1. Voos, K., Schonauer, E., Alhayek, A., Haupenthal, J., Andreas, A., Muller, R., Hartmann, R. W., Brandstetter, H., Hirsch, A. K. H., and Ducho, C. (2021) Phosphonate as a Stable Zinc-Binding Group for „Pathoblocker“ Inhibitors of Clostridial Collagenase H (ColH). ChemMedChem
  2. Lam van, T. V., Heindl, M. R., Schlutt, C., Bottcher-Friebertshauser, E., Bartenschlager, R., Klebe, G., Brandstetter, H., Dahms, S. O., and Steinmetzer, T. (2021) The Basicity Makes the Difference: Improved Canavanine-Derived Inhibitors of the Proprotein Convertase Furin. ACS Med Chem Lett 12, 426-432
  3. Korotchenko, E., Schiessl, V., Scheiblhofer, S., Schubert, M., Dall, E., Joubert, I. A., Strandt, H., Neuper, T., Sarajlic, M., Bauer, R., Geppert, M., Joedicke, D., Wildner, S., Schaller, S., Winkler, S., Gadermaier, G., Horejs-Hoeck, J., and Weiss, R. (2021) Laser-facilitated epicutaneous immunotherapy with hypoallergenic beta-glucan neoglycoconjugates suppresses lung inflammation and avoids local side effects in a mouse model of allergic asthma. Allergy 76, 210-222
  4. Hoppe, I. J., Brandstetter, H., and Schonauer, E. (2021) Biochemical characterisation of a collagenase from Bacillus cereus strain Q1. Sci Rep 11, 4187
  5. Elsasser, B., and Goettig, P. (2021) Mechanisms of Proteolytic Enzymes and Their Inhibition in QM/MM Studies. Int J Mol Sci 22




  1. Soh, W. T., Demir, F., Dall, E., Perrar, A., Dahms, S. O., Kuppusamy, M., Brandstetter, H., and Huesgen, P. F. (2020) ExteNDing Proteome Coverage with Legumain as a Highly Specific Digestion Protease. Anal Chem 92, 2961-2971
  2. Konstantinovic, J., Yahiaoui, S., Alhayek, A., Haupenthal, J., Schonauer, E., Andreas, A., Kany, A. M., Muller, R., Koehnke, J., Berger, F. K., Bischoff, M., Hartmann, R. W., Brandstetter, H., and Hirsch, A. K. H. (2020) N-Aryl-3-mercaptosuccinimides as Antivirulence Agents Targeting Pseudomonas aeruginosa Elastase and Clostridium Collagenases. J Med Chem 63, 8359-8368
  3. Eckhard, U., Blochl, C., Jenkins, B. G. L., Mansfield, M. J., Huber, C. G., Doxey, A. C., and Brandstetter, H. (2020) Identification and characterization of the proteolytic flagellin from the common freshwater bacterium Hylemonella gracilis. Sci Rep 10, 19052
  4. Dall, E., Zauner, F. B., Soh, W. T., Demir, F., Dahms, S. O., Cabrele, C., Huesgen, P. F., and Brandstetter, H. (2020) Structural and functional studies of Arabidopsis thaliana legumain beta reveal isoform specific mechanisms of activation and substrate recognition. J Biol Chem 295, 13047-13064
  5. Aglas, L., Soh, W. T., Kraiem, A., Wenger, M., Brandstetter, H., and Ferreira, F. (2020) Ligand Binding of PR-10 Proteins with a Particular Focus on the Bet v 1 Allergen Family. Curr Allergy Asthma Rep 20, 25



  1. Wildner, S., Griessner, I., Stemeseder, T., Regl, C., Soh, W. T., Stock, L. G., Volker, T., Alessandri, C., Mari, A., Huber, C. G., Stutz, H., Brandstetter, H., and Gadermaier, G. (2019) Boiling down the cysteine-stabilized LTP fold – loss of structural and immunological integrity of allergenic Art v 3 and Pru p 3 as a consequence of irreversible lanthionine formation. Mol Immunol 116, 140-150
  2. Van Lam van, T., Ivanova, T., Hardes, K., Heindl, M. R., Morty, R. E., Bottcher-Friebertshauser, E., Lindberg, I., Than, M. E., Dahms, S. O., and Steinmetzer, T. (2019) Design, Synthesis, and Characterization of Macrocyclic Inhibitors of the Proprotein Convertase Furin. ChemMedChem 14, 673-685
  3. Soh, W. T., Aglas, L., Mueller, G. A., Gilles, S., Weiss, R., Scheiblhofer, S., Huber, S., Scheidt, T., Thompson, P. M., Briza, P., London, R. E., Traidl-Hoffmann, C., Cabrele, C., Brandstetter, H., and Ferreira, F. (2019) Multiple roles of Bet v 1 ligands in allergen stabilization and modulation of endosomal protease activity. Allergy 74, 2382-2393
  4. Pereira, G. A. N., da Silva, E. B., Braga, S. F. P., Leite, P. G., Martins, L. C., Vieira, R. P., Soh, W. T., Villela, F. S., Costa, F. M. R., Ray, D., de Andrade, S. F., Brandstetter, H., Oliveira, R. B., Caffrey, C. R., Machado, F. S., and Ferreira, R. S. (2019) Discovery and characterization of trypanocidal cysteine protease inhibitors from the ‚malaria box‘. Eur J Med Chem 179, 765-778
  5. Goettig, P., Brandstetter, H., and Magdolen, V. (2019) Surface loops of trypsin-like serine proteases as determinants of function. Biochimie 166, 52-76
  6. Fang, H., Zogg, T., and Brandstetter, H. (2019) Maturation of coagulation factor IX during Xase formation as deduced using factor VIII-derived peptides. FEBS Open Bio 9, 1370-1378
  7. Dahms, S. O., Demir, F., Huesgen, P. F., Thorn, K., and Brandstetter, H. (2019) Sirtilins – the new old members of the vitamin K-dependent coagulation factor family. J Thromb Haemost 17, 470-481
  8. Bronger, H., Magdolen, V., Goettig, P., and Dreyer, T. (2019) Proteolytic chemokine cleavage as a regulator of lymphocytic infiltration in solid tumors. Cancer Metastasis Rev 38, 417-430
  9. Barbosa da Silva, E., Dall, E., Briza, P., Brandstetter, H., and Ferreira, R. S. (2019) Cruzain structures: apocruzain and cruzain bound to S-methyl thiomethanesulfonate and implications for drug design. Acta crystallographica. Section F, Structural biology communications 75, 419-427



