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Publikationen

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Substrates and catalytic mechanism of clostridial neurotoxins

 

Binz T (2013): Clostridial neurotoxin light chains: devices for SNARE cleavage mediated blockade of neurotransmission. Curr Top Microbiol Immunol 364, 139-157.

Review

http://www.ncbi.nlm.nih.gov/pubmed/23239352

 

Binz T, Sikorra S, and Mahrhold S (2010): Clostridial Neurotoxins: mechanism of SNARE cleavage and outlook on potential substrate specificity reengineering. Toxins 2, 665-682.

Review

http://www.ncbi.nlm.nih.gov/pubmed/22069605

 

Sikorra S, Henke T, Galli T, and Binz T (2008): Substrate recognition mechanism of VAMP/synaptobrevin cleaving clostridial neurotoxins. J Biol Chem 283, 21145-21152.

http://www.ncbi.nlm.nih.gov/pubmed/18511418

 

Jin R, Sikorra S, Stegmann CM, Pich A, Binz T, and Brunger AT (2007): Structural and biochemical studies of botulinum neurotoxin serotype C1 light chain protease: implications for dual substrate specificity. Biochemistry 46, 10685-10693.

http://www.ncbi.nlm.nih.gov/pubmed/17718519

 

Sikorra S, Henke T, Swaminathan S, Galli T, and Binz T (2006): Identification of the amino acid residues rendering TI-VAMP resistant towards botulinum neurotoxin B. J Mol Biol 357, 574-582.

http://www.ncbi.nlm.nih.gov/pubmed/16430921

 

Agarwal R, Binz T, and Swaminathan S (2005): Structural analysis of botulinum neurotoxin serotype F light chain: implications on substrate binding and inhibitor design. Biochemistry 44, 11758-11765.

http://www.ncbi.nlm.nih.gov/pubmed/16128577

 

Agarwal R, Binz T, and Swaminathan S (2005): Analysis of active site residues of botulinum neurotoxin E by mutational, functional and structural studies: Glu335Gln is an apoenzyme. Biochemistry 44, 8291-8302.

http://www.ncbi.nlm.nih.gov/pubmed/15938619

 

Rao KN, Kumaran D, Binz T, and Swaminathan S (2005): Structural analysis of the catalytic domain of tetanus neurotoxin. Toxicon 45, 929-939.

http://www.ncbi.nlm.nih.gov/pubmed/15904688

 

Agarwal R, Eswaramoorthy S, Kumaran D, Binz T, and Swaminathan S (2004): Structural analysis of botulinum neurotoxin type E catalytic domain and its mutant Glu212→Gln reveals the pivotal role of the Glu212 carboxylate in the catalytic pathway.

Biochemistry 43, 6637-6644.

http://www.ncbi.nlm.nih.gov/pubmed/15157097

 

Binz T, Bade S, Rummel A, Kollewe A, and Alves J (2002): Arg-362 and Tyr-365 of Botulinum Neurotoxin Type A Light Chain Are Involved in Transition State Stabilization.

Biochemistry 41, 1717-23.

http://www.ncbi.nlm.nih.gov/pubmed/11827515

 

Li L, Binz T, Niemann H, and Singh BR (2000): Probing the mechanistic role of glutamate residue in the zinc-binding motif of type A botulinum neurotoxin light chain. Biochemistry 39, 2399-405.

http://www.ncbi.nlm.nih.gov/pubmed/10694409

 

Vaidyanathan VV, Jahnz M, Dörries C, Bade S, Nauenburg S, Niemann H, and Binz T (1999): Proteolysis of SNAP-25 isoforms by Botulinum neurotoxin types A, C, and E: domains and amino acid residues controlling the formation of enzyme-substrate complexes and cleavage. J Neurochem 72, 327-37.

http://www.ncbi.nlm.nih.gov/pubmed/9886085

 

Binz T Blasi J, Yamasaki S, Baumeister A, Link E, Südhof TC, Jahn R, and Niemann H (1994): Proteolysis of SNAP-25 by types E and A botulinal neurotoxins. J Biol Chem 269, 1617-1620.

http://www.ncbi.nlm.nih.gov/pubmed/8294407

 

Blasi J, Binz T, Yamasaki S, Link E, Niemann H, and Jahn R (1994): Inhibition of neurotransmitter release by clostridial neurotoxins correlates with specific proteolysis of synaptosomal proteins. J Physiol (Paris) 88, 235-241.

