UB Paderborn / Katalog / Suche / in CDI

Crystal structure of the sodium-potassium pump

Nature, 2007-12, Vol.450 (7172), p.1043-1049

2007

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Neurological disease mutations of α3 Na+,K+-ATPase: Structural and functional perspectives and rescue of compromised function

Biochimica et biophysica acta, 2016-11, Vol.1857 (11), p.1807-1828

2016

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Relationship between Intracellular Na+ Concentration and Reduced Na+ Affinity in Na+,K+-ATPase Mutants Causing Neurological Disease

The Journal of biological chemistry, 2014-02, Vol.289 (6), p.3186-3197

2014

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The Rapid-onset Dystonia Parkinsonism Mutation D923N of the Na+,K+-ATPase α3 Isoform Disrupts Na+ Interaction at the Third Na+ Site

The Journal of biological chemistry, 2010-08, Vol.285 (34), p.26245-26254

2010

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

Philosophical transactions of the Royal Society of London. Series B. Biological sciences, 2009-01, Vol.364 (1514), p.217

2009

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Temperature instability of a mutation at a multidomain junction in Na,K-ATPase isoform ATP1A3 (p.Arg756His) produces a fever-induced neurological syndrome

The Journal of biological chemistry, 2023-01, Vol.299 (1), p.102758-102758, Article 102758

2023

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Identification and Function of a Cytoplasmic K+ Site of the Na+, K+-ATPase

The Journal of biological chemistry, 2008-10, Vol.283 (41), p.27982-27990

2008

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Importance of a Potential Protein Kinase A Phosphorylation Site of Na+,K+-ATPase and Its Interaction Network for Na+ Binding

The Journal of biological chemistry, 2016-05, Vol.291 (20), p.10934-10947

2016

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Functional consequences of the CAPOS mutation E818K of Na+,K+-ATPase

The Journal of biological chemistry, 2019-01, Vol.294 (1), p.269-280

2019

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The C Terminus of Na+,K+-ATPase Controls Na+ Affinity on Both Sides of the Membrane through Arg935

The Journal of biological chemistry, 2009-07, Vol.284 (28), p.18715-18725

2009

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A C-terminal mutation of ATP1A3 underscores the crucial role of sodium affinity in the pathophysiology of rapid-onset dystonia-parkinsonism

Human molecular genetics, 2009-07, Vol.18 (13), p.2370-2377

2009

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C Terminus of Na⁺,K⁺-ATPase Controls Na⁺ Affinity on Both Sides of the Membrane through Arg

The Journal of biological chemistry, 2009-07, Vol.284 (28), p.18715-18725

2009

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The Rapid-onset Dystonia Parkinsonism Mutation D923N of the Na+,K+-ATPase a3 Isoform Disrupts Na+ Interaction at the Third Na+ Site

The Journal of biological chemistry, 2010-08, Vol.285 (34), p.26245-26254

2010

Volltextzugriff (PDF)

The rapid-onset dystonia parkinsonism mutation D923N of the Na+, K+-ATPase alpha3 isoform disrupts Na+ interaction at the third Na+ site

The Journal of biological chemistry, 2010-08, Vol.285 (34), p.26245-26254

2010

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X-ray crystallographic studies of the pig renal Na + ,K + -ATPase

Acta crystallographica. Section A, Foundations of crystallography, 2009-08, Vol.65 (a1), p.s30-s30

2009

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Mutations Phe785Leu and Thr618Met in Na+,K+-ATPase, Associated with Familial Rapid-onset Dystonia Parkinsonism, Interfere with Na+ Interaction by Distinct Mechanisms

The Journal of biological chemistry, 2006-07, Vol.281 (27), p.18539-18548

2006

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Mutation of Gly-94 in transmembrane segment M1 of Na+,K+-ATPase interferes with Na+ and K+ binding in E2P conformation

Proceedings of the National Academy of Sciences - PNAS, 2005-08, Vol.102 (32), p.11254-11259

2005

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Interaction between the Catalytic Site and the A-M3 Linker Stabilizes E2/E2P Conformational States of Na+,K+-ATPase

The Journal of biological chemistry, 2005-03, Vol.280 (11), p.10210-10218

2005

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Importance of Glu(282) in transmembrane segment M3 of the Na(+),K(+)-ATPase for control of cation interaction and conformational changes

The Journal of biological chemistry, 2002-10, Vol.277 (41), p.38607

2002

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Functional Consequences of Alterations to Ile279, Ile283, Glu284, His285, Phe286, and His288 in the NH2-terminal Part of Transmembrane Helix M3 of the Na+,K+-ATPase

