Zobrazeno 1 - 5
of 5
pro vyhledávání: '"Maike, Bublitz"'
Autor:
Hok-Sau Kwong, Maike Bublitz, Claus Olesen, Vitaliy Mykhaylyk, Armin Wagner, Jesper V. Møller, Konstantinos Beis, Nada Mohamad, R. Duman, Kiran Bountra, Katja Schlegel, Maria Romano, Kamel El Omari
Publikováno v:
El Omari, K, Mohamad, N, Bountra, K, Duman, R, Romano, M, Schlegel, K, Kwong, H S, Mykhaylyk, V, Olesen, C, Moller, J V, Bublitz, M, Beis, K & Wagner, A 2020, ' Experimental phasing with vanadium and application to nucleotide-binding membrane proteins ', IUCrJ, vol. 7, pp. 1092-1101 . https://doi.org/10.1107/S2052252520012312
IUCrJ
IUCrJ, Vol 7, Iss 6, Pp 1092-1101 (2020)
IUCrJ
IUCrJ, Vol 7, Iss 6, Pp 1092-1101 (2020)
Crystal structure determination of membrane proteins can be challenging. Here, the use of vanadium phasing as an alternative experimental phasing method is described.
The structure determination of soluble and membrane proteins can be hindered b
The structure determination of soluble and membrane proteins can be hindered b
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::a28328d9c9902e5aac0e2af9ca97c9b7
https://pure.au.dk/portal/da/publications/experimental-phasing-with-vanadium-and-application-to-nucleotidebinding-membrane-proteins(dcfd4d87-3c0b-48c7-bd03-b434a797e37e).html
https://pure.au.dk/portal/da/publications/experimental-phasing-with-vanadium-and-application-to-nucleotidebinding-membrane-proteins(dcfd4d87-3c0b-48c7-bd03-b434a797e37e).html
Autor:
Johannes D. Clausen, Jens Peter Andersen, Maike Bublitz, Jesper V. Møller, Poul Nissen, Bertrand Arnou, Claus Olesen
Publikováno v:
Clausen, J D, Bublitz, M, Arnou, B J-P, Olesen, C, Andersen, J P, Møller, J V & Nissen, P 2016, ' Crystal Structure of the Vanadate-Inhibited Ca 2+-ATPase ', Structure, vol. 24, no. 4, pp. 617-623 . https://doi.org/10.1016/j.str.2016.02.018
Vanadate is the hallmark inhibitor of the P-type ATPase family; however, structural details of its inhibitory mechanism have remained unresolved. We have determined the crystal structure of sarcoplasmic reticulum Ca(2+)-ATPase with bound vanadate in
Autor:
Ole G. Mouritsen, Hanne Poulsen, J. Preben Morth, Himanshu Khandelia, Jan Egebjerg, Maike Bublitz, Poul Nissen
Publikováno v:
Poulsen, H, Khandelia, H, Morth, J P, Bublitz, M, Mouritsen, O G, Egebjerg, J & Nissen, P 2010, ' Neurological disease mutations compromise a C-terminal ion pathway in the Na(+)/K(+)-ATPase ', Nature, vol. 467, no. 7311, pp. 99-102 . https://doi.org/10.1038/nature09309
Nature
Nature
The Na+/K+-ATPase enzyme pumps three sodium ions out of the cell and two potassium ions into the cell while splitting a single molecule of ATP. This process generates the chemical gradients across the plasma membrane that are essential to electrical
Autor:
Birgit Schiøtt, Lea Thøgersen, Maria Musgaard, Poul Nissen, Jesper V. Møller, J. Preben Morth, Claus Olesen, Maike Bublitz, Hanne Poulsen
Publikováno v:
Bublitz, M, Musgaard, M, Poulsen, H, Thøgersen, L, Olesen, C, Schiøtt, B, Morth, P, Møller, J V & Nissen, P 2013, ' Ion Pathways in the Sarcoplasmic Reticulum Ca 2+-ATPase ', Journal of Biological Chemistry, vol. 288, pp. 10759-10765 . https://doi.org/10.1074/jbc.R112.436550
The sarco/endoplasmic reticulum Ca(2+)-ATPase (SERCA) is a transmembrane ion transporter belonging to the P(II)-type ATPase family. It performs the vital task of re-sequestering cytoplasmic Ca(2+) to the sarco/endoplasmic reticulum store, thereby als
Publikováno v:
Bublitz, M, Morth, J P & Nissen, P 2011, ' P-type ATPases at a glance ', Journal of Cell Science, vol. 124, no. Pt 15, pp. 2515-9 . https://doi.org/10.1242/jcs.088716
Journal of Cell Science
Journal of Cell Science
P-type ATPases are a large family of integral membrane transporters that are of vital importance in all kingdoms of life. In eponymous distinction from the other main classes of transport ATPase – the FF1 (F-), the vacuolar (V-) and the ATP-binding