http://www.ncbi.nlm.nih.gov/pubmed/7874084

 

Dayanithi G, Stecher B, Höhne-Zell B, Yamasaki S, Binz T, Weller U, Niemann H, and Gratzl M (1994): Exploring the functional domain and the target of the tetanus toxin light chain in neurohypophysial terminals. Neuroscience 58, 423-431.

http://www.ncbi.nlm.nih.gov/pubmed/8152548

 

Yamasaki S, Baumeister A, Binz T, Blasi J, Link E, Cornille F, Roques B, Fykse EM, Südhof TC, Jahn R, and Niemann H (1994): Cleavage of members of the synaptobrevin/VAMP family by types D and F botulinal neurotoxins and tetanus toxin. J Biol Chem 269, 12764-12772.

http://www.ncbi.nlm.nih.gov/pubmed/8175689

 

Yamasaki S, Binz T, Hayashi T, Szabo L, Yamasaki N, Eklund M, Jahn R, and Niemann H (1994): Botulinum neurotoxin type G proteolyses the Ala81-Ala82 bond of rat synaptobrevin 2. Biochem Biophys Res Commun 200, 829-835.

http://www.ncbi.nlm.nih.gov/pubmed/7910017

 

Yamasaki S, Hu Y, Binz T, Kalkuhl A, Kurazono H, Tamura T, Jahn R, Kandel E, and Niemann H (1994): Synaptobrevin of Aplysia californica: structure and degradation by tetanus toxin and botulinal neurotoxins type D and F. Proc Natl Acad Sci USA 91, 4688-4692.

http://www.ncbi.nlm.nih.gov/pubmed/8197120


Blasi J, Chapman ER, Link E, Binz T, Yamasaki S, DeCamilli P, Südhof TC, Niemann H, and Jahn R (1993): Botulinum neurotoxin A selectively cleaves the synaptic protein SNAP-25. Nature 365, 160-163.

http://www.ncbi.nlm.nih.gov/pubmed/8103915

 

Blasi J, Chapman ER, Yamasaki S, Binz T, Niemann H, and Jahn R (1993): Botulinum neurotoxin C blocks neurotransmitter release by means of cleaving HPC-1/syntaxin. EMBO J 12, 4821-4828.

http://www.ncbi.nlm.nih.gov/pubmed/7901002

 

Link E, Edelmann L, Chou J, Binz T, Yamasaki S, Eisel U, Baumert M, Südhof TC, Niemann H, and Jahn R (1992): Tetanus toxin action: inhibiton of neurotransmitter release linked to synaptobrevin proteolysis. Biochem Biophys Res Commun 189, 1017-1023.

http://www.ncbi.nlm.nih.gov/pubmed/1361727

 

Kurazono H, Mochida S, Binz T, Eisel U, Quanz M, Grebenstein O, Wernars K, Poulain B, Tauc L, and Niemann H (1992): Minimal essential domains specifying toxicity of the light chains of tetanus toxin and botulinum neurotoxin type A. J Biol Chem 267, 14721-14729.

http://www.ncbi.nlm.nih.gov/pubmed/1634516

 

 

Translocation of clostridial neurotoxin catalytic domains

 

Pirazzini M, Azarnia Tehran D, Zanetti G, Megighian A, Scorzeto M, Fillo S, Shone CC, Binz T, Rossetto O, Lista F, and Montecucco C(2014): Thioredoxin and its reductase are present on synaptic vesicles, and their inhibition prevents the paralysis induced by botulinum neurotoxins. Cell Reports 8, 1–9.

http://www.ncbi.nlm.nih.gov/pubmed/25220457

 

Pirazzini M, Henke T, Rossetto O, Mahrhold S, Krez N, Rummel A, Montecucco C, and Binz T (2013): Neutralisation of specific surface carboxylates speeds up translocation of botulinum neurotoxin type B enzymatic domain. FEBS Lett 587, 3831-3836.

http://www.ncbi.nlm.nih.gov/pubmed/24157364

 

Pirazzini M, Rossetto O, Bertasio C, Bordin F, Shone CC, Binz T, and Montecucco C (2013): Time course and temperature dependence of the membrane translocation of tetanus and botulinum neurotoxins C and D in neurons. Biochem Biophys Res Commun 430, 38-42.

http://www.ncbi.nlm.nih.gov/pubmed/23200837

 

