Zobrazeno 1 - 6
of 6
pro vyhledávání: '"Lise M Sjøgaard-Frich"'
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
Molecular basis for the binding and selective dephosphorylation of Na+/H+ exchanger 1 by calcineurin
Autor:
Ruth Hendus-Altenburger, Xinru Wang, Lise M. Sjøgaard-Frich, Elena Pedraz-Cuesta, Sarah R. Sheftic, Anne H. Bendsøe, Rebecca Page, Birthe B. Kragelund, Stine F. Pedersen, Wolfgang Peti
Publikováno v:
Nature Communications, Vol 10, Iss 1, Pp 1-13 (2019)
The mechanism by which Ser/Thr protein phosphatases specifically recruit and dephosphorylate their substrates is largely unclear. Hear, the authors elucidate how the Ser/Thr protein phosphatase calcineurin is recruited to its substrate NHE1 and how s
Externí odkaz:
https://doaj.org/article/5e565aa376cd44bab46f43a617043caa
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
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::3a76261a1c0b0cae9dde9830dbd4d4c4
https://pubmed.ncbi.nlm.nih.gov/33655882
https://pubmed.ncbi.nlm.nih.gov/33655882