Book:

• Proteases: Structure and Function, Klaudia Brix & Walter Stöcker (Eds.), Springer-Verlag Wien 2013. http://www.springer.com/de/book/9783709108840#aboutBook, ISBN 978-3-7091-0884-0, ISBN 978-3-7091-0885-7 (eBook)., doi:10.1007/978-3-7091-0885-7. , Springer Wien, Heidelberg, New York, Dordrecht, London. Library of Congress Control Number: 2013956226.

Selection (Original Articles / Reviews):

• Tamhane, T., R. Illukkumbura, S. Lu, G.M. Maelandsmo, M.H. Haugen, and K. Brix (2016). Nuclear cathepsin L activity is required for cell cycle progression of colorectal carcinoma cells. Biochimie 122, 208-218
• Rezk, A., A. Al-Hashimi, W. John, H. Schepker, M.S. Ullrich, and K. Brix (2015b). Assessment of cytotoxicity exerted by leaf extracts from plants of the genus Rhododendron towards epidermal keratinocytes and intestine epithelial cells. BMC Complement Altern Med. 15:364
• Szumska, J., M. Qatato, M. Rehders, D. Führer, H. Biebermann, D.K. Grandy, J. Köhrle, and K. Brix (2015). Trace amine-associated receptor 1 localization at the apical plasma membrane domain of Fisher rat thyroid epithelial cells is confined to cilia. Eur. Thyroid J. 4 (Suppl. 1), 30-41
• Führer, D. / K. Brix / H. Biebermann (2015). Understanding the healthy thyroid state in 2015. Eur. Thyroid J. 4 (Suppl. 1), 1-8
• Brix, K., J. McInnes, A. Al-Hashimi, M. Rehders, T. Tamhane, M.H. Haugen (2015). Proteolysis mediated by cysteine cathepsins and legumain - recent advances and cell biological challenges. Protoplasma 252, 755-774
• Rezk, A., J. Nolzen, H. Schepker, D.C. Albach, K. Brix, and M.S. Ullrich (2015a). Phylogenetic spectrum and analysis of antibacterial activities of leaf extracts from plants of the genus Rhododendron. BMC Complementary & Alternative Medicine 15:67
• Haugen, M.H., K. Boye, J.M. Nesland, S.J. Pettersen, E.V. Egeland, T. Tamhane, K. Brix, G.M. Maelandsmo, and K. Flatmark (2015).  High expression of the cysteine proteinase legumain in colorectal cancer - Implications for therapeutic targeting. Eur. J. Cancer 51, 9-17
• Tamhane, T. / M. Arampatzidou, V. Gerganova, M. Tacke, R. Illukkumbura, S. Dauth, N. Schaschke, C. Peters, T. Reinheckel, and K. Brix (2014). The activity and localization patterns of cathepsins B and X in cells of the mouse gastrointestinal tract differ along its length. Biol. Chem. 395, 1201-1219
• Führer, D. / K. Brix / H. Biebermann (2014). Übersicht / Review article: Schilddrüsenhormonwirkung – jenseits klassischer Konzepte. Das Schwerpunktprogramm „THYROID TRANS ACT“ (SPP1629) der Deutschen Forschungsgemeinschaft. Thyroid hormone action beyond classical concepts. The priority programme „THYROID TRANS ACT“ (SPP1629) of the German Research Foundation. Dtsch. Med. Wochenschr. 139, 492-496
• Haugen, M.H., H.T. Johansen, S.J. Pettersen, R. Solberg, K. Brix, K. Flatmark, and G.M. Maelandsmo (2013). Nuclear legumain activity in colorectal cancer. PLoS One 8(1), e52980
• Brix, K., D. Führer, and H. Biebermann (2011). Molecules imprtant for thyroid hormone synthesis and action - known facts and future perspectives. Thyroid Research 4 (Suppl 1), S9
• Dauth, S., R.F. Sirbulescu, S. Jordans, M. Rehders, L. Avena, J. Oswald, A. Lerchl, P. Saftig, and K. Brix (2011). Cathepsin K deficiency in mice induces structural and metabolic changes in the cenetral nervous system that are associated with learning and memory deficits. BMC Neuroscience 12, 74. 
• Dauth, S., M. Arampatzidou, M. Rehders, D. M. T. Yu, D. Führer, and K. Brix (2011). Thyroid cathepsin K - roles in physiology and thyroid disease. Clin. Rev. Bone Miner. Metab. 9, 94-106.
• Jordans, S., S. Jenko-Kokalj, N. M. Kühl, S. Tedelind, W. Sendt, D. Brömme, D. Turk, and K. Brix (2009). Monitoring compartment-specific substrate cleavage by cathepsins B, K, L, and S at physiological pH and redox conditions. BMC Biochemstry 10, 23. Highly Accessed.
• Mayer, K., A. Vreemann, H. Qu, and K. Brix (2009). Release of endo-lysosomal cathepsins B, D, and L from IEC6 cells in a cell culture model mimicking intestinal manipulation. Biol. Chem. 390, 471-480.
• Brix, K., A. Dunkhorst, K. Mayer, and S. Jordans (2008). Cysteine cathepsins: Cellular roadmap to different functions. Biochimie 90, 194-207
• Büth, H., P.L. Buttigieg, R. Ostafe, M. Rehders, S.R. Dannenmann, N. Schaschke, H.-J. Stark, P. Boukamp, and K. Brix (2007). Cathepsin B is essential for regeneration of scratch-wounded normal human epidermal keratinocytes. Eur. J. Cell Biol. 86, 747-761
• Brix, K., and S. Jordans (2005). News & Views: Watching proteases in action. Nature Chem. Biol. 1, 186-187.
• Brix, K. (2005). Chapter 05: Lysosomal Proteases: Revival of the Sleeping Beauty. In: Lysosomes, edited by Paul Saftig, Eurekah.com. Landes Bioscience. REVIEW.
• Friedrichs, B., C. Tepel, Th. Reinheckel, J. Deussing, K. von Figura, V. Herzog, Ch. Peters, P. Saftig, and K. Brix (2003). Thyroid functions of mouse cathepsins B, K, and L. J. Clin. Invest. 111, 1733-1745.
• Linke, M., V. Herzog, and K. Brix (2002). Trafficking of lysosomal cathepsin B – green fluorescent protein to the surface of thyroid epithelial cells involves the endosomal/lysosomal compartment. J. Cell Sci. 115, 4877-4889.
• Brix, K., M. Linke, C. Tepel, and V. Herzog (2001). Cysteine proteinases mediate extracellular prohormone processing in the thyroid. Review. Biol. Chem. 382, 717-725.
• Tepel, C., D. Brömme, V. Herzog, and K. Brix (2000). Cathepsin K in thyroid epithelial cells: Sequence, localization, and possible function in extracellular proteolysis of thyroglobulin. J. Cell Sci. 113, 4487-4498.
• Brix, K., P. Lemansky, and V. Herzog (1996). Evidence for extracellularly acting cathepsins mediating thyroid hormone liberation in thyroid epithelial cells. Endocrinology 137, 1963-1974.
• Brix, K., and V. Herzog (1994). Extrathyroidal release of thyroid hormones from thyroglobulin by J774 mouse macrophages. J. Clin. Invest. 93, 1388-1396.
• Stockem, W., and K. Brix (1994). Analysis of microfilament organization and contractile activities in Physarum. Int. Rev. Cytol. 149, 145-215.