The association
Im Zusammenhang mit dem Auftreten der ersten Fälle von BSE in Bayern wurden von der Bayerischen Staatsregierung Ende 2000 zusätzliche Maßnahmen zur Bekämpfung der Prionkrankheiten beschlossen. Anfang des Jahres 2001 wurde eine Forschungsinitiative gestartet, deren Ergebnis der Bayerische Forschungsverbund Prionen (FORPRION) ist. Dieser Forschungsverbund wird zu gleichen Teilen aus dem Etat des Ministeriums für Wissenschaft, Forschung und Kunst und aus dem Etat des Ministeriums für Gesundheit Ernährung und Verbraucherschutz finanziert.
Ziel des Forschungsverbundes ist es, sowohl durch Grundlagenforschung als auch durch anwendungsorientierte Forschung zu Erkenntnissen zu gelangen, die bei der Diagnostik und Therapie der Prionkrankheiten bei Mensch und Tier weiterführen und im Verbraucherschutz Anwendung finden. Der Forschungsverbund hat folgende Schwerpunkte:
Grundlagenforschung
Pathogenese der Prionkrankheiten
Therapie
Diagnostik
Epidemiologie und Veterinärmedizin
Genetik der BSE
Verbraucherschutz
Netzwerk:
Der Forschungsverbund vernetzt 25 Projekte, angesiedelt an 5 bayerischen Universitäten und an Instituten der Max-Planck-Gesellschaft. Das Netzwerk von FORPRION umfaßt die Universität Nürnberg-Erlangen, Würzburg, Bayreuth, Ludwig-Maximilians-Universität München, die Technische Universität München und das Max-Planck-Institut für Biochemie, Martinsried.
Alle Forschungsgruppen des Bayerischen Forschungsverbundes Prionen (FORPRION) stehen über die Nationale TSE-Forschungsplattform in wissenschaftlichem Austausch mit den in der Prionforschung arbeitenden Gruppen in der Bundesrepublik Deutschland. Außerdem ist der Forschungsverbund FORPRION mit der Deutschen CJD Surveillance und dem <link http: www.neuropathologie.med.uni-muenchen.de neurobiobank_muenchen index.html _blank>Brain-Net , dem Deutschen Referenzzentrum für Erkrankungen des ZNS, verbunden.
Organisation
Spokesperson
General Management
Managing-committee
Head of Research Division
- Dr. Ralf Alsfasser
- Prof. Dr. Johann Bauer
- Prof. Dr. Cord-Michael Becker
- Dr. Uwe Bertsch
- Prof. Dr. Thomas Brocker
- Prof. Dr. Volker Erfle
- Prof. Dr. Hans-Rudolf Fries
- Prof. Dr. Martin Förster
- Prof.Dr. Manfred Gareis
- Prof. Dr. Manfred Gerlach
- Dr. Armin Giese
- Dr. Martin Groschup
- Prof. Dr. Christian Haass
- Prof. Dr. Ulrich Hartl
- Prof. Dr. Jochen Herms
- Prof. Dr. Bertold Hock
- Prof. Dr. Wolfgang Klee
- Prof. Dr. Michael Klein
- Prof. Dr. Hans Kretzschmar
- Prof. Dr. Rudolf Martini
- Prof. Dr Ortwin Meyer
- Prof. Dr. Luis Moroder
- Prof. Dr. Erwin Märtlbauer
- Prof. Dr. Fritz G. Parak
- Prof. Dr. Monika Pischetsrieder
- Prof. Dr. Peter Riederer
- Prof. Dr. rer.nat. Siegfried Scherer
- Prof. Dr. Katrin Schiebel
- Prof. Dr. Wolfgang Schmahl
- Prof. Dr. Hermann M. Schätzl
- Prof. Dr. Michael Sendtner
- Prof. Dr. Andreas Stolle
- Prof. Dr. Jörg Tatzelt
- Prof. Dr. Paul Tavan
- Prof. Dr. Volker ter Meulen
- Prof. Dr. Uwe Truyen
- Prof. Dr. Rudi van Eldik
- Dr. Stefan Weiss
- Dr. Stefan Wiese
- Prof. Dr. Eckhard Wolf
Scientists
- Christian Bach
- Angela Bahlo
- T Düthorn
- Sabine Ebner
- Dipl.-Humanbiol. Alexa Ertmer
- Dr. Eckhard Flechsig
- Ulrike Frankenberg
- Dr. rer. nat. Holger Geue
- Dipl.Phys. Klaus Grantner
- Dr. Alex Greenwood
- Prof. Dr. Karl Heinritzi
- Judith Holtbecker
- PD Dr. rer. nat Andreas Humeny
- Dipl.Ing.agr.Univ Katrin Juling
- Dr. Xenia Kashkevich
- Dr. Regina Klose
- Igor Kobsar
- Priv.-Doz. Dr. Karl Kramer
- Prof. Dr. Christine Leib-Mösch
- O. Lipp
- Dr. Marko Maringer
- Dr. Ute Marx
- Dr. Ivica Medugorac
- Dipl.Phys. Matthias Mentler
- Prof. Dr. Franz Meußdorfer
- Prof. Dr. Karsten Meyer
- Mali Miyashita
- Dr. Simone Mueller
- Nicole Niklas
- Cindy Nitschke
- Anton Nowotni
- Dr. Birgit Oidtmann
- Dr. Rothraud Pichner
- Dr. Christian Renner
- Dr. Barbara Sandmeier
- Dipl. Biologin Christina Scherbel
- Dr. Christian Schörner
- Dr Martin Seifert
- Dr. Shneh Sethi
- Martina Stork
- Prof. Dr. Klaus Troeger
- Armgard Uehlhoff
- Dr.rer.nat. Carmen Villmann
- Jens Wagner
- Dr. Petra Weber
- Dipl. Biol. Stephan Weinhardt
- Andreas Weiss
- Dr. Heike Wendel
- Dr. Konstanze F. Winklhofer
- Dr.vetmed. Gerda Wuensch
- Dr. sc.hum. Seong-Wook Yun
- Achim Zahl
- Dr. Valeri Zakhartchenko
Partner
Scientific partner
- BFAV
- Institut für neue und neuartige Tierseuchenerreger
- Bundesanstalt für Fleischforschung
- Institut für Mikrobiologie und Toxikologie
- FORPRION
- c/o LMU München, Zentrum für Neuropathologie und Prionforschung
- GSF
- Institut für molekulare Virologie
- Julius-Maximilians-Universität Würzburg
- Institut für Virologie und Immunbiologie
- Klinik für Psychiatrie und Psychotherapie, Klinische Neurochemie
- Neurologische Klinik, Experimentelle Entwicklungsneurobiologie