Pirazzini M, Bordin F, Rossetto O, Shone CC, Binz T, and Montecucco C (2013): The Thioredoxin Reductase-Thioredoxin System is involved in the Entry of Tetanus and Botulinum Neurotoxins in the Cytosol of Nerve Terminals. FEBS Lett 587, 150-155.

http://www.ncbi.nlm.nih.gov/pubmed/23178719

Bade S, Rummel A, Reisinger C, Karnath T, Ahnert-Hilger G, Bigalke H, and Binz T (2004): Botulinum neurotoxin type D enables cytosolic delivery of enzymatically active cargo proteins to neurons via unfolded translocation intermediates. J Neurochem 91, 1461-1472.

http://www.ncbi.nlm.nih.gov/pubmed/15584922

 

 

Nerve cell receptors of clostridial neurotoxins

 

Strotmeier J, Mahrhold S, Krez N, Janzen C, Lou J, Marks JD, Binz T, and Rummel A (2014): Identification of the synaptic vesicle glycoprotein 2 receptor binding site in botulinum neurotoxin A. FEBS Lett 588, 1087-1093.

http://www.ncbi.nlm.nih.gov/pubmed/24583011

 

Höltje M, Schulze S, Strotmeier J, Mahrhold S, Richter K, Binz T, Bigalke H, Ahnert-Hilger G, and Rummel A (2013): Exchanging the minimal cell binding fragments of tetanus neurotoxin in botulinum neurotoxin A and B impacts their toxicity at the neuromuscular junction and central neurons. Toxicon 75, 108-121.

http://www.ncbi.nlm.nih.gov/pubmed/23817019

 

Willjes G, Mahrhold S, Strotmeier J, Eichner T, Rummel A, and Binz T (2013): Botulinum neurotoxin G binds synaptotagmin-II in a mode similar to that of serotype B: tyrosine 1186 and lysine 1191 cause its lower affinity. Biochemistry 52, 3930-3938.

http://www.ncbi.nlm.nih.gov/pubmed/23647335

 

Mahrhold S, Strotmeier J, Garcia-Rodriguez C, Lou J, Marks, JD, Rummel A, and Binz T (2013): Identification of the SV2-Protein Receptor Binding Site of Botulinum Neurotoxin Type E. Biochem J 453, 37-47.

http://www.ncbi.nlm.nih.gov/pubmed/23621114

 

Strotmeier J, Willjes G, Binz T, and Rummel A (2012): Human synaptotagmin-II is not a high affinity receptor for botulinum neurotoxin B and G: increased therapeutic dosage and immunogenicity. FEBS Lett 586, 310-313.

http://www.ncbi.nlm.nih.gov/pubmed/22265973

 

Rummel A, Mahrhold S, Bigalke H, and Binz T (2011): Exchange of the HCC domain mediating the double receptor recognition improves the pharmacodynamic properties of botulinum neurotoxin. FEBS J 278, 4506-4515.

http://www.ncbi.nlm.nih.gov/pubmed/21624052

 

Strotmeier J, Gu S, Jutzi S, Mahrhold S, Zhou J, Pich A, Eichner T, Bigalke H, Rummel A, Jin R, and Binz T (2011): The biological activity of botulinum neurotoxin type C is dependent upon novel types of ganglioside binding sites. Mol Microbiol 81, 143-156.

http://www.ncbi.nlm.nih.gov/pubmed/21542861

 

Strotmeier J, Lee K, Völker AK, Mahrhold S, Zong Y, Zeiser J, Zhou J, Pich A, Bigalke H, Binz T, Rummel A, Jin R (2010): Botulinum neurotoxin serotype D attacks neurons via two carbohydrate binding sites in a ganglioside dependent manner. Biochem J 431, 207-216.

http://www.ncbi.nlm.nih.gov/pubmed/20704566

 

Binz T and Rummel A (2009): Cell entry strategy of clostridial neurotoxins. J Neurochem 109, 1584-1595.

