PUBLICATIONS

2022 2021 2020 2019 2018 2017 2016 2015 2013 2012 2011 2010 2009 2008 2007 2006 2005 2004 2003 2001 2000 1999 1998 1997 1996 1995 1994 1993 1992

2022

LUBAC assembles a ubiquitin signaling platform at mitochondria for signal amplification and transport of NF-κB to the nucleus
Wu Z, Berlemann LA, Bader V, Sehr DA, Dawin E, Covallero A, Meschede J, Angersbach L, Showkat C, Michaelis JB, Münch C, Rieger B, Namgaladze D, Herrera MG, Fiesel FC, Springer W, Mendes M, Stepien J, Barkovits K, Marcus K, Sickmann A, Dittmar G, Busch KB, Riedel D, Brini M, Tatzelt J, Cali T, Winklhofer KF
EMBO J. 18; e112006.

Bivalent metal ions induce formation of α-synuclein fibril polymorphs with different cytotoxicities
Atarod D, Mamashli F, Ghasemi A, Moosavi-Movahedi F, Pirhaghi M, Nedaei H, Muronetz V, Haertlé T, Tatzelt J, Riazi G, Saboury AA.
Sci Rep . 12(1): 11898.

2021

Ligands binding to the prion protein induce its proteolytic release with therapeutic potential in neurodegenerative proteinopathies.
Linsenmeier L, Mohammadi B, Shafiq M, Frontzek K, Bär J, Shrivastava AN, Damme M, Song F, Schwarz A, Da Vela S, Massignan T, Jung S, Correia A, Schmitz M, Puig B, Hornemann S, Zerr I, Tatzelt J, Biasini E, Saftig P, Schweizer M, Svergun D, Amin L, Mazzola F, Varani L, Thapa S, Gilch S, Schätzl H, Harris DA, Triller A, Mikhaylova M, Aguzzi A, Altmeppen HC, Glatzel M.
Science Advances 7(48): eabj1826.

Biological Functions of the Intrinsically Disordered N-Terminal Domain of the Prion Protein: A Possible Role of Liquid-Liquid Phase Separation
Polido SA, Kamps J, Tatzelt J.
Biomolecules 11(8): 1201.

Remodeling of the Fibrillation Pathway of α-Synuclein by Interaction with Antimicrobial Peptide LL-III
Oliva R, Mukherjee SK, Ostermeier L, Pazurek LA, Kriegler S, Bader V, Prumbaum D, Raunser S, Winklhofer KF, Tatzelt J, Winter RHA.
Chemistry 27(46): 11845-11851.

The N-terminal domain of the prion protein is required and sufficient for liquid-liquid phase separation: A crucial role of the Aβ-binding domain
Kamps J,Lin YH, Oliva R, Bader V, Winter R, Winklhofer KF, Tatzelt J.
J Biol Chem 297(1): 100860.

The G127V variant of the prion protein interferes with dimer formation in vitro but not in cellulo
Sangeetham SB, Engelke AD, Fodor E, Krausz SL, Tatzelt J, Welker E.
Sci Rep. 11(1): 3116.

The key role of solvent in condensation: Mapping hydration water in liquid-liquid phase-separated FUS
Ahlers J, Adams EM, Bader V, Pezzotti S, Winklhofer KF, Tatzelt J, Havenith M.
Biophys J. 120(7): 1266-1275.

2020

SecY-mediated quality control prevents the translocation of non-gated porins.
Jung S, Bader V, Natriashvili, A, Koch HG, Winklhofer KF, Tatzelt J.
Sci Rep. 10(1): 16347.

Transgenic Overexpression of the Disordered Prion Protein N1 Fragment in Mice Does Not Protect Against Neurodegenerative Diseases Due to Impaired ER Translocation.
Mohammadi B, Linsenmeier L, Shafiq M, Puig B, Galliciotti G, Giudici C, Willem M, Eden T, Koch-Nolte F, Lin YH, Tatzelt J, Glatzel M, Altmeppen HC.
Mol Neurobiol. 57(6): 2812-2829

The parkin-coregulated gene product PACRG promotes TNF signaling by stabilizing LUBAC.
Meschede J, Šadić M, Furthmann N, Miedema T, Sehr DA, Müller-Rischart AK, Bader V, Berlemann LA, Pilsl A, Schlierf A, Barkovits K, Kachholz B, Rittinger K, Ikeda F, Marcus K, Schaefer L, Tatzelt J, Winklhofer KF.
Sci Signal. 13(617)