- Neurologische Klinik, Institut für Klinische Neurobiologie
- LMU München
- Fakultät für Physik, Sektion Physik
- II. Med. Tierklinik
- Institut für Biochemie
- Institut für Hygiene und Technologie der Lebensmittel tierischen Ursprungs
- Institut für Immunologie
- Institut für molekulare Tierzucht und Biotechnologie
- Institut für Tierpathologie
- Institut für Tierzucht
- Institut für Zoologie und Fischereibiologie
- Lehrstuhl für Hygiene und Technologie der Milch
- Lehrstuhl für Krankheiten des Schweines
- Lehrstuhl für Stoffwechselbiochemie
- Zentrum für Neuropathologie und Prionforschung
- Max Planck Institut
- TU München
- Center of Life Sciences
- Institut für Klinische Virologie
- Institut für Mikrobiologie, Forschungszentrum für Milch und Lebensmittel Weihenstephan
- Institut für Molekulare Virologie
- Lehrstuhl für Tierhygiene
- Lehrstuhl für Tierzucht
- Physik Department E17
- Universität Bayreuth
- Lehrstuhl für Mikrobiologie
- Lehrstuhl für Struktur und Chemie der Biopolymere
- Universität Erlangen
- Institut für Anorganische Chemie
- Institut für Biochemie
- Institut für Pharmazie und Lebensmittelchemie
- Zentralinstitut für Tiergesundheit, Bayern
Partner of the industry
- Cenas AG
Fields of work
Projects
- Diagnosis of prion diseases
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Epidemiology and Veterinary medicine
- Bay 1 Occurence of TSE in natural habitats: Transmission of prions through wild animals and farmed wild ruminants in Northern Bavaria
- LMU 13 Studies the genetic diversity of the porcine prion protein
- LMU 19 Clinical and Epidemiological Investigations of BSE in Bavaria
- LMU 19 a Occurrence and Stability of the BSE Agent in Foodstuff (primarily in Milk and Milk Products) and in the Environment
- LMU 21 Investigation of Sporadically Occurring Spongiform Brain Lesions in Cattle
- Genetics
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Basic research on prion diseases
- Erl 8 Metal Ion Induced Conformational Changes in Peptides: A Putative Mechanism for the Formation of Abnormal Prion Protein Isoforms
- LMU 2 Cu(II)-binding of PrPC: Influence on Structure, Conformational Dynamics and Infectivity
- LMU 6 In Vivo Phosphorylation and Cellular Transport of Mutant and WT Prion Proteins in Living Neurons
- LMU 9 Phenotyping of Prion Diseases using GFP-PrP Chimeras in Transgenic Mice
- LMU 5 Analysis of Bovine and Human Prions in Cell Culture Systems for Diagnostic, Analytical and Therapeutic Purposes
- Therapy of prion diseases
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Pathogenesis of prion diseases
- LMU 11 Function of Dendritic Cells (DC) in the Pathogenesis of Prion Disease
- TUM 7 The Role of Activated Retroviral Genes as Cofactors in Prion-induced Spongiform Encephalopathy: Studies with a Mouse Model for Pathogenesis and Therapy
- Wü 1 Pathogenesis of Prion Diseases I
- Wü 1 Pathogenesis of Prion Diseases II
- Wü 1 Pathogenesis of Prion Diseases III
- Wü 1 Pathogenesis of Prion Diseases IV
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Consumer protection
- Erl 3 High Sensitive Immunassay for Detection of Central Nervous Tissue in Food
- LMU 19 a Occurrence and Stability of the BSE Agent in Foodstuff (primarily in Milk and Milk Products) and in the Environment
- LMU 20 Species specific detection of central nervous tissue or other TSE risk material in meat products
- TUM 12 Natural Isotope Ratio of Bioelements as an Indicator of the Origin of Animal Products and of Animal Protein in Ruminant Feed
News
Press
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22.05.2007
Bernhard: Verbraucherschutz profitiert von BSE-Forschung und Vorsorgemaßnahmen
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Publications
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Unaltered susceptibility to scrapie in serotonin transporter deficient mice
Mössner R, Yun S-W, Lesch K-P, Gerlach M, Klein MA, Riederer P Neurochem Int 49: 454-458 (2006)
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Zum Vorkommen Transmissibler Spongiformer Enzephalopathien beim Rehwild (Capreolus capreolus), Rotwild (Cervuc elphus) und Gamswild (Rupicapra rupicarpa) in Bayern
K. Schwaiger, B Stierstorfer, W. Schmahl und J. Bauer Berliner und Münchner Tierärztliche Wochenschrift 2004;117:24-29.
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Unaltered susceptibility scrapie in serotonin transporter deficient mice
Moessner R, Yun SW, Lesch KP, Gerlach M, Klein MA, Riederer, P. Neurochemistry International 49: 454-458 (2006)
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Unaltered prion protein cleavage in plasminogen-deficient mice
Barnewitz K, Maringer M, Mitteregger G, Giese A, Bertsch U, Kretzschmar HA. Neuroreport. 2006 Apr 3;17(5):527-30.
