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1دورية أكاديمية
المؤلفون: Hang N. Nielsen, Rikke Holm, Ryan Sweazey, Jens Peter Andersen, Pablo Artigas, Bente Vilsen
المصدر: Biomolecules, Vol 14, Iss 1, p 135 (2024)
مصطلحات موضوعية: Na+,K+-pump, Na+ site, K+ site, Na+ affinity, K+ affinity, P-type ATPase, Microbiology, QR1-502
وصف الملف: electronic resource
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2
المؤلفون: Ryuta Kanai, Flemming Cornelius, Bente Vilsen, Chikashi Toyoshima
المصدر: FEBS Letters. 596:2513-2524
مصطلحات موضوعية: Structural Biology, Genetics, Biophysics, Cell Biology, Molecular Biology, Biochemistry
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المؤلفون: Kerri Spontarelli, Daniel T. Infield, Hang N. Nielsen, Rikke Holm, Victoria C. Young, Jason D. Galpin, Christopher A. Ahern, Bente Vilsen, Pablo Artigas
المصدر: Spontarelli, K, Infield, D T, Nielsen, H N, Holm, R, Young, V C, Galpin, J D, Ahern, C A, Vilsen, B & Artigas, P 2022, ' Role of a conserved ion-binding site tyrosine in ion selectivity of the Na + /K + pump ', Journal of General Physiology, vol. 154, no. 7, e202113039 . https://doi.org/10.1085/jgp.202113039
Spontarelli, K, Infield, D T, Nielsen, H N, Holm, R, Young, V C, Galpin, J D, Ahern, C A, Vilsen, B & Artigas, P 2022, ' Role of a conserved ion-binding site tyrosine in ion selectivity of the Na/K pump ', pp. 27 . < https://www.cell.com/biophysj/pdf/S0006-3495(21)03555-4.pdf >مصطلحات موضوعية: Binding Sites, Physiology, Cations, Sodium, Potassium, Biophysics, Animals, Tyrosine, Sodium-Potassium-Exchanging ATPase
URL الوصول: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::3eef491355124e8ee3bbb378878c337a
https://pure.au.dk/portal/da/publications/role-of-a-conserved-ionbinding-site-tyrosine-in-ion-selectivity-of-the-nak-pump(bfb93d49-7234-4b6b-bbca-43b48d5d24fd).html -
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المؤلفون: Ryuta, Kanai, Flemming, Cornelius, Bente, Vilsen, Chikashi, Toyoshima
المصدر: Proceedings of the National Academy of Sciences of the United States of America. 119(15)
مصطلحات موضوعية: Cardiac Glycosides, Adenosine Triphosphate, Cardiotonic Agents, Protein Domains, Cations, Cryoelectron Microscopy, Etiocholanolone, Sodium, Magnesium, Sodium-Potassium-Exchanging ATPase, Ouabain
URL الوصول: https://explore.openaire.eu/search/publication?articleId=pmid________::c29e6b52c42fd305a6cbff94407e357c
https://pubmed.ncbi.nlm.nih.gov/35380894 -
5Cryoelectron microscopy of Na+,K+-ATPase in the two E2P states with and without cardiotonic steroids
المؤلفون: Ryuta Kanai, Flemming Cornelius, Bente Vilsen, Chikashi Toyoshima
المصدر: Kanai, R, Cornelius, F, Vilsen, B & Toyoshima, C 2022, ' Cryoelectron microscopy of Na +,K +-ATPase in the two E2P states with and without cardiotonic steroids ', PNAS (Proceedings of the National Academy of Sciences of the United States of America), vol. 119, no. 15, e2123226119 . https://doi.org/10.1073/pnas.2123226119
مصطلحات موضوعية: Multidisciplinary, cardiotonic steroids, sodium pump, cryoelectron microscopy, Na+,K+-ATPase
URL الوصول: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::7c1b6e220a20ae95495f7eae7806b003
https://pure.au.dk/portal/da/publications/cryoelectron-microscopy-of-nakatpase-in-the-two-e2p-states-with-and-without-cardiotonic-steroids(336736ba-7afe-41e3-b4ff-7afcc9b0b5dd).html -
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المؤلفون: Ryuta Kanai, Flemming Cornelius, Kanna Motoyama, Bente Vilsen, Haruo Ogawa, Chikashi Toyoshima
المصدر: Kanai, R, Cornelius, F, Ogawa, H, Motoyama, K, Vilsen, B & Toyoshima, C 2021, ' Binding of cardiotonic steroids to Na +,K +-ATPase in the E2P state ', Proceedings of the National Academy of Sciences of the United States of America, vol. 118, no. 1, 2020438118 . https://doi.org/10.1073/pnas.2020438118
