Zobrazeno 1 - 10
of 18
pro vyhledávání: '"Jürgen Zezula"'
Autor:
Jürgen Zezula, Ruth Herbst, Dana Matzen, Ingrid Walter, Gergana Galabova-Kovacs, Alcino Silva, Manuela Baccarini, Gloria Reyes, Federica Catalanotti
Publikováno v:
The Journal of Cell Biology
Mutations in the extracellular signal-regulated kinase (ERK) pathway, particularly in the mitogen-activated protein kinase/ERK kinase (MEK) activator B-Raf, are associated with human tumorigenesis and genetic disorders. Hence, B-Raf is a prime target
Autor:
Ingrid Gsandtner, Jürgen Zezula, Christoforos Charalambous, Michael Freissmuth, Eduard Stefan, Egon Ogris
Publikováno v:
Journal of Biological Chemistry. 280:31898-31905
The A2A adenosine receptor is a prototypical Gs-coupled receptor, but it also signals, e.g. to mitogen-activated protein (MAP) kinase, via a pathway that is independent of heterotrimeric G proteins. Truncation of the carboxyl terminus affects the str
Autor:
Hans Lassmann, Matthias Artaker, Sabine Lagger, Simon Weissmann, Christian Seiser, Jim Selfridge, Julia Krahmer, Yunli Xie, Patrick Matthias, Jürgen A. Knoblich, Jürgen Zezula, Alexandra Leopoldi, Christian Schöfer, Gerald Brosch, Astrid Hagelkruys, Michaela Schlederer, Oliver Pusch
Publikováno v:
Development (Cambridge, England)
The histone deacetylases HDAC1 and HDAC2 are crucial regulators of chromatin structure and gene expression, thereby controlling important developmental processes. In the mouse brain, HDAC1 and HDAC2 exhibit different developmental stage- and lineage-
Autor:
Michael Freissmuth, Wolfgang Schütz, Anton Karel, Jürgen Zezula, Caroline Hutter, Veronika Sexl
Publikováno v:
Journal of Biological Chemistry. 272:29967-29974
Long-term application of the phorbol ester phorbol 12,13-dibutyrate (PDBu) inhibits the proliferation of human venous endothelial cells. The cyclin-dependent kinase inhibitor p21 cip1 is a potential candidate mediating the PDBu-induced delayed entry
Publikováno v:
European Journal of Pharmacology: Molecular Pharmacology. 291:99-105
The allosteric modulation of [3H]flunitrazepam binding by gamma-aminobutyric acid (GABA), pentobarbital, (+)-etomidate, etazolate, alphaxalone, propofol and chlormethiazole was investigated in cerebellar membranes and membranes from human embryonic k
Publikováno v:
European Journal of Pharmacology. 281:93-96
[ 3 H]Propyl-6-azido-β-carboline-3-carboxylate ([ 3 H]ACCP) exhibited a high affinity for GABA A receptors affinity purified from the brains of adult rats, and binding of this compound could be inhibited by several ligands of the benzodiazepine bind
Autor:
Christoph Gruber, Simon Keuerleber, Michael Freissmuth, Ingrid Gsandtner, Jürgen Zezula, Patrick Thurner
Publikováno v:
BMC Pharmacology & Toxicology
Background The A2A adenosine receptor is of interest because of several reasons. (i) It is a frequently blocked pharmacological target, because it is the site of action of caffeine. (ii) It has a long C-terminus that provides a docking site for sever
Autor:
Marc G. Caron, Alexandra Kattinger, Harald Reither, Christian Pifl, Oleh Hornykiewicz, Jürgen Zezula, Andreas Spittler
Publikováno v:
Scopus-Elsevier
Europe PubMed Central
Europe PubMed Central
SPECIFIC AIMSThe aim of our study was to determine the mechanism and site of action of the cytotoxic potential of the catecholamine transmitters dopamine (DA) and norepinephrine (NE). We established SK-N-MC neuroblastoma cell lines stably transfected
Immunohistochemical localization of the α1, α2 and α3 subunit of the GABAA receptor in the rat brain
Publikováno v:
Neuroscience Letters. 127:125-128
The immunohistochemical distribution of the α 1 , α 2 and α 3 subunit of the γ-aminobutyric acid-A (GABA A ) receptor was investigated in the rat brain using affinity-purified antibodies against unique parts of the amino acid sequence of the resp
Autor:
Christoforos, Charalambous, Ingrid, Gsandtner, Simon, Keuerleber, Laura, Milan-Lobo, Oliver, Kudlacek, Michael, Freissmuth, Jürgen, Zezula
Publikováno v:
The Journal of biological chemistry. 283(14)
The A(2A)-adenosine receptor is a prototypical G(s) protein-coupled receptor but stimulates MAPK/ERK in a G(s)-independent way. The A(2A) receptor has long been known to undergo restricted collision coupling with G(s); the mechanistic basis for this