Review

http://www.ncbi.nlm.nih.gov/pubmed/19457120

 

Rummel A, Häfner K, Mahrhold S, Darashchonak N, Holt M, Jahn R, Beermann S, Karnath T, Bigalke H, and Binz T (2009): Botulinum neurotoxins C, E and F bind gangliosides via a conserved binding site prior to stimulation-dependent uptake with botulinum neurotoxin F utilising the three isoforms of SV2 as second receptor. J Neurochem 110, 1942-1954.

http://www.ncbi.nlm.nih.gov/pubmed/19650874

 

Rummel A, Eichner T, Weil T, Karnath T, Gutcaits A, Mahrhold S, Sandhoff K, Proia R, Acharya K R, Bigalke H, and Binz T (2007): Identification of the protein receptor binding site of botulinum neurotoxins B and G proves the double receptor concept. Proc Natl Acad Sci USA 104, 359-364.

http://www.ncbi.nlm.nih.gov/pubmed/17185412

 

Jin R, Rummel A, Binz T, and Brunger AT (2006): Botulinum neurotoxin B recognizes its protein receptor with high affinity and specificity. Nature 444, 1092-1095.
http://www.ncbi.nlm.nih.gov/pubmed/17167421

 

Mahrhold S, Rummel A, Bigalke H, Davletov B, and Binz T (2006): The synaptic vesicle protein 2C mediates the uptake of botulinum neurotoxin A into phrenic nerves. FEBS Lett 580, 2011-2014.

http://www.ncbi.nlm.nih.gov/pubmed/16545378

 

Rummel A, Karnath T, Henke T, Bigalke H, and Binz T (2004): Synaptotagmins I and II act as nerve cell receptors for botulinum neurotoxin G. J Biol Chem 279, 30865-30870.

http://www.ncbi.nlm.nih.gov/pubmed/15123599

 

Rummel A, Mahrhold S, Bigalke H, and Binz T (2004): The HCC-domain of botulinum neurotoxins A and B exhibits a singular ganglioside binding site displaying serotype specific carbohydrate interaction. Mol Microbiol 51, 631-643.

http://www.ncbi.nlm.nih.gov/pubmed/14731268

 

Rummel A, Bade S, Alves J, Bigalke H, and Binz T (2003): Two carbohydrate binding sites in the HCC-domain of tetanus neurotoxin are required for toxicity. J Mol Biol 326, 835-847.

http://www.ncbi.nlm.nih.gov/pubmed/12581644

 


 

Clostridial neurotoxins as tools to study vesicular fusion

 

Arsenault J, Cuijpers SA, Ferrari E, Niranjan D, Rust A, Leese C, O'Brien JA, Binz T, and Davletov B (2014): Botulinum protease-cleaved SNARE fragments induce cytotoxicity in neuroblastoma cells. J Neurochem 129, 781-791.

http://www.ncbi.nlm.nih.gov/pubmed/24372287

 

Zylbersztejn K, Petkovic M, Burgo A, Deck M, Garel S, Marcos S, Bloch-Gallego E, Nothias F, Serini G, Bagnard D, Binz T, and Galli T (2012): The vesicular SNARE Synaptobrevin is required for Semaphorin 3A axonal repulsion. J Cell Biol 196, 37-46.

http://www.ncbi.nlm.nih.gov/pubmed/22213797

 

Gutierrez-Martin Y, Bustillo D, Gomez-Villafuertes R, Sanchez-Nogueiro J, Torregrosa-Hetland C, Binz T, Gutierrez LM, Miras-Portugal MT, and Artalejo AR (2011): P2X7 receptors trigger ATP exocytosis and modify secretory vesicle dynamics in neuroblastoma cells. J Biol Chem 286, 11370-11381.

http://www.ncbi.nlm.nih.gov/pubmed/21292765

 

Nouvian R, Neef J, Bulankina AV, Reisinger E, Pangrsic T, Frank T, Sikorra S, Brose N, Binz T, and Moser T (2011): Exocytosis at the hair cell ribbon synapse apparently operates without neuronal SNARE proteins. Nat Neurosci 14, 411-413.

http://www.ncbi.nlm.nih.gov/pubmed/21378973

 

Darios F, Niranjan D, Ferrari E, Zhang F, Soloviev M, Rummel A, Bigalke H, Suckling J, Ushkaryov Y, Naumenko N, Shakirzyanova A, Giniatullin R, Maywood E, Hastings M, Binz T, and Davletov B (2010): SNARE tagging allows stepwise assembly of a multimodular medicinal toxin. Proc Natl Acad Sci USA 107, 18197-18201.

http://www.ncbi.nlm.nih.gov/pubmed/20921391

 

Darios F, Wasser C, Shakirzyanova A, Giniatullin A, Goodman K, Munoz-Bravo JL, Raingo J, Jorgačevski J, Kreft M, Zorec R, Rosa JM, Gandia L, Gutiérrez LM, Binz T, Giniatullin R, Kavalali ET, and Davletov B (2009): Sphingosine facilitates SNARE complex assembly and activates synaptic vesicle exocytosis. Neuron 62, 683-694.

