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| Magnus Abrahamson, Lund, Sweden | Novel human cystatins |
| Marcia Alvarez Fernandez, Lund, Sweden | (no presentation) |
| Ennes Auerswald, Munich, Germany | Chicken cystatin variants: What did they tell us? |
| Francesc X. Aviles, Barcelona, Spain | Structural determinants in the functionality of metallo- procarboxypeptidases |
| Antonio Baici, Zürich, Switzerland | Who drills the holes in osteoarthritic cartilage? The misdeeds of cathepsin B |
| Beatrice Bachmeier, Munich, Germany | Comparison of protease profiles of human keratinocyte cell lines with different tumorigenicities |
| Agnieszka Banbula, Cracow, Poland | Crystal structure of Staphylococcus aureus metalloproteinase |
| Alan J. Barrett, Cambridge, UK | Cysteine proteinases old and new |
| Wolfgang P. Baumeister, Martinsried, Germany | Tricorn protease - the core of a modular proteolytic system |
| Jules Beekwilder, Wageningen, Netherlands | Applying phage display to direct plant protease inhibitors to insect proteases |
| Selma Berbic, Tuzla, Bosnia and Herzegovina | Human cathepsin D: Isolation and immunochemical characterization |
| Maria Bjarnadottir, Lund, Sweden | Expression of wild-type and L68Q-mutated cystatin C in mammalian cells |
| Judith Bond, Hershey, USA | Mutational analysis of structure, biosynthesis, and activation of astacin family metalloendopeptidases |
| Ernst Bergmann, Edmonton, Canada | A structural perspective on the polyprotein processing of hepatitis A virus (preliminary title) |
| Andreas Bergner, Martinsried, Germany | Crystal structures of TIMPs and their interaction with MMPs |
| Joseph G. Bieth, Illkirch, France | Regulation of serpin activity |
| Matthias Bochtler, Martinsried, Germany | Crystal structure of ClpQ, a multimeric E. coli protease |
| Wolfram Bode, Martinsried, Germany | How TIMPs inhibit MMPs |
| Klaudia Brix, Bonn, Germany | Cathepsin B mediated extracellular proteolysis by thyroid epithelial cells |
| Maryanne Brown, Ridgefield, USA | (no presentation) |
| Nils Brünner, Copenhagen, Denmark | The urokinase plasminogen activator receptor in blood from cancer patients |
| Marcin Bugno, Cracow, Poland | Regulation of TIMP-1 and TIMP-3 expression under inflammatory conditions |
| Ye Chen, Tokushima, Japan | (no presentation) |
| Nina Cimerman, Ljubljana, Slovenia | 24 hour changes of cathepsins B, H, L, and cystatin C levels in normal and asthmatic sera |
| Theresa H.T. Coetzer, Pietermaritzburg, South Africa | Cysteine and serine proteases as targets for trypanocidal agents |
| Howard Crawford, Nashvile, USA | Tumorigenesis in MMP knockout mice |
| Soren Weis Dahl, Horsholm, Denmark | Transferase activity of cathepsin C active site cleft mutants |
| Clive Dennison, Pietermaritzburg, South Africa | Lysosomes and lysosomal proteolysis revisited |
| Carlos Fernandez Catalan, Martinsried, Germany | Crystal structures of TIMPs and their interaction with MMPs (with Dr. Andreas Bergner) |
| Meta Filipic, Ljubljana, Slovenia | Application of in vitro invasion assay for studying proteinase inhibitors |
| Peter Friedrich, Budapest, Hungary | Activation mechanisms of calpains from mammals and Drosophila |
| Hans Fritz, Munich, Germany | (organizer - no presentation) |
| Leopold Froehlich, Martinsried, Germany | Gene structure, recombinant expression and functional properties of murine proteinase 3 |
| Pablo Fuentes-Prior, Martinsried, Germany | Crystal structure of thrombin in complex with triabin, an exosite binding inhibitor with a lipocalin fold |
| Bernhard Gabriel, Martinsried, Germany | Structure-based design of benzamidine-type inhibitors of factor Xa |
| Francis Gauthier, Tours, France | Substrate specificity and regulation of trypanosomal cysteine proteinases |
