B. Vilsen

发表

Dissection of the Functional Differences between Sarco(endo)plasmic Reticulum Ca2+-ATPase (SERCA) 1 and 2 Isoforms and Characterization of Darier Disease (SERCA2) Mutants by Steady-state and Transient Kinetic Analyses*

A. Hovnanian, L. Dode, J. Andersen, 2003, Journal of Biological Chemistry.

Asparagine 905 of the mammalian phospholipid flippase ATP8A2 is essential for lipid substrate–induced activation of ATP8A2 dephosphorylation

R. Molday, J. Andersen, B. Vilsen, 2019, The Journal of Biological Chemistry.

Crystal Structure of D351A and P312A Mutant Forms of the Mammalian Sarcoplasmic Reticulum Ca2+-ATPase Reveals Key Events in Phosphorylation and Ca2+ Release*

P. Nissen, C. Jaxel, C. Olesen, 2008, Journal of Biological Chemistry.

Roles of transmembrane segment M1 of Na+,K+-ATPase and Ca2+-ATPase, the gatekeeper and the pivot

A. P. Einholm, J. Andersen, B. Vilsen, 2007, Journal of bioenergetics and biomembranes.

ATP-binding Modes and Functionally Important Interdomain Bonds of Sarcoplasmic Reticulum Ca2+-ATPase Revealed by Mutation of Glycine 438, Glutamate 439, and Arginine 678*

J. Andersen, B. Vilsen, J. D. Clausen, 2007, Journal of Biological Chemistry.

Dissection of the Functional Differences between Human Secretory Pathway Ca2+/Mn2+-ATPase (SPCA) 1 and 2 Isoenzymes by Steady-state and Transient Kinetic Analyses*

L. Missiaen, L. Raeymaekers, F. Wuytack, 2006, Journal of Biological Chemistry.

Functional Comparison between Secretory Pathway Ca2+/Mn2+-ATPase (SPCA) 1 and Sarcoplasmic Reticulum Ca2+-ATPase (SERCA) 1 Isoforms by Steady-state and Transient Kinetic Analyses*

L. Missiaen, L. Raeymaekers, F. Wuytack, 2005, Journal of Biological Chemistry.

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

A. P. Einholm, J. Andersen, B. Vilsen, 2005, Proceedings of the National Academy of Sciences of the United States of America.

Roles of Conserved P Domain Residues and Mg2+ in ATP Binding in the Ground and Ca2+-activated States of Sarcoplasmic Reticulum Ca2+-ATPase*

D. Maclennan, J. Andersen, B. Vilsen, 2004, Journal of Biological Chemistry.

Glutamate-183 in the conserved TGES motif of domain A of sarcoplasmic reticulum Ca2+-ATPase assists in catalysis of E2/E2P partial reactions.

A. P. Einholm, J. Andersen, B. Vilsen, 2004, Proceedings of the National Academy of Sciences of the United States of America.

Mutagenesis of Residues Involved in Control of the Ca2+ Entry Pathway and Conformational Changes Associated with Ca2+ Binding in the SR Ca2+‐ATPase

A. P. Einholm, J. Andersen, B. Vilsen, 2003, Annals of the New York Academy of Sciences.

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*

B. Vilsen, M. Toustrup-Jensen, Mads S. Toustrup-Jensen, 2003, Journal of Biological Chemistry.

Functional consequences of charge reversals of acidic residues in M1 of the SR Ca-ATPase.

A. P. Einholm, J. Andersen, B. Vilsen, 2003, Annals of the New York Academy of Sciences.

ATP Binding Residues of Sarcoplasmic Reticulum Ca2+‐ATPase

D. Maclennan, J. Andersen, B. Vilsen, 2003, Annals of the New York Academy of Sciences.

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

B. Vilsen, M. Toustrup-Jensen, 2002, The Journal of Biological Chemistry.

Importance of Transmembrane Segment M3 of the Sarcoplasmic Reticulum Ca2+-ATPase for Control of the Gateway to the Ca2+ Sites*

J. Andersen, B. Vilsen, T. Sørensen, 2001, The Journal of Biological Chemistry.

Mutagenesis of Segment 487Phe-Ser-Arg-Asp-Arg-Lys492 of Sarcoplasmic Reticulum Ca2+-ATPase Produces Pumps Defective in ATP Binding*

J. Andersen, B. Vilsen, D. McIntosh, 1996, The Journal of Biological Chemistry.

ATP1A2- and ATP1A3-associated early profound epileptic encephalopathy and polymicrogyria.