2019

A protein quality control pathway regulated by linear ubiquitination.
van Well EM, Bader V, Patra M, Sánchez-Vicente A, Meschede J, Furthmann N, Schnack C, Blusch A, Longworth J, Petrasch-Parwez E, Mori K, Arzberger T, Trümbach D, Angersbach L, Showkat C, Sehr DA, Berlemann LA, Goldmann P, Clement AM, Behl C, Woerner AC, Saft C, Wurst W, Haass C, Ellrichmann G, Gold R, Dittmar G, Hipp MS, Hartl FU, Tatzelt J, Winklhofer KF.
EMBO J, 38(9): doi: 10.15252/embj.2018100730.
News & Views

The signal peptide plus a cluster of positive charges in prion protein dictate chaperone-mediated Sec61 channel gating.
Ziska A, Tatzelt J, Dudek J, Paton AW, Paton JC, Zimmermann R, Haßdenteufel S.
Biol Open, 8(3): doi: 10.1242/bio.040691.

GPI-anchor signal sequence influences PrPC sorting, shedding and signalling, and impacts on different pathomechanistic aspects of prion disease in mice.
Puig B, Altmeppen HC, Linsenmeier L, Chakroun K, Wegwitz F, Piontek UK, Tatzelt J, Bate C, Magnus T, Glatzel M.
PLoS Pathog. 15(1): e1007520.

The prion protein in neuroimmune crosstalk.
Salvesen Ø, Tatzelt J, Tranulis MA.
Neurochem Int. 130: 104335.

2018

Alterations in the brain interactome of the intrinsically disordered N-terminal domain of the cellular prion protein (PrPC) in Alzheimer's disease.
Ulbrich S, Janning P, Seidel R, Matschke J, Gonsberg A, Jung S, Glatzel M, Engelhard M, Winklhofer KF, Tatzelt J.
PLoS One, 13(5): e0197659.

Dimerization of the cellular prion protein inhibits propagation of scrapie prions.
Engelke AD, Gonsberg A, Thapa S, Jung S, Ulbrich S, Seidel RP, Basu S, Multhaup G, Baier M, Engelhard M, Schätzl HM, Winklhofer KF, Tatzelt J.
J Biol Chem. 293(21): 8020-8031.

Structural and mechanistic aspects influencing the ADAM10-mediated shedding of the prion protein.
Linsenmeier L, Mohammadi B, Wetzel S, Puig B, Jackson WS, Hartmann A, Uchiyama K, Sakaguchi S, Endres K, Tatzelt J, Saftig P, Glatzel M, Altmeppen HC.
Mol Neurodegener., 13(1): 18.

Impaired transport of intrinsically disordered proteins through the Sec61 and SecY translocon; implications for prion diseases.
Jung S and Tatzelt J.
Prion, 12(2): 88-92.

2017

Substitutions of PrP N-terminal histidine residues modulate scrapie disease pathogenesis and incubation time in transgenic mice.
Eigenbrod S, Frick P, Bertsch U, Mitteregger-Kretzschmar G, Mielke J, Maringer M, Piening N, Hepp A, Daude N, Windl O, Levin J, Giese A, Sakthivelu V, Tatzelt J, Kretzschmar H, Westaway D.
PLoS One. 12(12): e0188989. doi: 10.1371/journal.pone.0188989.

The Sec61/SecY complex is inherently deficient in translocating intrinsically disordered proteins.
Gonsberg A, Jung S, Ulbrich S, Origi A, Ziska A, Baier M, Koch HG, Zimmermann R, Winklhofer KF, Tatzelt J.
J Biol Chem. 292(52): 21383-21396.
*Recommended in F1000 Prime

The N-terminus of the prion protein is a toxic effector regulated by the C-terminus.
Wu B, McDonald AJ, Markham K, Rich CB, Mchugh KP, Tatzelt J, Colby DW, Millhauser GL, Harris DA.
Elife 6 doi: 10.7554/eLife.23473.

The RAB GTPase RAB18 modulates macroautophagy and proteostasis.
Feldmann A, Bekbulat F, Huesmann H, Ulbrich S, Tatzelt J, Behl C, Kern A.
Biochem Biophys Res Commun. 486(3): 738-743.

