FORPRION

• Institut für neue und neuartige Tierseuchenerreger

• Institut für Mikrobiologie und Toxikologie

• c/o LMU München, Zentrum für Neuropathologie und Prionforschung

• Institut für molekulare Virologie

• Institut für Virologie und Immunbiologie
• Klinik für Psychiatrie und Psychotherapie, Klinische Neurochemie
• Neurologische Klinik, Experimentelle Entwicklungsneurobiologie
• Neurologische Klinik, Institut für Klinische Neurobiologie

• 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

• AG Bioorganische Chemie

• 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

• Lehrstuhl für Mikrobiologie
• Lehrstuhl für Struktur und Chemie der Biopolymere

• Institut für Anorganische Chemie
• Institut für Biochemie
• Institut für Pharmazie und Lebensmittelchemie

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)

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.

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)

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.

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).

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

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

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)

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

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)

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.

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.

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

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

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).

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).

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

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

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]

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

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

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

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

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

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

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

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]

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]

Strategies to eliminate PrPc as substrate for conversion into PrPSc

Gilch, S., Nunziante, M., Ertmer, A. & Schätzl, H.M Vet. Microbiol. (in press)

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

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

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

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

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

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

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)

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

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

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

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

Prion diseases: from molecular biology to intervention strategies

Nunziante, M., Gilch, S., Schatzl, H. M Chembiochem. (2003),4,1268-84

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

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

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

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.

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

Perspektiven des Klonens in der Tierzucht und in der biomedizinischen Forschung.

Wolf E LEOPOLDINA (R. 3) 51, 407-414

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.

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

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

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

Nachweis von ZNS-Kontaminationen in Fleisch

Sandmeier B., Becker C.-M., Rotheneder R., Gareis M., Pischetsrieder M Lebensmittelchemie, 57: 84 – 85, 2003

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

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

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)

Multiple administrations of Oligodeoxynucleotides containing CpG motifs influence Ig

Sethi S., Ebner S., Hinske C., Kretzschmar H Immunopharmacol Immunotoxicol: 27: 447-460, 2005

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)

Molecular basis of cerebral neurodegeneration in prion diseases

Tatzelt, J. and Schatzl, H.M FEBS J, 274, 606-611

Molecular basis of cerebral neurodegeneration in prion diseases

Tatzelt, J. &, Schätzl, H.M FEBS Journal 274, 606-611

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

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

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

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

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

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

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

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.

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

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)

Inhibition of Complex Glycosylation Increases the Formation of PrPsc

Winklhofer,K.F.; Heller,U.; Reintjes,A.; Tatzelt,J. Traffic 2003, 4(5), 313 - 322

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

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

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

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

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

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)

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

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

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.

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)

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

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)

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

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)

Folding and misfolding of the prion protein in the secretory pathway

Tatzelt, J. and Winklhofer, K.F. Amyloid, 11, 162-172.

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)

Erzeugung von PrPC-defizienten Rindern und

Klose R, Zakhartchenko V, Brem G, Wolf E Nova Acta Leopoldina NF 87, 163-175

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)

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)

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

Effect of metal ions on de novo aggregation

Giese A, Levin J, Bertsch U, Kretzschmar H: Biochem. Biophys. Res. Commun. (2004) 320, 1240-

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)

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

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

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

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

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).

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.

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

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

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

Cellular prion protein function in copper homeostasis and redox signalling at the synapse

Vassallo N., Herms J. J.Neurochem. 86(3), 538 - 544

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

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

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

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)

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.

Biotechnologische Ansätze zur Klärung der physiologischen Bedeutung

Klose R, Brem G, Wolf E Nova Acta Leopoldina NF 94, 237-247

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

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

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

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

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

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)

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]

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

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

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

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

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

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)

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

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.

A major genetic component of BSE susceptibility

Juling, K., Schwarzenbacher H., Williams, J.L., Fries R. BMC Biology 2006, 4:33

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)

Abschlusssymposium des Bayerischen Forschungsverbundes Prionen

Treffen des Bayerischen Forschungsverbundes Prionen 2006

Treffen des Bayerischen Forschungsverbundes 2005

Treffen des Bayerischen Forschungsverbundes Prionen 2004

Treffen des Bayerischen Forschungsverbundes Prionen 2003

Prionerkrankungen, Krebs, Infektionen: Die molekulare Medizin vor neuen Herausforderungen

Treffen des Bayerischen Forschungsverbundes Prionen 2002