http://www.ncbi.nlm.nih.gov/pubmed/19524527

 

Sedej S, Gurung, IS, Binz T, and Rupnik M (2009): Phosphatidylinositol-4,5-bisphosphate-dependent facilitation of the ATP-dependent secretory activity in mouse pituitary cells. Ann N Y Acad Sci 1152, 165-173.

http://www.ncbi.nlm.nih.gov/pubmed/19161387

 

Scheuber A, Rudge R, Danglot L, Raposo G, Binz T, Poncer JC, and Galli T (2006): Loss of AP3 function affects spontaneous and evoked release at hippocampal mossy fiber synapses. Proc Natl Acad Sci USA 103, 16562-16567.

http://www.ncbi.nlm.nih.gov/pubmed/17056716

 

Davletov B, Bajohrs M, and Binz T (2005): Beyond BOTOX: advantages and limitations of individual botulinum neurotoxins. Trends Neurosci 28, 446-452.

Review

http://www.ncbi.nlm.nih.gov/pubmed/15979165

 

Yelamanchili SV, Reisinger C, Becher A, Sikorra S, Bigalke H, Binz T, and Ahnert-Hilger G (2005): The C-terminal transmembrane region of synaptobrevin binds synaptophysin from adult synaptic vesicles. Eur J Cell Biol 84, 467-475.

http://www.ncbi.nlm.nih.gov/pubmed/15900706

 

Bajohrs M, Rickman C, Binz T, and Davletov B (2004): A molecular basis underlying differences in the toxicity of botulinum serotypes A and E. EMBO Rep 5, 1090-1095.

http://www.ncbi.nlm.nih.gov/pubmed/15486565

 

Nagy G, Reim K, Matti U, Brose N, Binz T, Rettig J, Neher E, and Sørensen JB (2004): Regulation of releasable vesicle pool sizes by protein kinase A-dependent phosphorylation of SNAP-25. Neuron 41, 351-365.

http://www.ncbi.nlm.nih.gov/pubmed/14766180

 

Rickman C, Meunier FA, Binz T, and Davletov B (2004): High affinity interaction of syntaxin and SNAP-25 on the plasma membrane is abolished by botulinum toxin E. J Biol Chem 279, 644-651.

http://www.ncbi.nlm.nih.gov/pubmed/14551199

 

Nagy G, Matti U, Nehring RB., Binz T, Rettig J, Neher E, and Sørensen JB (2002): Protein kinase C dependent phosphorylation of SNAP-25 at Ser187 potentiates vesicle recruitment. J Neurosci 22, 9278-9286.

http://www.ncbi.nlm.nih.gov/pubmed/12417653

 

Sørensen JB, Matti U, Wei SH, Nehring RB, Voets T, Ashery U, Binz T, Neher E, and Rettig J (2002): The SNARE protein SNAP-25 is linked to fast calcium triggering of exocytosis. Proc Natl Acad Sci USA 99, 1627-32.

http://www.ncbi.nlm.nih.gov/pubmed/11830673

 

Xu T, Binz T, Niemann H, and Neher E (1998): Multiple kinetic components of exocytosis distinguished by neurotoxin sensitivity.

Nature Neurosci 1, 192-200.

http://www.ncbi.nlm.nih.gov/pubmed/10195143

 

Hayashi T, Yamasaki S, Nauenburg S, Binz T, and Niemann H (1995): Disassembly of the reconstituted synaptic vesicle membrane fusion complex in vitro. EMBO J 14, 2317-2325.

http://www.ncbi.nlm.nih.gov/pubmed/7774590


 

Galli T, Chilcote T, Mundigl O, Binz T, Niemann H, and DeCamilli P (1994): Tetanus toxin-mediated cleavage of cellubrevin impairs exocytosis of transferrin receptor containing vesicles in CHO cells. J Cell Biol 125, 1015-1024.

http://www.ncbi.nlm.nih.gov/pubmed/8195285

 

Hayashi T, McMahon H, Yamasaki S, Binz T, Hata Y, Südhof TC, and Niemann H (1994): Synaptic vesicle membrane fusion complex: action of clostridial neurotoxins on assembly. EMBO J 13, 5051-5061.

http://www.ncbi.nlm.nih.gov/pubmed/7957071

 

Link E, Blasi J, Chapman ER, Edelmann L, Baumeister A, Binz T, Yamasaki S, Niemann H, and Jahn R (1994): Tetanus and botulinal neurotoxins: tools to understand exocytosis in neurons. Adv. Second Messenger & Phoshoprotein Res 29, 47-58.

