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Structural and functional asymmetry of the nucleotide-binding domains of P-glycoprotein investigated by attenuated total reflection Fourier transform infrared spectroscopy.

par Vigano, Catherine ;Julien, Michel;Carrier, Isabelle;Gros, Philippe;Ruysschaert, Jean Marie
Référence The Journal of biological chemistry, 277, 7, page (5008-5016)
Publication Publié, 2002-02

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Titre:	Structural and functional asymmetry of the nucleotide-binding domains of P-glycoprotein investigated by attenuated total reflection Fourier transform infrared spectroscopy.
Auteur:	Vigano, Catherine; Julien, Michel; Carrier, Isabelle; Gros, Philippe; Ruysschaert, Jean Marie
Informations sur la publication:	The Journal of biological chemistry, 277, 7, page (5008-5016)
Statut de publication:	Publié, 2002-02
Sujet CREF:	Chimie
MeSH keywords:	Adenosine Triphosphatases -- metabolism
	Adenosine Triphosphate -- metabolism
	Animals
	Benzimidazoles -- pharmacology
	Binding Sites
	Catalysis
	Cell Membrane -- metabolism
	Fluorescent Dyes
	Hydrolysis
	Kinetics
	Lipid Metabolism
	Liposomes -- metabolism
	Mice
	Mice, Mutant Strains
	Mutation
	P-Glycoprotein -- chemistry
	Protein Binding
	Protein Structure, Secondary
	Protein Structure, Tertiary
	Protein Transport
	Spectroscopy, Fourier Transform Infrared -- methods
	Time Factors
Note générale:	Journal Article
	Research Support, Non-U.S. Gov't
Langue:	Anglais
Identificateurs:	urn:issn:0021-9258
	info:doi/10.1074/jbc.M107928200
	info:pii/M107928200
	info:scp/0037085284
	info:pmid/11741934