Research Topics
| Joachim KrebsSummaryAffiliation: Swiss Federal Institute of Technology Country: Switzerland Publications
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Detail Information
Publications
Calmodulin kinase IV: expression and function during rat brain developmentJ Krebs
Laboratory of Biochemistry III, Institute of Biochemistry, Swiss Federal Institute of Technology, Zurich, Switzerland
Biochim Biophys Acta 1313:217-22. 1996..Convergence of signal transduction pathways on this transcription factor by using different protein kinases may explain the importance of CREB for the regulation of different cellular processes...
Calmodulin-dependent protein kinase IV: regulation of function and expressionJ Krebs
Institute of Biochemistry III, Swiss Federal Institute of Technology ETH, Zurich
Biochim Biophys Acta 1448:183-9. 1998..In the present contribution the gene structure, regulation of activity, the role in Ca2+-dependent gene expression, and the hormonal induction and controlled expression of CaMKIV during tissue development are reviewed...
The role of calcium in apoptosisJ Krebs
Institute of Biochemistry, Swiss Federal Institute of Technology, Zurich, Switzerland
Biometals 11:375-82. 1998..Its possible involvement in the decision process whether T-cell activation leads to proliferation or apoptosis is discussed...
The ALG-2/AIP-complex, a modulator at the interface between cell proliferation and cell death? A hypothesisJ Krebs
Institute of Biochemistry, Swiss Federal Institute of Technology, Zurich, Switzerland
Biochim Biophys Acta 1498:153-61. 2000..The two proteins interact with each other in a Ca(2+)-dependent manner, and the role of the complex ALG-2/AIP as a possible modulator at the interface between cell proliferation and cell death is discussed...
ALG-2: a Ca2+ -binding modulator protein involved in cell proliferation and in cell deathJoachim Krebs
Institute of Biochemistry, Swiss Federal Institute of Technology ETH, HPM1, CH 8093, Zurich, Switzerland
Biochim Biophys Acta 1600:68-73. 2002..The role of ALG-2 as a possible clinical marker and, molecularly, as a possible modulator at the interface between cell proliferation and cell death is discussed...
A structural model of the complex formed by phospholamban and the calcium pump of sarcoplasmic reticulum obtained by molecular mechanicsMichael C Hutter
Max-Planck-Institute of Biophysics, Kennedyallee 70, 60596 Frankfurt, Germany
Chembiochem 3:1200-8. 2002..Our model of the complex also offers a plausible structural explanation for the preference of protein kinase A for phosphorylation of Ser16 of PLN...
Structural characterization of Ca(2+)-ATPase-bound phospholamban in lipid bilayers by solid-state nuclear magnetic resonance (NMR) spectroscopyKarsten Seidel
Max Planck Institute for Biophysical Chemistry, 37070 Gottingen, Germany
Biochemistry 47:4369-76. 2008..A combination of our spectroscopic data with biophysical and biochemical data using flexible protein-protein docking simulations provides a structural basis for understanding the interaction between PLN and SERCA1a...
