Book as Editor

Proteases: Structure and Function, edited by Klaudia Brix and Walter Stöcker, Springer-Verlag Wien 2013. 564 p. 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.



  • Führer, D. / K. Brix / H. Biebermann (2015). Understanding the healthy thyroid state in 2015. Eur. Thyroid J. 4 (Suppl. 1), 1-8. doi: 10.1159/000431318
  • 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. doi: 10.1007/s00709-014-0730-0.
  • 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. doi:10.1055/s-0034-1369822
  • Brix, K. / D. Führer / H. Biebermann (2011). Molecules important for thyroid hormone synthesis and action – known facts and future perspectives. Thyroid Research 4 (Suppl 1), S9. doi:10.1186/1756-6614-4-S1-S9
  • 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. doi:10.1007/s12018-011-9093-7
  • Arampatzidou, M., M. Rehders, S. Dauth, D.M.T. Yu, S. Tedelind, and K. Brix (2011). Imaging of protease functions – current guide to spotting cysteine cathepsins in classical and novel scenes of action in mammalian epithelial cells and tissues. It. J. Anat. Embryol. 116, 1-19.
  • Brix, K., A. Dunkhorst, K. Mayer, and S. Jordans (2008). Cysteine cathepsins: Cellular roadmap to different functions. Biochimie 90, 194-207. doi:10.1016/j.biochi.2007.07.024
  • Brix, K., and S. Jordans (2005). News & Views: Watching proteases in action. Nature Chem. Biol. 1, 186-187.
  • Brix, K., M. Linke, C. Tepel, and V. Herzog (2001). Cysteine proteinases mediate extracellular prohormone processing in the thyroid. Biol. Chem. 382, 717-725.
  • Stockem, W., and K. Brix (1994). Analysis of microfilament organization and contractile activities in Physarum. Int. Rev. Cytol. 149, 145-215.