2016

Secretory pathway retention of mutant prion protein induces p38-MAPK activation and lethal disease in mice.
Puig B, Altmeppen HC, Ulbrich S, Linsenmeier L, Krasemann S, Chakroun K, Acevedo-Morantes CY, Wille H, Tatzelt J, Glatzel M.
Sci Rep 6: 24970

Cytoplasmic protein aggregates interfere with nucleo-cytoplasmic transport of protein and RNA.
Woerner AC, Frottin F, Hornburg D, Feng LR, Meissner F, Patra M, Tatzelt J, Mann M, Winklhofer KF, Hartl FU, Hipp MS.
Science 351(6269): 173-176.

2015

The cellular prion protein: a player in immunological quiescence.
Bakkebø MK, Mouillet-Richard S, Espenes A, Goldmann W, Tatzelt J, Tranulis MA.
Front. Immunol. 6: 450.

Parkin cooperates with GDNF/RET signaling to prevent dopaminergic neuron degeneration.
Meka DP, Müller-Rischart AK, Nidadavolu P, Mohammadi B, Motori E, Ponna SK, Aboutalebi H, Bassal M, Annamneedi A, Finckh B, Miesbauer M, Rotermund N, Lohr C, Tatzelt J, Winklhofer KF, Kramer ER.
J Clin Invest. 125(5): 1873-1885.

2013

Nanomedicine for prion disease treatment: New insights into the role of dendrimers.
McCarthy JM, Appelhans D, Tatzelt J, Rogers MS.
Prion. 7(3): 198-202.

Prion disease: a tale of folds and strains.
Kretzschmar H, Tatzelt J.
Brain Pathol. 23(3): 321-332.

The alpha-helical structure of prodomains promotes translocation of intrinsically disordered neuropeptide hormones into the endoplasmic reticulum.
Dirndorfer D, Seidel RP, Nimrod G, Miesbauer M, Ben-Tal N, Engelhard M, Zimmermann R, Winklhofer KF, Tatzelt J.
J Biol Chem. 288(20): 13961-13973.

Structural features within the nascent chain regulate alternative targeting of secretory proteins to mitochondria.
Pfeiffer NV, Dirndorfer D, Lang S, Resenberger UK, Restelli LM, Hemion C, Miesbauer M, Frank S, Neutzner A, Zimmermann R, Winklhofer KF, Tatzelt J.
EMBO J. 32(7): 1036-1051.

The E3 ligase parkin maintains mitochondrial integrity by increasing linear ubiquitination of NEMO.
Müller-Rischart AK, Pilsl A, Beaudette P, Patra M, Hadian K, Funke M, Peis R, Deinlein A, Schweimer C, Kuhn PH, Lichtenthaler SF, Motori E, Hrelia S, Wurst W, Trümbach D, Langer T, Krappmann D, Dittmar G, Tatzelt J, Winklhofer KF.
Mol Cell. 49(5): 908-921.

Anti-prion drug mPPIg5 inhibits PrP(C) conversion to PrP(Sc).
McCarthy JM, Franke M, Resenberger UK, Waldron S, Simpson JC, Tatzelt J, Appelhans D, Rogers MS.
PLoS One. 8(1): e55282.

2012

The heat shock response is modulated by and interferes with toxic effects of scrapie prion protein and amyloid β.
Resenberger UK, Müller V, Munter LM, Baier M, Multhaup G, Wilson MR, Winklhofer KF, Tatzelt J.
J Biol Chem. 287(52): 43765-43776.

Different effects of Sec61α, Sec62 and Sec63 depletion on transport of polypeptides into the endoplasmic reticulum of mammalian cells.
Lang S, Benedix J, Fedeles SV, Schorr S, Schirra C, Schäuble N, Jalal C, Greiner M, Hassdenteufel S,Tatzelt J, Kreutzer B, Edelmann L, Krause E, Rettig J, Somlo S, Zimmermann R, Dudek J.
J Cell Sci. 125(Pt 8): 1958-1969.

Cellular prion protein mediates toxic signaling of amyloid beta.
Resenberger UK, Winklhofer KF, Tatzelt J.
Neurodegener Dis. 10(1-4): 298-300.

2011

Prion proteins.
Tatzelt J.
Top Curr Chem. 305: IX-X.

Neuroprotective and neurotoxic signaling by the prion protein.
Resenberger UK, Winklhofer KF, Tatzelt J.
Top Curr Chem. 305: 101-119.

The cellular prion protein mediates neurotoxic signalling of β-sheet-rich conformers independent of prion replication.
Resenberger UK, Harmeier A, Woerner AC, Goodman JL, Müller V, Krishnan R, Vabulas RM, Kretzschmar HA, Lindquist S, Hartl FU, Multhaup G, Winklhofer KF, Tatzelt J.
EMBO J. 30(10): 2057-2070.

