Zobrazeno 1 - 10
of 43
pro vyhledávání: '"Mathias Dreger"'
Autor:
Maria Joosten, Sebastian Ginzel, Christian Blex, Dmitri Schmidt, Michael Gombert, Cai Chen, René Martin Linka, Olivia Gräbner, Anika Hain, Burkhard Hirsch, Anke Sommerfeld, Anke Seegebarth, Uschi Gruber, Corinna Maneck, Langhui Zhang, Katharina Stenin, Henrik Dieks, Michael Sefkow, Carsten Münk, Claudia D. Baldus, Ralf Thiele, Arndt Borkhardt, Michael Hummel, Hubert Köster, Ute Fischer, Mathias Dreger, Volkhard Seitz
Publikováno v:
Molecular Oncology, Vol 10, Iss 8, Pp 1232-1244 (2016)
Histone deacetylase (HDAC) inhibitors such as suberoylanilide hydroxamic acid (SAHA) are not commonly used in clinical practice for treatment of B‐cell lymphomas, although a subset of patients with refractory or relapsed B‐cell lymphoma achieved
Externí odkaz:
https://doaj.org/article/8c0b9682d8d14e8aab687d3b139b6d0e
Autor:
Uschi Gruber, Mathias Dreger, Christian Blex, Matthias Hakelberg, Anett Marais, Frederick Gyapon Quast, Friedrich Kroll, Kathrin Bartho, Anna K. Schrey, Hubert Köster, Oliver Popp, Michael Sefkow, Jens Furkert, Ralf Schülein, Jenny Eichhorst, Sylvia Niquet, Simon Michaelis
Publikováno v:
ChemBioChem. 18:1639-1649
Unbiased chemoproteomic profiling of small-molecule interactions with endogenous proteins is important for drug discovery. For meaningful results, all protein classes have to be tractable, including G protein-coupled receptors (GPCRs). These receptor
Autor:
Anika Hain, Volkhard Seitz, Burkhard Hirsch, Uschi Gruber, Arndt Borkhardt, Mathias Dreger, René M. Linka, Olivia Gräbner, Corinna Maneck, Christian Blex, Sebastian Ginzel, Henrik Dieks, Carsten Münk, Claudia D. Baldus, Michael Hummel, Anke Seegebarth, Anke Sommerfeld, Katharina Stenin, Michael Gombert, Michael Sefkow, Maria Joosten, Hubert Köster, Dmitri Schmidt, Ute Fischer, Ralf Thiele, Cai Chen, Langhui Zhang
Publikováno v:
Molecular Oncology. 10:1232-1244
Histone deacetylase (HDAC) inhibitors such as suberoylanilide hydroxamic acid (SAHA) are not commonly used in clinical practice for treatment of B-cell lymphomas, although a subset of patients with refractory or relapsed B-cell lymphoma achieved part
Autor:
Olivia Y. Graebner, Hubert Koester, Simon Michaelis, Lisa von Kleist, Anna K. Schrey, Kathrin Bartho, Mathias Dreger, Friedrich Kroll, Yan Luo, Marén Schlief, Michael Sefkow
Publikováno v:
Journal of medicinal chemistry. 59(10)
Structurally related inhibitors of a shared therapeutic target may differ regarding potential toxicity issues that are caused by different off-target bindings. We devised a differential competition capture compound mass spectrometry (dCCMS) strategy
Publikováno v:
Journal of Proteomics. 75:100-115
The isolation of proteome subsets on the basis of the interactions of small molecules with proteins is an emerging paradigm in proteomics. Depending on the nature of the small molecule used as a bait, entire protein families can be monitored in biolo
Autor:
Friedrich Kroll, Mathias Dreger
Publikováno v:
Future Medicinal Chemistry. 2:1613-1617
Autor:
Yan Luo, Mathias Dreger, Michael Sefkow, Hubert Köster, Christian Blex, Mirko Glinski, Olivia Baessler
Publikováno v:
Molecular & Cellular Proteomics. 8:2843-2856
The profiling of subproteomes from complex mixtures on the basis of small molecule interactions shared by members of protein families or small molecule interaction domains present in a subset of proteins is an increasingly important approach in funct
Autor:
Anna K. Schrey, Simon Michaelis, Hubert Koester, Friedrich Kroll, Mathias Dreger, Jenny J. Fischer, Olivia Baessler, Mirko Glinski
Publikováno v:
Toxicological Sciences. 113:243-253
Capture compound mass spectrometry (CCMS) is a novel technology that helps understand the molecular mechanism of the mode of action of small molecules. The Capture Compounds are trifunctional probes: A selectivity function (the drug) interacts with t
Publikováno v:
Molecular & Cellular Proteomics : MCP
There is increasing interest in the role of antibodies targeting specific membrane proteins in neurological and other diseases. The target(s) of these pathogenic antibodies is known in a few diseases, usually when candidate cell surface proteins have
Publikováno v:
Protein Science. 18:1448-1458
We describe a method for studying quantitative changes in accessibility of surface lysine residues of the PB1 subunit of the influenza RNA polymerase as a result of association with the PA subunit to form a PB1-PA heterodimer. Our method combines two