  1. Zauner, F. B., Elsasser, B., Dall, E., Cabrele, C., and Brandstetter, H. (2018) Structural analyses of Arabidopsis thaliana legumain gamma reveal differential recognition and processing of proteolysis and ligation substrates. The Journal of biological chemistry 293, 8934-8946
  2. Zauner, F. B., Dall, E., Regl, C., Grassi, L., Huber, C. G., Cabrele, C., and Brandstetter, H. (2018) Crystal Structure of Plant Legumain Reveals a Unique Two-Chain State with pH-Dependent Activity Regulation. The Plant cell 30, 686-699
  3. Winters, B. R., Vakar-Lopez, F., Brown, L., Montgomery, B., Seiler, R., Black, P. C., Boormans, J. L., Dall Era, M., Davincioni, E., Douglas, J., Gibb, E. A., van Rhijn, B. W. G., van der Heijden, M. S., Hsieh, A. C., Wright, J. L., and Lam, H. M. (2018) Mechanistic target of rapamycin (MTOR) protein expression in the tumor and its microenvironment correlates with more aggressive pathology at cystectomy. Urol Oncol 36, 342 e347-342 e314
  4. Schinagl, A., Kerschbaumer, R. J., Sabarth, N., Douillard, P., Scholz, P., Voelkel, D., Hollerweger, J. C., Goettig, P., Brandstetter, H., Scheiflinger, F., and Thiele, M. (2018) Role of the Cysteine 81 Residue of Macrophage Migration Inhibitory Factor as a Molecular Redox Switch. Biochemistry 57, 1523-1532
  5. Schilling, O., Biniossek, M. L., Mayer, B., Elsasser, B., Brandstetter, H., Goettig, P., Stenman, U. H., and Koistinen, H. (2018) Specificity profiling of human trypsin-isoenzymes. Biol Chem 399, 997-1007
  6. Magnen, M., Elsasser, B. M., Zbodakova, O., Kasparek, P., Gueugnon, F., Petit-Courty, A., Sedlacek, R., Goettig, P., and Courty, Y. (2018) Kallikrein-related peptidase 5 and seasonal influenza viruses, limitations of the experimental models for activating proteases. Biol Chem 399, 1053-1064
  7. Loessner, D., Goettig, P., Preis, S., Felber, J., Bronger, H., Clements, J. A., Dorn, J., and Magdolen, V. (2018) Kallikrein-related peptidases represent attractive therapeutic targets for ovarian cancer. Expert Opin Ther Targets 22, 745-763
  8. Kahler, U., Fuchs, J. E., Goettig, P., and Liedl, K. R. (2018) An unexpected switch in peptide binding mode: from simulation to substrate specificity. J Biomol Struct Dyn 36, 4072-4084
  9. Hollerweger, J. C., Hoppe, I. J., Regl, C., Stock, L. G., Huber, C. G., Lohrig, U., Stutz, H., and Brandstetter, H. (2018) Analytical Cascades of Enzymes for Sensitive Detection of Structural Variations in Protein Samples. Anal Chem 90, 5055-5065
  10. Guo, S., Briza, P., Magdolen, V., Brandstetter, H., and Goettig, P. (2018) Activation and activity of glycosylated KLKs 3, 4 and 11. Biol Chem 399, 1009-1022
  11. Debela, M., Magdolen, V., Skala, W., Elsasser, B., Schneider, E. L., Craik, C. S., Biniossek, M. L., Schilling, O., Bode, W., Brandstetter, H., and Goettig, P. (2018) Structural determinants of specificity and regulation of activity in the allosteric loop network of human KLK8/neuropsin. Sci Rep 8, 10705
  12. Dall, E., Hollerweger, J. C., Dahms, S. O., Cui, H., Haussermann, K., and Brandstetter, H. (2018) Structural and functional analysis of cystatin E reveals enzymologically relevant dimer and amyloid fibril states. The Journal of biological chemistry 293, 13151-13165
  13. Dahms, S. O., Hardes, K., Steinmetzer, T., and Than, M. E. (2018) X-ray Structures of the Proprotein Convertase Furin Bound with Substrate Analogue Inhibitors Reveal Substrate Specificity Determinants beyond the S4 Pocket. Biochemistry 57, 925-934
  14. Chen, C. Y., Melo, E., Jakob, P., Friedlein, A., Elsasser, B., Goettig, P., Kueppers, V., Delobel, F., Stucki, C., Dunkley, T., Fauser, S., Schilling, O., and Iacone, R. (2018) N-Terminomics identifies HtrA1 cleavage of thrombospondin-1 with generation of a proangiogenic fragment in the polarized retinal pigment epithelial cell model of age-related macular degeneration. Matrix Biol 70, 84-101