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Transesterification and amide cis-trans isomerization in Zn and Cd complexes of the chelating amino acid ligand Boc-Asp(Dpa)-OBzl
Niklas, N., Zahl, A. & Alsfasser, R. . Dalton Trans, 154-62 (2007).
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Toward semisynthetic lipoproteins by convergent strategies based on click and ligation chemistry
Musiol HJ, Dong S, Kaiser M, Bausinger R, Zumbusch A, Moroder L Chem Biochem (2005) 6, 625-628
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The tyrosine kinase inhibitor STI571 induces cellular clearance of PrPSc in prion-infected cells
Ertmer A, Gilch S, Yun SW, Flechsig E, Klebl B, Stein-Gerlach M, Klein MA, Schatzl HM., J Biol Chem. 2004 Oct 1;279(40):41918-27
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The tyrosine kinase inhibitor STI571 induces cellular clearance of PrPSc in prion-infected cells
Ertmer,A.; Gilch,S.; Yun,S.W.; Flechsig,E.; Klebl,B.; Stein-Gerlach,M.; Klein,M.A.; Schatzl,H.M. J Biol Chem (2004)
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The tyrosine kinase inhibitor imatinib mesylate delays prion neuroinvasion by inhibiting prion propagation in the periphery
Yun, S.-W., Ertmer, A., Gilch, S., Flechsig, E., Riederer, P., Gerlach, M., Schätzl, H. and Klein, MA. J NeuroVirology 2007, #UJNV-07-02-0166.R1,in press
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The tyrosinase kinase inhibitor Imatinib mesylate delays prion neuroinvasion by inhibiting prion propagation in the periphery
Yun S-W, Ertmer A, Flechsig, E, Gilch S, Riederer P, Gerlach M, Schätzl HM, Klein A J NeuroVirol 13: 1-10 (2007)
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The structural transition of the prion protein into its pathogenic conformation is induced by unmasking hydrophobic sites
Leffers KW, Schell J, Jansen K, Lucassen R, Kaimann T, Nagel-Steger L, Tatzelt J, Riesner D J Mol Biol. 2004 Nov 26;344(3):839-53.
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The role of chaperones in Parkinson's disease and prion diseases
Winklhofer, K.F. and Tatzelt, J. In Gaestel, M. (ed.), Molecular chaperones in health and diseases. Springer-Verlag, Vol. 172, 221-258.
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The reactivity of N-coordinated amides in metallopeptide frameworks: molecular events in metal-induced pathogenic pathways?
Niklas,N.; Hampel,F.; Liehr,G.; Zahl,A.; Alsfasser,R. Chemistry (2001), 7 (23), 5135 - 5142
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The prion-like protein Doppel fails to interact with itself, the prion protein and the 37 kDa/67 kDa laminin receptor in the yeast two-hybrid system
Christoph Hundt and Stefan Weiss Biochim Biophys Acta 1689 1 1-5
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The Configuration of the Cu2+ Binding Region in Full-Length Human Prion Protein Compared With the Isolated Octapeptid
Andreas Weiss, Pablo del Pino, Uwe Bertsch, Christian Renner, Matthias Mentler, Klaus Vet. Microbiol. (in press) (2007).
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The chemistry of nitrogen coordinated tertiary carboxamides: a spectroscopic study on bis(picolyl)amidecopper(II) complexes
Niklas, N. & Alsfasser, R. . Dalton Trans, 3188-99 (2006).
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The cellular prion protein modulates the intracellular calcium response to hydrogen peroxide
Krebs, B., Wiebelitz, A. Balitzki-Korte, B., Vassallo, N., Paluch, S., Onodera T., Kretzschmar, H., Herms, J. J Neurochem. 100:358-67, 2007
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The C-terminal globular domain of the prion protein is necessary and sufficient for import into the endoplasmic reticulum
Heske,J.; Heller,U.; Winklhofer,K.F.; Tatzelt,J. J. Biol. Chem.(2004), 279 (7), 5435 - 5443
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The anticancer drug imatinib induces cellular autophagy
Ertmer A., Huber V., Gilch S., Yoshimori T., Erfle V., Duyster J., Elsasser H.P. & Schätzl H.M Leukemia. 2007 Mar 1; [Epub ahead of print]
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The 37-kDa/67-kDa laminin receptor acts as the cell-surface receptor for the cellular prion protein
Gauczynski,S.; Peyrin,J.M.; Haik,S.; Leucht,C.; Hundt,C.; Rieger,R.; Krasemann,S.; Deslys,J.P.; Dormont,D.; Lasmezas,C.I.; Weiss,S. EMBO J (2001), 20 (21), 5863 - 5875
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The 37 kDa/67 kDa laminin receptor is required for PrP(Sc) propagation in scrapie-infected neuronal cells
Leucht,C.; Simoneau,S.; Rey,C.; Vana,K.; Rieger,R.; Lasmezas,C.I.; Weiss,S. EMBO Rep. (2003), 4 (3), 290 - 295
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The 37 kDa/67 kDa laminin receptor acts as a receptor for infectious prions and is inhibited by polysulfated glycanes
Gauczynski, S., Nikles, D., El-Gogo, S., Papy-Garcia, D., Rey, C., Alban,S., Barritault, D., Lasmézas, C.I. and Weiss, S Journal of Infectious Diseases, 194, 702-709, 2007
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Systematic identification of anti-prion drugs by high-throughput screening based on scanning for intensely fluorescent targets.
