Zobrazeno 1 - 9
of 9
pro vyhledávání: '"Birgit Zech"'
Autor:
Erik H. Heijne, Christopher D. Hupp, John W. Cuozzo, Anthony D. Keefe, Rob Winkel, L. Babiss, Wendy van Bruggen, Louis Renzetti, Mark J. Mulvihill, Birgit Zech, Andrew J. McRiner, Johan J. N. Veerman, Eddy Damen, Yorik B. Bruseker, Heather A. Thomson, Julie Liu, Gerhard Müller, Koen F. W. Hekking, Ying Zhang, Peter van Rijnsbergen
Publikováno v:
ACS Medicinal Chemistry Letters. 12:555-562
Herein we report the discovery of 2,4-1H-imidazole carboxamides as novel, biochemically potent, and kinome selective inhibitors of transforming growth factor β-activated kinase 1 (TAK1). The target was subjected to a DNA-encoded chemical library (DE
Autor:
Johan J N, Veerman, Yorik B, Bruseker, Eddy, Damen, Erik H, Heijne, Wendy, van Bruggen, Koen F W, Hekking, Rob, Winkel, Christopher D, Hupp, Anthony D, Keefe, Julie, Liu, Heather A, Thomson, Ying, Zhang, John W, Cuozzo, Andrew J, McRiner, Mark J, Mulvihill, Peter, van Rijnsbergen, Birgit, Zech, Louis M, Renzetti, Lee, Babiss, Gerhard, Müller
Publikováno v:
ACS Med Chem Lett
[Image: see text] Herein we report the discovery of 2,4-1H-imidazole carboxamides as novel, biochemically potent, and kinome selective inhibitors of transforming growth factor β-activated kinase 1 (TAK1). The target was subjected to a DNA-encoded ch
Autor:
Birgit Zech, Christian Wohlfarth
Publikováno v:
Die Makromolekulare Chemie. 193:2433-2444
Solvent activities were measured by an isopiestic sorption technique for solutions of poly(butyl methacrylate) and poly(tert-butyl methacrylate), respectively, in various solvents between 323 K and 373 K (or 403 K). The experimental data were reduced
Publikováno v:
Molecularcellular proteomics : MCP. 3(5)
Bisindolylmaleimide compounds such as GF109203X are potent inhibitors of protein kinase C (PKC) activity. Although bisindolylmaleimides are not entirely selective for PKC and are known to inhibit a few other protein kinases, these reagents have been
Caspases are critical for the initiation and execution of apoptosis. Nitric oxide (NO) or derived species can prevent programmed cell death in several cell types, reportedly through S-nitrosation and inactivation of active caspases. Although we find
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::16d8120432bda4163f0bd10af9ae216e
https://europepmc.org/articles/PMC1223357/
https://europepmc.org/articles/PMC1223357/
Autor:
Sabine Obert, Matthew Cotten, Dennis Strand, Alexander Kurtenbach, Henrik Daub, Ralf Bartenschlager, Monika Morbitzer, Thomas Herget, Josef Wissing, Nicole Krieger, Birgit Zech, Kostas Salassidis, Stephanie Blencke
Publikováno v:
The Journal of general virology. 84(Pt 3)
The hepatitis C virus (HCV) NS5A protein is highly phosphorylated by cellular protein kinases. To study how NS5A might be integrated in cellular kinase signalling, we isolated phosphoproteins from HuH-7 hepatoma cells that specifically interacted wit
Publikováno v:
The Journal of biological chemistry. 274(30)
Caspases are a family of cysteine proteases activated during apoptosis. Modification of caspases by nitric oxide and its relevance during apoptosis is currently a controversial subject. In this study we analyzed the S-nitrosated form of caspase-3 at
Publikováno v:
Biochemical and biophysical research communications. 238(2)
Apoptotic signaling cascades converge in the activation of caspases (interleukin-1β converting enzyme like proteases). Treatment of the human promyelocytic leukaemia cell line U937 with actinomycin D resulted in the activation of caspase-3 also know
Autor:
György Kéri, Henrik Daub, Zoltán Greff, Stephanie Blencke, Zoltán Horváth, Birgit Zech, Ola Engkvist, Axel Ullrich, Laszlo Orfi
Publikováno v:
Chemistry & Biology. (5):691-701
Some protein kinases are known to acquire resistance to selective small molecule inhibitors upon mutation of a conserved threonine at the ATP binding site to a larger residue. Here, we performed a comprehensive mutational analysis of this structural