Publikationsliste:  PUBMED



Santos, N. P., Soh, W. T., Demir, F., Tenhaken, R., Briza, P., Huesgen, P. F., Brandstetter, H., and Dall, E. (2023) Phytocystatin 6 is a context-dependent, tight-binding inhibitor of Arabidopsis thaliana legumain isoform beta. Plant J

Santos, N. P., Brandstetter, H., and Dall, E. (2023) Arabidopsis thaliana Phytocystatin 6 Forms Functional Oligomer and Amyloid Fibril States. Biochemistry

Holzner, C., Bottinger, K., Blochl, C., Huber, C. G., Dahms, S. O., Dall, E., and Brandstetter, H. (2023) Legumain Functions as a Transient TrkB Sheddase. Int J Mol Sci 24


Elamin, T., Santos, N. P., Briza, P., Brandstetter, H., and Dall, E. (2022) Structural and functional studies of legumain-mycocypin complexes revealed a competitive, exosite-regulated mode of interaction. J Biol Chem 298, 102502

Elamin, T., Brandstetter, H., and Dall, E. (2022) Legumain Activity Is Controlled by Extended Active Site Residues and Substrate Conformation. Int J Mol Sci 23

Dall, E., Licht, A., and Brandstetter, H. (2022) Production of Functional Plant Legumain Proteases Using the Leishmania tarentolae Expression System. Methods Mol Biol 2447, 35-51


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

Dall, E., Stanojlovic, V., Demir, F., Briza, P., Dahms, S. O., Huesgen, P. F., Cabrele, C., and Brandstetter, H. (2021) The Peptide Ligase Activity of Human Legumain Depends on Fold Stabilization and Balanced Substrate Affinities. ACS Catal 11, 11885-11896


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

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


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 Crystallogr F Struct Biol Commun 75, 419-427


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. J Biol Chem 293, 8934-8946

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. Plant Cell 30, 686-699

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. J Biol Chem 293, 13151-13165


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. Nat Commun 8, 14740

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. Int J Mol Sci 18

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. Int J Mol Sci 18

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 Catal 7, 5585-5593


Dall, E., and Brandstetter, H. (2016) Structure and function of legumain in health and disease. Biochimie 122, 126-150


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. Sci Rep 5, 12707

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


Dall, E., and Brandstetter, H. (2013) Mechanistic and structural studies on legumain explain its zymogenicity, distinct activation pathways, and regulation. Proc Natl Acad Sci U S A 110, 10940-10945


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