I. Scheffer, H. Mefford, G. Cioni, 2021, Brain : a journal of neurology.

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

S. Petrou, Melody Li, J. Andersen, 2018, The Journal of Biological Chemistry.

Genetic suppression of agrin reduces mania‐like behavior in Na+, K+‐ATPase α3 mutant mice

J. Roder, S. Clapcote, M. Ralph, 2012, Genes, brain, and behavior.

Structure‐function relationships of cation translocation by Ca2+‐ and Na+,K+‐ATPases studied by site‐directed mutagenesis

B. Vilsen, Jens Peter Anderssen, Jens Peter Anderssen, 1995 .

Reaction of phenylhydrazine with erythrocytes. Cross-linking of spectrin by disulfide exchange with oxidized hemoglobin.

B. Vilsen, H. Nielsen, 1984, Biochemical pharmacology.

CORRECTIONS

M. Cortez, S. Clapcote, Y. Yücel, 1993, The Lancet.

The α2β2 isoform combination dominates the astrocytic Na+/K+‐ATPase activity and is rendered nonfunctional by the α2.G301R familial hemiplegic migraine type 2‐associated mutation

F. Vilhardt, M. Assentoft, N. MacAulay, 2017, Glia.

Critical roles of isoleucine-364 and adjacent residues in a hydrophobic gate control of phospholipid transport by the mammalian P4-ATPase ATP8A2

M. dal Peraro, L. Molday, R. Molday, 2014, Proceedings of the National Academy of Sciences.

Transmembrane segment M3 is essential to thapsigargin sensitivity of the sarcoplasmic reticulum Ca(2+)-ATPase.

J. Andersen, B. Vilsen, A. Nørregaard, 1994, The Journal of biological chemistry.

Germline De Novo Mutations in ATP1A1 Cause Renal Hypomagnesemia, Refractory Seizures, and Intellectual Disability.

M. Tarailo-Graovac, C. V. van Karnebeek, Jessica J. Y. Lee, 2018, American journal of human genetics.

Glutamate transporter activity promotes enhanced Na+/K+‐ATPase‐mediated extracellular K+ management during neuronal activity

N. MacAulay, B. Vilsen, Rikke Holm, 2016, The Journal of physiology.

Molecular Cloning and Characterization of Porcine Na+/K+-ATPase Isoforms α1, α2, α3 and the ATP1A3 Promoter

C. Oxvig, C. Bendixen, K. Larsen, 2013, PloS one.

Mutant Glu781-->Ala of the rat kidney Na+,K(+)-ATPase displays low cation affinity and catalyzes ATP hydrolysis at a high rate in the absence of potassium ions.

B. Vilsen, 1995, Biochemistry.

Glutamate 329 located in the fourth transmembrane segment of the alpha-subunit of the rat kidney Na+,K+-ATPase is not an essential residue for active transport of sodium and potassium ions.

B. Vilsen, 1993, Biochemistry.

Occlusion of 22Na+ and 86Rb+ in membrane-bound and soluble protomeric alpha beta-units of Na,K-ATPase.

P. L. Jørgensen, J. Petersen, J. Andersen, 1987, Progress in clinical and biological research.

Somatic ATP1A1, ATP2B3, and KCNJ5 Mutations in Aldosterone-Producing Adenomas

F. Beuschlein, I. Castellano, F. Veglio, 2014, Hypertension.

ATP2B3, and KCNJ5 Mutations in Aldosterone-Producing Adenomas

R. Schack, F. Beuschlein, F. Veglio, 2022 .

Characterization of detergent-solubilized sarcoplasmic reticulum Ca2+-ATPase by high-performance liquid chromatography.

J. Møller, J. Andersen, B. Vilsen, 1986, Biochemistry.

Functional consequences of alterations to Gly310, Gly770, and Gly801 located in the transmembrane domain of the Ca(2+)-ATPase of sarcoplasmic reticulum.

D. Maclennan, J. Andersen, B. Vilsen, 1992, The Journal of biological chemistry.

Dissection of the Functional Differences between Sarco(endo)plasmic Reticulum Ca2+-ATPase (SERCA) 1 and 3 Isoforms by Steady-state and Transient Kinetic Analyses*

K. Van Baelen, F. Wuytack, L. Dode, 2002, The Journal of Biological Chemistry.

Fast Kinetic Analysis of Conformational Changes in Mutants of the Ca2+-ATPase of Sarcoplasmic Reticulum*

J. Andersen, B. Vilsen, T. Sørensen, 2000, The Journal of Biological Chemistry.

Mutagenesis of Sarcoplasmic Reticulum Ca(2+)-ATPase.

