/JBC.271.22.12795

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16 October 2019

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16 October 2019

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