Kanai, R, Cornelius, F, Ogawa, H, Motoyama, K, Vilsen, B & Toyoshima, C 2021, ' Binding of cardiotonic steroids to Na +,K +-ATPase in the E2P state ', Proceedings of the National Academy of Sciences of the United States of America, vol. 118, no. 1, e2020438118 . https://doi.org/10.1073/pnas.2020438118مصطلحات موضوعية: 030110 physiology, 0301 basic medicine, Gene isoform, K+-ATPASE, P-I, OUABAIN, NA+, Inhibitory postsynaptic potential, Ouabain, SODIUM-POTASSIUM PUMP, Cell membrane, INORGANIC-PHOSPHATE, 03 medical and health sciences, crystal structures, sodium pump, medicine, CRYSTAL-STRUCTURE, Na+/K+-ATPase, Cardiotonic steroids, Multidisciplinary, Chemistry, isoform specificity, respiratory system, Na+,K+-ATPase, 030104 developmental biology, Istaroxime, medicine.anatomical_structure, cardiotonic steroids, LIGAND-BINDING, Biophysics, SITE-DIRECTED MUTAGENESIS, Sodium pump, NA,K-ATPASE ALPHA-SUBUNIT, medicine.drug
URL الوصول: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::521d5eef2fd6c207f669b9901d57cd01
https://pure.au.dk/portal/da/publications/binding-of-cardiotonic-steroids-to-nakatpase-in-the-e2p-state(2e957c44-03f9-4c8f-8283-f06307775924).html -
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المؤلفون: Ryuta, Kanai, Flemming, Cornelius, Haruo, Ogawa, Kanna, Motoyama, Bente, Vilsen, Chikashi, Toyoshima
المصدر: Proc Natl Acad Sci U S A
مصطلحات موضوعية: Cardiac Glycosides, Models, Molecular, Digoxin, Sodium, Molecular Conformation, Animals, Protein Isoforms, respiratory system, Sodium-Potassium-Exchanging ATPase, Biological Sciences, Ouabain, Biophysical Phenomena
URL الوصول: https://explore.openaire.eu/search/publication?articleId=pmid________::6842cd69c8d2a81c0285e21c002d88ae
https://pubmed.ncbi.nlm.nih.gov/33318128 -
8دورية أكاديمية
المؤلفون: Carina Henriksen, Kasper Kjaer-Sorensen, Anja Pernille Einholm, Lone Bruhn Madsen, Jamal Momeni, Christian Bendixen, Claus Oxvig, Bente Vilsen, Knud Larsen
المصدر: PLoS ONE, Vol 8, Iss 11, p e79127 (2013)
وصف الملف: electronic resource
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المؤلفون: Kerri Spontarelli, Anja P. Einholm, Hang N Nielsen, Pablo Artigas, Jens Peter Andersen, Bente Vilsen, Rikke Holm
المصدر: Scientific Reports, Vol 9, Iss 1, Pp 1-14 (2019)
Nielsen, H N, Spontarelli, K, Holm, R, Andersen, J P, Einholm, A P, Artigas, P & Vilsen, B 2019, ' Distinct effects of Q925 mutation on intracellular and extracellular Na+ and K+ binding to the Na+, K+-ATPase ', Scientific Reports, vol. 9, no. 1, 13344 . https://doi.org/10.1038/s41598-019-50009-2مصطلحات موضوعية: 0301 basic medicine, Multidisciplinary, Stereochemistry, Chemistry, lcsh:R, Mutant, Mutagenesis, lcsh:Medicine, Gating, 03 medical and health sciences, Transmembrane domain, 030104 developmental biology, 0302 clinical medicine, Protein structure, TheoryofComputation_ANALYSISOFALGORITHMSANDPROBLEMCOMPLEXITY, Extracellular, lcsh:Q, Na+/K+-ATPase, lcsh:Science, 030217 neurology & neurosurgery, Intracellular
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المؤلفون: Stine A. Mikkelsen, Bente Vilsen, Jens Peter Andersen, Rasmus Gantzel, Anna L. Vestergaard, Louise S Mogensen, Robert S. Molday
المصدر: Scientific Reports, Vol 7, Iss 1, Pp 1-11 (2017)
Scientific Reports
Gantzel, R H, Mogensen, L S, Mikkelsen, S A, Vilsen, B, Molday, R S, Vestergaard, A L & Andersen, J P 2017, ' Disease mutations reveal residues critical to the interaction of P4-ATPases with lipid substrates ', Scientific Reports, vol. 7, no. 1, doi: 10.1038/s41598-017-10741-z., pp. 10418 . https://doi.org/10.1038/s41598-017-10741-z
Gantzel, R H, Mogensen, L S, Mikkelsen, S A, Vilsen, B, Molday, R S, Vestergaard, A L & Andersen, J P 2017, ' Disease mutations reveal residues critical to the interaction of P4-ATPases with lipid substrates ', Scientific Reports, vol. 7, 10418 . https://doi.org/10.1038/s41598-017-10741-zمصطلحات موضوعية: 0301 basic medicine, Models, Molecular, Arginine, Protein Conformation, Phospholipid, Gene Expression, lcsh:Medicine, Plasma protein binding, Article, Substrate Specificity, 03 medical and health sciences, chemistry.chemical_compound, Structure-Activity Relationship, Protein structure, Phosphatidylcholine, Journal Article, Animals, Genetic Predisposition to Disease, Phospholipid Transfer Proteins, lcsh:Science, Phospholipids, Adenosine Triphosphatases, Multidisciplinary, Binding Sites, lcsh:R, Flippase, Phosphatidylserine, Lipid Metabolism, Enzyme Activation, Transmembrane domain, 030104 developmental biology, chemistry, Mutation, Biophysics, Cattle, lcsh:Q, Protein Binding
وصف الملف: application/pdf