Comparison of a homology model of P-glycoprotein in the ATP-bound state with experimental data indicates intrinsic flexibility of the transmembrane domains

T. Stockner; S.J. de Vries; A.M. Bonvin; G.F. Ecker; P. Chiba

Comparison of a homology model of P-glycoprotein in the ATP-bound state with experimental data indicates intrinsic flexibility of the transmembrane domains

T. Stockner, S.J. de Vries, A.M. Bonvin, G.F. Ecker, P. Chiba

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Publikation: Beitrag in Fachzeitschrift › Artikel › Begutachtung

Originalsprache	Englisch
Seiten (von - bis)	964-972
Seitenumfang	9
Fachzeitschrift	FEBS Journal
Volume	276
Publikationsstatus	Veröffentlicht - 2009

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@article{e7f61711fe264367a3c2053bae2271d1,

title = "Comparison of a homology model of P-glycoprotein in the ATP-bound state with experimental data indicates intrinsic flexibility of the transmembrane domains",

author = "T. Stockner and {de Vries}, S.J. and A.M. Bonvin and G.F. Ecker and P. Chiba",

year = "2009",

language = "English",

volume = "276",

pages = "964--972",

journal = "FEBS Journal",

issn = "1742-464X",

publisher = "Wiley-Blackwell Publishing Ltd",

}

TY - JOUR

T1 - Comparison of a homology model of P-glycoprotein in the ATP-bound state with experimental data indicates intrinsic flexibility of the transmembrane domains

AU - Stockner, T.

AU - de Vries, S.J.

AU - Bonvin, A.M.

AU - Ecker, G.F.

AU - Chiba, P.

PY - 2009

Y1 - 2009

M3 - Article

SN - 1742-464X

VL - 276

SP - 964

EP - 972

JO - FEBS Journal

JF - FEBS Journal

ER -