Bertsch,U., Winklhofer,K.F., Hirschberger,Th., Bieschke,J., Weber,P., Hartl,F.U., Tavan,P., Tatzelt,J., Kretzschmar HA, and Giese,A. (2005) J Virol 79, 7785-7791
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Systematic identification of anti-prion drugs by high-throughput screening based on scanning for intensely fluorescent targets
Bertsch,U., Winklhofer,K.F., Hirschberger,Th., Bieschke,J., Weber,P., Hartl,F.U., Tavan,P., Tatzelt,J., Kretzschmar HA, and Giese,A. (2005) J Virol 79, 7785-7791
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Systematic identification of anti-prion drugs by high-throughput screening based on scanning for intensely fluorescent targets
Bertsch,U., Winklhofer,K.F., Hirschberger,Th., Bieschke,J., Weber,P., Hartl,F.U., Tavan,P., Tatzelt,J., Kretzschmar HA, and Giese,A. (2005 J Virol 79, 7785-7791
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Surveillance for Prion Disease in Cervids, Germany
Schettler,E; Steinbach,F; Eschenbacher-Kaps,I; Gerst, K; Meussdoerffer, F; Risch, K; Streich, W.J; Fröhlich, K. Emerging Infectious Diseases 12, 2, 2006
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Structural Instability of the Prion Protein upon M205S/R Mutations Revealed by Molecular Dynamics Simulations
Hirschberger T, Stork M, Schropp B, Winklhofer KF, Tatzelt J, Tavan P. Biophys J. 2006 Mar 2; [Epub ahead of print]
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Structural Instability of the Prion Protein upon M205S/R Mutations Revealed by Molecular Dynamics Simulations
Hirschberger T, Stork M, Schropp B, Winklhofer KF, Tatzelt J, Tavan P. Biophys J. 2006 Mar 2; [Epub ahead of print]
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Strategies to eliminate PrPc as substrate for conversion into PrPSc
Gilch, S., Nunziante, M., Ertmer, A. & Schätzl, H.M Vet. Microbiol. (in press)
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Spectroscopic investigation on the Cu2+ binding of full-length human prion protein
del Pino P, Weiss A, Bertsch U, Renner C, Mentler M, Grantner K, Fiorino F, Meyer-Klaucke W, Moroder L, Kretzschmar HA, Parak FG Eur Biophys J (2007) 36, 239-252
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Single particle analysis of manganese-induced prion protein aggregates. Biochem
Levin,J., Bertsch,U., Kretzschmar,H., and Giese,A. Biochem. Biophys. Res. Commun. 329, 1200-1207
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Single chain Fv antibodies directed against the 37kDa/ 67kDa laminin receptor as therapeutic tools in prion diseases
Zuber, C., Knackmuss, S., Rey, C., Reusch, U., Röttgen, P., Fröhlich, P., Arnold, G.J., Pace, C., Mitteregger, G., Little, M. and Weiss, S Molecular Immunology 2007, in press
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Selective Rac1 inhibition in dendritic cells diminishes apoptotic cell uptake and cross-presentation in vivo.
Kerksiek, K. M., F. Niedergang, P. Chavrier, D. H. Busch, and T. Brocker. Blood 105:742-749, 2005
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Role of the CD8+ dendritic cell subset in transmission of prions
Sethi S., Kerksiek KM, Brocker T, Kretzschmar H. J. Virology 2007 Feb 14; Epub ahead of print
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Recognition of luminal prion protein aggregates by post-ER quality control mechanisms is mediated by the pre-octarepeat region of PrP
Gilch, S, Nunziante, M., Ertmer, A., Wopfner, F., Laszlo, L., and Schätzl, H.M. Traffic (2004), in press
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PRNP promoter polymorphisms are associated with BSE susceptibility in Swiss and German cattle
B. Haase, M. G. Doherr, T. Seuberlich, C. Drogemuller, G. Dolf, P.Nicken, K.Schiebel, U. Ziegler, M. H. Groschup, A. Zurbriggen, T. Leeb BMC Genomics 8, 5 (2007)
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Prion protein-related proteins from zebrafish are complex glycosylated and contain a glycosylphosphatidylinositol anchor
Margit Miesbauer, Theresa Bamme, Constanze Riemer, Birgit Oidtmann, Konstanze F. Winklhofer, Michael Baier and Jörg Tatzelt Biochemical and Biophysical Research Communications 341 (2006) 218–224
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Prion protein-related proteins from zebrafish are complex glycosylated and contain a glycosylphosphatidylinositol anchor
Margit Miesbauer, Theresa Bamme, Constanze Riemer, Birgit Oidtmann, Konstanze F. Winklhofer, Michael Baier and Jörg Tatzelt Biochemical and Biophysical Research Communications 341 (2006) 218–224
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Prion protein expression in bovine podocytes and extraglomerular mesangial
Amselgruber WM, Steffl M, Didier A, Martlbauer E, Pfaff E, Buttner M. Cell Tissue Res. 2006 Jun;324(3):497-505. Epub 2006 Feb 17
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Prion infection influences murine endogenous retrovirus expression in neuronal cells
Anna Stengel, Christian Bach, Ina Vorberg, Oliver Frank, Sabine Gilch, Gloria Lutzny, Wolfgang Seifarth, Volker Erfle, Elke Maas, Hermann Schätzl, Christine Leib-Mösch, Alex D. Greenwood BBRC 343 (2006): 825-831
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Prion diseases: from molecular biology to intervention strategies
Nunziante, M., Gilch, S., Schatzl, H. M Chembiochem. (2003),4,1268-84
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Presenilin-1 affects trafficking and processing of betaAPP and is targeted in a complex with nicastrin to the plasma membrane
Kaether,C.; Lammich,S.; Edbauer,D.; Ertl,M.; Rietdorf,J.; Capell,A.; Steiner,H.; Haass,C. J. Cell Biol. (2002), 156,551 - 561
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Post-translational import of the prion protein into the endoplasmic reticulum interferes with cell viability: A critical role for the putative transmembrane domain
Heller,U.; Winklhofer,K.F.; Heske,J.; Reintjes,A.; Tatzelt,J. J. Biol. Chem.(2003) 278 (38), 36139 - 36147
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Post exposure prophylaxis against prion disease with a stimulator of innate immunity
Sethi S., Lipford G., Wagner H., Kretzschmar H Lancet: 360: 229-230, 2002
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Polyclonal anti-PrP auto-antibodies induced with dimeric PrP interfere efficiently with PrPSc propagation in prion-infected cells
Gilch, S., Wopfner, F., Renner-Müller, I., Kremmer, E., Bauer, C., Wolf, E., Brem, G., Groschup, M. & Schätzl, H.M. J. Biol. Chem. (2003) 278: 18524-18531.
