World's Best Scientists 2026 revealed!
Bente Vilsen

Bente Vilsen

D-Index & Metrics

Chemistry

D-Index
51
Citations
7271
World Ranking
14176
National Ranking
115

Biology and Biochemistry

D-Index
56
Citations
8954
World Ranking
14653
National Ranking
163

Overview

Bente Vilsen is affiliated with Aarhus University in Denmark. Their research primarily spans the field of Biochemistry, Genetics and Molecular Biology, with a focus on subfields such as Molecular Biology, Clinical Biochemistry, Cellular and Molecular Neuroscience, Psychiatry and Mental Health, and Endocrinology, Diabetes and Metabolism.

The scientist's work extensively covers several key topics, including:

  • Ion Transport and Channel Regulation
  • ATP Synthase and ATPases Research
  • Ion Channel Regulation and Function
  • Mitochondrial Function and Pathology
  • Metabolism and Genetic Disorders
  • Photosynthetic Processes and Mechanisms
  • Neuroscience and Neuropharmacology Research

Bente Vilsen has contributed to a number of recent papers, published from 2020 to 2023, in notable scientific journals:

  • ATP1A2- and ATP1A3-associated early profound epileptic encephalopathy and polymicrogyria, 2021, Brain
  • Binding of cardiotonic steroids to Na +,K +-ATPase in the E2P state, 2020, Proceedings of the National Academy of Sciences
  • Cryoelectron microscopy of Na +,K +-ATPase in the two E2P states with and without cardiotonic steroids, 2022, Proceedings of the National Academy of Sciences
  • On the track of the lipid transport pathway of the phospholipid flippase ATP8A2 - Mutation analysis of residues of the transmembrane segments M1, M2, M3 and M4, 2023, Biochimica et Biophysica Acta (BBA) - Molecular Cell Research
  • Temperature instability of a mutation at a multidomain junction in Na,K-ATPase isoform ATP1A3 (p.Arg756His) produces a fever-induced neurological syndrome, 2022, Journal of Biological Chemistry

The frequent publication venues for Vilsen's work include:

  • Proceedings of the National Academy of Sciences
  • FEBS Letters
  • Brain
  • Biochimica et Biophysica Acta (BBA) - Molecular Cell Research
  • Journal of Biological Chemistry

Collaborations have been a component of Vilsen's research, with regular co-authors including:

  • Rikke Holm
  • R. Kanai
  • Flemming Cornelius
  • Chikashi Toyoshima
  • Hang N. Nielsen

Best Publications

  • Crystal structure of the sodium–potassium pump

    J. Preben Morth;J. Preben Morth;Bjørn P. Pedersen;Bjørn P. Pedersen;Mads S. Toustrup-Jensen;Mads S. Toustrup-Jensen;Thomas L.-M. Sørensen

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

    Felix Beuschlein;Sheerazed Boulkroun;Sheerazed Boulkroun;Andrea Osswald;Thomas Wieland

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

    J. Preben Morth;Bjørn P. Pedersen;Bjørn P. Pedersen;Bjørn P. Pedersen;Morten J. Buch-Pedersen;Morten J. Buch-Pedersen;Jens Peter Andersen;Jens Peter Andersen

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

    Ryuta Kanai;Haruo Ogawa;Bente Vilsen;Flemming Cornelius

  • Distinct neurological disorders with ATP1A3 mutations

    Erin L Heinzen;Alexis Arzimanoglou;Allison Brashear;Steven J Clapcote

  • 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.

    Leonard Dode;Jens Peter Andersen;Natalie Leslie;Jittima Dhitavat

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

    Tracy Ann Williams;Silvia Monticone;Vivien R. Schack;Julia Stindl

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

    Steven J. Clapcote;Steven Duffy;Gang Xie;Greer Kirshenbaum

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

    B Vilsen;J P Andersen;D M Clarke;D H MacLennan

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

    Laure Yatime;Morten J. Buch-Pedersen;Morten J. Buch-Pedersen;Maria Musgaard;J. Preben Morth;J. Preben Morth

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

    Greer S. Kirshenbaum;Steven J. Clapcote;Steven Duffy;Christian R. Burgess

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

    Jens Peter Anderssen;Bente Vilsen

  • Dissection of the functional differences between sarco(endo)plasmic reticulum Ca2+-ATPase (SERCA) 1 and 3 isoforms by steady-state and transient kinetic analyses.

    Leonard Dode;Bente Vilsen;Kurt Van Baelen;Frank Wuytack

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

    B Vilsen;J P Andersen;D H MacLennan

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

    Anna L. Vestergaard;Jonathan A. Coleman;Thomas Lemmin;Stine A. Mikkelsen

  • 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.

    Bente Vilsen;Jens Peter Andersen

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

    J P Andersen;B Vilsen

  • Mutant Glu781 .fwdarw. 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

    Bente Vilsen

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

    J. Preben Morth;Hanne Poulsen;Mads S Toustrup-Jensen;Vivien Rodacker Schack

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

    G. S. Kirshenbaum;G. S. Kirshenbaum;K. Saltzman;B. Rose;J. Petersen

  • Crystal structure of a Na+-bound Na+,K+-ATPase preceding the E1P state without oligomycin

    R. Kanai;H. Ogawa;B. Vilsen;F. Cornelius

Frequent Co-Authors

Jens Peter Andersen
Jens Peter Andersen Aarhus University
Poul Nissen
Poul Nissen Aarhus University
Chikashi Toyoshima
Chikashi Toyoshima University of Tokyo
Robert S. Molday
Robert S. Molday University of British Columbia
John C. Roder
John C. Roder University of Toronto
Jesper V. Møller
Jesper V. Møller Aarhus University
David H. MacLennan
David H. MacLennan University of Toronto
Frank Wuytack
Frank Wuytack KU Leuven
Michael G. Palmgren
Michael G. Palmgren University of Copenhagen

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