J. Andersen, B. Vilsen, 1998, Trends in cardiovascular medicine.

Functional consequences of mutations in the beta-strand sector of the Ca2(+)-ATPase of sarcoplasmic reticulum.

E. Leberer, D. Maclennan, J. Andersen, 1989, The Journal of biological chemistry.

Cryo‐electron microscopy of Na+,K+‐ATPase reveals how the extracellular gate locks in the E2·2K+ state

C. Toyoshima, R. Kanai, F. Cornelius, 2022, FEBS letters.

Somatic ATP 1 A 1 , ATP 2 B 3 , and KCNJ 5 Mutations in Aldosterone-Producing Adenomas

F. Beuschlein, I. Castellano, F. Veglio, 2022 .

Chapter 1 Primary ion pumps

J. Andersen, B. Vilsen, 1996 .

Deduced amino acid sequence and E1–E2 equilibrium of the sarcoplasmic reticulum Ca2+‐ATPase of frog skeletal muscle Comparison with the Ca2+‐ATPase of rabbit fast twitch muscle

J. Andersen, B. Vilsen, 1992, FEBS letters.

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

A. P. Einholm, B. Vilsen, M. Toustrup-Jensen, 2016, The Journal of Biological Chemistry.

Molecular cloning, functional expression and tissue distribution of the cDNA encoding frog skeletal muscle calsequestrin.

S. Treves, F. Zorzato, J. Andersen, 1992, The Biochemical journal.

Crystal structure of the sodium–potassium pump

P. Nissen, J. P. Morth, B. P. Pedersen, 2007, Nature.

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

Hugo Gutiérrez-de-Terán, Angel Carracedo, H. Gutiérrez‐de‐Terán, 2009, Human molecular genetics.

A structural overview of the plasma membrane Na+,K+-ATPase and H+-ATPase ion pumps

Poul Nissen, Michael G. Palmgren, P. Nissen, 2010, Nature Reviews Molecular Cell Biology.

Use of a small TSK GSW high-performance liquid chromatographic column for large-zone chromatographic studies of monomer-oligomer equilibria of membrane protein.

J. Andersen, B. Vilsen, 1988, Journal of chromatography.

Occlusion of Ca2+ in soluble monomeric sarcoplasmic reticulum Ca2+-ATPase.

J. Andersen, B. Vilsen, 1986, Biochimica et biophysica acta.

Methods for Studying Calcium Pumps

L. Missiaen, L. Raeymaekers, F. Wuytack, 2005 .

Functional consequences of alterations to amino acids located in the hinge domain of the Ca(2+)-ATPase of sarcoplasmic reticulum.

D. Maclennan, J. Andersen, B. Vilsen, 1991, Journal of Biological Chemistry.

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

L. Ozelius, A. Brashear, K. Sweadner, 2022, The Journal of biological chemistry.

Crystal structure of a Na+-bound Na+,K+-ATPase preceding the E1P state

C. Toyoshima, R. Kanai, H. Ogawa, 2013, Nature.

Binding of cardiotonic steroids to Na+,K+-ATPase in the E2P state

C. Toyoshima, R. Kanai, H. Ogawa, 2020, Proceedings of the National Academy of Sciences.

Distinct effects of Q925 mutation on intracellular and extracellular Na+ and K+ binding to the Na+, K+-ATPase

A. P. Einholm, J. Andersen, B. Vilsen, 2019, Scientific Reports.

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

A. P. Einholm, J. Andersen, B. Vilsen, 2016, Biochimica et biophysica acta.

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

A. P. Einholm, J. Andersen, B. Vilsen, 2010, The Journal of Biological Chemistry.

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

M. Sobrido, A. P. Einholm, T. Clausen, 2013, The Journal of Biological Chemistry.

Functional consequences of alterations to Pro328 and Leu332 located in the 4th transmembrane segment of the α‐subunit of the rat kidney Na+,K+‐ATPase

B. Vilsen, 1992, FEBS letters.

Asparagine 706 and Glutamate 183 at the Catalytic Site of Sarcoplasmic Reticulum Ca2+-ATPase Play Critical but Distinct Roles in E2 States*