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Photo-induced crosslinking of prion protein oligomers and prions
Piening N, Weber P, Högen T, Beekes M, Kretzschmar H, Giese A Amyloid (2006) 13, 67-77
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Perspektiven des Klonens in der Tierzucht und in der biomedizinischen Forschung.
Wolf E LEOPOLDINA (R. 3) 51, 407-414
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Pathogenic mutations located in the hydrophobic core of the prion protein interfere with folding and attachment of the glycosylphosphatidylinositol anchor
Kiachopoulos S, Bracher A, Winklhofer KF, Tatzelt J J Biol Chem. 2005 Mar 11;280(10):9320-9.
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Oxidative stress in the brain at early preclinical stages of mouse scrapie
Yun, S. W.; Gerlach, M.; Riederer, P.; Klein, M. A. Exp Neurol, June 26, 2006
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Oxidative stress in the brain at early preclinical stage of mouse scrapie
Yun SW, Gerlach M, Riederer P, Klein MA Experimental Neurology 201: 90-98, 2006
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Neuropathological findings in brains of bavarian cattle clinically suspected of bovine spongiform encephalopathy
Miyashita,M.; Stierstorfer,B.; Schmahl,W. J.Vet.Med B Infect.Dis.Vet.Public Health, 2004,51 (5),209 - 215
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Nachweis von ZNS-Kontaminationen in Fleisch
Sandmeier B., Becker C.-M., Rotheneder R., Gareis M., Pischetsrieder M Lebensmittelchemie, 57: 84 – 85, 2003
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Myelin Proteolipid Protein as a new target for the detection of central nervous tissues in food
Sandmeier B, Villmann C, Becker, C-M, Düthorn T, Gareis M, Pischetsrieder M Lebensmittelchemie, 60: 19, 2006
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Myelin Proteolipid Protein als neues Markerprotein zum Nachweis von ZNS-Kontaminationen in Fleisch und Fleischerzeugnissen
Sandmeier B, Becker C-M, Düthorn T, Gareis M, Pischetsrieder M Lebensmittelchemie, 58: 153, 2004
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Myelin protein (PLP) as a marker antigen of central nervous system for routine food control
Villmann C, S. B., Pischetsrieder M, Becker C-M J Agric Food Chem (2007)
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Multiple administrations of Oligodeoxynucleotides containing CpG motifs influence Ig
Sethi S., Ebner S., Hinske C., Kretzschmar H Immunopharmacol Immunotoxicol: 27: 447-460, 2005
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Molecular dynamics simulations of proteins and peptides: Problems, achievements, and perspectives
P Tavan, H Carstens and G Mathias In: Protein Folding Handbook. Part 1. J Buchner and T Kiefhaber (Eds.), Wiley-VCH, Weinheim, 1170-Handbook. Part 1. J Buchner and T Kiefhaber (Eds.), Wiley-VCH, Weinheim, 1170-1195 (2005)
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Molecular basis of cerebral neurodegeneration in prion diseases
Tatzelt, J. and Schatzl, H.M FEBS J, 274, 606-611
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Molecular basis of cerebral neurodegeneration in prion diseases
Tatzelt, J. &, Schätzl, H.M FEBS Journal 274, 606-611
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Modulation of L-type voltage-gated calcium channels by recombinant prion protein
Korte,S.; Vassallo,N.; Kramer,M.L.; Kretzschmar,H.A.; Herms,J. J.Neurochem.(2003) 87 (4), 1037 -1042
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Misfolding of the prion protein at the plasma membrane induces endocytosis, intracellular retention and degradation
Kiachopoulos,S.; Heske,J.; Tatzelt,J.; Winklhofer,K.F. Traffic 2004,5(6), 426-436
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Misfolded proteinase K-resistant hyperphosphorylated alpha-synuclein in aged transgenic mice with locomotor deterioration and in human alpha-synucleinopathies
Neumann,M.; Kahle,P.J.; Giasson,B.I.; Ozmen,L.; Borroni,E.; Spooren,W.; Muller,V.; Odoy,S.; Fujiwara,H.; Hasegawa,M.; Iwatsubo,T.; Trojanowski,J.Q.; Kretzschmar,H.A.; Haass,C. J. Clin.Invest. (2002), 110, 1429 -1439
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Micellar environments induce structuring of the N-terminal tail of the prion protein
Renner,C.; Fiori,S.; Fiorino,F.; Landgraf,D.; Deluca,D.; Mentler,M.; Grantner,K.; Parak,F.G.; Kretzschmar,H.; Moroder,L. Biopolymers 2004, 73 (4), 421 - 433
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Methods for studying synaptosomal copper release
Hopt,A.; Korte,S.; Fink,H.; Panne,U.; Niessner,R.; Jahn,R.; Kretzschmar,H.; Herms,J. J.Neurosci.Methods (2003) 128 (1-2), 159 -172
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MD simulations indicate a possible role of parallel beta helices in seeded aggregation of poly-Gln
Stork M, Giese A, Kretzschmar HA, Tavan P Biophys J BioFAST, published on January 21,2005
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Loss of the cellular prion protein affects the Ca2+ homeostasis in hippocampal CA1 neurons.