  1. Zhang, Z., Obianyo, O., Dall, E., Du, Y., Fu, H., Liu, X., Kang, S. S., Song, M., Yu, S. P., Cabrele, C., Schubert, M., Li, X., Wang, J. Z., Brandstetter, H., and Ye, K. (2017) Inhibition of delta-secretase improves cognitive functions in mouse models of Alzheimer’s disease. Nature communications 8, 14740
  2. Wildner, S., Elsasser, B., Stemeseder, T., Briza, P., Soh, W. T., Villalba, M., Lidholm, J., Brandstetter, H., and Gadermaier, G. (2017) Endolysosomal Degradation of Allergenic Ole e 1-Like Proteins: Analysis of Proteolytic Cleavage Sites Revealing T Cell Epitope-Containing Peptides. Int J Mol Sci 18
  3. Stemeseder, T., Freier, R., Wildner, S., Fuchs, J. E., Briza, P., Lang, R., Batanero, E., Lidholm, J., Liedl, K. R., Campo, P., Hawranek, T., Villalba, M., Brandstetter, H., Ferreira, F., and Gadermaier, G. (2017) Crystal structure of Pla l 1 reveals both structural similarity and allergenic divergence within the Ole e 1-like protein family. J Allergy Clin Immunol 140, 277-280
  4. Soh, W. T., Briza, P., Dall, E., Asam, C., Schubert, M., Huber, S., Aglas, L., Bohle, B., Ferreira, F., and Brandstetter, H. (2017) Two Distinct Conformations in Bet v 2 Determine Its Proteolytic Resistance to Cathepsin S. International journal of molecular sciences 18
  5. Schonauer, E., Kany, A. M., Haupenthal, J., Husecken, K., Hoppe, I. J., Voos, K., Yahiaoui, S., Elsasser, B., Ducho, C., Brandstetter, H., and Hartmann, R. W. (2017) Discovery of a Potent Inhibitor Class with High Selectivity toward Clostridial Collagenases. J Am Chem Soc 139, 12696-12703
  6. Ivanova, T., Hardes, K., Kallis, S., Dahms, S. O., Than, M. E., Kunzel, S., Bottcher-Friebertshauser, E., Lindberg, I., Jiao, G. S., Bartenschlager, R., and Steinmetzer, T. (2017) Optimization of Substrate-Analogue Furin Inhibitors. ChemMedChem 12, 1953-1968
  7. Hofer, H., Weidinger, T., Briza, P., Asam, C., Wolf, M., Twaroch, T. E., Stolz, F., Neubauer, A., Dall, E., Hammerl, P., Jacquet, A., and Wallner, M. (2017) Comparing Proteolytic Fingerprints of Antigen-Presenting Cells during Allergen Processing. International journal of molecular sciences 18
  8. Elsasser, B., Zauner, F. B., Messner, J., Soh, W. T., Dall, E., and Brandstetter, H. (2017) Distinct Roles of Catalytic Cysteine and Histidine in the Protease and Ligase Mechanisms of Human Legumain As Revealed by DFT-Based QM/MM Simulations. ACS catalysis 7, 5585-5593
  9. Dahms, S. O., Jiao, G. S., and Than, M. E. (2017) Structural Studies Revealed Active Site Distortions of Human Furin by a Small Molecule Inhibitor. ACS Chem Biol 12, 1211-1216
  10. Dahms, S. O., Jiao, G. S., and Than, M. E. (2017) Structural Studies Revealed Active Site Distortions of Human Furin by a Small Molecule Inhibitor. ACS Chem Biol 12, 2474
  11. Braga, S. F., Martins, L. C., da Silva, E. B., Sales Junior, P. A., Murta, S. M., Romanha, A. J., Soh, W. T., Brandstetter, H., Ferreira, R. S., and de Oliveira, R. B. (2017) Synthesis and biological evaluation of potential inhibitors of the cysteine proteases cruzain and rhodesain designed by molecular simplification. Bioorg Med Chem 25, 1889-1900



  1. Wolkerstorfer, S., Schwaiger, E., Rinnerthaler, M., Karina Gratz, I., Zoegg, T., Brandstetter, H., and Achatz-Straussberger, G. (2016) HAX1 deletion impairs BCR internalization and leads to delayed BCR-mediated apoptosis. Cell Mol Immunol 13, 451-461
  2. Machado, Y., Freier, R., Scheiblhofer, S., Thalhamer, T., Mayr, M., Briza, P., Grutsch, S., Ahammer, L., Fuchs, J. E., Wallnoefer, H. G., Isakovic, A., Kohlbauer, V., Hinterholzer, A., Steiner, M., Danzer, M., Horejs-Hoeck, J., Ferreira, F., Liedl, K. R., Tollinger, M., Lackner, P., Johnson, C. M., Brandstetter, H., Thalhamer, J., and Weiss, R. (2016) Fold stability during endolysosomal acidification is a key factor for allergenicity and immunogenicity of the major birch pollen allergen. J Allergy Clin Immunol 137, 1525-1534
  3. Kristensen, L. H., Olsen, O. H., Blouse, G. E., and Brandstetter, H. (2016) Releasing the brakes in coagulation Factor IXa by co-operative maturation of the substrate-binding site. Biochem J 473, 2395-2411
  4. Jung, S., Fischer, J., Spudy, B., Kerkow, T., Sonnichsen, F. D., Xue, L., Bonvin, A. M., Goettig, P., Magdolen, V., Meyer-Hoffert, U., and Grotzinger, J. (2016) The solution structure of the kallikrein-related peptidases inhibitor SPINK6. Biochem Biophys Res Commun 471, 103-108
  5. Guo, S., Skala, W., Magdolen, V., Briza, P., Biniossek, M. L., Schilling, O., Kellermann, J., Brandstetter, H., and Goettig, P. (2016) A Single Glycan at the 99-Loop of Human Kallikrein-related Peptidase 2 Regulates Activation and Enzymatic Activity. J Biol Chem 291, 593-604
  6. Goettig, P. (2016) Effects of Glycosylation on the Enzymatic Activity and Mechanisms of Proteases. Int J Mol Sci 17
  7. Debela, M., Magdolen, V., Bode, W., Brandstetter, H., and Goettig, P. (2016) Structural basis for the Zn2+ inhibition of the zymogen-like kallikrein-related peptidase 10. Biol Chem 397, 1251-1264
  8. Dall, E., and Brandstetter, H. (2016) Structure and function of legumain in health and disease. Biochimie 122, 126-150
  9. Dahms, S. O., Creemers, J. W., Schaub, Y., Bourenkov, G. P., Zogg, T., Brandstetter, H., and Than, M. E. (2016) The structure of a furin-antibody complex explains non-competitive inhibition by steric exclusion of substrate conformers. Sci Rep 6, 34303
  10. Dahms, S. O., Arciniega, M., Steinmetzer, T., Huber, R., and Than, M. E. (2016) Structure of the unliganded form of the proprotein convertase furin suggests activation by a substrate-induced mechanism. Proc Natl Acad Sci U S A 113, 11196-11201
  11. Brandstetter, H. (2016) The FELASA Award 2016 – A major award for laboratory animal science within Europe. Lab Anim 50, 317-318
  12. Ahmed, N., Dorn, J., Napieralski, R., Drecoll, E., Kotzsch, M., Goettig, P., Zein, E., Avril, S., Kiechle, M., Diamandis, E. P., Schmitt, M., and Magdolen, V. (2016) Clinical relevance of kallikrein-related peptidase 6 (KLK6) and 8 (KLK8) mRNA expression in advanced serous ovarian cancer. Biol Chem 397, 1265-1276
  13. Abfalter, C. M., Schonauer, E., Ponnuraj, K., Huemer, M., Gadermaier, G., Regl, C., Briza, P., Ferreira, F., Huber, C. G., Brandstetter, H., Posselt, G., and Wessler, S. (2016) Cloning, Purification and Characterization of the Collagenase ColA Expressed by Bacillus cereus ATCC 14579. PLoS One 11, e0162433



