Zobrazeno 1 - 10
of 18
pro vyhledávání: '"Ruth Hendus-Altenburger"'
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:
Signe M. Schenstrøm, Caio A. Rebula, Michael H. Tatham, Ruth Hendus-Altenburger, Isabelle Jourdain, Ronald T. Hay, Birthe B. Kragelund, Rasmus Hartmann-Petersen
Publikováno v:
Cell Reports, Vol 25, Iss 4, Pp 862-870 (2018)
Summary: Dss1 (also known as Sem1) is a conserved, intrinsically disordered protein with a remarkably broad functional diversity. It is a proteasome subunit but also associates with the BRCA2, RPA, Csn12-Thp1, and TREX-2 complexes. Accordingly, Dss1
Externí odkaz:
https://doaj.org/article/a5aeda8ecbde481c8d4936444ea5853b
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
Autor:
Stine F. Pedersen, Kresten Lindorff-Larsen, Birthe B. Kragelund, Thilde Terkelsen, Ruth Hendus-Altenburger, Elena Papaleo, Matteo Lambrughi
Publikováno v:
Hendus-Altenburger, R, Lambrughi, M, Terkelsen, T B, Pedersen, S H F, Papaleo, E, Lindorff-Larsen, K & Kragelund, B B 2017, ' A phosphorylation-motif for tuneable helix stabilisation in intrinsically disordered proteins-Lessons from the sodium proton exchanger 1 (NHE1) ', Cellular Signalling, vol. 37, pp. 40-51 . https://doi.org/10.1016/j.cellsig.2017.05.015
Intrinsically disordered proteins (IDPs) are involved in many pivotal cellular processes including phosphorylation and signalling. The structural and functional effects of phosphorylation of IDPs remain poorly understood and difficult to predict. Thu
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::a5494636ed16f9a0821b476a2f591785
https://doi.org/10.1016/j.cellsig.2017.05.015
https://doi.org/10.1016/j.cellsig.2017.05.015
Autor:
Nanna Wickmann, Birthe B. Kragelund, Wouter Boomsma, Karen Skriver, Lasse Staby, Andreas Prestel, Ruth Hendus-Altenburger, João M. Martins
Publikováno v:
University of Copenhagen
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::0f6a4decacc25f986754aae70654f3bf
https://doi.org/10.1016/j.bpj.2019.11.2720
https://doi.org/10.1016/j.bpj.2019.11.2720
Autor:
Andreas, Prestel, Katrine, Bugge, Lasse, Staby, Ruth, Hendus-Altenburger, Birthe B, Kragelund
Publikováno v:
Methods in enzymology. 611
NMR spectroscopy has proven to be a key method for studying intrinsically disordered proteins (IDPs). Nonetheless, traditional NMR methods developed for solving structures of ordered protein complexes are insufficient for the full characterization of
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::492457fc3d5b568d685f03a88b9deb9b
https://pubmed.ncbi.nlm.nih.gov/30471688
https://pubmed.ncbi.nlm.nih.gov/30471688
Autor:
Rasmus Hartmann-Petersen, Ruth Hendus-Altenburger, Michael H. Tatham, Caio A. Rebula, Isabelle Jourdain, Signe M. Schenstrøm, Birthe B. Kragelund, Ronald T. Hay
Publikováno v:
Schenstrøm, S M, Rebula, C A, Tatham, M H, Hendus-Altenburger, R, Jourdain, I, Hay, R T, Kragelund, B B & Hartmann-Petersen, R 2018, ' Expanded Interactome of the Intrinsically Disordered Protein Dss1 ', Cell Reports, vol. 25, no. 4, pp. 862-870 . https://doi.org/10.1016/j.celrep.2018.09.080
Cell Reports
Cell Reports, Vol 25, Iss 4, Pp 862-870 (2018)
Cell Reports
Cell Reports, Vol 25, Iss 4, Pp 862-870 (2018)
Summary Dss1 (also known as Sem1) is a conserved, intrinsically disordered protein with a remarkably broad functional diversity. It is a proteasome subunit but also associates with the BRCA2, RPA, Csn12-Thp1, and TREX-2 complexes. Accordingly, Dss1 f
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::3e4aeca9a7084ecce156a1cdd738aa5d
https://curis.ku.dk/portal/da/publications/expanded-interactome-of-the-intrinsically-disordered-protein-dss1(35864465-0f92-49cf-b1e0-fe9d263cdfb2).html
https://curis.ku.dk/portal/da/publications/expanded-interactome-of-the-intrinsically-disordered-protein-dss1(35864465-0f92-49cf-b1e0-fe9d263cdfb2).html
NMR spectroscopy has proven to be a key method for studying intrinsically disordered proteins (IDPs). Nonetheless, traditional NMR methods developed for solving structures of ordered protein complexes are insufficient for the full characterization of
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::6f0862d87bf815af01cd033ed56378ec
https://doi.org/10.1016/bs.mie.2018.08.026
https://doi.org/10.1016/bs.mie.2018.08.026
Autor:
Stine F. Pedersen, Ruth Hendus-Altenburger, Birthe B. Kragelund, Elena Papaleo, Christina W. Olesen, Jeff A. Schnell, Elena Pedraz-Cuesta, Jonathan T. S. Hopper, Carol V. Robinson
Publikováno v:
BMC Biology
Hendus-Altenburger, R, Pedraz Cuesta, E, Olesen, C W, Papaleo, E, Schnell, J A, Hopper, J T S, Robinson, C V, Pedersen, S H F & Kragelund, B B 2016, ' The human Na + /H + exchanger 1 is a membrane scaffold protein for extracellular signal-regulated kinase 2 ', BMC Biology, vol. 14, 31 . https://doi.org/10.1186/s12915-016-0252-7
Hendus-Altenburger, R, Pedraz Cuesta, E, Olesen, C W, Papaleo, E, Schnell, J A, Hopper, J T S, Robinson, C V, Pedersen, S H F & Kragelund, B B 2016, ' The human Na + /H + exchanger 1 is a membrane scaffold protein for extracellular signal-regulated kinase 2 ', BMC Biology, vol. 14, 31 . https://doi.org/10.1186/s12915-016-0252-7
Background Extracellular signal-regulated kinase 2 (ERK2) is an S/T kinase with more than 200 known substrates, and with critical roles in regulation of cell growth and differentiation and currently no membrane proteins have been linked to ERK2 scaff
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::be983ff3d12679027a1b840e38faa4ff
http://europepmc.org/articles/PMC4833948
http://europepmc.org/articles/PMC4833948
Autor:
Rickard Nilsson, Emma Salomonsson, Christopher T. Öberg, Michael C. Carlsson, Barbro Kahl-Knutson, Anna Karlsson, Eva Nordberg-Karlsson, Hakon Leffler, Ulf J. Nilsson, Veronica Osla, James M. Rini, Anders Sundin, Ruth Hendus-Altenburger
Publikováno v:
The Journal of Biological Chemistry
Galectins are defined by a conserved β-galactoside binding site that has been linked to many of their important functions in e.g. cell adhesion, signaling, and intracellular trafficking. Weak adjacent sites may enhance or decrease affinity for natur
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::a43adf36fef41c6f1cc3aafef55b1a5b
http://europepmc.org/articles/PMC2966122
http://europepmc.org/articles/PMC2966122