J. Andersen, B. Vilsen, J. D. Clausen, 2006, Journal of Biological Chemistry.

Importance of Transmembrane Segment M1 of the Sarcoplasmic Reticulum Ca2+-ATPase in Ca2+ Occlusion and Phosphoenzyme Processing*

A. P. Einholm, J. Andersen, B. Vilsen, 2004, Journal of Biological Chemistry.

Importance of Conserved N-domain Residues Thr441, Glu442, Lys515, Arg560, and Leu562 of Sarcoplasmic Reticulum Ca2+-ATPase for MgATP Binding and Subsequent Catalytic Steps

J. Andersen, B. Vilsen, J. D. Clausen, 2003, Journal of Biological Chemistry.

Interaction of Nucleotides with Asp351 and the Conserved Phosphorylation Loop of Sarcoplasmic Reticulum Ca2+-ATPase*

D. Maclennan, J. Andersen, B. Vilsen, 1999, The Journal of Biological Chemistry.

Mutation Lys758 → Ile of the Sarcoplasmic Reticulum Ca2+-ATPase Enhances Dephosphorylation ofE 2 P and Inhibits theE 2 to E 1Ca2Transition*

J. Andersen, B. Vilsen, T. Sørensen, 1997, The Journal of Biological Chemistry.

Functional domains of sarcoplasmic reticulum Ca2+-ATPase studied by site-directed mutagenesis

J. Andersen, B. Vilsen, 1994 .

Functional consequences of substitution of the seven-residue segment LysIleArgAspGlnMetAla240 located in the stalk helix S3 of the Ca(2+)-ATPase of sarcoplasmic reticulum.

J. Andersen, B. Vilsen, 1993, Biochemistry.

Mutational analysis of the role of Glu309 in the sarcoplasmic reticulum Ca2+‐ATPase of frog skeletal muscle

J. Andersen, B. Vilsen, 1992, FEBS letters.

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

B. Vilsen, M. Toustrup-Jensen, Mads S. Toustrup-Jensen, 2003, The Journal of Biological Chemistry.

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

B. Vilsen, M. Toustrup-Jensen, Vivien Rodacker, 2006, Journal of Biological Chemistry.

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

P. Nissen, J. P. Morth, H. Poulsen, 2009, Philosophical Transactions of the Royal Society B: Biological Sciences.

Decreased neuronal Na+,K+‐ATPase activity in Atp1a3 heterozygous mice increases susceptibility to depression‐like endophenotypes by chronic variable stress

J. Roder, K. Saltzman, B. Vilsen, 2011, Genes, brain, and behavior.

P-type ATPases as drug targets: tools for medicine and science.

P. Nissen, J. P. Morth, M. Palmgren, 2009, Biochimica et biophysica acta.

Functional consequences of alterations to hydrophobic amino acids located at the M4S4 boundary of the Ca(2+)-ATPase of sarcoplasmic reticulum.

D. Maclennan, J. Andersen, B. Vilsen, 1991, The Journal of biological chemistry.

Alteration of intracellular Ca2+ transients in COS-7 cells transfected with the cDNA encoding skeletal-muscle ryanodine receptor carrying a mutation associated with malignant hyperthermia.

T. Steinberg, S. Treves, Michael Koval, 1994, The Biochemical journal.

Mania-like behavior induced by genetic dysfunction of the neuron-specific Na+,K+-ATPase α3 sodium pump

J. Roder, C. Burgess, M. Cortez, 2011, Proceedings of the National Academy of Sciences.

Somatic mutations in ATP1A1 and ATP2B3 lead to aldosterone-producing adenomas and secondary hypertension

T. Wieland, T. Meitinger, T. Strom, 2013, Nature Genetics.

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

P. Nissen, J. P. Morth, A. P. Einholm, 2009, The Journal of Biological Chemistry.

Mutation I810N in the α3 isoform of Na+,K+-ATPase causes impairments in the sodium pump and hyperexcitability in the CNS

C. Ackerley, J. Roder, J. Lerch, 2009, Proceedings of the National Academy of Sciences.

Functional consequences of alterations to Glu329 and other residues in the transmembrane sector of Na+/K+-ATPase

B. Vilsen, 1994 .

Localization of E1–E2 conformational transitions of sarcoplasmic reticulum Ca-ATPase by tryptic cleavage and hydrophobic labeling

J. H. Collins, P. L. Jørgensen, J. Andersen, 2005, The Journal of Membrane Biology.

Equilibrium between monomers and oligomers of soluble Ca2+‐ATPase during the functional cycle

J. Andersen, B. Vilsen, 1985, FEBS letters.

Distinct neurological disorders with ATP1A3 mutations

Mohamad A Mikati, Allison Brashear, David B Goldstein, 2014, The Lancet Neurology.

