Zobrazeno 1 - 10
of 14
pro vyhledávání: '"Marc Severin"'
Autor:
Kathrine Lundø, Oksana Dmytriyeva, Louise Spøhr, Eliana Goncalves-Alves, Jiayi Yao, Laia P. Blasco, Mette Trauelsen, Muthulakshmi Ponniah, Marc Severin, Albin Sandelin, Marie Kveiborg, Thue W. Schwartz, Stine F. Pedersen
Publikováno v:
BMC Cancer, Vol 23, Iss 1, Pp 1-20 (2023)
Abstract Background The lactate receptor GPR81 contributes to cancer development through unclear mechanisms. Here, we investigate the roles of GPR81 in three-dimensional (3D) and in vivo growth of breast cancer cells and study the molecular mechanism
Externí odkaz:
https://doaj.org/article/4dce1bc40e524fe2bbe93834d25ecd0f
Autor:
Lise M Sjøgaard-Frich, Andreas Prestel, Emilie S Pedersen, Marc Severin, Kristian Kølby Kristensen, Johan G Olsen, Birthe B Kragelund, Stine Falsig Pedersen
Publikováno v:
eLife, Vol 10 (2021)
Calmodulin (CaM) engages in Ca2+-dependent interactions with numerous proteins, including a still incompletely understood physical and functional interaction with the human Na+/H+-exchanger NHE1. Using nuclear magnetic resonance (NMR) spectroscopy, i
Externí odkaz:
https://doaj.org/article/8fa94761a445436db31f06400ba914f9
Autor:
Christina Wilkens Olesen, Jens Vogensen, Ida Axholm, Marc Severin, Julie Schnipper, Isabella Skandorff Pedersen, Jakob Hjorth von Stemann, Jacob Morville Schrøder, Dan Ploug Christensen, Stine Falsig Pedersen
Publikováno v:
Scientific Reports, Vol 8, Iss 1, Pp 1-16 (2018)
Abstract The Na+;HCO3− co-transporter NBCn1 (SLC4A7) is a major regulator of intracellular pH yet its trafficking and turnover are essentially unstudied. Here, we used MDCK-II and MCF-7 cells to investigate these processes in epithelial cells. GFP-
Externí odkaz:
https://doaj.org/article/88514809b5334da8bc2989f2186a830f
Autor:
Adélaïde Doray, Roxane Lemoine, Marc Severin, Stéphanie Chadet, Osbaldo Lopez-Charcas, Audrey Héraud, Christophe Baron, Pierre Besson, Arnaud Monteil, Stine Falsig Pedersen, Sébastien Roger
Publikováno v:
Cells, Vol 10, Iss 7, p 1624 (2021)
The SCN4B gene, coding for the NaVβ4 subunit of voltage-gated sodium channels, was recently found to be expressed in normal epithelial cells and down-regulated in several cancers. However, its function in normal epithelial cells has not been charact
Externí odkaz:
https://doaj.org/article/06e6f870a2d74cdba520fb71bbbadb45
Autor:
Mette Flinck, Sofie Hagelund, Andrej Gorbatenko, Marc Severin, Elena Pedraz-Cuesta, Ivana Novak, Christian Stock, Stine Falsig Pedersen
Publikováno v:
Cells, Vol 9, Iss 2, p 465 (2020)
Increased metabolic acid production and upregulation of net acid extrusion render pH homeostasis profoundly dysregulated in many cancers. Plasma membrane activity of vacuolar H+ ATPases (V-ATPases) has been implicated in acid extrusion and invasivene
Externí odkaz:
https://doaj.org/article/3f069b3cd9134730a7e12715e3ff9504
Autor:
Marc Severin, Emma Lind Pedersen, Magnus Thane Borre, Ida Axholm, Frederik Bendix Christiansen, Muthulakshmi Ponniah, Dominika Czaplinska, Tanja Larsen, Luis Angel Pardo, Stine Falsig Pedersen
Publikováno v:
Journal of Cell Science. 136
Finely tuned regulation of transport protein localization is vital for epithelial function. The Na+-HCO3− co-transporter NBCn1 (also known as SLC4A7) is a key contributor to epithelial pH homeostasis, yet the regulation of its subcellular localizat
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::2e8c512fce9ef322198c40e68889b7e6
https://doi.org/10.1242/jcs.260687
https://doi.org/10.1242/jcs.260687
Autor:
Marc Severin, Emma Lind Pedersen, Magnus Thane Borre, Ida Axholm, Frederik Bendix Christiansen, Muthulakshmi Ponniah, Dominika Czaplinska, Tanja Larsen, Luis Angel Pardo, Stine Falsig Pedersen
Finely tuned regulation of transport protein localization is vital for epithelial function. Sodium-bicarbonate co-transporter NBCn1 (SLC4A7) is a key contributor to epithelial pH homeostasis, yet the regulation of its subcellular localization is not
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::5fa24607e401d2af7aa0115257928549
https://doi.org/10.1101/2022.10.05.510992
https://doi.org/10.1101/2022.10.05.510992
Autor:
Emilie S Pedersen, Johan G. Olsen, Lise M. Sjøgaard-Frich, Stine F. Pedersen, Andreas Prestel, Marc Severin, Kristian Kølby Kristensen, Birthe B. Kragelund
Publikováno v:
Sjøgaard-Frich, L M, Prestel, A, Pedersen, E S, Severin, M, Kristensen, K K, Olsen, J G, Kragelund, B B & Pedersen, S F 2021, ' Dynamic Na + /H + exchanger 1 (NHE1)-calmodulin complexes of varying stoichiometry and structure regulate Ca 2+-dependent NHE1 activation ', eLife, vol. 10, e60889 . https://doi.org/10.7554/eLife.60889
eLife, Vol 10 (2021)
eLife, Vol 10 (2021)
Calmodulin (CaM) engages in Ca2+-dependent interactions with numerous proteins, including a still incompletely understood physical and functional interaction with the human Na+/H+-exchanger NHE1. Using nuclear magnetic resonance (NMR) spectroscopy, i
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::51f7d0525ea785a44ebb5867e45c3c97
https://curis.ku.dk/ws/files/260544981/elife_60889_v2.pdf
https://curis.ku.dk/ws/files/260544981/elife_60889_v2.pdf
Autor:
Johan G. Olsen, Stine F. Pedersen, Lise M. Sjøgaard-Frich, Birthe B. Kragelund, Marc Severin, Andreas Prestel, Kristian Kølby Kristensen, Emilie S Pedersen
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::967a12437c6a6228c40306718e5f4181
https://doi.org/10.7554/elife.60889.sa2
https://doi.org/10.7554/elife.60889.sa2
Autor:
Birthe B. Kragelund, Emilie S Pedersen, Lise M. Sjøgaard-Frich, Marc Severin, Stine F. Pedersen, Andreas Prestel, Johan G. Olsen
Calmodulin (CaM) engages in Ca2+-dependent interactions with numerous proteins, including human Na+/H+-exchanger NHE1. Using nuclear magnetic resonance (NMR) spectroscopy, isothermal titration calorimetry, and fibroblasts expressing wildtype and muta
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::e6db05da980eb41f577d13df4503337e
https://doi.org/10.1101/2020.08.04.236463
https://doi.org/10.1101/2020.08.04.236463