Conserved stress-protective activity between prion protein and Shadoo.
Sakthivelu V, Seidel RP, Winklhofer KF, Tatzelt J.
J Biol Chem. 286(11): 8901-8908.

Conditional modulation of membrane protein expression in cultured cells mediated by prion protein recognition of short phosphorothioate oligodeoxynucleotides.
Karpuj MV, Gelibter-Niv S, Tiran A, Rambold A, Tatzelt J, Nunziante M, Schatzl HM.
J Biol Chem. 286(9): 6911-6917.

Parkin is transcriptionally regulated by ATF4: evidence for an interconnection between mitochondrial stress and ER stress.
Bouman L, Schlierf A, Lutz AK, Shan J, Deinlein A, Kast J, Galehdar Z, Palmisano V, Patenge N, Berg D, Gasser T, Augustin R, Trümbach D, Irrcher I, Park DS, Wurst W, Kilberg MS, Tatzelt J, Winklhofer KF.
Cell Death Differ. 18(5): 769-782.

2010

Protein immobilization on liposomes and lipid-coated nanoparticles by protein trans-splicing.
Chu NK, Olschewski D, Seidel R, Winklhofer KF, Tatzelt J, Engelhard M, Becker CF.
J Pept Sci. 16(10): 582-588.

Parkin is protective against proteotoxic stress in a transgenic zebrafish model.
Fett ME, Pilsl A, Paquet D, van Bebber F, Haass C, Tatzelt J, Schmid B, Winklhofer KF.
PLoS One. 5(7): e11783.

The novel membrane protein TMEM59 modulates complex glycosylation, cell surface expression, and secretion of the amyloid precursor protein.
Ullrich S, Münch A, Neumann S, Kremmer E, Tatzelt J, Lichtenthaler SF.
J Biol Chem. 285(27): 20664-20674.

Targeting of the prion protein to the cytosol: mechanisms and consequences.
Miesbauer M, Rambold AS, Winklhofer KF, Tatzelt J.
Curr Issues Mol Biol. 12(2): 109-118.

The prion protein: friend and foe.
Tatzelt J.
Curr Issues Mol Biol. 12(2): 49.

Synthesis of a GPI anchor module suitable for protein post-translational modification.
Schumacher MC1, Resenberger U, Seidel RP, Becker CF, Winklhofer KF, Oesterhelt D, Tatzelt J, Engelhard M.
Biopolymers 94(4): 457-64.

2009

alpha-Helical domains promote translocation of intrinsically disordered polypeptides into the endoplasmic reticulum.
Miesbauer M, Pfeiffer NV, Rambold AS, Müller V, Kiachopoulos S, Winklhofer KF, Tatzelt J.
J Biol Chem. 284(36): 24384-24393.

Loss of parkin or PINK1 function increases Drp1-dependent mitochondrial fragmentation.
Lutz AK, Exner N, Fett ME, Schlehe JS, Kloos K, Lämmermann K, Brunner B, Kurz-Drexler A, Vogel F, Reichert AS, Bouman L, Vogt-Weisenhorn D, Wurst W, Tatzelt J, Haass C, Winklhofer KF.
J Biol Chem. 284(34): 22938-22951.

2008

Green tea extracts interfere with the stress-protective activity of PrP and the formation of PrP.
Rambold AS, Miesbauer M, Olschewski D, Seidel R, Riemer C, Smale L, Brumm L, Levy M, Gazit E, Oesterhelt D, Baier M, Becker CF, Engelhard M, Winklhofer KF, Tatzelt J.
J Neurochem. 107(1): 218-229.

Stress-protective signalling of prion protein is corrupted by scrapie prions.
Rambold AS, Müller V, Ron U, Ben-Tal N, Winklhofer KF, Tatzelt J.
EMBO J. 27(14): 1974-1984.

Genes contributing to prion pathogenesis.
Tamgüney G, Giles K, Glidden DV, Lessard P, Wille H, Tremblay P, Groth DF, Yehiely F, Korth C, Moore RC, Tatzelt J, Rubinstein E, Boucheix C, Yang X, Stanley P, Lisanti MP, Dwek RA, Rudd PM, Moskovitz J, Epstein CJ, Cruz TD, Kuziel WA, Maeda N, Sap J, Ashe KH, Carlson GA, Tesseur I, Wyss-Coray T, Mucke L, Weisgraber KH, Mahley RW, Cohen FE, Prusiner SB.
J Gen Virol. 89(Pt 7): 1777-1788.