| Bernd Gerhartz, Lund, Sweden | Structural and functional characterisation of the amyloid forming L68Q mutant of cystatin C and its dimerisation |
| Michael Groll, Martinsried, Germany | Crystal structure of the yeast proteasome |
| Katarina Håkansson, Lund, Sweden | Properties and distribution of mouse, rat and human cystatin C |
| Andrej Hasilik, Marburg, Germany | Human procathepsin D |
| Karl-Peter Hopfner, Martinsried, Germany | Structure-function studies of coagulation factor IXa/Xa chimeras |
| Martin Horn, Prague, Czech Republic | Cysteine proteinase inhibitors isolated from insect (Colorado potato beetle). |
| Robert Huber, Martinsried, Germany | Opening lecture |
| Shinobu Ikeda, Nagasaki, Japan | Construction and characterization of N-glycosylation-site deficient mutants of cathepsin E expressed in NRK-cells |
| Shoichi Ishiura, Tokyo, Japan | Alzheimer amyloid precursor protein and proteinases |
| Ciro Isidoro, Torino, Italy | Lysosomal proteolysis and apoptosis by TNF and anti-neoplastic drug |
| Sybille Jäger, Stuttgart, Germany | The active sites of the eucaryotic 20S proteasome and their involvement in subunit precursor processing |
| Mikko Järvinen, Oulu, Finland | Rhabdovirus-induced apoptosis of a carp cell line is inhibited by cystatin A |
| Dieter Jenne, Martinsried, Germany | (coauthor, see at Froehlich, Wilharm) |
| Maarten A. Jongsma, Wageningen, The Netherlands | Combatting inhibitor-insensitive proteases of insect pests |
| Tomoko Kadowaki, Fukuoka, Japan | Roles of Arg-gingipain in processing and translocation of the membrane and secretory proteins in Porphyromonas gingivalis |
| KeWon Kang, Taejon, Korea | The guamerin-derived synthetic peptide on elastase and acute pancreatitis |
| Jan-Olof Karlsson, Gotenburg, Sweden | Proteolytic activity in monolayers of polarized epithelial cells as determined by a cell-permeable fluorogenic calpain substrate |
| Nobuhiko Katunuma, Tokushima, Japan | Lysosomal cathepsin B plays an essential role in the processing of ovalbumin as an exogenous antigen
Develpoment of selective inhibitors of cathepsin L, S, C, K and B, and protection of bone resorption by CLIK |
| Seiichi Kawashima, Tokyo, Japan | Calpainolysis and lens cataractogenesis |
| Hiroshi Kido, Tokushima, Japan | Role of tryptase in T cell activation: Implications for function both as protease and molecular chaperone (tentative title) |
| Eiki Kominami, Tokyo, Japan | Intracellular processing of cathepsins and their inclusion into lysosomes and phagosomes |
| Nataša Kopitar Jerala, Ljulbjana, Slovenia | Cloning and expression of A22 anti-stefin A Fab and epitope mapping using site-directed mutagenesis |
| Bruce D. Korant, Wilmington, USA | Viral protease action is cytotoxic and may precede apoptosis |
| Janko Kos, Ljubljana, Slovenia | Clinical relevance of cathepsins and their inhibitors in cancer and some other diseases |
| Nechama S. Kosower, Palo Alto, USA | Calpain-calpastatin system in myoblast differentiation and fusion: Implications for other biological systems |
| Edward M.Kosower, Tel Aviv, Israel | Red cell membrane proteins and the calpain-calpastatin system in the aged |
| Stefan Kreusch, Jena, Germany | Mutants of the conserved ERFNIN motif in human cathepsin S reveal essential functions of this motif for maturation |
| Tamara Lah, Ljubljana, Slovenia | Cysteine proteinase inhibitors and cathepsins in breast tumor progression |
| Maria Lalioti, Geneva, Switzerland | A dodecamer repeat expansion in the cystatin B gene is the most common mutation in progressive myoclonus epilepsy (EPM1) |
| Brigita Lenarcic, Ljubljana, Slovenia | A thyroglobulin type-1 domain inhibitors of cysteine proteinases |