  1. Lu, Y., Hardes, K., Dahms, S. O., Bottcher-Friebertshauser, E., Steinmetzer, T., Than, M. E., Klenk, H. D., and Garten, W. (2015) Peptidomimetic furin inhibitor MI-701 in combination with oseltamivir and ribavirin efficiently blocks propagation of highly pathogenic avian influenza viruses and delays high level oseltamivir resistance in MDCK cells. Antiviral Res 120, 89-100
  2. Hoefgen, S., Dahms, S. O., Oertwig, K., and Than, M. E. (2015) The amyloid precursor protein shows a pH-dependent conformational switch in its E1 domain. J Mol Biol 427, 433-442
  3. Hardes, K., Becker, G. L., Lu, Y., Dahms, S. O., Kohler, S., Beyer, W., Sandvig, K., Yamamoto, H., Lindberg, I., Walz, L., von Messling, V., Than, M. E., Garten, W., and Steinmetzer, T. (2015) Novel Furin Inhibitors with Potent Anti-infectious Activity. ChemMedChem 10, 1218-1231
  4. Freier, R., Dall, E., and Brandstetter, H. (2015) Protease recognition sites in Bet v 1a are cryptic, explaining its slow processing relevant to its allergenicity. Scientific reports 5, 12707
  5. Fittler, H., Depp, A., Avrutina, O., Dahms, S. O., Than, M. E., Empting, M., and Kolmar, H. (2015) Engineering a Constrained Peptidic Scaffold towards Potent and Selective Furin Inhibitors. Chembiochem 16, 2441-2444
  6. Dall, E., Fegg, J. C., Briza, P., and Brandstetter, H. (2015) Structure and mechanism of an aspartimide-dependent peptide ligase in human legumain. Angew Chem Int Ed Engl 54, 2917-2921
  7. Dahms, S. O., Mayer, M. C., Roeser, D., Multhaup, G., and Than, M. E. (2015) Interaction of the amyloid precursor protein-like protein 1 (APLP1) E2 domain with heparan sulfate involves two distinct binding modes. Acta Crystallogr D Biol Crystallogr 71, 494-504



  1. Skala, W., Utzschneider, D. T., Magdolen, V., Debela, M., Guo, S., Craik, C. S., Brandstetter, H., and Goettig, P. (2014) Structure-function analyses of human kallikrein-related peptidase 2 establish the 99-loop as master regulator of activity. J Biol Chem 289, 34267-34283
  2. Sabala, I., Jagielska, E., Bardelang, P. T., Czapinska, H., Dahms, S. O., Sharpe, J. A., James, R., Than, M. E., Thomas, N. R., and Bochtler, M. (2014) Crystal structure of the antimicrobial peptidase lysostaphin from Staphylococcus simulans. FEBS J 281, 4112-4122
  3. Reinmuth-Selzle, K., Ackaert, C., Kampf, C. J., Samonig, M., Shiraiwa, M., Kofler, S., Yang, H., Gadermaier, G., Brandstetter, H., Huber, C. G., Duschl, A., Oostingh, G. J., and Poschl, U. (2014) Nitration of the birch pollen allergen Bet v 1.0101: efficiency and site-selectivity of liquid and gaseous nitrating agents. J Proteome Res 13, 1570-1577
  4. Kofler, S., Ackaert, C., Samonig, M., Asam, C., Briza, P., Horejs-Hoeck, J., Cabrele, C., Ferreira, F., Duschl, A., Huber, C., and Brandstetter, H. (2014) Stabilization of the dimeric birch pollen allergen Bet v 1 impacts its immunological properties. J Biol Chem 289, 540-551
  5. Hoefgen, S., Coburger, I., Roeser, D., Schaub, Y., Dahms, S. O., and Than, M. E. (2014) Heparin induced dimerization of APP is primarily mediated by E1 and regulated by its acidic domain. J Struct Biol 187, 30-37
  6. Guo, S., Skala, W., Magdolen, V., Brandstetter, H., and Goettig, P. (2014) Sweetened kallikrein-related peptidases (KLKs): glycan trees as potential regulators of activation and activity. Biol Chem 395, 959-976
  7. Grutsch, S., Fuchs, J. E., Freier, R., Kofler, S., Bibi, M., Asam, C., Wallner, M., Ferreira, F., Brandstetter, H., Liedl, K. R., and Tollinger, M. (2014) Ligand binding modulates the structural dynamics and compactness of the major birch pollen allergen. Biophys J 107, 2972-2981
  8. Eibl, C., Hessenberger, M., Wenger, J., and Brandstetter, H. (2014) Structures of the NLRP14 pyrin domain reveal a conformational switch mechanism regulating its molecular interactions. Acta Crystallogr D Biol Crystallogr 70, 2007-2018
  9. Eckhard, U., Huesgen, P. F., Brandstetter, H., and Overall, C. M. (2014) Proteomic protease specificity profiling of clostridial collagenases reveals their intrinsic nature as dedicated degraders of collagen. J Proteomics 100, 102-114
  10. Dorn, J., Beaufort, N., Schmitt, M., Diamandis, E. P., Goettig, P., and Magdolen, V. (2014) Function and clinical relevance of kallikrein-related peptidases and other serine proteases in gynecological cancers. Crit Rev Clin Lab Sci 51, 63-84
  11. Dockal, M., Hartmann, R., Fries, M., Thomassen, M. C., Heinzmann, A., Ehrlich, H., Rosing, J., Osterkamp, F., Polakowski, T., Reineke, U., Griessner, A., Brandstetter, H., and Scheiflinger, F. (2014) Small peptides blocking inhibition of factor Xa and tissue factor-factor VIIa by tissue factor pathway inhibitor (TFPI). J Biol Chem 289, 1732-1741
  12. Deressa, T., Stoecklinger, A., Wallner, M., Himly, M., Kofler, S., Hainz, K., Brandstetter, H., Thalhamer, J., and Hammerl, P. (2014) Structural integrity of the antigen is a determinant for the induction of T-helper type-1 immunity in mice by gene gun vaccines against E. coli beta-galactosidase. PLoS One 9, e102280
  13. Dahms, S. O., Hardes, K., Becker, G. L., Steinmetzer, T., Brandstetter, H., and Than, M. E. (2014) X-ray structures of human furin in complex with competitive inhibitors. ACS Chem Biol 9, 1113-1118
  14. Ackaert, C., Kofler, S., Horejs-Hoeck, J., Zulehner, N., Asam, C., von Grafenstein, S., Fuchs, J. E., Briza, P., Liedl, K. R., Bohle, B., Ferreira, F., Brandstetter, H., Oostingh, G. J., and Duschl, A. (2014) The impact of nitration on the structure and immunogenicity of the major birch pollen allergen Bet v 1.0101. PLoS One 9, e104520



