Aarhus University Seal / Aarhus Universitets segl

P-type ATPases

Publikation: Bidrag til tidsskrift/Konferencebidrag i tidsskrift /Bidrag til avisTidsskriftartikelForskningpeer review

Standard

P-type ATPases. / Palmgren, Michael Broberg; Nissen, Poul.

I: Annual Review of Biophysics, Bind 40, 2011, s. 243-66.

Publikation: Bidrag til tidsskrift/Konferencebidrag i tidsskrift /Bidrag til avisTidsskriftartikelForskningpeer review

Harvard

Palmgren, MB & Nissen, P 2011, 'P-type ATPases', Annual Review of Biophysics, bind 40, s. 243-66. https://doi.org/10.1146/annurev.biophys.093008.131331

APA

Palmgren, M. B., & Nissen, P. (2011). P-type ATPases. Annual Review of Biophysics, 40, 243-66. https://doi.org/10.1146/annurev.biophys.093008.131331

CBE

Palmgren MB, Nissen P. 2011. P-type ATPases. Annual Review of Biophysics. 40:243-66. https://doi.org/10.1146/annurev.biophys.093008.131331

MLA

Palmgren, Michael Broberg og Poul Nissen. "P-type ATPases". Annual Review of Biophysics. 2011, 40. 243-66. https://doi.org/10.1146/annurev.biophys.093008.131331

Vancouver

Palmgren MB, Nissen P. P-type ATPases. Annual Review of Biophysics. 2011;40:243-66. https://doi.org/10.1146/annurev.biophys.093008.131331

Author

Palmgren, Michael Broberg ; Nissen, Poul. / P-type ATPases. I: Annual Review of Biophysics. 2011 ; Bind 40. s. 243-66.

Bibtex

@article{d0fc35d9c6c44dc3abd298867bf65a7f,
title = "P-type ATPases",
abstract = "P-type ATPases form a large superfamily of cation and lipid pumps. They are remarkably simple with only a single catalytic subunit and carry out large domain motions during transport. The atomic structure of P-type ATPases in different conformations, together with ample mutagenesis evidence, has provided detailed insights into the pumping mechanism by these biological nanomachines. Phylogenetically, P-type ATPases are divided into five subfamilies, P1-P5. These subfamilies differ with respect to transported ligands and the way they are regulated.",
keywords = "Adenosine Triphosphatases, Binding Sites, Computer Simulation, Ion Channel Gating, Lipid Metabolism, Lipids, Models, Biological, Models, Chemical, Protein Binding, Protein Structure, Tertiary",
author = "Palmgren, {Michael Broberg} and Poul Nissen",
year = "2011",
doi = "10.1146/annurev.biophys.093008.131331",
language = "English",
volume = "40",
pages = "243--66",
journal = "Annual Review of Biophysics",
issn = "1936-122X",
publisher = "Annual Reviews",

}

RIS

TY - JOUR

T1 - P-type ATPases

AU - Palmgren, Michael Broberg

AU - Nissen, Poul

PY - 2011

Y1 - 2011

N2 - P-type ATPases form a large superfamily of cation and lipid pumps. They are remarkably simple with only a single catalytic subunit and carry out large domain motions during transport. The atomic structure of P-type ATPases in different conformations, together with ample mutagenesis evidence, has provided detailed insights into the pumping mechanism by these biological nanomachines. Phylogenetically, P-type ATPases are divided into five subfamilies, P1-P5. These subfamilies differ with respect to transported ligands and the way they are regulated.

AB - P-type ATPases form a large superfamily of cation and lipid pumps. They are remarkably simple with only a single catalytic subunit and carry out large domain motions during transport. The atomic structure of P-type ATPases in different conformations, together with ample mutagenesis evidence, has provided detailed insights into the pumping mechanism by these biological nanomachines. Phylogenetically, P-type ATPases are divided into five subfamilies, P1-P5. These subfamilies differ with respect to transported ligands and the way they are regulated.

KW - Adenosine Triphosphatases

KW - Binding Sites

KW - Computer Simulation

KW - Ion Channel Gating

KW - Lipid Metabolism

KW - Lipids

KW - Models, Biological

KW - Models, Chemical

KW - Protein Binding

KW - Protein Structure, Tertiary

U2 - 10.1146/annurev.biophys.093008.131331

DO - 10.1146/annurev.biophys.093008.131331

M3 - Journal article

C2 - 21351879

VL - 40

SP - 243

EP - 266

JO - Annual Review of Biophysics

JF - Annual Review of Biophysics

SN - 1936-122X

ER -