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The structure of the Na+,K+-ATPase and mapping of isoform differences and disease-related mutations

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The structure of the Na+,K+-ATPase and mapping of isoform differences and disease-related mutations. / Morth, J Preben; Poulsen, Hanne; Toustrup-Jensen, Mads S; Schack, Vivien Rodacker; Egebjerg, Jan; Andersen, Jens Peter; Vilsen, Bente; Nissen, Poul.

I: Royal Society of London. Philosophical Transactions. Biological Sciences, Bind 364, Nr. 1514, 2009, s. 217-27.

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

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Morth, J Preben o.a.. "The structure of the Na+,K+-ATPase and mapping of isoform differences and disease-related mutations". Royal Society of London. Philosophical Transactions. Biological Sciences. 2009, 364(1514). 217-27. https://doi.org/10.1098/rstb.2008.0201

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Morth, J Preben ; Poulsen, Hanne ; Toustrup-Jensen, Mads S ; Schack, Vivien Rodacker ; Egebjerg, Jan ; Andersen, Jens Peter ; Vilsen, Bente ; Nissen, Poul. / The structure of the Na+,K+-ATPase and mapping of isoform differences and disease-related mutations. I: Royal Society of London. Philosophical Transactions. Biological Sciences. 2009 ; Bind 364, Nr. 1514. s. 217-27.

Bibtex

@article{e1003610ab2511dd889c000ea68e967b,
title = "The structure of the Na+,K+-ATPase and mapping of isoform differences and disease-related mutations",
abstract = "The Na+,K+-ATPase transforms the energy of ATP to the maintenance of steep electrochemical gradients for sodium and potassium across the plasma membrane. This activity is tissue specific, in particular due to variations in the expressions of the alpha subunit isoforms one through four. Several mutations in alpha2 and 3 have been identified that link the specific function of the Na+,K+-ATPase to the pathophysiology of neurological diseases such as rapid-onset dystonia parkinsonism and familial hemiplegic migraine type 2. We show a mapping of the isoform differences and the disease-related mutations on the recently determined crystal structure of the pig renal Na+,K+-ATPase and a structural comparison to Ca2+-ATPase. Furthermore, we present new experimental data that address the role of a stretch of three conserved arginines near the C-terminus of the alpha subunit (Arg1003-Arg1005).",
author = "Morth, {J Preben} and Hanne Poulsen and Toustrup-Jensen, {Mads S} and Schack, {Vivien Rodacker} and Jan Egebjerg and Andersen, {Jens Peter} and Bente Vilsen and Poul Nissen",
year = "2009",
doi = "10.1098/rstb.2008.0201",
language = "English",
volume = "364",
pages = "217--27",
journal = "Philosophical Transactions of the Royal Society B: Biological Sciences",
issn = "0962-8436",
publisher = "ROYAL SOC",
number = "1514",

}

RIS

TY - JOUR

T1 - The structure of the Na+,K+-ATPase and mapping of isoform differences and disease-related mutations

AU - Morth, J Preben

AU - Poulsen, Hanne

AU - Toustrup-Jensen, Mads S

AU - Schack, Vivien Rodacker

AU - Egebjerg, Jan

AU - Andersen, Jens Peter

AU - Vilsen, Bente

AU - Nissen, Poul

PY - 2009

Y1 - 2009

N2 - The Na+,K+-ATPase transforms the energy of ATP to the maintenance of steep electrochemical gradients for sodium and potassium across the plasma membrane. This activity is tissue specific, in particular due to variations in the expressions of the alpha subunit isoforms one through four. Several mutations in alpha2 and 3 have been identified that link the specific function of the Na+,K+-ATPase to the pathophysiology of neurological diseases such as rapid-onset dystonia parkinsonism and familial hemiplegic migraine type 2. We show a mapping of the isoform differences and the disease-related mutations on the recently determined crystal structure of the pig renal Na+,K+-ATPase and a structural comparison to Ca2+-ATPase. Furthermore, we present new experimental data that address the role of a stretch of three conserved arginines near the C-terminus of the alpha subunit (Arg1003-Arg1005).

AB - The Na+,K+-ATPase transforms the energy of ATP to the maintenance of steep electrochemical gradients for sodium and potassium across the plasma membrane. This activity is tissue specific, in particular due to variations in the expressions of the alpha subunit isoforms one through four. Several mutations in alpha2 and 3 have been identified that link the specific function of the Na+,K+-ATPase to the pathophysiology of neurological diseases such as rapid-onset dystonia parkinsonism and familial hemiplegic migraine type 2. We show a mapping of the isoform differences and the disease-related mutations on the recently determined crystal structure of the pig renal Na+,K+-ATPase and a structural comparison to Ca2+-ATPase. Furthermore, we present new experimental data that address the role of a stretch of three conserved arginines near the C-terminus of the alpha subunit (Arg1003-Arg1005).

U2 - 10.1098/rstb.2008.0201

DO - 10.1098/rstb.2008.0201

M3 - Journal article

C2 - 18957371

VL - 364

SP - 217

EP - 227

JO - Philosophical Transactions of the Royal Society B: Biological Sciences

JF - Philosophical Transactions of the Royal Society B: Biological Sciences

SN - 0962-8436

IS - 1514

ER -