| Nataša Levicar, Ljubljana, Slovenia | Relative prognostic significance of cysteine proteinases, urokinase and their inhibitors in breast cancer patients |
| Lukas Mach, Nedlands, Australia | Murine squamous carcinoma cells require misrouted lysosomal cysteine proteinases for invasion through basement membrane |
| Hiroshi Maeda, Kumamoto, Japan | PMN collagenase activation in microbial infection |
| Viktor Magdolen, Munich, Germany | (coauthor, see at Schmitt) |
| Jianxin Mai, Detroit, USA | Interacting proteins for procathepsin B detected by yeast two-hybrid interaction trap screening |
| Robert W. Mason, Wilmington, USA | Targeted protease inhibitors identify endosomal proteases |
| Janez Mavri, Ljubljana, Slovenia | Ireversible inhibition of the HIV-1 protease: A quantum mechanical calculation study |
| Shahriar Mobashery, Detroit, USA | Computational insight into structures, substrate preference and inhibition by protein inhibitors of human gelatinases |
| John S. Mort, Montreal, Canada | Endopeptidase and exopeptidase activities of cathepsin B and the biological consequences |
| Rory E. Morty, Pietermaritzburg, South Africa | A serine oligopeptidase from Trypanosoma brucei: Potential role in disease pathogenesis and as a therapeutic target |
| Constanze Mueller, Martinsried, Germany | Cysteine-based inhibitors of matrix-metalloproteases |
| Dorit Nägler, Montreal, Canada | Major increase in endopeptidase activity of human cathepsin B upon removal of occluding loop contacts |
| Carl-Michael Nathansson, Lund, Sweden | (Title not communicated so far) |
| Yukio Nishimura, Fukuoka, Japan | Malignant transformation alters intracellular trafficking of lysosomal cathepsins in breast epithelial cells |
| Kuniaki Okamoto, Fukuoka, Japan | Construction and characterization of a lysine-specific cysteine proteinase (Lys-gingipain)-deficient mutant of Porphyromonas gingivalis |
| Akira Okuyama, Tsukuba, Japan | Inhibition of human tumor growth in nude mice by matrix metalloproteinase inhibitors |
| Steve Olson, Chicago, USA | New insights into the novel mechanism of proteinase inhibition by serpin family inhibitors (preliminary title) |
| Yasumiko Ozaki, Nagoya, Japan | Selective neuronal death induced by activation of nuclear pro micro-calpain under conditions of hypoxia |
| Marina A.A. Parry, Martinsried, Germany | Crystal structure of TSV-PA, a plasminogen activator from snake venom |
| Lowri H. Phylip, Cardiff, UK | Protein inhibitors of aspartic proteinases |
| Iva Pichova, Prague, Czech Republic | Peptidomimetic inhibitors of aspartic proteinases of Candida albicans and Candida tropicalis |
| Adrian R. Pierotti, Glasgow, UK | Promoter sequence of rat thimet oligopeptidase |
| Tatjana Popovic, Ljubljana, Slovenia | Cysteine proteinases and their inhibitor in Phaesolus vulgaris leaves |
| Jan Potempa, Cracow, Poland | Clinical implications of interaction between Porphyromonas gingivalis proteinases (gingipains) and blood coagulation cascade |
| Brendon Price, Scottsville, South Africa | Immunocytochemical localisation and granule designation of neutrophil TIMP-1 |
| Galina Pungercic, Ljubljana, Slovenia | Inhibition of papain-like cysteine proteinases by thyroglobulin |
| Gerald Reeck, Manhattan (KS), USA | The corn inhibitor of activated Hageman factor: Three-dimensional structure and functional properties of reactive-site variants |
| Martin Renatus, Martinsried, Germany | Crystal structures of single-chain plasminogen activators |
| Ulrich Rester, Martinsried, Germany | Crystal structure of the thrombin complex formed with rhodniin |
| Jennifer Rivett, Bristol, UK | Proteasome localization and the effects of gamma-interferon |
