Zobrazeno 1 - 6
of 6
pro vyhledávání: '"Emilie S Pedersen"'
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:
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
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
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
Autor:
Nanditha Shyam Prasad, Jens Vogensen, Stine F. Pedersen, Marité Cárdenas, Ruth Hendus-Altenburger, Birthe B. Kragelund, Elena Pedraz-Cuesta, Emilie S Pedersen, Raul Araya-Secchi, Anne H. Bendsoe, Alessandra Luchini, Lise Arleth, Andreas Prestel
Publikováno v:
Hendus-Altenburger, R, Vogensen, J, Pedersen, E S, Luchini, A, Araya-Secchi, R, Bendsoe, A H, Prasad, N S, Prestel, A, Cardenas, M, Pedraz-Cuesta, E, Arleth, L, Pedersen, S H F & Kragelund, B B 2020, ' The intracellular lipid-binding domain of human Na + /H + exchanger 1 forms a lipid-protein co-structure essential for activity ', Communications Biology, vol. 3, no. 1, 731 . https://doi.org/10.1038/s42003-020-01455-6
Communications Biology
Communications Biology
Dynamic interactions of proteins with lipid membranes are essential regulatory events in biology, but remain rudimentarily understood and particularly overlooked in membrane proteins. The ubiquitously expressed membrane protein Na+/H+-exchanger 1 (NH
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::334005090442e757ab4e4672536ac7b8
http://urn.kb.se/resolve?urn=urn:nbn:se:mau:diva-37152
http://urn.kb.se/resolve?urn=urn:nbn:se:mau:diva-37152