Claus Kerkhoff
Institute of Immunology
Helmholtz Centre for Infection Research
Inhoffenstr. 7
D-38124 Braunschweig
Germany
Name/email consistency: high
- Double-Stranded RNA Induces MMP-9 Gene Expression in HaCaT Keratinocytes by Tumor Necrosis Factor-α. Voss, A., Gescher, K., Hensel, A., Nacken, W., Kerkhoff, C. Inflamm. Allergy. Drug. Targets (2011)
- The arachidonic acid-binding protein S100A8/A9 promotes NADPH oxidase activation by interaction with p67phox and Rac-2. Kerkhoff, C., Nacken, W., Benedyk, M., Dagher, M.C., Sopalla, C., Doussiere, J. FASEB J. (2005)
- Binding of two nuclear complexes to a novel regulatory element within the human S100A9 promoter drives the S100A9 gene expression. Kerkhoff, C., Hofmann, H.A., Vormoor, J., Melkonyan, H., Roth, J., Sorg, C., Klempt, M. J. Biol. Chem. (2002)
- Interaction of S100A8/S100A9-arachidonic acid complexes with the scavenger receptor CD36 may facilitate fatty acid uptake by endothelial cells. Kerkhoff, C., Sorg, C., Tandon, N.N., Nacken, W. Biochemistry (2001)
- The two calcium-binding proteins, S100A8 and S100A9, are involved in the metabolism of arachidonic acid in human neutrophils. Kerkhoff, C., Klempt, M., Kaever, V., Sorg, C. J. Biol. Chem. (1999)
- Zinc binding reverses the calcium-induced arachidonic acid-binding capacity of the S100A8/A9 protein complex. Kerkhoff, C., Vogl, T., Nacken, W., Sopalla, C., Sorg, C. FEBS Lett. (1999)
- The regulatory role of MRP8 (S100A8) and MRP14 (S100A9) in the transendothelial migration of human leukocytes. Kerkhoff, C., Eue, I., Sorg, C. Pathobiology (1999)
- Novel insights into structure and function of MRP8 (S100A8) and MRP14 (S100A9). Kerkhoff, C., Klempt, M., Sorg, C. Biochim. Biophys. Acta (1998)