Journal papers, peer-reviewed

  • Badziong, J., S. Ting, S. Synoracki, V. Tiedje, K. Brix, G. Brabant, L.C. Moeller, K.W. Schmid, D. Führer, D. Zwanziger (2017). Differential regulation of monocarboxylate transporter 8 expression in thyroid cancer and hyperthyroidism. Eur. J. Endocrinol., in press. doi:10.1530/EJE-17-0279.
  • Hakeem Said, I.H., A. Rezk, I. Hussain, A. Grimbs, A. Shrestha, H. Schepker, K. Brix, M.S. Ullrich, and N. Kuhnert (2017). Metabolome comparison of bioactive and inactive Rhododendron extracts and identification of an antibacterial cannabinoid from Rhododendron collettianum. Phytochemical Analysis, in press. DOI:10.1002/pca.2694
  • Grimbs, A., A. Shrestha, A.S.D. Rezk, S. Grimbs, I. Hakeem Said, H. Schepker, M.-T. Hütt, D.C. Albach, K. Brix, N. Kuhnert, and M.S. Ullrich (2017). Bioactivity in Rhododendron: A systemic analysis of antimicrobial and cytotoxic activities and their phylogenetic and phytochemical origins. Frontiers in Plant Science, 8, Article 551. Doi: 10.3389/fpls.2017.00551
  • Weber, J., J. McInnes, C. Kizilirmak, M. Rehders, M. Qatato, E.K. Wirth, U. Schweizer, F. Verrey, H. Heuer, and K. Brix (2017). Interdependence of thyroglobulin processing and thyroid hormone export in the mouse thyroid gland. Eur. J. Cell Biol., in press. doi: 10.1016/j.ejcb.2017.02.002
  • Engels, K. / H. Rakov, D. Zwanziger, S.G. Hoenes, M. Rehders, K. Brix, J. Köhrle, L.C. Moeller, D. Führer (2016). Efficacy of protocols for induction of chronic hyperthyroidism in male and female mice. Endocrine 54, 47-54. doi: 10.1007/s12020-016-1020-8
  • Elsadig Karar, M.G., L. Quiet, A. Rezk, R. Jaiswal, M. Rehders, M.S. Ullrich, K. Brix, and N. Kuhnert (2016). Phenolic profile and in vitro assessment of cytotoxicity and antibacterial activity of Ziziphus spina-christi leaf extracts. Med. Chem. (Los Angeles) 6, 143-156. doi: 10.4172/2161-0444.1000339;
  • 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. doi: 10.1016/j.biochi.2015.09.003
  • Tamhane, T., B.K. Wolters, R. Illukkumbura, G.M. Maelandsmo, M.H. Haugen, and K. Brix (2015). Construction of a plasmid coding for green fluorescent protein tagged cathepsin L and data on expression in colorectal carcinoma cells. Data in Brief 5, 468-475. doi: 10.1016/j.dib.2015.09.022
  • 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. doi: 10.1186/s12906-015-0860-8
  • 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. doi: 10.1159/000434717
  • 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. DOI 10.1186/s12906-015-0596-5.
  • Engels, K. / H. Rakov, D. Zwanziger, L.C. Moeller, G. Homuth, J. Köhrle, K. Brix, and D. Führer (2015) Differences in mouse hepatic thyroid hormone transporter expression with age and hyperthyroidism. Eur. Thyroid J. 4 (Suppl. 1),81-86. doi: 10.1159/000381020
  • Fischer, J., G. Kleinau, A. Müller, P. Kühnen, D. Zwanziger, A. Kinne, M. Rehders, L.C. Moeller, D. Führer, A. Grüters, H. Krude, K. Brix, and H. Biebermann (2015). Modulation of monocarboxylate transporter 8 oligomerization by specific pathogenic mutations. J. Mol. Endocrinol. 54, 39-50. doi: 10.1530/JME-14-0272
  • 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. doi: 10.1016/j.ejca.2014.10.020.
  • Mühlhaus, J., J. Dinter, D. Nürnberg, M. Rehders, M. Depke, J. Golchert, G. Homuth, C.-X. Yi, S. Morin, J. Köhrle, K. Brix, M. Tschöp, G. Kleinau, and H. Biebermann (2014). Analysis of Human TAAR8 and Murine Taar8b Mediated Signaling Pathways and Expression Profile. Int. J. Mol. Sci. 15, 20638-20655. doi: 10.3390/ijms151120638
  • 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. doi:10.1515/hsz-2014-0151
  • Müller, S., A. Faulhaber, C. Sieber, D. Pfeifer, T. Hochberg, M. Gansz, S.D. Deshmukh, S. Dauth, K. Brix, P. Saftig, C. Peters, P. Henneke, and T. Reinheckel (2014). The endolysosomal cysteine cathepsins L and K are involved in macrophage-mediated clearance of Staphylococcus aureus and the concomitant cytokine induction. FASEB J. 28, 162-175. doi: 10.1096/fj.13-232272.
  • McInnes, J., M. Rehders, J.R. McFaline-Figueroa, K. Brix, L.A. Pon, and E. Nevoigt (2013). Defects in mitochondrial distribution during the prolonged lag phase of Saccharomyces cerevisiae preceding growth in glycerol as the sole source of carbon. FEMS Yeast Res. 13, 706-710. doi: 10.1111/1567-1364.12085.
  • 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. doi: 10.1371/journal.pone.0052980