  1. Zogg, T., Sponring, M., Schindler, S., Koll, M., Schneider, R., Brandstetter, H., and Auer, B. (2013) Crystal structures of the viral protease Npro imply distinct roles for the catalytic water in catalysis. Structure 21, 929-938
  2. Wenger, J., Klinglmayr, E., Frohlich, C., Eibl, C., Gimeno, A., Hessenberger, M., Puehringer, S., Daumke, O., and Goettig, P. (2013) Functional mapping of human dynamin-1-like GTPase domain based on x-ray structure analyses. PLoS One 8, e71835
  3. Skala, W., Goettig, P., and Brandstetter, H. (2013) Do-it-yourself histidine-tagged bovine enterokinase: a handy member of the protein engineer’s toolbox. J Biotechnol 168, 421-425
  4. Hoy, B., Brandstetter, H., and Wessler, S. (2013) The stability and activity of recombinant Helicobacter pylori HtrA under stress conditions. J Basic Microbiol 53, 402-409
  5. Eckhard, U., Schonauer, E., and Brandstetter, H. (2013) Structural basis for activity regulation and substrate preference of clostridial collagenases G, H, and T. J Biol Chem 288, 20184-20194
  6. Dall, E., and Brandstetter, H. (2013) Mechanistic and structural studies on legumain explain its zymogenicity, distinct activation pathways, and regulation. Proceedings of the National Academy of Sciences of the United States of America 110, 10940-10945
  7. Dahms, S. O., Kuester, M., Streb, C., Roth, C., Strater, N., and Than, M. E. (2013) Localization and orientation of heavy-atom cluster compounds in protein crystals using molecular replacement. Acta Crystallogr D Biol Crystallogr 69, 284-297
  8. Coburger, I., Dahms, S. O., Roeser, D., Guhrs, K. H., Hortschansky, P., and Than, M. E. (2013) Analysis of the overall structure of the multi-domain amyloid precursor protein (APP). PLoS One 8, e81926



  1. Kofler, S., Asam, C., Eckhard, U., Wallner, M., Ferreira, F., and Brandstetter, H. (2012) Crystallographically mapped ligand binding differs in high and low IgE binding isoforms of birch pollen allergen bet v 1. J Mol Biol 422, 109-123
  2. Dall, E., and Brandstetter, H. (2012) Activation of legumain involves proteolytic and conformational events, resulting in a context- and substrate-dependent activity profile. Acta Crystallogr Sect F Struct Biol Cryst Commun 68, 24-31
  3. Dahms, S. O., Konnig, I., Roeser, D., Guhrs, K. H., Mayer, M. C., Kaden, D., Multhaup, G., and Than, M. E. (2012) Metal binding dictates conformation and function of the amyloid precursor protein (APP) E2 domain. Journal of molecular biology 416, 438-452



  1. Zogg, T., and Brandstetter, H. (2011) Complex assemblies of factors IX and X regulate the initiation, maintenance, and shutdown of blood coagulation. Prog Mol Biol Transl Sci 99, 51-103
  2. Weidensee, S., Goettig, P., Bertone, M., Haas, D., Magdolen, V., Kiechle, M., Meindl, A., van Kuilenburg, A. B., and Gross, E. (2011) A mild phenotype of dihydropyrimidine dehydrogenase deficiency and developmental retardation associated with a missense mutation affecting cofactor binding. Clin Biochem 44, 722-724
  3. Tochowicz, A., Goettig, P., Evans, R., Visse, R., Shitomi, Y., Palmisano, R., Ito, N., Richter, K., Maskos, K., Franke, D., Svergun, D., Nagase, H., Bode, W., and Itoh, Y. (2011) The dimer interface of the membrane type 1 matrix metalloproteinase hemopexin domain: crystal structure and biological functions. J Biol Chem 286, 7587-7600
  4. Kuester, M., Kemmerzehl, S., Dahms, S. O., Roeser, D., and Than, M. E. (2011) The crystal structure of death receptor 6 (DR6): a potential receptor of the amyloid precursor protein (APP). J Mol Biol 409, 189-201
  5. Ginzinger, S. W., Gruber, M., Brandstetter, H., and Sippl, M. J. (2011) Real space refinement of crystal structures with canonical distributions of electrons. Structure 19, 1739-1743
  6. Eckhard, U., Schonauer, E., Nuss, D., and Brandstetter, H. (2011) Structure of collagenase G reveals a chew-and-digest mechanism of bacterial collagenolysis. Nat Struct Mol Biol 18, 1109-1114
  7. Eckhard, U., and Brandstetter, H. (2011) Polycystic kidney disease-like domains of clostridial collagenases and their role in collagen recruitment. Biol Chem 392, 1039-1045



