Zobrazeno 1 - 10
of 62
pro vyhledávání: '"Rudolf Volkmer-Engert"'
Autor:
Christiane Landgraf, Simona Panni, Luisa Montecchi-Palazzi, Luisa Castagnoli, Jens Schneider-Mergener, Rudolf Volkmer-Engert, Gianni Cesareni
Publikováno v:
PLoS Biology, Vol 2, Iss 1, p E14 (2004)
A substantial proportion of protein interactions relies on small domains binding to short peptides in the partner proteins. Many of these interactions are relatively low affinity and transient, and they impact on signal transduction. However, neither
Externí odkaz:
https://doaj.org/article/8f616cbe453f48a1aa3fcc2db37d3653
Autor:
Angela Bachi, Andrea Cabibbo, Lars Kiemer, Luisa Montecchi-Palazzi, Luisa Castagnoli, Simona Panni, Gianni Cesareni, Elena Santonico, Rudolf Volkmer-Engert, Christiane Landgraf, Serena Paoluzi
Publikováno v:
PROTEOMICS. 11:128-143
Large-scale interaction studies contribute the largest fraction of protein interactions information in databases. However, co-purification of non-specific or indirect ligands, often results in data sets that are affected by a considerable number of f
Publikováno v:
Journal of Biological Chemistry. 281:12833-12840
The signal-transducing protein EIIA(Glc), a component of the phosphoenolpyruvate-glucose phosphotransferase system, plays a key role in carbon regulation in enteric bacteria, such as Escherichia coli and Salmonella typhimurium. The phosphorylation st
Autor:
Fred Schaper, Claudia Stross, Christa Gerlach, Simone Radtke, Heike M. Hermanns, Peter C. Heinrich, Thomas Clahsen, Rudolf Volkmer-Engert
Publikováno v:
Journal of Biological Chemistry. 281:8458-8468
Down-regulation of interleukin (IL)-6-type cytokine signaling has been shown to occur, among other mechanisms, via induction of the feedback inhibitor SOCS3 (suppressor of cytokine signaling 3). Binding of SOCS3 to the phosphorylated Tyr(759) in the
Autor:
Michael Hörtner, Wiltrud Frisch, Fred Schaper, Peter C. Heinrich, Rudolf Volkmer-Engert, Ulrike Sommer, Tanya Smyczek, Ute Lehmann, Serge Haan
Publikováno v:
Cellular Signalling. 18:40-49
In recent years, the elucidation of the structures of many signalling molecules has allowed new insights into the molecular mechanisms that govern signal transduction events. In the field of cytokine signalling, the solved structures of cytokine/rece
Autor:
Victor Tapia, Michal Or-Guil, Johannes Schuchhardt, Cornelius Frömmel, Rudolf Volkmer-Engert, Armin A. Weiser, Astrid Leichsenring
Publikováno v:
Analytical Biochemistry. 342:300-311
Peptide arrays prepared by the SPOT synthesis technology have emerged as a proteomic tool to study molecular recognition and identify biologically active peptides. However, it was previously not clear how accurately signal intensities obtained by pro
Autor:
Jessica Nolte, Gerrit Hennecke, Jens Schneider-Mergener, Rudolf Volkmer-Engert, Susanne Behrens
Publikováno v:
Journal of Biological Chemistry. 280:23540-23548
The Escherichia coli periplasmic chaperone and peptidyl-prolyl isomerase (PPIase) SurA facilitates the maturation of outer membrane porins. Although the PPIase activity exhibited by one of its two parvulin-like domains is dispensable for this functio
Autor:
André Halbach, Rudolf Volkmer-Engert, Christiane Landgraf, Stephan Lorenzen, Ralf Erdmann, Hanspeter Rottensteiner
Publikováno v:
Journal of Biological Chemistry. 280:21176-21182
We predicted in human peroxisomal membrane proteins (PMPs) the binding sites for PEX19, a key player in the topogenesis of PMPs, by virtue of an algorithm developed for yeast PMPs. The best scoring PEX19-binding site was found in the adrenoleukodystr
Autor:
Urs Wiedemann, Prisca Boisguerin, Gerd Krause, Dietmar Leitner, Rainer Leben, Karin Moelling, Rudolf Volkmer-Engert, Hartmut Oschkinat
Publikováno v:
Journal of Molecular Biology. 343:703-718
Transient macromolecular complexes are often formed by protein-protein interaction domains (e.g. PDZ, SH2, SH3, WW) which recognize linear sequence motifs with in vitro affinities typically in the micromolar range. The analysis of the resulting inter
Autor:
Ralf Erdmann, Katharina Stein, Stephan Lorenzen, Christiane Landgraf, Rudolf Volkmer-Engert, Hanspeter Rottensteiner, Achim Kramer
Publikováno v:
Molecular Biology of the Cell. 15:3406-3417
Targeting of peroxisomal membrane proteins (PMPs) is a multistep process that requires not only recognition of PMPs in the cytosol but also their insertion into the peroxisomal membrane. As a consequence, targeting signals of PMPs (mPTS) are rather c