  • Arampatzidou, M., A. Schütte, G.C. Hansson, P. Saftig, and K. Brix (2012). Effects of cathepsin K deficiency on intercellular junction proteins, luminal mucus layers, and extracellular matrix constituents in the mouse colon. Biol. Chem. 393, 1391-1403. doi:10.1515/hsz-2012-0204
  • Dauth, S. / M.M. Schmidt, M. Rehders, F. Dietz, S. Kelm, and R. Dringen / K. Brix (2012). Characterization and metabolism of astroglia-rich primary cultures from cathepsin K-deficient mice. Biol. Chem. 393, 959-970. doi: 10.1515/hsz-2012-0145
  • Arampatzidou, M., K. Mayer, M.E. Iolyeva, S. Gebre Asrat, M. Ravichandran, T. Günther, R. Schüle, T. Reinheckel, and K. Brix (2011). Studies of intestinal morphology and cathepsin B expressing in a transgenic mouse aiming at intestine-specific expression of Cath B-EGFP. Biol. Chem. 392, 983-993. doi:10.1515/BC.2011.096
  • 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 central nervous system that are associated with learning and memory deficits. BMC Neuroscience 12, 74. doi:10.1186/1471-2202-12-74
  • Tedelind, S., S. Jordans, H. Resemann, G. Blum, M. Bogyo, D. Führer, and K. Brix (2011). Cathepsin B trafficking in thyroid carcinoma cells. Thyroid Research 4 (Suppl 1), S2. doi:10.1186/1756-6614-4-S1-S2
  • Rehders, M., B.B. Grosshäuser, A. Smarandache, A. Sadhukhan, U. Mirastschijski, J. Kempf, M. Dünne, K. Slenzka, and K. Brix (2011). Effects of lunar and mars dust simulants on HaCaT keratinocytes and CHO-K1 fibroblasts. Adv. Space Res. 47, 1200-1213. doi:10.1016/j.asr.2010.11.033
  • Tedelind, S., K. Poliakova, A. Valeta, R. Hunegnaw, E. Lemma Yemanaberhan, N.-E. Heldin, J. Kurebayashi, E. Weber, N. Kopitar-Jerala, B. Turk, M. Bogyo, and K. Brix (2010). Nuclear cysteine cathepsin variants in thyroid carcinoma cells. Biol. Chem. 391, 923-935.
  • Uzunova, V.D., C. Cullinane, K. Brix, W.M. Nau, and A.I. Day (2010). Toxicity of cucurbit[7]uril and cucurbit[8]uril: an exploratory in vitro and in vivo study. Org. Biomol. Chem. 8, 2037-2042. doi:10.1039/B925555A
  • Berger, M., A. Farcas, M. Geertz, P. Zhelyaszkova, K. Brix, A. Travers, and G. Muskhelishvili (2010). Coordination of genomic structure and transcription by the main bacterial nucleoid-associated protein HU. EMBO Reports 11, 59-64. doi:10.1038/embor.2009.232
  • Donfack, P., M. Rehders, K. Brix, P. Boukamp, and A. Materny (2010). Micro Raman spectroscopy for monitoring alterations between human skin keratinocytes HaCaT and their tumorigenic derivatives A5RT3 – toward a Raman characterization of a skin carcinoma model. J. Raman Spectrosc. 41, 16-26. doi:10.1002/jrs.2400
  • 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 Biochemistry 10, 23. doi:10.1186/1471-2091-10-23
  • Vreemann, A., H. Qu, K. Mayer, L. Bjorkholt Andersen, M.I. Stefana, S. Wehner, M. Lysson, A.M. Farcas, C. Peters, T. Reinheckel, J. Kalff, and K. Brix (2009). Cathepsin B release from rodent intestine mucosa due to mechanical injury results in extracellular matrix damage in early post-traumatic phases. Biol. Chem. 390, 481-492. doi:10.1515/BC.2009.055
  • 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. doi:10.1515/BC.2009.047
  • Mayer, K., M.E. Iolyeva, U. Meyer-Grahle, and K. Brix (2008). Intestine-specific expression of green fluorescent protein-tagged cathepsin B: proof-of-principle experiments. Biol. Chem. 389, 1085-1096. doi 10.1515/BC.2008.360
  • Waldron, E., C. Heilig, A. Schweitzer, N. Nadella, S. Jaeger, A.M. Martin, S. Weggen, K. Brix, and C.U. Pietrzik (2008). LRP1 modulates APP trafficking along early compartments of the secretory pathway. Neurobiology of Disease 31, 188-197. doi:10.1016/J.nbd.2008.04.006
  • Kubica, M., K. Guzik, J. Koziel, M. Zarebski, W. Richter, B. Gajkowska, A. Golda, A. Maciag-Gudowska, K. Brix, L. Shaw, T. Foster, and J. Potempa (2008). A potential new pathway for Staphylococcus aureus dissemination: The silent survival and intracellular proliferation of S. aureus phagocytosed by human monocyte-derived macrophages. PLoS ONE 3, e1409. doi:10.1371/journal.pone.0001409
  • Ong, P.C., S. McGowan, M.C. Pearce, J.A. Irving, W.-T.Kan, S.A. Grigoryev, B. Turk, G.A. Silverman, K. Brix, S.P. Bottomley, and J.C. Whisstock, R. Pike (2007). DNA accelerates the inhibition of human cathepsin V by serpins. J. Biol. Chem. 282, 36980-36986. doi:10.1074/jbc.M706991200
  • 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, 747-76. doi:10.1016/j.ejcb.2007.03.009
  • Büth, H., B. Wolters, B. Hartwig, R. Meier-Bornheim, H. Veith, M. Hansen, C.P. Sommerhoff, N. Schaschke, W. Machleidt, N.E. Fusenig, P. Boukamp, and K. Brix (2004). HaCaT keratinocytes secrete lysosomal cysteine proteinases during migration. Eur. J. Cell Biol. 83, 781-795.
