Zobrazeno 1 - 10
of 43
pro vyhledávání: '"Arnd Kieser"'
Autor:
Fabian Giehler, Michael S. Ostertag, Thomas Sommermann, Daniel Weidl, Kai R. Sterz, Helmut Kutz, Andreas Moosmann, Stephan M. Feller, Arie Geerlof, Brigitte Biesinger, Grzegorz M. Popowicz, Johannes Kirchmair, Arnd Kieser
Publikováno v:
Nature Communications, Vol 15, Iss 1, Pp 1-18 (2024)
Abstract Epstein-Barr virus (EBV) latent membrane protein 1 (LMP1) drives viral B cell transformation and oncogenesis. LMP1’s transforming activity depends on its C-terminal activation region 2 (CTAR2), which induces NF-κB and JNK by engaging TNF
Externí odkaz:
https://doaj.org/article/6129e63ef175431f88dcfe4bca0f1328
Autor:
Bram W. van Os, Pascal J. H. Kusters, Myrthe den Toom, Linda Beckers, Claudia M. van Tiel, Winnie G. Vos, Elize de Jong, Arnd Kieser, Cindy van Roomen, Christoph J. Binder, Myrthe E. Reiche, Menno P. de Winther, Laura A. Bosmans, Esther Lutgens
Publikováno v:
Frontiers in Cardiovascular Medicine, Vol 10 (2023)
BackgroundAtherosclerosis is the underlying cause of many cardiovascular diseases, such as myocardial infarction or stroke. B cells, and their production of pro- and anti-atherogenic antibodies, play an important role in atherosclerosis. In B cells,
Externí odkaz:
https://doaj.org/article/b457cc8d45844f5ca3e8e23782d56612
Autor:
Stefanie Voigt, Kai R. Sterz, Fabian Giehler, Anne-Wiebe Mohr, Joanna B. Wilson, Andreas Moosmann, Arnd Kieser
Publikováno v:
Nature Communications, Vol 11, Iss 1, Pp 1-16 (2020)
IKK2 is the main mediator of the NF-kappaB pathway. Here, the authors demonstrate that LMP1 sustains the survival of Epstein-Barr virus-transformed human B cells and post-transplant lymphoma through IKK2 that induces JNK signaling through TPL2.
Externí odkaz:
https://doaj.org/article/a2305298494b481ca6cef8d55610d0b9
Autor:
Anna Shkoda, Jennifer A Town, Janine Griese, Michael Romio, Hakan Sarioglu, Thomas Knöfel, Fabian Giehler, Arnd Kieser
Publikováno v:
PLoS Biology, Vol 10, Iss 8, p e1001376 (2012)
The tumor necrosis factor-receptor-associated factor 2 (TRAF2)- and Nck-interacting kinase (TNIK) is a ubiquitously expressed member of the germinal center kinase family. The TNIK functions in hematopoietic cells and the role of TNIK-TRAF interaction
Externí odkaz:
https://doaj.org/article/a79f619f7332437aa3a8c9f9ef747b27
Autor:
Frank Schneider, Julia Neugebauer, Janine Griese, Nicola Liefold, Helmut Kutz, Cinthia Briseño, Arnd Kieser
Publikováno v:
PLoS Biology, Vol 6, Iss 1, p e8 (2008)
The tumor necrosis factor (TNF)-receptor 1-associated death domain protein (TRADD) mediates induction of apoptosis as well as activation of NF-kappaB by cellular TNF-receptor 1 (TNFR1). TRADD is also recruited by the latent membrane protein 1 (LMP1)
Externí odkaz:
https://doaj.org/article/b38f4d0400934f4a8d62c4c573719f6f
Autor:
Fabian Giehler, Michael Ostertag, Thomas Sommermann, Daniel Weidl, Kai Sterz, Helmut Kutz, Stephan Feller, Arie Geerlof, Brigitte Biesinger, Grzegorz Popowicz, Johannes Kirchmair, Arnd Kieser
The latent membrane protein 1 (LMP1) of Epstein-Barr virus (EBV) drives viral B cell transformation and oncogenesis. LMP1's transforming activity depends on its cytoplasmic C-terminal activation region 2 (CTAR2), which induces NF-κB and JNK by engag
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::0c49aa69b05fde27bbf65d7b7894f478
https://doi.org/10.21203/rs.3.rs-1295699/v1
https://doi.org/10.21203/rs.3.rs-1295699/v1
Autor:
Anne-Wiebe Mohr, Arnd Kieser, Joanna B. Wilson, Andreas Moosmann, Stefanie Voigt, Fabian Giehler, Kai R. Sterz
Publikováno v:
Nature Communications
Nature Communications, Vol 11, Iss 1, Pp 1-16 (2020)
Nat. Commun. 11:685 (2020)
Nature Communications, Vol 11, Iss 1, Pp 1-16 (2020)
Nat. Commun. 11:685 (2020)
IκB kinase 2 (IKK2) is well known for its pivotal role as a mediator of the canonical NF-κB pathway, which has important functions in inflammation and immunity, but also in cancer. Here we identify a novel and critical function of IKK2 and its co-f
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::254d2635c26d127486aab161413a5994
https://eprints.gla.ac.uk/210507/1/210507.pdf
https://eprints.gla.ac.uk/210507/1/210507.pdf
Autor:
Roy Schrijver, Oliver Soehnlein, Claudia M. van Tiel, Tom Seijkens, Barbara Zarzycka, Tina Ritschel, Tilman M. Hackeng, Sander B. Nabuurs, Jochen Grommes, Gert Vriend, Esther Lutgens, Fabian Giehler, Arnd Kieser, Christian Weber, Gerry A. F. Nicolaes
Publikováno v:
Journal of Chemical Information and Modeling, 55(2), 294-307. American Chemical Society
Journal of chemical information and modeling, 55(2), 294-307. American Chemical Society
Journal of Chemical Information and Modeling, 55, 2, pp. 294-307
Journal of Chemical Information and Modeling, 55, 294-307
Journal of chemical information and modeling, 55(2), 294-307. American Chemical Society
Journal of Chemical Information and Modeling, 55, 2, pp. 294-307
Journal of Chemical Information and Modeling, 55, 294-307
Item does not contain fulltext The CD154-CD40 receptor complex plays a pivotal role in several inflammatory pathways. Attempts to inhibit the formation of this complex have resulted in systemic side effects. Downstream inhibition of the CD40 signalin
Autor:
Kamyar Hadian, Maria Kuzikov, Kenji Schorpp, Fabian Giehler, Elena Salmina, Igor V. Tetko, Jay Gopalakrishnan, Sheraz Gul, Jara Kerstin Brenke, Ina Rothenaigner, Larissa Ringelstetter, Arnd Kieser, Scarlett Dornauer
In high-throughput screening (HTS) campaigns, the binding of glutathione S-transferase (GST) to glutathione (GSH) is used for detection of GST-tagged proteins in protein-protein interactions or enzyme assays. However, many false-positives, so-called
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::7937dda188be76c7e2a1798a1cfa8569
https://publica.fraunhofer.de/handle/publica/246075
https://publica.fraunhofer.de/handle/publica/246075
Autor:
Arnd Kieser
Publikováno v:
bchm. 389:1261-1271
The pro-apoptotic tumor necrosis factor (TNF)-receptor 1-associated death domain protein (TRADD) was initially identified as the central signaling adapter molecule of TNF-receptor 1 (TNFR1). Upon stimulation with the pro-inflammatory cytokine TNFα,