Fuhrmann, M., Mitteregger, G. Moosmang S. Kretzschmar H., Herms J. J Neurochem. 98(6):1876-85, 2006
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Knock-down of the 37-kDa/67-kDa laminin receptor in mouse brain by transgenic expression of specific antisense LRP RNA
Leucht C, Vana K, Renner-Muller I, Dormont D, Lasmezas CI, Wolf E, Weiss S Transgenic Res. 2004 Feb;13(1):81-5.
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Intra- and interspecies interactions between prion proteins and effects of mutations and polymorphisms
Hundt,C.; Gauczynski,S.; Leucht,C.; Riley,M.L.; Weiss,S. Biol. Chem. (2003), 384 (5), 791 -803
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Inhibition of prion replication in vivo by tyrosine kinase inhibitor STI571
Yun, S.-W., Ertmer, A., Flechsig, E., Riederer, P., Gerlach, P., Schätzl, H.M. & Klein, M.A Neurovirology (in press)
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Inhibition of Complex Glycosylation Increases the Formation of PrPsc
Winklhofer,K.F.; Heller,U.; Reintjes,A.; Tatzelt,J. Traffic 2003, 4(5), 313 - 322
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Infectivity of scrapie prion protein (PrPSc) following in vitro digestion with bovine
Scherbel C., R. Pichner, M.H. Groschup, S. Müller-Hellwig, S. Scherer, R. Dietrich, E. Märtlbauer, and Zoonoses and Public Health (formerly Journal of Veterinary Medicine
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Immunologically induced, complement-dependent up-regulation of the prion protein in the mouse spleen: follicular dendritic cells versus capsule and trabeculae
Lotscher M, Recher M, Hunziker L, Klein MA. J Immunol. 2003 Jun 15;170(12):6040-7
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Immunochemische Detektion von zentralem Nervengewebe (ZNS) in Fleischerzeugnissen über den Nachweis von Myelin Proteolipid Protein (PLP)
Hammon, A., Düthorn, T., Bäuerlein, R., Becker, C.-M., Pischetsrieder, M., Gareis, M Amtstierärztlicher Dienst und Lebensmittelkontrolle Sonderausgabe 2006: 221
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Immunisation strategies against prion diseases: prime-boost immunisation with a PrP DNA vaccine containing foreign helper T-cell epitopes does not prevent mouse scrapie
Nitschke, C., Flechsig, E., van den Brandt, J., Lindner, N., J., Lührs, T., Dittmer, U. and Klein MA Veterinary Microbiology 2007, # VETMIC 3641, in press
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Identification of the heparan sulfate binding sites in the cellular prion protein
Warner,R.G.; Hundt,C.; Weiss,S.; Turnbull,J.E. J.Biol. Chem. (2002), 277 (21), 18421 - 18430
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Identification of polymorphisms within the bovine prion protein gene (Prnp) by DNA sequencing and genotyping by MALDI-TOF-MS
Humeny,A.; Schiebel,K.; Seeber,S.; Becker,C.M. Neurogenetics, 4 (1), 59 - 60 (2002)
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Identification of interaction domains of the prion protein with its 37- kDa/67-kDa laminin receptor
Hundt,C.; Peyrin,J.M.; Haik,S.; Gauczynski,S.; Leucht,C.; Rieger,R.; Riley,M.L.; Deslys,J.P.; Dormont,D.; Lasmezas,C.I.; Weiss,S. EMBO J (2001), 20 (21), 5876 - 5886
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Identification of cDNAs from Japanese Pufferfish (Fugu rubripes) and Atlantic Salmon (Salmo salar) coding for homologues to tetrapod prion proteins
Oidtmann B; Simon D.; Holtkamp N; Hoffmann R; Maier M FEBS Lett 2003, 538 (1-3),96-100
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Identification of anti-prion compounds as efficient inhibitors of polyglutamine protein aggregation in a zebrafish model
NW Schiffer, SA Broadley, T Hirschberger, P Tavan, HA Kretzschmar, A Giese, C J. Biol. Chem. 282, 9195-9203.
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Human endogenous retrovirus expression profiles from brains of patients with schizophrenia and bipolar disorders
Frank O., Giehl G., Zheng C., Hehlmann R., Leib-Mösch C., Seifarth W. J. Virol. 79:10890-10901 (2005)
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Homogeneity of the prion protein gene in various European and Asian pig breeds
Lipp,O.; Ritzmann,M.; Kixmoller,M.; Heinritzi,K.; Hensel,A.; Truyen,U. J.Vet.Med.B Infect.Dis.Vet.Public Health 2004, 51 (3), 97 - 98
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Generation of genuine prion infectivity by serial PMCA.
Weber P, Giese A, Piening N, Mitteregger G., Thomzig A, Beekes M, Kretzschmar HA Vet. Microbiol. (in press)
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Generation and characterisation of monoclonal antibodies to Rainbow trout (Oncorhynchus mykiss) prion protein
Maddison,B.C.; Patel,S.; James,R.F.; Conlon,H.E.; Oidtmann,B.; Baier,M.; Whitelam,G.C.; Gough,K.C. J Immunol Methods
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Functional relevance of DNA polymorphisms within the promoter region of the prion protein gene and their association to BSE infection
K. Kashkevich, A. Humeny, U. Ziegler, M. H. Groschup, P. Sander, T. Leeb, C. Fischer, C.-M. Becker, K. Schiebel FASEB J. 21,1547-55 (2007)
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Folding and misfolding of the prion protein in the secretory pathway
Tatzelt, J. and Winklhofer, K.F. Amyloid, 11, 162-172.
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Expression profiles of endogenous retrovirus in Old World monkeys
Stengel, A., Roos, C., Hunsmann, G., Seifarth, W., Leib-Mösch, C. and Greenwood, A.D J. Virol. 80:4415-4421, (2006)
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Erzeugung von PrPC-defizienten Rindern und
Klose R, Zakhartchenko V, Brem G, Wolf E Nova Acta Leopoldina NF 87, 163-175
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Electrostatics of proteins in dielectric solvent continua: II. First applications in molecular dynamics simulations.