Review

http://www.ncbi.nlm.nih.gov/pubmed/7848727

 

McMahon HT, Ushkaryov YA, Edelmann L, Link E, Binz T, Niemann H, Jahn R, and Südhof TC (1993): Cellubrevin is a ubiquitous tetanus-toxin substrate homologous to a putative synaptic vesicle fusion protein. Nature 364, 346-349.

http://www.ncbi.nlm.nih.gov/pubmed/833219

 

Mochida S, Poulain B, Eisel U, Binz T, Kurazono H, Niemann H, and Tauc L (1990): Molecular biology of clostridial toxins: expression of mRNAs encoding tetanus and botulinum neurotoxins in Aplysia neurons. J Physiol (Paris) 84, 278-284.

http://www.ncbi.nlm.nih.gov/pubmed/2079664

 

Mochida S, Poulain B, Eisel U, Binz T, Kurazono H, Niemann H, and Tauc L (1990): Exogenous mRNA encoding tetanus or botulinum neurotoxins expressed in Aplysia neurons. Proc Natl Acad Sci USA 87, 7844-7848.

http://www.ncbi.nlm.nih.gov/pubmed/2236000

 

 

Genetics and immunology of clostridial neurotoxins

 

Marvaud JC, Eisel U, Binz T, Niemann H, and Popoff MR (1998): TetR is a positive regulator of the Tetanus toxin gene in Clostridium tetani and is homolgous to BotR. Infect Immun 66, 5698-702.

http://www.ncbi.nlm.nih.gov/pubmed/9826344

 

Niemann H, Binz T, Grebenstein O, Kurazono H, Thierer J, Mochida S, Poulain B, and Tauc L (1991): Clostridial neurotoxins: from toxins to therapeutic tools? Behring Inst Mitt 89, 153-162.

Review

http://www.ncbi.nlm.nih.gov/pubmed/1930094


 

Binz T, Kurazono H, Popoff MR, Eklund MW, Sakaguchi G, Kozaki S, Kriegelstein K, Henschen A, Gill DM, and Niemann H (1990): Nucleotide sequence of the gene encoding Clostridium botulinum neurotoxin type D. Nucl Acids Res 18, 5556.

http://www.ncbi.nlm.nih.gov/pubmed/2216736

 

Binz T, Kurazono H, Wille M, Frevert J, Wernars K, and Niemann H (1990): The complete sequence of botulinum neurotoxin type A and comparison with other clostridial neurotoxins. J Biol Chem 265, 9153-9158.

http://www.ncbi.nlm.nih.gov/pubmed/2160960

 

Hauser D, Eklund MW, Kurazono H, Binz T, Niemann H, Gill DM, Boquet P, and Popoff MR (1990): Nucleotide sequence of Clostridium botulinum C1 neurotoxin. Nucl Acids Res 18, 4924.

http://www.ncbi.nlm.nih.gov/pubmed/2204031

 

Andersen-Beckh B, Binz T, Kurazono H, Mayer T, Eisel U, and Niemann H (1989): Expression of tetanus toxin subfragments in vitro and characterization of epitopes. Infect Immun 57, 3498-3505.

http://www.ncbi.nlm.nih.gov/pubmed/2478475

 

 

Borna Disease Virus

 

Kliche S, Stitz L, Mangalam H, Shi L, Binz T, Niemann H, Briese T, and Lipkin WI (1996): Characterization of the Borna disease virus phosphoprotein, p23. J Virol 70, 8133-8137.

http://www.ncbi.nlm.nih.gov/pubmed/8892940

 

Binz T, Lebelt J, Niemann H, and Hagenau K (1994): Sequence analyses of the p24 gene of Borna disease virus in naturally infected horse, donkey and sheep. Virus Res 34, 281-289.

http://www.ncbi.nlm.nih.gov/pubmed/7856315

 

Thierer J, Riehle H, Grebenstein O, Binz T, Herzog S, Thiedemann N, Stitz L, Rott R, Lottspeich F, and Niemann H (1992): The 24K protein of Borna disease virus. J Gen Virol 73, 413-416.

http://www.ncbi.nlm.nih.gov/pubmed/1538196


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