Mutant Phe788 --> Leu of the Na+,K+-ATPase is inhibited by micromolar concentrations of potassium and exhibits high Na+-ATPase activity at low sodium concentrations.

B. Vilsen, 1999, Biochemistry.

Effect of phospholipid, detergent and protein-protein interaction on stability and phosphoenzyme isomerization of soluble sarcoplasmic reticulum Ca-ATPase.

J. Andersen, B. Vilsen, 1987, European Journal of Biochemistry.

Characterization of CrATP-induced calcium occlusion in membrane-bound and soluble monomeric sarcoplasmic reticulum Ca2+-ATPase.

J. Andersen, B. Vilsen, 1987, Biochimica et biophysica acta.

Structure-function relationships of cation translocation by Ca(2+)- and Na+, K(+)-ATPases studied by site-directed mutagenesis.

J. Andersen, B. Vilsen, 1995, FEBS letters.

Radiation inactivation analysis of sarcoplasmic reticulum Ca‐ATPase in membrane‐bound form and in detergent‐solubilized monomeric states

J. Andersen, B. Vilsen, 1988, FEBS letters.

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

P. Nissen, J. P. Morth, J. Andersen, 2008, Journal of Biological Chemistry.

Localization of a K+-binding Site Involved in Dephosphorylation of the Sarcoplasmic Reticulum Ca2+-ATPase*

P. Nissen, J. Møller, J. Andersen, 2004, Journal of Biological Chemistry.

Functional consequences of proline mutations in the cytoplasmic and transmembrane sectors of the Ca2(+)-ATPase of sarcoplasmic reticulum.

D. Clarke, D. Maclennan, J. Andersen, 1989, The Journal of biological chemistry.

Disease mutations reveal residues critical to the interaction of P4-ATPases with lipid substrates

R. Molday, J. Andersen, B. Vilsen, 2017, Scientific Reports.

Specific mutations in mammalian P4‐ATPase ATP8A2 catalytic subunit entail differential glycosylation of the accessory CDC50A subunit

R. Molday, J. Coleman, J. Andersen, 2015, FEBS letters.

Role of a conserved ion-binding site tyrosine in ion selectivity of the Na+/K+ pump

J. Galpin, C. Ahern, B. Vilsen, 2022, The Journal of general physiology.

Critical role of a transmembrane lysine in aminophospholipid transport by mammalian photoreceptor P4-ATPase ATP8A2

R. Molday, J. Coleman, B. Vilsen, 2012, Proceedings of the National Academy of Sciences.

Importance of Leu99 in Transmembrane Segment M1 of the Na+,K+-ATPase in the Binding and Occlusion of K+*

A. P. Einholm, J. Andersen, B. Vilsen, 2007, Journal of Biological Chemistry.

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

B. Vilsen, M. Toustrup-Jensen, Mads S. Toustrup-Jensen, 2005, Journal of Biological Chemistry.

Mutation to the glutamate in the fourth membrane segment of Na+,K+-ATPase and Ca2+-ATPase affects cation binding from both sides of the membrane and destabilizes the occluded enzyme forms.

J. Andersen, B. Vilsen, 1998, Biochemistry.

Leucine 332 at the boundary between the fourth transmembrane segment and the cytoplasmic domain of Na+,K+-ATPase plays a pivotal role in the ion translocating conformational changes.

B. Vilsen, 1997, Biochemistry.

Arginine substitution of a cysteine in transmembrane helix M8 converts Na+,K+-ATPase to an electroneutral pump similar to H+,K+-ATPase

A. P. Einholm, J. Andersen, B. Vilsen, 2016, Proceedings of the National Academy of Sciences.

Rescue of Na+ Affinity in Aspartate 928 Mutants of Na+,K+-ATPase by Secondary Mutation of Glutamate 314*

A. P. Einholm, J. Andersen, B. Vilsen, 2015, The Journal of Biological Chemistry.

Chimeric Ca(2+)-ATPase/Na+,K(+)-ATPase molecules. Their phosphoenzyme intermediates and sensitivity to Ca2+ and thapsigargin.