M Stork and P Tavan J. Chem. Phys. 126, 165106, 1-13 (2007)
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Electrostatics of proteins in dielectric solvent continua: I. Newton's third law marries qE forces
M Stork and P Tavan J. Chem. Phys. 126, 165105,1-15 (2007)
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Effect of metal ions on de novo aggregation of full-length prion protein
Giese,A.; Levin,J; Bertsch,U; Kretzschmar,H. Biochemical and Biophysical Research Communications, 2004, 320 (4), 1240 - 1246
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Effect of metal ions on de novo aggregation
Giese A, Levin J, Bertsch U, Kretzschmar H: Biochem. Biophys. Res. Commun. (2004) 320, 1240-
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DNA polymorphisms of the prion doppel gene region in four different German cattle breeds and cows tested positive for bovine spongiform encephalopathy
Balbus,N.; Humeny,A.; Kashkevich,K.; Henz,I.; Fischer,C.; Becker,C.M.; Schiebel,K. Mamm. Genome 16 (11), 884-892 (2005)
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Different isoforms of the non-integrin laminin receptor are present in mouse brain and bind PrP
Simoneau,S.; Haik,S.; Leucht,C.; Dormont,D.; Deslys,J.P.; Weiss,S.; Lasmezas,C. Biol. Chem. (2003) 384 (2), 243 -246
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Determinants of the in vivo folding of the prion protein:a bipartite function of helix 1 in folding and aggregation
Winklhofer,K.F.; Heske,J.; Heller,U.; Reintjes,A.; Muranyi,W.; Moarefi,I.; Tatzelt,J. J. Biol. Chem. (2003) 278, 17: 14961 - 14970
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Degradation of scrapie associated prion protein (PrPSc) by the gastrointestinal microbiota of cattle
Christina Scherbel, Rohtraud Pichner, Matin H.Groschup, Simone Mueller.Hellwig, Siegfried Scherer, Richard Dietrich, Erwin Maertlbauer, Manfred Gareis Vet Res. 37 (2006) 695-703
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Detection of central nervous system tissue in meat and meat products with a newly developed immunoassay selective for Myelin proteolipid protein
Sandmeier B, Villmann C, Düthorn T, Gareis M, Becker C-M, Pischetsrieder M Food Chemistry doi: 10.1016/j.foodchem.2007.01.071
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Copper(II) Complexes of the Tetraazamacrocyclic Tertiary Amide Ligand Alanyl Cyclam.
Schickaneder, C. H., F.W.; Alsfasser, . Eur. J. Inorg. Chem. 2006, 2357-2363 (2006).
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Click and ligation chemistry for the synthesis of GPI-anchored membrane proteins
Musiol, H.-J.; Dong, S.; Kaiser, M.; Bausinger, R.; Zumbusch, A.; Moroder, L In: Peptides 2004 (Flegel, M.; Fridkin, M.; Gilon, C.; Slaninovva, J.. eds.) pp. 595-596, Kenes International, Geneva, Switzerland.
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Cellular prion protein/laminin receptor: distribution in adult central nervous system and characterization of an isoform associated with a subtype of cortical neurons
Hasna Baloui, Ysander von Boxberg, Joëlle Vinh, Stefan Weiss, Jean Rossier, Fatiha Nothias and Olivier Stettler European Journal of Neuroscience 2004, Vol 20 (10): 2605
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Charged bipolar suramin derivatives induce aggregation of the prion protein at the cell surface and inhibit PrPSc replication
Nunziante M., Kehler C., Maas E., Kassack M.U., Groschup M. & Schätzl H.M J Cell Sci. 118: 4959-73, 2005
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Cellular Prion Protein in the Bovine Mammary Gland Is Selectively Expressed in Active Lactocytes
Didier A, Dietrich R, Steffl M, Gareis M, Groschup MH, Muller-Hellwig S, J Histochem Cytochem. 2006 Jul 24; 1255-1261
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Cellular prion protein function in copper homeostasis and redox signalling at the synapse
Vassallo N., Herms J. J.Neurochem. 86(3), 538 - 544
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Cell-free formation of misfolded prion protein with authentic prion infectivity.
Weber P, Giese A, Piening N, Mitteregger G, Thomzig A, Beekes M, Kretzschmar HA Proc. Natl. Acad. Sci. USA (2006) 103, 15818-15823
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Cell Line Dependent RNA Expression Profiles of Prion-infected Mouse Neuronal Cells
Greenwood,A.D.; Horsch,M.; Stengel,A.; Vorberg,I.; Lutzny,G.; Maas,E.; Schadler,S.; Erfle,V.; Beckers,J.; Schatzl,H.; Leib-Mosch,C. J Mol.Biol. 349(3),487-500, 2005
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Breakage of PrP aggregates is essential for efficient autocatalytic propagation of misfolded prion protein
Piening N, Weber P, Giese A, Kretzschmar H BBRC 326 (2005) 339-343
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Bovine prion protein gene (PRNP) promoter polymorphisms modulate PRNP expression and may be responsible for differences in bovine spongiform encephalopathy susceptibility
Sander, P.;Hamann, H.; Drogemuller, C.; Kashkevich, K.; Schiebel, K.; Leeb, T. J Biol Chem 280 (45): 37408-14 (2005)
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Bovine Prion Is Endocytosed by Human Enterocytes via the 37 kDa/67 kDa Laminin Receptor
Etienne Morel, Thibault Andrieu , Fabrice Casagrande , Sabine Gauczynski , Stefan Weiss , Jacques Grassi , Monique Rousset, Dominique Dormont and Jean Chambaz American Journal of Pathology. 2005;167:1033-1042.
