Zobrazeno 1 - 5
of 5
pro vyhledávání: '"Lea Marie Esser"'
Autor:
Lea Marie Esser, Katharina Schmitz, Frank Hillebrand, Steffen Erkelenz, Heiner Schaal, Björn Stork, Matthias Grimmler, Sebastian Wesselborg, Christoph Peter
Publikováno v:
Computational and Structural Biotechnology Journal, Vol 21, Iss , Pp 2100-2109 (2023)
The spliceosome, responsible for all mature protein-coding transcripts of eukaryotic intron-containing genes, consists of small uridine-rich nuclear ribonucleoproteins (UsnRNPs). The assembly of UsnRNPs depends, on one hand, on the arginine methylati
Externí odkaz:
https://doaj.org/article/104567e091404490bf1af5bf1619f414
Autor:
Adrian Krzyzanowski, Lea Marie Esser, Anthony Willaume, Renaud Prudent, Christoph Peter, Peter ‘t Hart, Herbert Waldmann
Publikováno v:
Journal of Medicinal Chemistry. 65:15300-15311
The PRMT5-MEP50 methyltransferase is a major target for anticancer drug discovery, and modulators of its interactions with different regulatory proteins are in high demand because they modulate PRMT5 substrate selectivity. We describe a strategy for
Autor:
Grimmler, Thomas Masetto, Kai Matzenbach, Thomas Reuschel, Sebastian-Alexander Tölke, Klaus Schneider, Lea Marie Esser, Marco Reinhart, Laura Bindila, Christoph Peter, Matthias
Publikováno v:
International Journal of Molecular Sciences; Volume 24; Issue 13; Pages: 10963
Sepsis is a life-threatening organ dysfunction caused by a dysregulated host response to infection. The fast and accurate diagnosis of sepsis by procalcitonin (PCT) has emerged as an essential tool in clinical medicine. Although in use in the clinica
Autor:
Jan Cox, Lea Marie Esser, Maximilian Jüdt, Katharina Schmitz, Kaja Reiffert, Matthias Grimmler, Björn Stork, Sebastian Wesselborg, Christoph Peter
Publikováno v:
Biological Chemistry. 403:907-915
Protein-arginine methylation is a common posttranslational modification, crucial to various cellular processes, such as protein-protein interactions or binding to nucleic acids. The central enzyme of symmetric protein arginine methylation in mammals
Autor:
Steffen Erkelenz, Dieter Willbold, Katharina Schmitz, David Schlütermann, Stefan Klinker, Björn Stork, Frank Hillebrand, Katja Sander, Heiner Schaal, Christoph Peter, Antje S. Löffler, Martin Voss, Luitgard Nagel-Steger, Thilo Kähne, Matthias Grimmler, Jan Cox, Sebastian Wesselborg, Sabine Seggewiß, Lea Marie Esser, Tao Zhang
Publikováno v:
Nucleic acids research 49(11), 6437-6455 (2021). doi:10.1093/nar/gkab452
Nucleic Acids Research
Nucleic Acids Research
The biogenesis of small uridine-rich nuclear ribonucleoproteins (UsnRNPs) depends on the methylation of Sm proteins catalyzed by the methylosome and the subsequent action of the SMN complex, which assembles the heptameric Sm protein ring onto small n
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::e1df557cb4c3043b2814ab2104146c58
https://hdl.handle.net/2128/29693
https://hdl.handle.net/2128/29693