The Journal of biological chemistry, 2003-10, Vol.278 (40), p.38653-38664

2003

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Importance of Transmembrane Segment M3 of Na+,K+-ATPase for Control of Conformational Changes and the Cytoplasmic Entry Pathway for Na+

Annals of the New York Academy of Sciences, 2003-04, Vol.986 (1), p.50-57

2003

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Mutational Effects on Conformational Changes of the Dephospho- and Phospho-forms of the Na+,K+-ATPase

Biochemistry (Easton), 2001-05, Vol.40 (18), p.5521-5532

2001

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Importance of Conserved Thr214 in Domain A of the Na+,K+-ATPase for Stabilization of the Phosphoryl Transition State Complex in E 2P Dephosphorylation

The Journal of biological chemistry, 2003-03, Vol.278 (13), p.11402-11410

2003

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Importance of Thr214 in the Conserved TGES Sequence of the Na+,K+-ATPase for Vanadate Binding and Hydrolysis of E2P

Annals of the New York Academy of Sciences, 2003-04, Vol.986 (1), p.267-269

2003

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Importance of Glu282 in Transmembrane Segment M3 of the Na+,K+-ATPase for Control of Cation Interaction and Conformational Changes

The Journal of biological chemistry, 2002-10, Vol.277 (41), p.38607-38617

2002

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Crystal structure of the sodium-potassium pump

Neurological disease mutations of α3 Na+,K+-ATPase: Structural and functional perspectives and rescue of compromised function

Relationship between Intracellular Na+ Concentration and Reduced Na+ Affinity in Na+,K+-ATPase Mutants Causing Neurological Disease

The Rapid-onset Dystonia Parkinsonism Mutation D923N of the Na+,K+-ATPase α3 Isoform Disrupts Na+ Interaction at the Third Na+ Site

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

Temperature instability of a mutation at a multidomain junction in Na,K-ATPase isoform ATP1A3 (p.Arg756His) produces a fever-induced neurological syndrome

Identification and Function of a Cytoplasmic K+ Site of the Na+, K+-ATPase

Importance of a Potential Protein Kinase A Phosphorylation Site of Na+,K+-ATPase and Its Interaction Network for Na+ Binding

Functional consequences of the CAPOS mutation E818K of Na+,K+-ATPase

The C Terminus of Na+,K+-ATPase Controls Na+ Affinity on Both Sides of the Membrane through Arg935

A C-terminal mutation of ATP1A3 underscores the crucial role of sodium affinity in the pathophysiology of rapid-onset dystonia-parkinsonism

C Terminus of Na⁺,K⁺-ATPase Controls Na⁺ Affinity on Both Sides of the Membrane through Arg

The Rapid-onset Dystonia Parkinsonism Mutation D923N of the Na+,K+-ATPase a3 Isoform Disrupts Na+ Interaction at the Third Na+ Site

The rapid-onset dystonia parkinsonism mutation D923N of the Na+, K+-ATPase alpha3 isoform disrupts Na+ interaction at the third Na+ site

X-ray crystallographic studies of the pig renal Na + ,K + -ATPase

Mutations Phe785Leu and Thr618Met in Na+,K+-ATPase, Associated with Familial Rapid-onset Dystonia Parkinsonism, Interfere with Na+ Interaction by Distinct Mechanisms

Mutation of Gly-94 in transmembrane segment M1 of Na+,K+-ATPase interferes with Na+ and K+ binding in E2P conformation

Interaction between the Catalytic Site and the A-M3 Linker Stabilizes E2/E2P Conformational States of Na+,K+-ATPase

Importance of Glu(282) in transmembrane segment M3 of the Na(+),K(+)-ATPase for control of cation interaction and conformational changes

Functional Consequences of Alterations to Ile279, Ile283, Glu284, His285, Phe286, and His288 in the NH2-terminal Part of Transmembrane Helix M3 of the Na+,K+-ATPase

Importance of Transmembrane Segment M3 of Na+,K+-ATPase for Control of Conformational Changes and the Cytoplasmic Entry Pathway for Na+

Mutational Effects on Conformational Changes of the Dephospho- and Phospho-forms of the Na+,K+-ATPase

Importance of Conserved Thr214 in Domain A of the Na+,K+-ATPase for Stabilization of the Phosphoryl Transition State Complex in E 2P Dephosphorylation

Importance of Thr214 in the Conserved TGES Sequence of the Na+,K+-ATPase for Vanadate Binding and Hydrolysis of E2P

Importance of Glu282 in Transmembrane Segment M3 of the Na+,K+-ATPase for Control of Cation Interaction and Conformational Changes

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