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By interacting with the C-terminal Phe of apelin, Phe255 and Trp259 in helix VI of the apelin receptor are critical for internalization.

par Iturrioz, Xavier;Gerbier, Romain ;Leroux, Vincent ;Alvear-Perez, Rodrigo;Maigret, Bernard;Llorens-Cortes, Catherine
Référence The Journal of biological chemistry, 285, 42, page (32627-32637)
Publication Publié, 2010-10

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Titre:	By interacting with the C-terminal Phe of apelin, Phe255 and Trp259 in helix VI of the apelin receptor are critical for internalization.
Auteur:	Iturrioz, Xavier; Gerbier, Romain; Leroux, Vincent; Alvear-Perez, Rodrigo; Maigret, Bernard; Llorens-Cortes, Catherine
Informations sur la publication:	The Journal of biological chemistry, 285, 42, page (32627-32637)
Statut de publication:	Publié, 2010-10
Sujet CREF:	Sciences bio-médicales et agricoles
	Sciences exactes et naturelles
MeSH keywords:	Amino Acid Sequence
	Animals
	CHO Cells
	Cricetinae
	Cricetulus
	Cyclic AMP -- metabolism
	Humans
	Intercellular Signaling Peptides and Proteins -- chemistry -- genetics -- metabolism
	Models, Molecular
	Molecular Sequence Data
	Mutagenesis, Site-Directed
	Phenylalanine -- metabolism
	Protein Conformation
	Radioligand Assay
	Rats
	Receptors, G-Protein-Coupled -- genetics -- metabolism
	Recombinant Fusion Proteins -- genetics -- metabolism
	Tryptophan -- metabolism
Langue:	Anglais
Identificateurs:	urn:issn:0021-9258
	info:doi/10.1074/jbc.M110.127167
	info:pii/M110.127167
	info:pmid/20675385
	PMC2952265