Aberrant folding of pathogenic Parkin mutants: aggregation versus degradation.
Schlehe JS, Lutz AK, Pilsl A, Lämmermann K, Grgur K, Henn IH,Tatzelt J, Winklhofer KF.
J Biol Chem. 283(20): 13771-13779.

The two faces of protein misfolding: gain- and loss-of-function in neurodegenerative diseases.
Winklhofer KF, Tatzelt J, Haass C.
EMBO J. 27(2): 336-349.

Observing fibrillar assemblies on scrapie-infected cells.
Wegmann S, Miesbauer M, Winklhofer KF,Tatzelt J, Muller DJ.
Pflugers Arch. 456(1): 83-93.

2007

Semisynthetic murine prion protein equipped with a GPI anchor mimic incorporates into cellular membranes.
Olschewski D, Seidel R, Miesbauer M, Rambold AS, Oesterhelt D, Winklhofer KF, Tatzelt J, Engelhard M, Becker CF.
Chem Biol. 14(9): 994-1006.

Parkin mediates neuroprotection through activation of IkappaB kinase/nuclear factor-kappaB signaling.
Henn IH, Bouman L, Schlehe JS, Schlierf A, Schramm JE, Wegener E, Nakaso K, Culmsee C, Berninger B, Krappmann D, Tatzelt J, Winklhofer KF.
J Neurosci. 27(8): 1868-1878.

Molecular basis of cerebral neurodegeneration in prion diseases.
Tatzelt J, Schätzl HM.
FEBS J. 274(3): 606-611.

2006

Association of Bcl-2 with misfolded prion protein is linked to the toxic potential of cytosolic PrP.
Rambold AS, Miesbauer M, Rapaport D, Bartke T, Baier M, Winklhofer KF, Tatzelt J.
Mol Biol Cell. 17(8): 3356-3368.

The role of chaperones in Parkinson's disease and prion diseases.
Winklhofer KF, Tatzelt J.
Handb Exp Pharmacol. 172: 221-258.

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. 90(11): 3908-3918.

Prion protein-related proteins from zebrafish are complex glycosylated and contain a glycosylphosphatidylinositol anchor.
Miesbauer M, Bamme T, Riemer C, Oidtmann B, Winklhofer KF, Baier M, Tatzelt J.
Biochem Biophys Res Commun. 341(1): 218-224.

2005

Systematic identification of antiprion drugs by high-throughput screening based on scanning for intensely fluorescent targets.
Bertsch U, Winklhofer KF, Hirschberger T, Bieschke J, Weber P, Hartl FU, Tavan P, Tatzelt J, Kretzschmar HA, Giese A.
J Virol. 79(12): 7785-7791.

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(7): 5137-5140.

The polysaccharide scaffold of PrP 27-30 is a common compound of natural prions and consists of alpha-linked polyglucose.
Dumpitak C1, Beekes M, Weinmann N, Metzger S, Winklhofer KF, Tatzelt J, Riesner D.
Biol Chem 386(11): 1149-1155.

Pathogenic mutations inactivate parkin by distinct mechanisms.
Henn IH, Gostner JM, Lackner P, Tatzelt J, Winklhofer KF.
J Neurochem. 92(1): 114-122.

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, Kiachopoulos S, Bracher A, Winklhofer KF, Kiachopoulos S, Bracher A, Winklhofer KF, Tatzelt, J.
J Biol Chem. 280(10): 9320-9329.

2004

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. 344(3): 839-853.

Folding and misfolding of the prion protein in the secretory pathway.
Tatzelt J, Winklhofer KF.
Amyloid. 11(3): 162-172.

Misfolding of the prion protein at the plasma membrane induces endocytosis, intracellular retention and degradation.
Kiachopoulos S, Heske J, Tatzelt J, Winklhofer KF.
Traffic. 5(6): 426-436.

The C-terminal globular domain of the prion protein is necessary and sufficient for import into the endoplasmic reticulum.
Heske J, Heller U, Winklhofer KF, Tatzelt J.
J Biol Chem. 279(7): 5435-5443.

2003

Inactivation of parkin by oxidative stress and C-terminal truncations: a protective role of molecular chaperones.
Winklhofer KF, Henn IH, Kay-Jackson PC, Heller U, Tatzelt J.
J Biol Chem. 278(47): 47199-47208.