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Biotechnologische Ansätze zur Klärung der physiologischen Bedeutung
Klose R, Brem G, Wolf E Nova Acta Leopoldina NF 94, 237-247
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Biochemical evidence for the proteolytic degradation of infectious prion protein PrPSc in hamster brain homogenates by foodborne bacteria
Müller-Hellwig S, Groschup MH, Pichner R, Gareis M, Märtlbauer E, Scherer S, Loessner MJ Syst Appl Microbiol 2006 Mar; 29 (2): 165-71
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Beta-amyloid plaque formation and prion infection in adult primary brain cell long-term culture model
Yun S-W, Kouznetsova E, Nitschke C, Heinitz K, Schliebs R, Gerlach M, Riederer P, Klein MA Biochem Biophys Res Commun, in press
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Automated PrPres amplification using indirect sonication
Sarafoff,N.I., Bieschke,J., Giese,A., Weber,P., Bertsch,U., and Kretzschmar,H.A J Biochem. Biophys. Methods 2005, epub ahead of print
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Automated PrPres amplification using indirect sonication
Sarafoff,N.I., Bieschke,J., Giese,A., Weber,P., Bertsch,U., and Kretzschmar,H.A.J Biochem. Biophys. Methods. J Biochem. Biophys. Methods.2005, epub ahead of print
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Autocatalytic self-propagation of misfolded prion protein
Bieschke,J.; Weber,P.; Sarafoff,N.; Beekes,M.; Giese,A.; Kretzschmar,H. PNAS 101(33): 12207-11, 2004
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Atypical BSE in Germany--proof of transmissibility and biochemical characterization
A. Buschmann, A. Gretzschel, A.G. Biacabe, K. Schiebel, C. Corona, C. Hoffmann, M. Eiden, T. Baron, C. Casalone, M.H. Groschup Vet. Microbiol. 117, 103-16. (2006)
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Association of Bcl-2 with misfolded prion protein is linked to the toxic potential of cytosolic PrP
Rambold, A.S., Miesbauer, M., Rapaport, D., Bartke, T., Baier, M., Winklhofer, K.F., and Tatzelt, J Biol Cell, 2006, May 17; [Epub ahead of print]
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Apical sorting of beta-secretase limits amyloid beta-peptide production
Capell,A.; Meyn,L.; Fluhrer,R.; Teplow,D.B.; Walter,J.; Haass,C. J.Biol.Chem.(2002), 277, 5637 -5643
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Amyloidogenic processing of the Alzheimer beta-amyloid precursor protein depends on lipid rafts
Ehehalt,R.; Keller,P.; Haass,C.; Thiele,C.; Simons,K. J. Cell Biol. (2002), 160, 113 -123
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Activation of the tertiary carboxamide C-N bond in Werner complexes: a classical structure-function relationship
Niklas,N.; Heinemann,F.W.; Hampel,F.; Alsfasser,R. Angew. Chem. Int. Ed. Engl.(2002),41(18),3386-3388
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Activation of phosphatidylinositol 3-kinase by cellular prion protein and its role in cell survival
Vassallo,N.; Herms,J.; Behrens,C.; Krebs,B.; Saeki,K.; Onodera,T.; Windl,O.; Kretzschmar,H.A. Biochem.Biophys.Res.Commun 332(1),75-82, 2005
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A Trans-dominant Negative 37 kDa/67 kDa Laminin Receptor Mutant Impairs PrPSc Propagation in Scrapie-infected Neuronal Cells
Karen Vana and Stefan Weiss Journal of Molecular Biology 358 (1):57 -66; 2006
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A pathogenic PrP mutation and doppel interfere with polarized sorting of the prion protein
Uelhoff A, Tatzelt J, Aguzzi A, Winklhofer KF, Haass C J Biol Chem. 280, 5137-5140 (2005)
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A Pathogenic PrP Mutation and Doppel Interfere with Polarized Sorting of the Prion Protein
Armgard Uelhoff , Jörg Tatzelt , Adriano Aguzzi, Konstanze F. Winklhofer , and Christian Haass J. Biol. Chem., Vol. 280 (7): 5137-5140, 2005
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A new method to determine the structure of the metal environment in metalloproteins: Investigation of the prion protein octapeptide repeat Cu2+ -complex
Mentler, M., Weiss, A., Grantner, K., del Pino, P., Deluca, D., Fiori, S., Renner, C., Meyer-Klaucke, W., Moroder, L., Bertsch, U., Kretschmer, H.A., Tavan, P. and Parak, F.G. Eur. Biophys. J., in press.
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A major genetic component of BSE susceptibility
Juling, K., Schwarzenbacher H., Williams, J.L., Fries R. BMC Biology 2006, 4:33
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A basolateral sorting signal directs ADAM10 to adherens junctions and is required for its function in cell migration
Wild-Bode C, Fellerer K, Kugler J, Haass C, Capell A. Biol. Chem. 281, 23824-23829 (2006)
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Events
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22.05.2007
Abschlusssymposium des Bayerischen Forschungsverbundes Prionen
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30.05.2006
Treffen des Bayerischen Forschungsverbundes Prionen 2006
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04.07.2005
Treffen des Bayerischen Forschungsverbundes 2005
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15.07.2004
Treffen des Bayerischen Forschungsverbundes Prionen 2004
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10.07.2003
Treffen des Bayerischen Forschungsverbundes Prionen 2003
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04.06.2003
Prionerkrankungen, Krebs, Infektionen: Die molekulare Medizin vor neuen Herausforderungen
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15.07.2002
Treffen des Bayerischen Forschungsverbundes Prionen 2002
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Contact
Dr. Rosi Lederer
Universität Regensburg
Klinik und Poliklinik für Neurologie am Bezirksklinikum Regensburg
Universitätsstr. 84
93053 Regensburg
Telefon: +49-89-2180 75258
Email: forneurocell@klinik.uni-regensburg.de