  1. Seiz, L., Kotzsch, M., Grebenchtchikov, N. I., Geurts-Moespot, A. J., Fuessel, S., Goettig, P., Gkazepis, A., Wirth, M. P., Schmitt, M., Lossnitzer, A., Sweep, F. C., and Magdolen, V. (2010) Polyclonal antibodies against kallikrein-related peptidase 4 (KLK4): immunohistochemical assessment of KLK4 expression in healthy tissues and prostate cancer. Biol Chem 391, 391-401
  2. Nuss, D., Goettig, P., Magler, I., Denk, U., Breitenbach, M., Schneider, P. B., Brandstetter, H., and Simon-Nobbe, B. (2010) Crystal structure of the NADP-dependent mannitol dehydrogenase from Cladosporium herbarum: Implications for oligomerisation and catalysis. Biochimie 92, 985-993
  3. Magler, I., Nuss, D., Hauser, M., Ferreira, F., and Brandstetter, H. (2010) Molecular metamorphosis in polcalcin allergens by EF-hand rearrangements and domain swapping. FEBS J 277, 2598-2610
  4. Goettig, P., Magdolen, V., and Brandstetter, H. (2010) Natural and synthetic inhibitors of kallikrein-related peptidases (KLKs). Biochimie 92, 1546-1567
  5. Dahms, S. O., Hoefgen, S., Roeser, D., Schlott, B., Guhrs, K. H., and Than, M. E. (2010) Structure and biochemical analysis of the heparin-induced E1 dimer of the amyloid precursor protein. Proc Natl Acad Sci U S A 107, 5381-5386



  1. Zogg, T., and Brandstetter, H. (2009) Activation mechanisms of coagulation factor IX. Biol Chem 390, 391-400
  2. Zogg, T., and Brandstetter, H. (2009) Structural basis of the cofactor- and substrate-assisted activation of human coagulation factor IXa. Structure 17, 1669-1678
  3. Yoon, H., Blaber, S. I., Debela, M., Goettig, P., Scarisbrick, I. A., and Blaber, M. (2009) A completed KLK activome profile: investigation of activation profiles of KLK9, 10, and 15. Biol Chem 390, 373-377
  4. Eckhard, U., Schonauer, E., Ducka, P., Briza, P., Nuss, D., and Brandstetter, H. (2009) Biochemical characterization of the catalytic domains of three different Clostridial collagenases. Biol Chem 390, 11-18
  5. Ducka, P., Eckhard, U., Schonauer, E., Kofler, S., Gottschalk, G., Brandstetter, H., and Nuss, D. (2009) A universal strategy for high-yield production of soluble and functional clostridial collagenases in E. coli. Appl Microbiol Biotechnol 83, 1055-1065



  1. Wisniewska, M., Goettig, P., Maskos, K., Belouski, E., Winters, D., Hecht, R., Black, R., and Bode, W. (2008) Structural determinants of the ADAM inhibition by TIMP-3: crystal structure of the TACE-N-TIMP-3 complex. J Mol Biol 381, 1307-1319
  2. Eckhard, U., Nuss, D., Ducka, P., Schonauer, E., and Brandstetter, H. (2008) Crystallization and preliminary X-ray characterization of the catalytic domain of collagenase G from Clostridium histolyticum. Acta Crystallogr Sect F Struct Biol Cryst Commun 64, 419-421
  3. Debela, M., Beaufort, N., Magdolen, V., Schechter, N. M., Craik, C. S., Schmitt, M., Bode, W., and Goettig, P. (2008) Structures and specificity of the human kallikrein-related peptidases KLK 4, 5, 6, and 7. Biol Chem 389, 623-632
  4. Andersson, J., Salander, P., Brandstetter-Hiltunen, M., Knutsson, E., and Hamberg, K. (2008) Is it possible to identify patient’s sex when reading blinded illness narratives? An experimental study about gender bias. Int J Equity Health 7, 21



  1. Tochowicz, A., Maskos, K., Huber, R., Oltenfreiter, R., Dive, V., Yiotakis, A., Zanda, M., Pourmotabbed, T., Bode, W., and Goettig, P. (2007) Crystal structures of MMP-9 complexes with five inhibitors: contribution of the flexible Arg424 side-chain to selectivity. J Mol Biol 371, 989-1006
  2. Debela, M., Hess, P., Magdolen, V., Schechter, N. M., Steiner, T., Huber, R., Bode, W., and Goettig, P. (2007) Chymotryptic specificity determinants in the 1.0 A structure of the zinc-inhibited human tissue kallikrein 7. Proc Natl Acad Sci U S A 104, 16086-16091
  3. Debela, M., Goettig, P., Magdolen, V., Huber, R., Schechter, N. M., and Bode, W. (2007) Structural basis of the zinc inhibition of human tissue kallikrein 5. J Mol Biol 373, 1017-1031
  4. Barazza, A., Gotz, M., Cadamuro, S. A., Goettig, P., Willem, M., Steuber, H., Kohler, T., Jestel, A., Reinemer, P., Renner, C., Bode, W., and Moroder, L. (2007) Macrocyclic statine-based inhibitors of BACE-1. Chembiochem 8, 2078-2091



  1. Debela, M., Magdolen, V., Schechter, N., Valachova, M., Lottspeich, F., Craik, C. S., Choe, Y., Bode, W., and Goettig, P. (2006) Specificity profiling of seven human tissue kallikreins reveals individual subsite preferences. J Biol Chem 281, 25678-25688
  2. Debela, M., Magdolen, V., Grimminger, V., Sommerhoff, C., Messerschmidt, A., Huber, R., Friedrich, R., Bode, W., and Goettig, P. (2006) Crystal structures of human tissue kallikrein 4: activity modulation by a specific zinc binding site. J Mol Biol 362, 1094-1107