  • 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. Featured in Journal Highlights
  • Novak, N., C. Tepel, S. Koch, K. Brix, Th. Bieber, and St. Kraft (2003). Evidence for a differential expression of the FceRIg chain in dendritic cells of atopic and nonatopic donors. J. Clin. Invest. 111, 1047-1056.
  • 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.
  • Linke, M., S. Jordans, L. Mach, V. Herzog, and K. Brix (2002). Thyroid stimulating hormone upregulates secretion of cathepsin B from thyroid epithelial cells. Biol. Chem. 383, 773-784.
  • Krüger, O., J.L. Beny, F. Chabaud, O. Traub, M. Theis, K. Brix, S. Kirchhoff, and K. Willecke (2002). Altered dye diffusion and upregulation of connexin37 in mouse aortic endothelium deficient in connexin40. J. Vasc. Res. 39, 160-172.
  • Hitzel, C., H. Kanzler, A. König, M.P. Kummer, K. Brix, V. Herzog, and N. Koch (2000). Thyroglobulin type I-like domains in invariant chain fusion proteins mediate resistance to cathepsin L digestion. FEBS Lett. 485, 67-70.
  • 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.
  • Saber-Lichtenberg, Y., K. Brix, A. Schmitz, J.E. Heuser, J.H. Wilson, L. Lorand, and V. Herzog (2000). Covalent cross-linking of secreted bovine thyroglobulin by transglutaminase. FASEB J. 14, 1005-1014.
  • Dombrowski, F., L. Klotz, H.J. Hacker, Y. Li, D. Klingmüller, K. Brix, V. Herzog, and P. Bannasch (2000). Hyperproliferative
  • Ohl, C., K. Brix, and W. Stockem (1991). Studies on microplasmodia of Physarum polycephalum. VIII. Quantitative analysis of contractile activities and microfilament organization. Cell Tissue Res. 264, 283-291.
  • Brix, K., A. Reinecke, and W. Stockem (1990). Dynamics of the cytoskeleton in Amoeba proteus. III. Influence of microinjected antibodies on the organization and function of the microfilament system. Eur. J. Cell Biol. 51, 279-284.
  • Sodeik, B., K. Brix, and W. Stockem (1989). Sequestration of microinjected molecular probes from the cytoplasm of Amoeba proteus. Europ. J. Protistol. 25, 75-84.
  • Christofidou-Solomidou, M., K. Brix, and W. Stockem (1989). Induced pinocytosis and cytoskeletal organization in Amoeba proteus – a combined fluorescence and electron microscopic study. Europ. J. Protistol. 24, 336-345.
  • Brix, K., and W. Stockem (1989). Functional analysis of actin fibrils in Physarum polycephalum. A morphological and quantitative study. Cell Tissue Res. 257, 115-122.
  • Kukulies, J., K. Brix, and W. Stockem (1987). Studies on microplasmodia of Physarum polycephalum. VI. Functional analysis of a cortical and fibrillar actin system by use of fluorescent-analog cytochemistry. Cell Tissue Res. 250, 125-134.
  • Brix, K., W. Stockem, and J. Kukulies (1987). Chemically induced changes in the morphology, dynamic activity and cytoskeletal organization of Physarum cell fragments. Cell Biol. Int. Rep. 11, 803-811.
  • Brix, K., J. Kukulies, and W. Stockem (1987). Studies on microplasmodia of Physarum polycephalum. V. Correlation of cell surface morphology, microfilament organization and motile activity. Protoplasma 137, 156-167.
  • Brix, K., and W. Stockem (1987). Studies on microplasmodia of Physarum polycephalum. VII. Adhesion-dependent changes in the organization of the fibrillar actin system. Cell Biol. Int. Rep. 11, 529-536.
  • Kukulies, J., K. Brix, and W. Stockem (1985). Fluorescent analog cytochemistry of the actin system and cell surface morphology in Physarum microplasmodia. Eur. J. Cell Biol. 39, 62-69.


Book Chapters

Brix, K., M. Qatato, J. Szumska, V. Venugopalan, M. Rehders (in press). Thyroglobulin storage and degradation for thyroid hormone liberation. In: The Thyroid and Its Diseases, edited by Markus Luster, Leonidas Duntas, and Leonard Wartofsky. Springer-Verlag, Heidelberg.

Brix, K., C.J. Scott, M.M.S. Heck (2013) Compartmentalization of Proteolysis. In: Proteases: Structure and Function, edited by Klaudia Brix and Walter Stöcker, Springer-Verlag Wien.

Brix, K. (2005). Chapter 05: Lysosomal Proteases: Revival of the Sleeping Beauty. In: Lysosomes, edited by Paul Saftig, Landes Bioscience.

Stockem, W., J. Kukulies, and K. Brix (1987). Analysis of cytoplasmic actomyosin functions in Physarum polycephalum by fluorescent analog cytochemistry. Internationales Symposium an der Akademie der Wissenschaften, Mainz. In: Fortschritte der Zoologie, 34: Nature and Function of Cytoskeletal Proteins in Motility and Transport. K.-E. Wohlfarth-Bottermann editor. Gustav Fischer Verlag, Stuttgart. 25-30.