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Your search keyword '"Müller, Stefan"' showing total 18 results
Start Over Author "Müller, Stefan" Journal journal of biological chemistry
18 results on '"Müller, Stefan"'

3. Proteolytic Processing Regulates Placental Growth Factor Activities

Author

Hoffmann, Daniel C., primary, Willenborg, Sebastian, additional, Koch, Manuel, additional, Zwolanek, Daniela, additional, Müller, Stefan, additional, Becker, Ann-Kathrin A., additional, Metzger, Stephanie, additional, Ehrbar, Martin, additional, Kurschat, Peter, additional, Hellmich, Martin, additional, Hubbell, Jeffrey A., additional, and Eming, Sabine A., additional

Published
2013
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9. RICK Activates a NF-κB-dependent Anti-human Cytomegalovirus Response

Author

Eickhoff, Jan, primary, Hanke, Miriam, additional, Stein-Gerlach, Matthias, additional, Kiang, Tan Poi, additional, Herzberger, Katrin, additional, Habenberger, Peter, additional, Müller, Stefan, additional, Klebl, Bert, additional, Marschall, Manfred, additional, Stamminger, Thomas, additional, and Cotten, Matt, additional

Published
2004
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18. RICK activates a NF-kappaB-dependent anti-human cytomegalovirus response.

Author

Eickhoff J, Hanke M, Stein-Gerlach M, Kiang TP, Herzberger K, Habenberger P, Müller S, Klebl B, Marschall M, Stamminger T, and Cotten M

Subjects
Cell Line, Fibroblasts metabolism, Fibroblasts virology, Humans, Receptor-Interacting Protein Serine-Threonine Kinase 2, Virus Replication, Cytomegalovirus physiology, Cytomegalovirus Infections metabolism, NF-kappa B metabolism, Protein Kinases metabolism
Abstract

The adapter kinase receptor interacting protein-like interacting caspase-like apoptosis regulatory protein kinase (RICK, also called RIP2 and CARDIAK) was found to be elevated at both the protein and RNA levels during human cytomegalovirus (HCMV) replication, suggesting either that the virus may require RICK for replication or that RICK is part of an unsuccessful host attempt to inhibit HCMV replication. It is demonstrated here that forced expression of RICK in either a kinase active or inactive form activates nuclear factor (NF)-kappaB by means of its intermediate domain and potently blocks HCMV replication in human fibroblasts. Importantly, NF-kappaB activation, which exerted a modestly positive effect on the early phase of infection, clearly had a strongly negative impact during later viral steps. A stable inhibitor of NF-kappaB (IkappaB) reverses the RICK inhibitory effect, and activation of NF-kappaB by IkappaB kinase beta expression is inhibitory to HCMV, demonstrating that NF-kappaB activation is part of a potent anti-HCMV response. Supernatant transfer experiments identified interferon-beta as a downstream component of the RICK inhibitory pathway. RICK expression was found to synergize with HCMV infection in the induction of interferon-beta expression. This study identifies an endogenous RICK-activated, NF-kappaB- and interferon-beta-dependent antiviral pathway that is either inhibited or faulty under normal HCMV replication conditions; efforts to bolster this pathway may lead to novel anti-viral approaches.

Published
2004
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