  1. Messerschmidt, A., Macieira, S., Velarde, M., Badeker, M., Benda, C., Jestel, A., Brandstetter, H., Neuefeind, T., and Blaesse, M. (2005) Crystal structure of the catalytic domain of human atypical protein kinase C-iota reveals interaction mode of phosphorylation site in turn motif. J Mol Biol 352, 918-931
  2. Kyrieleis, O. J., Goettig, P., Kiefersauer, R., Huber, R., and Brandstetter, H. (2005) Crystal structures of the tricorn interacting factor F3 from Thermoplasma acidophilum, a zinc aminopeptidase in three different conformations. J Mol Biol 349, 787-800
  3. Groll, M., Bochtler, M., Brandstetter, H., Clausen, T., and Huber, R. (2005) Molecular machines for protein degradation. Chembiochem 6, 222-256
  4. Goettig, P., Brandstetter, H., Groll, M., Gohring, W., Konarev, P. V., Svergun, D. I., Huber, R., and Kim, J. S. (2005) X-ray snapshots of peptide processing in mutants of tricorn-interacting factor F1 from Thermoplasma acidophilum. J Biol Chem 280, 33387-33396
  5. Brandstetter, H., Scheer, M., Heinekamp, C., Gippner-Steppert, C., Loge, O., Ruprecht, L., Thull, B., Wagner, R., Wilhelm, P., Scheuber, H. P., and Working Group on Evaluation of, I. V. C. S. o. t. A. W. I. C. f. B. R. o. t. F. o. M. (2005) Performance evaluation of IVC systems. Lab Anim 39, 40-44
  6. Azim, M. K., Goehring, W., Song, H. K., Ramachandran, R., Bochtler, M., and Goettig, P. (2005) Characterization of the HslU chaperone affinity for HslV protease. Protein Sci 14, 1357-1362



  1. Sichler, K., Kopetzki, E., Huber, R., Bode, W., Hopfner, K. P., and Brandstetter, H. (2003) Physiological fIXa activation involves a cooperative conformational rearrangement of the 99-loop. J Biol Chem 278, 4121-4126
  2. Ksiazek, D., Brandstetter, H., Israel, L., Bourenkov, G. P., Katchalova, G., Janssen, K. P., Bartunik, H. D., Noegel, A. A., Schleicher, M., and Holak, T. A. (2003) Structure of the N-terminal domain of the adenylyl cyclase-associated protein (CAP) from Dictyostelium discoideum. Structure 11, 1171-1178
  3. Groll, M., Brandstetter, H., Bartunik, H., Bourenkow, G., and Huber, R. (2003) Investigations on the maturation and regulation of archaebacterial proteasomes. J Mol Biol 327, 75-83
  4. Engel, M., Hoffmann, T., Wagner, L., Wermann, M., Heiser, U., Kiefersauer, R., Huber, R., Bode, W., Demuth, H. U., and Brandstetter, H. (2003) The crystal structure of dipeptidyl peptidase IV (CD26) reveals its functional regulation and enzymatic mechanism. Proc Natl Acad Sci U S A 100, 5063-5068



  1. Sichler, K., Hopfner, K. P., Kopetzki, E., Huber, R., Bode, W., and Brandstetter, H. (2002) The influence of residue 190 in the S1 site of trypsin-like serine proteases on substrate selectivity is universally conserved. FEBS Lett 530, 220-224
  2. Sichler, K., Banner, D. W., D’Arcy, A., Hopfner, K. P., Huber, R., Bode, W., Kresse, G. B., Kopetzki, E., and Brandstetter, H. (2002) Crystal structures of uninhibited factor VIIa link its cofactor and substrate-assisted activation to specific interactions. J Mol Biol 322, 591-603
  3. Kim, J. S., Groll, M., Musiol, H. J., Behrendt, R., Kaiser, M., Moroder, L., Huber, R., and Brandstetter, H. (2002) Navigation inside a protease: substrate selection and product exit in the tricorn protease from Thermoplasma acidophilum. J Mol Biol 324, 1041-1050
  4. Goettig, P., Groll, M., Kim, J. S., Huber, R., and Brandstetter, H. (2002) Structures of the tricorn-interacting aminopeptidase F1 with different ligands explain its catalytic mechanism. EMBO J 21, 5343-5352
  5. Cha, H., Kopetzki, E., Huber, R., Lanzendorfer, M., and Brandstetter, H. (2002) Structural basis of the adaptive molecular recognition by MMP9. J Mol Biol 320, 1065-1079
  6. Brandstetter, H., Kim, J. S., Groll, M., Gottig, P., and Huber, R. (2002) Structural basis for the processive protein degradation by tricorn protease. Biol Chem 383, 1157-1165



  1. Schroder, J., Henke, A., Wenzel, H., Brandstetter, H., Stammler, H. G., Stammler, A., Pfeiffer, W. D., and Tschesche, H. (2001) Structure-based design and synthesis of potent matrix metalloproteinase inhibitors derived from a 6H-1,3,4-thiadiazine scaffold. J Med Chem 44, 3231-3243
  2. Grams, F., Brandstetter, H., D’Alo, S., Geppert, D., Krell, H. W., Leinert, H., Livi, V., Menta, E., Oliva, A., Zimmermann, G., Gram, F., Brandstetter, H., D’Alo, S., Geppert, D., Krell, H. W., Leinert, H., Livi, V. E., Oliva, A., and Zimmermann, G. (2001) Pyrimidine-2,4,6-Triones: a new effective and selective class of matrix metalloproteinase inhibitors. Biol Chem 382, 1277-1285
  3. Brandstetter, H., Kim, J. S., Groll, M., and Huber, R. (2001) Crystal structure of the tricorn protease reveals a protein disassembly line. Nature 414, 466-470
  4. Brandstetter, H., Grams, F., Glitz, D., Lang, A., Huber, R., Bode, W., Krell, H. W., and Engh, R. A. (2001) The 1.8-A crystal structure of a matrix metalloproteinase 8-barbiturate inhibitor complex reveals a previously unobserved mechanism for collagenase substrate recognition. J Biol Chem 276, 17405-17412