| Thomas Ruppert, Munich, Germany | A mutational hotspot in p53 alters proteasome mediated processing of the flanking CTL epitope and protects cells from lysis by CTL specific for this epitope |
| Eiichi Saitoh, Niigata, Japan | Preparation and characterization of two proteins, SA1 and SA2, given by two alleles of the CST2 locus coding for human cystatin SA, by genetic engineering approaches |
| Andrej Sali, New York, USA | Proteases in baker's yeast: A genome analysis |
| Guy Salvesen, San Diego, USA | Regulation of caspase activation and activity |
| Makoto Sasaki, Nagoya, Japan | Selective neuronal death induced by activation of pro micro-calpain under conditions of hypoxia |
| Ulrich Sauer, Munich, Germany | (no presentation) |
| Manfred Schmitt, Munich, Germany | The plasminogen activator system, a new target for tumor therapy |
| Ana Schweiger, Ljubljana, Slovenia | Detection of human cathepsin H in normal and tumor cytosols and sera |
| Abelardo M. Silva, Frederick, USA | Structure and inhibition of plasmepsin II, a hemoglobin degradig enzyme from Plasmodium falciparum |
| Christian Sommerhoff, Munich, Germany | Novel proteinase inhibitors from the medical leech: Properties, structures, and tools to elucidate pathomechanisms |
| Georgia Sotiropoulou, Patras, Greece | Cloning, expression and functional characterization of cystatin M and protease M |
| Eberhard Spiess, Heidelberg, Germany | Inhibitory capacity of synthetic cathepsin B inhibitors at the cellular level |
| Gwendolyn Spizz, ResearchTriangle Park, NC, USA | MARCKS: A protein kinase C regulated cellular substrate for cathepsin B |
| Valentin M. Stepanov, Moscow, Russia | Glutamyl endopeptidases |
| Veronika Stoka, Ljubljana, Slovenia | Inactivation of cruzipain: Kinetical and structural studies |
| Kvido Strisovsky, Prague, Czech Republic | Inhibition study of tethered dimers of the HIV-1 proteinase |
| Natalie J. Tigue, Cardiff, UK | Human herpes virus-6 proteinase |
| Hideaki Tsuge, Tokushima, Japan | (no presentation) |
| Toshifumi Tsukahara, Tokyo, Japan | Identification and physiological role of an alternative spliced form of caspase-3 |
| Boris Turk, Ljubljana, Slovenia | pH as an important factor for the regulation of activity of lysosomal cysteine proteinases |
| Dušan Turk, Ljubljana, Slovenia | Crystal structure of porcine cathepsin H determined at 2.1 A resolution |
| Bertus Van den Burg, Groningen, The Netherlands | Probing possible catalytic hinge bending motions in thermolysin-like proteases by Gly to Ala mutations |
| Klaus von der Helm, Munich, Gemany | Retroviral proteinases: HIV proteinase inhibitors as effective chemotherapy and the problem of resistance mutation |
| Bernd Werle, Heidelberg, Germany | Cathepsins and cystatins: Prognostic factors in human lung cancer |
| Bernd Wiederanders, Jena, Germany | The various functions of cysteine peptidase propeptides |
| Elke Wilharm, Martinsried, Germany | Refolding of human granzyme K expressed in E. coli yields enzymatically active protein |
| Andrew Winter, Glasgow, UK | Characterization of the NRD convertase gene promoter |
| Margaret Worrall, Dublin, Ireland | (Title will be announced later) |
| Kenji Yamamoto, Fukuoka, Japan | Roles of cathepsin E and cathepsin D in neuronal death mechanisms |
Back to the homepage of the Brdo '97 Symposium: http://bio.ijs.muzej.si/conf/brdo97.htm
Department of Biochemistry and Molecular Biology
Jo"zef Stefan Institute
Jamova 39
SI-61111 Ljubljana
Slovenia
tel.: (+386 61) 1773 900
fax: (+386 61) 273 594
E-mail: Marko.Dolinar@IJS.SI
Send Email to the local
organising committee.
Link to the homepage of local organisers: Department of Biochemistry and Molecular Biology, J. Stefan Institute, Ljubljana, Slovenia.
Last updated September 23, 1997. Send comments to Marko.Dolinar@IJS.SI.