Zobrazeno 1 - 5
of 5
pro vyhledávání: '"Louise S. Mogensen"'
Autor:
Francesco Tadini‐Buoninsegni, Stine A. Mikkelsen, Louise S. Mogensen, Rikke Holm, Robert S. Molday, Jens Peter Andersen
Publikováno v:
Tadini-Buoninsegni, F, Mikkelsen, S, Mogensen, L, Holm, R, Molday, R S & Andersen, J P 2023, ' Electrogenic reaction step and phospholipid translocation pathway of the mammalian P4-ATPase ATP8A2 ', FEBS Letters, vol. 597, no. 4, pp. 495-503 . https://doi.org/10.1002/1873-3468.14459
ATP8A2 is a mammalian P4-ATPase (flippase) that translocates the negatively charged lipid substrate phosphatidylserine from the exoplasmic leaflet to the cytoplasmic leaflet of cellular membranes. Using an electrophysiological method based on solid s
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::95be0ed70dd1692d08ab046c2b12defe
https://pure.au.dk/portal/da/publications/electrogenic-reaction-step-and-phospholipid-translocation-pathway-of-the-mammalian-p4atpase-atp8a2(000cab4d-9ad0-4048-b947-202201082f54).html
https://pure.au.dk/portal/da/publications/electrogenic-reaction-step-and-phospholipid-translocation-pathway-of-the-mammalian-p4atpase-atp8a2(000cab4d-9ad0-4048-b947-202201082f54).html
Autor:
Stine A. Mikkelsen, Bente Vilsen, Jens Peter Andersen, Rasmus Gantzel, Anna L. Vestergaard, Louise S Mogensen, Robert S. Molday
Publikováno v:
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-z
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-z
Phospholipid flippases (P4-ATPases) translocate specific phospholipids from the exoplasmic to the cytoplasmic leaflet of membranes. While there is good evidence that the overall molecular structure of flippases is similar to that of P-type ATPase ion
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::aeb049f3898290add340eaf71d8d73c9
http://link.springer.com/article/10.1038/s41598-017-10741-z
http://link.springer.com/article/10.1038/s41598-017-10741-z
Autor:
Louise S Mogensen, Francesco Tadini-Buoninsegni, Robert S. Molday, Stine A. Mikkelsen, Jens Peter Andersen
Publikováno v:
Tadini-Buoninsegni, F, Mikkelsen, S A, Mogensen, L S, Molday, R S & Andersen, J P 2019, ' Phosphatidylserine flipping by the P4-ATPase ATP8A2 is electrogenic ', Proceedings of the National Academy of Sciences of the United States of America, vol. 116, no. 33, pp. 16332-16337 . https://doi.org/10.1073/pnas.1910211116
Phospholipid flippases (P4-ATPases) utilize ATP to translocate specific phospholipids from the exoplasmic leaflet to the cytoplasmic leaflet of biological membranes, thus generating and maintaining transmembrane lipid asymmetry essential for a variet
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::6d6f1645dbf52d6c43620ddb98c7891f
https://pure.au.dk/portal/da/publications/phosphatidylserine-flipping-by-the-p4atpase-atp8a2-is-electrogenic(ad73d2f3-5787-4ac1-bbcb-777134f3f740).html
https://pure.au.dk/portal/da/publications/phosphatidylserine-flipping-by-the-p4atpase-atp8a2-is-electrogenic(ad73d2f3-5787-4ac1-bbcb-777134f3f740).html
Autor:
Louise S Mogensen, Robert S. Molday, Stine A. Mikkelsen, Jens Peter Andersen, Bente Vilsen, Anna L. Vestergaard
Publikováno v:
Mikkelsen, S A, Mogensen, L S, Vilsen, B, Molday, R S, Vestergaard, A L & Andersen, J P 2019, ' Asparagine-905 of the mammalian phospholipid flippase ATP8A2 is essential for lipid substrate-induced activation of ATP8A2 dephosphorylation ', Journal of Biological Chemistry, vol. 294, no. 15, pp. 5970-5979 . https://doi.org/10.1074/jbc.RA118.007240
The P-type ATPase protein family includes, in addition to ion pumps such as Ca(2+)-ATPase and Na(+),K(+)-ATPase, also phospholipid flippases that transfer phospholipids between membrane leaflets. P-type ATPase ion pumps translocate their substrates o
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::046c435946ec05d3e30aa5c69e80cb34
https://pure.au.dk/portal/da/publications/asparagine905-of-the-mammalian-phospholipid-flippase-atp8a2-is-essential-for-lipid-substrateinduced-activation-of-atp8a2-dephosphorylation(40a2f586-c05f-4f31-ae96-2f6c19a43f41).html
https://pure.au.dk/portal/da/publications/asparagine905-of-the-mammalian-phospholipid-flippase-atp8a2-is-essential-for-lipid-substrateinduced-activation-of-atp8a2-dephosphorylation(40a2f586-c05f-4f31-ae96-2f6c19a43f41).html
Autor:
Jens Peter Andersen, Robert S. Molday, Anna L. Vestergaard, Louise S Mogensen, Stine A. Mikkelsen, Madhavan Chalat
Publikováno v:
Frontiers in Physiology
P4-ATPases comprise a family of P-type ATPases that actively transport or flip phospholipids across cell membranes. This generates and maintains membrane lipid asymmetry, a property essential for a wide variety of cellular processes such as vesicle b
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::632010a83b0148a4e13e599c15f8c6cd
https://pubmed.ncbi.nlm.nih.gov/27458383
https://pubmed.ncbi.nlm.nih.gov/27458383