  1. Hopfner, K. P., Lang, A., Karcher, A., Sichler, K., Kopetzki, E., Brandstetter, H., Huber, R., Bode, W., and Engh, R. A. (1999) Coagulation factor IXa: the relaxed conformation of Tyr99 blocks substrate binding. Structure 7, 989-996
  2. Brandstetter, H., Whittington, D. A., Lippard, S. J., and Frederick, C. A. (1999) Mutational and structural analyses of the regulatory protein B of soluble methane monooxygenase from Methylococcus capsulatus (Bath). Chem Biol 6, 441-449



  1. Graf von Roedern, E., Grams, F., Brandstetter, H., and Moroder, L. (1998) Design and synthesis of malonic acid-based inhibitors of human neutrophil collagenase (MMP8). J Med Chem 41, 339-345
  2. Graf von Roedern, E., Brandstetter, H., Engh, R. A., Bode, W., Grams, F., and Moroder, L. (1998) Bis-substituted malonic acid hydroxamate derivatives as inhibitors of human neutrophil collagenase (MMP8). J Med Chem 41, 3041-3047
  3. Chang, J., Jin, J., Lollar, P., Bode, W., Brandstetter, H., Hamaguchi, N., Straight, D. L., and Stafford, D. W. (1998) Changing residue 338 in human factor IX from arginine to alanine causes an increase in catalytic activity. J Biol Chem 273, 12089-12094
  4. Brandstetter, H., Engh, R. A., Von Roedern, E. G., Moroder, L., Huber, R., Bode, W., and Grams, F. (1998) Structure of malonic acid-based inhibitors bound to human neutrophil collagenase. A new binding mode explains apparently anomalous data. Protein Sci 7, 1303-1309



  1. Rosenzweig, A. C., Brandstetter, H., Whittington, D. A., Nordlund, P., Lippard, S. J., and Frederick, C. A. (1997) Crystal structures of the methane monooxygenase hydroxylase from Methylococcus capsulatus (Bath): implications for substrate gating and component interactions. Proteins 29, 141-152
  2. Hopfner, K. P., Brandstetter, H., Karcher, A., Kopetzki, E., Huber, R., Engh, R. A., and Bode, W. (1997) Converting blood coagulation factor IXa into factor Xa: dramatic increase in amidolytic activity identifies important active site determinants. EMBO J 16, 6626-6635
  3. Bode, W., Brandstetter, H., Mather, T., and Stubbs, M. T. (1997) Comparative analysis of haemostatic proteinases: structural aspects of thrombin, factor Xa, factor IXa and protein C. Thromb Haemost 78, 501-511



  1. Engh, R. A., Brandstetter, H., Sucher, G., Eichinger, A., Baumann, U., Bode, W., Huber, R., Poll, T., Rudolph, R., and von der Saal, W. (1996) Enzyme flexibility, solvent and ‚weak‘ interactions characterize thrombin-ligand interactions: implications for drug design. Structure 4, 1353-1362
  2. Brandstetter, H., Kuhne, A., Bode, W., Huber, R., von der Saal, W., Wirthensohn, K., and Engh, R. A. (1996) X-ray structure of active site-inhibited clotting factor Xa. Implications for drug design and substrate recognition. J Biol Chem 271, 29988-29992



  1. Sturzl, M., Brandstetter, H., Zietz, C., Eisenburg, B., Raivich, G., Gearing, D. P., Brockmeyer, N. H., and Hofschneider, P. H. (1995) Identification of interleukin-1 and platelet-derived growth factor-B as major mitogens for the spindle cells of Kaposi’s sarcoma: a combined in vitro and in vivo analysis. Oncogene 10, 2007-2016
  2. Brandstetter, H., Bauer, M., Huber, R., Lollar, P., and Bode, W. (1995) X-ray structure of clotting factor IXa: active site and module structure related to Xase activity and hemophilia B. Proc Natl Acad Sci U S A 92, 9796-9800
  3. Bergner, A., Bauer, M., Brandstetter, H., Sturzebecher, J., and Bode, W. (1995) The X-ray crystal structure of thrombin in complex with N alpha-2-naphthylsulfonyl-L-3-amidino-phenylalanyl-4-methylpiperidide: the beneficial effect of filling out an empty cavity. J Enzyme Inhib 9, 101-110



  1. Sciacca, F. L., Sturzl, M., Bussolino, F., Sironi, M., Brandstetter, H., Zietz, C., Zhou, D., Matteucci, C., Peri, G., Sozzani, S., and et al. (1994) Expression of adhesion molecules, platelet-activating factor, and chemokines by Kaposi’s sarcoma cells. J Immunol 153, 4816-4825



  1. Bauer, M., Brandstetter, H., Turk, D., Sturzebecher, J., and Bode, W. (1993) Crystallographic determination of thrombin complexes with small synthetic inhibitors as a starting point for the receptor-based design of antithrombotics. Semin Thromb Hemost 19, 352-360



  1. Sturzl, M., Brandstetter, H., and Roth, W. K. (1992) Kaposi’s sarcoma: a review of gene expression and ultrastructure of KS spindle cells in vivo. AIDS Res Hum Retroviruses 8, 1753-1763
  2. Roth, W. K., Brandstetter, H., and Sturzl, M. (1992) Cellular and molecular features of HIV-associated Kaposi’s sarcoma. AIDS 6, 895-913
  3. Brandstetter, H., Turk, D., Hoeffken, H. W., Grosse, D., Sturzebecher, J., Martin, P. D., Edwards, B. F., and Bode, W. (1992) Refined 2.3 A X-ray crystal structure of bovine thrombin complexes formed with the benzamidine and arginine-based thrombin inhibitors NAPAP, 4-TAPAP and MQPA. A starting point for improving antithrombotics. J Mol Biol 226, 1085-1099