J. Andersen, B. Vilsen, A. Nørregaard, 1993, FEBS letters.

Primary ion pumps.

J. Andersen, B. Vilsen, 1990, Current opinion in cell biology.

Site‐Directed Mutagenesis Analysis of the Role of the M5S5 Sector of the Sarcoplasmic Reticulum Ca2+‐ATPase a

J. Andersen, B. Vilsen, T. Sørensen, 1997 .

CORRECTIONS

M. Cortez, S. Clapcote, Y. Yücel, 1993, The Lancet.

Cryoelectron microscopy of Na+,K+-ATPase in the two E2P states with and without cardiotonic steroids

C. Toyoshima, R. Kanai, F. Cornelius, 2022, Proceedings of the National Academy of Sciences of the United States of America.

Inhibition of Phosphorylation of Na+,K+-ATPase by Mutations Causing Familial Hemiplegic Migraine*

B. Vilsen, Rikke Holm, Vivien R. Schack, 2011, The Journal of Biological Chemistry.

Crystal structures of Na+,K+‐ATPase reveal the mechanism that converts the K+‐bound form to Na+‐bound form and opens and closes the cytoplasmic gate

C. Toyoshima, R. Kanai, F. Cornelius, 2023, FEBS letters.

Amino acids Asn796 and Thr799 of the Ca(2+)-ATPase of sarcoplasmic reticulum bind Ca2+ at different sites.

J. Andersen, B. Vilsen, 1994, The Journal of biological chemistry.

Functional consequences of alterations to Glu309, Glu771, and Asp800 in the Ca(2+)-ATPase of sarcoplasmic reticulum.

J. Andersen, B. Vilsen, 1992, The Journal of biological chemistry.

Structure-function relationships of the calcium binding sites of the sarcoplasmic reticulum Ca(2+)-ATPase.

J. Andersen, B. Vilsen, 1998, Acta physiologica Scandinavica. Supplementum.

Functional consequences of mutation Asn326→Leu in the 4th transmembrane segment of the a‐subunit of the rat kidney Na+,K+‐ATPase

B. Vilsen, 1995, FEBS letters.

A Glu329→ Gln variant of the α‐subunit of the rat kidney Na+K+‐ATPase can sustain active transport of Na+ and K+ and Na+K+‐activated ATP hydrolysis with normal turnover number

B. Vilsen, 1993, FEBS letters.

Functional consequences of alterations to hydrophobic amino acids located in the M4 transmembrane sector of the Ca(2+)-ATPase of sarcoplasmic reticulum.

W. Rice, D. Clarke, D. Maclennan, 1993, The Journal of biological chemistry.

Distinct neurological disorders with ATP1A3 mutations

D. Goldstein, B. Neville, E. Heinzen, 2014, The Lancet Neurology.

Mutation I810N in the α3 isoform of Na+,K+-ATPase causes impairments in the sodium pump and hyperexcitability in the CNS

C. Ackerley, J. Roder, J. Lerch, 2009, Proceedings of the National Academy of Sciences.

Crystal structure of a Na+-bound Na+,K+-ATPase preceding the E1P state

C. Toyoshima, R. Kanai, H. Ogawa, 2013, Nature.

Arginine substitution of a cysteine in transmembrane helix M8 converts Na+,K+-ATPase to an electroneutral pump similar to H+,K+-ATPase

A. P. Einholm, J. Andersen, B. Vilsen, 2016, Proceedings of the National Academy of Sciences.

Critical roles of isoleucine-364 and adjacent residues in a hydrophobic gate control of phospholipid transport by the mammalian P4-ATPase ATP8A2

M. dal Peraro, L. Molday, R. Molday, 2014, Proceedings of the National Academy of Sciences.

Na+,K+-ATPase with Disrupted Na+ Binding Sites I and III Binds Na+ with Increased Affinity at Site II and Undergoes Na+-Activated Phosphorylation with ATP

B. Vilsen, P. Artigas, Rikke Holm, 2024, Biomolecules.

Functional Consequences of Mutations in the Transmembrane Core Region for Cation Translocation and Energy Transduction in the Na+, K+‐ATPase and the SR Ca2+‐ATPase a

J. Andersen, B. Vilsen, Dorte Ramlov, 1997, Annals of the New York Academy of Sciences.