Zobrazeno 1 - 5
of 5
pro vyhledávání: '"Maximilian Wallbott"'
Autor:
Jascha T. Manschwetus, Maximilian Wallbott, Alexandra Fachinger, Claudia Obergruber, Sabine Pautz, Daniela Bertinetti, Sven H. Schmidt, Friedrich W. Herberg
Publikováno v:
Frontiers in Neuroscience, Vol 14 (2020)
Proteins of the 14-3-3 family are well known modulators of the leucine-rich repeat kinase 2 (LRRK2) regulating kinase activity, cellular localization, and ubiquitylation. Although binding between those proteins has been investigated, a comparative st
Externí odkaz:
https://doaj.org/article/5be20f9c0f714af0be35aee3436feb13
Autor:
Matthias J. Knape, Maximilian Wallbott, Nicole C. G. Burghardt, Daniela Bertinetti, Jan Hornung, Sven H. Schmidt, Robin Lorenz, Friedrich W. Herberg
Publikováno v:
Cells, Vol 9, Iss 6, p 1548 (2020)
cAMP-dependent protein kinase (PKA) is the major receptor of the second messenger cAMP and a prototype for Ser/Thr-specific protein kinases. Although PKA strongly prefers serine over threonine substrates, little is known about the molecular basis of
Externí odkaz:
https://doaj.org/article/805e36a159e441b8a7fbffef26b07b35
Autor:
Bjørn Steen Skålhegg, Susan S. Taylor, Lily Vu, Maximilian Wallbott, Jian Wu, Jessica G.H. Bruystens, Friedrich W. Herberg, Erik M F Machal, Blaine Baker, Kristoffer Søberg, Elimelda Moige Ongeri, Francesco Raimondi, Faihaa Ahmed
Publikováno v:
Biochemical Journal. 478:2101-2119
3′,5′-cyclic adenosine monophosphate (cAMP) dependent protein kinase or protein kinase A (PKA) has served as a prototype for the large family of protein kinases that are crucially important for signal transduction in eukaryotic cells. The PKA cat
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::0eaa8b0037ae445a37c267eda66d661a
https://doi.org/10.1042/bcj20200867
https://doi.org/10.1042/bcj20200867
Autor:
Jessica H. Bruystens, Jian Wu, Maximilian Wallbott, Daniela Bertinetti, Friedrich W. Herberg, Susan S. Taylor
Publikováno v:
The FASEB Journal. 36
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::757aef4b1a40fc3d17a7e9fdbf014fda
https://doi.org/10.1096/fasebj.2022.36.s1.r6147
https://doi.org/10.1096/fasebj.2022.36.s1.r6147
Autor:
Steve Silletti, Stefan Knapp, Friedrich W. Herberg, Phillip C. Aoto, Junru Hu, Sven H. Schmidt, Elizabeth A. Komives, Sebastian Mathea, Susan S. Taylor, Maximilian Wallbott, Daniela Boassa, Jui-Hung Weng
Publikováno v:
Proceedings of the National Academy of Sciences of the United States of America, vol 118, iss 23
Proceedings of the National Academy of Sciences
Proceedings of the National Academy of Sciences of the United States of America
Proceedings of the National Academy of Sciences
Proceedings of the National Academy of Sciences of the United States of America
Significance To achieve a mechanistic understanding of LRRK2, a multidomain protein kinase, we must understand how the conformational landscape is changed by specific mutations that cause LRRK2 to become a driver of Parkinson’s disease (PD). To mee
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::01cc0525661681d71ed99cfc528ea344
https://doi.org/10.1101/2020.07.13.198069
https://doi.org/10.1101/2020.07.13.198069
