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Proceedings of the National Academy of Sciences of the United States of America|June 19, 2013
Mechanistic and structural studies on legumain explain its zymogenicity, distinct activation pathways, and regulationElfriede Dall, Hans BrandstetterStructure (London, England : 1993)|December 17, 2009
Structural basis of the cofactor- and substrate-assisted activation of human coagulation factor IXaThomas Zögg, Hans BrandstetterBiochimie|September 26, 2015
Structure and function of legumain in health and diseaseElfriede Dall, Hans BrandstetterProgress in Molecular Biology and Translational Science|January 18, 2011
Complex assemblies of factors IX and X regulate the initiation, maintenance, and shutdown of blood coagulationThomas Zögg, Hans BrandstetterBiological Chemistry|April 14, 2009
Activation mechanisms of coagulation factor IXThomas Zögg, Hans BrandstetterBiological Chemistry|August 30, 2011
Polycystic kidney disease-like domains of clostridial collagenases and their role in collagen recruitmentUlrich Eckhard, Hans BrandstetterActa Crystallographica. Section F, Structural Biology and Crystallization Communications|January 11, 2012
Activation of legumain involves proteolytic and conformational events, resulting in a context- and substrate-dependent activity profileElfriede Dall, Hans BrandstetterInternational Journal of Molecular Sciences|October 27, 2022
Legumain Activity Is Controlled by Extended Active Site Residues and Substrate ConformationTasneem Elamin, Hans Brandstetter, Elfriede DallJournal of Biotechnology|November 5, 2013
Do-it-yourself histidine-tagged bovine enterokinase: a handy member of the protein engineer's toolboxWolfgang Skala, Peter Goettig, Hans BrandstetterBiochimie|September 11, 2019
Surface loops of trypsin-like serine proteases as determinants of functionPeter Goettig, Hans Brandstetter, Viktor MagdolenPageof 12