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 KF, Heske J, Reintjes A, Tatzelt J.
J Biol Chem. 278(38): 36139-36147.

Inhibition of complex glycosylation increases the formation of PrPsc.
Winklhofer KF, Heller U, Reintjes A, Tatzelt J.
Traffic. 4(5): 313-322.

Determinants of the in vivo folding of the prion protein. A bipartite function of helix 1 in folding and aggregation.
Winklhofer KF, Heske J, Heller U, Reintjes A, Muranyi W, Moarefi I, Tatzelt J.
J Biol Chem. 278(17): 14961-14970.

2001

Geldanamycin restores a defective heat shock response in vivo.
Winklhofer KF, Reintjes A, Hoener MC, Voellmy R, Tatzelt J.
J Biol Chem. 276(48): 45160-45167.

A sensitive filter retention assay for the detection of PrP(Sc) and the screening of anti-prion compounds.
Winklhofer KF, Hartl FU, Tatzelt J.
FEBS Lett. 503(1): 41-45.

Intracellular re-routing of prion protein prevents propagation of PrP(Sc) and delays onset of prion disease.
Gilch S, Winklhofer KF, Groschup MH, Nunziante M, Lucassen R, Spielhaupter C, Muranyi W, Riesner D, Tatzelt J, Schätzl HM.
EMBO J. 20(15): 3957-3966.

2000

Cationic lipopolyamines induce degradation of PrPSc in scrapie-infected mouse neuroblastoma cells.
Winklhofer KF, Tatzelt J.
Biol Chem. 381(5-6): 463-469.

1999

Kinetics of prion protein accumulation in the CNS of mice with experimental scrapie.
Tatzelt J, Groth DF, Torchia M, Prusiner SB, DeArmond SJ.
J Neuropathol Exp Neurol. 58(12): 1244-1249.

1998

Abnormalities in stress proteins in prion diseases.
Tatzelt J, Voellmy R, Welch WJ.
Cell Mol Neurobiol. 18(6): 721-729.

1997

Prion protein expression in Chinese hamster ovary cells using a glutamine synthetase selection and amplification system.
Blochberger TC, Cooper C, Peretz D, Tatzelt J, Griffith OH, Baldwin MA, Prusiner SB.
Protein Eng. 10(12): 1465-1473.

Propagation of prion strains through specific conformers of the prion protein.
Scott MR, Groth D, Tatzelt J, Torchia M, Tremblay P, DeArmond SJ, Prusiner SB.
J Virol. 71(12): 9032-9044.

A hypothalamic neuronal cell line persistently infected with scrapie prions exhibits apoptosis.
Schätzl HM, Laszlo L, Holtzman DM, Tatzelt J, DeArmond SJ, Weiner RI, Mobley WC, Prusiner SB.
J Virol. 71(11): 8821-8831.

1996

Chemical chaperones interfere with the formation of scrapie prion protein.
Tatzelt J, Prusiner SB, Welch WJ.
EMBO J. 15(23): 6363-6373.

Scrapie in mice deficient in apolipoprotein E or glial fibrillary acidic protein.
Tatzelt J, Maeda N, Pekny M, Yang SL, Betsholtz C, Eliasson C, Cayetano J, Camerino AP, DeArmond SJ, Prusiner SB.
Neurology. 47(2): 449-453.

1995

Scrapie prions selectively modify the stress response in neuroblastoma cells.
Tatzelt J, Zuo J, Voellmy R, Scott M, Hartl U, Prusiner SB, Welch WJ.
Proc Natl Acad Sci U S A. 92(7): 2944-2948.

The mechanism of adenovirus DNA integration: studies in a cell-free system.
Fechteler K, Tatzelt J, Huppertz S, Wilgenbus P, Doerfler W.
Curr Top Microbiol Immunol. 199( Pt 2): 109-137.

1993

Fractionated nuclear extracts from hamster cells catalyze cell-free recombination at selective sequences between adenovirus DNA and a hamster preinsertion site.
Tatzelt J, Fechteler K, Langenbach P, Doerfler W.
Proc Natl Acad Sci U S A. 90(15): 7356-7360.

1992

Recombination between adenovirus type 12 DNA and a hamster preinsertion sequence in a cell-free system. Patch homologies and fractionation of nuclear extracts.
Tatzelt J, Scholz B, Fechteler K, Jessberger R, Doerfler W.
J Mol Biol. 228(4): 1275.

Biochemistry of Neurodegenerative Diseases

Publications