Chabry, J., Priola, S. A., Wehrly, K., et al. (1999). Species-independent
inhibition of abnormal prion protein (PrP) formation by a peptide con-
taining a conserved PrP sequence. J. Virol. 73: 6245­6250.
Defective Interfering Particles
Chesebro, B. (1999). Prion protein and the transmissible spongiform
encephalopathy diseases. Neuron 24: 503­506.
Roux, L. (1999). Defective interfering viruses. In Encyclopedia of Virology
Gossert, A. D., Bonjour, S., Lysek, D. A., Fiorito, F., and Wüthrich, K.
(A. Granoff and R. G. Webster, Eds.), San Diego, Academic Press, Vol.
(2005). Prion protein NMR structures of elk and of mouse/elk hybrids.
1, pp. 371­375.
Proc. Natl. Acad. Sci. U.S.A. 102: 646­650.
Haywood, A. M. (2004). Transmissible spongiform encephalopathies.
In Infections of the Central Nervous System, 3rd edition (W. M. Scheld,
R. J. Whitley, and C. M. Marra, Eds.), Philadelphia, Lippincott, Williams
& Wilkins, pp. 261­272.
Flores, R., Di Serio, F., and Hernández, C. (1997). Viroids: the noncoding
Hegde, R. S., Mastrianni, J. A., Scott, M. R., et al. (1998). A transmem-
genomes. Semin. Virol. 8: 65­73.
brane form of the prion protein in neurodegenerative disease. Science
Pelchat, M., Lévesque, D., Ouellet, J., et al. (2000). Sequencing of peach
279: 827­834.
latent mosaic viroid variants from nine North American peach cultivars
Lysek, A. A., Schorn, C., Nivon, L. G., et al. (2005). Prion protein NMR
shows that this RNA folds into a complex secondary structure. Virology
structures of cats, dogs, pigs, and sheep. Proc. Natl. Acad. Sci. U.S.A.
271: 37­45.
102: 640­645.
Peretz, D., Supattapone, S., Giles, K., et al. (2006). Inactivation of prions by
Hepatitis Delta
acidic sodium dodecyl sulfate. J. Virol. 80: 322­331.
Prusiner, S. B. (Ed.) (1999). Prion Biology and Diseases. Cold Spring
Casey, J. L. (2002). RNA editing in hepatitis delta virus genotype III requires
Harbor, NY, Cold Spring Harbor Laboratory Press.
a branched double-hairpin RNA structure. J. Virol. 76: 7385­7397.
Prusiner, S. (2006). Prions. Chapter 79 in: Fields Virology, Fifth Edition
Macnaughton, T. B., Shi, S. T., Modahl, L. E., and Lai, M. M. C. (2002).
(D. M. Knipe and P. M. Howley, Eds. in chief), Philadelphia, Lippincott
Rolling circle replication of hepatitis delta virus RNA is carried out by
Williams & Wilkins, pp. 3059­3091.
two different cellular RNA polymerases. J. Virol. 76: 3920­3927.
Rhodes, R. (1997). Deadly Feasts. New York, Simon & Schuster.
Modahl, L. E., and Lai, M. M. C. (2000). Hepatitis delta virus: the molecu-
Riek, R., Hornemann, S., Wider, G., et al. (1996). NMR Structure of the
lar basis of laboratory diagnosis. Crit. Rev. Clin. Lab. Sci. 37: 45­92.
mouse prion protein domain PrP(121­231). Nature 382: 180­183.
Polson, A. G., Ley, H. J. III, Bass, B. L., et al. (1998). Hepatitis delta virus
Ross, E. D., Edskes, H. K., Terry, M. J., and Wickner, R. B. (2005). Primary
RNA editing is highly specific for amber/W site and is suppressed by
sequence independence for prion formation. Proc. Natl. Acad. Sci.
hepatitis delta antigen. Mol. Cell. Biol. 18: 1919­1926.
U.S.A. 102: 12825­12830.
Taylor, J. M., Farci, P., and Purcell, R. H. (2006). Hepatitis Delta Virus
Safar, J. G., Geschwind, M. D., Deering, C., et al. (2005). Diagnosis of
Chapter 77 in: Fields Virology, Fifth Edition (D. M. Knipe and P. M.
human prion disease. Proc. Natl. Acad. Sci. U.S.A. 102: 3501­3506.
Howley, Eds. in chief), Philadelphia, Lippincott Williams & Wilkins,
Schonberger, L. B. (1998). New-variant Creutzfeldt-Jakob disease and
pp. 3031­3046.
bovine spongiform encephalopathy: the strengthening etiologic link
between two emerging diseases. In Emerging Infections 2 (W. M.
Scheld, W. A. Craig, and J. M. Hughes, Eds.), Washington, DC, ASM
Prions and Prion Diseases
Press, pp. 1­15.
Weissmann, C. (1996). Molecular biology of transmissible spongiform
Anderson, R. M., Donnelly, C. A., Ferguson, N. M., et al. (1996).
encephalopathies. FEBS Lett. 389: 3­11.
Transmission dynamics and epidemiology of BSE in British cattle.
Windl, O., Buchholz, M., Neubauer, A., et al. (2005). Breaking an abso-
Nature 382: 779­788.
lute species barrier: transgenic mice expressing the mink PrP gene
Angers, R. C., Browning, S. R., Seward, T. S., et al. (2006). Prions in skel-
are susceptible to transmissible mink encephalopathy. J. Virol. 79:
etal muscles of deer with chronic wasting disease. Science 311: 1117.
Baker, H. F., and Ridley, R. M. (1996). What went wrong in BSE? From
Zhang, C. C., Steele, A. D., Lindquist, S., and Lodish, H. F. (2006). Prion
prion disease to public disaster. Brain Res. Bull. 40: 237­244.
protein is expressed on long-term repopulating hematopoietic stem cells
Baron, G. S., Magalhães, A. C., Prado, M. A. M., and Caughey, B.
and is important for their self-renewal. Proc. Natl. Acad. Sci. U.S.A.
(2006). Mouse-adapted scrapie infection of SN56 cells: greater effi-
103: 2184­2189.
ciency with microsome-associated versus purified PrP-res. J. Virol.
80: 2106­2117.
Bons, N., Mestre-Frances, N., Belli, P., et al. (1999). Natural and
Yeast Prions
experimental oral infection of nonhuman primates by bovine spongi-
form encephalopathy agents. Proc. Natl. Acad. Sci. U.S.A. 96:
King, C.-Y., and Diaz-Avalos, R. (2004). Protein-only transmission of three
yeast prion strains. Nature 428: 319­328.
Brown, P. (2004). Mad-cow disease in cattle and human beings. American
Roberts, B. T., and Wickner, R. B. (2003). Heritable activity: a prion that
Scientist 92: 334­341.
propagates by covalent autoactivation. Genes Dev. 17: 2083­2087.
Calzolai, L., Lysek, D. A., Pérez, D. R., Güntert, P., and Wüthrich, K.
Wickner, R. B., Taylor, K. L., Edskes, H. K., et al. (1999). Prions in
(2005). Prion protein NMR structures of chickens, turtles, and frogs.
Saccharomyces and Podospora spp.: protein-based inheritance.
Proc. Natl. Acad. Sci. U.S.A. 102: 651­655.
Microbiol. Mol. Biol. Rev. 63: 844­861.
Search WWH :
Custom Search
Previous Page
Viruses And Human Disease Topic Index
Next Page
Viruses And Human Disease Bookmarks