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of 2
pro vyhledávání: '"Anne H. Bendsoe"'
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:
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