Dynamics of the nucleated polymerization model of prion replication

Biophysical Chemistry

Volumn 125, Issue 2-3, 2007, Pages 360-367

  Rubenstein, R ^a   Gray, P C ^b   Cleland, T J ^b   Piltch, M S ^b   Hlavacek, W S ^b   Roberts, R M ^b   Ambrosiano, J ^b   Kim, J I ^c  

^a SUNY DOWNSTATE MEDICAL CENTER   (United States)

^b LOS ALAMOS NATIONAL LABORATORY   (United States)

^c NEW YORK STATE INSTITUTE FOR BASIC RESEARCH IN DEVELOPMENTAL DISABILITIES   (United States)

Author keywords

Model system; Nucleated polymerization; Prion replication; Protein misfolding cyclic amplification (PMCA); PrP aggregation; TSE

Indexed keywords

ISOPROTEIN; PRION PROTEIN; PROTEIN PRP C; PROTEIN PRP SC; PROTEINASE; UNCLASSIFIED DRUG;

ALPHA HELIX; ARTICLE; BETA SHEET; BIOLOGICAL MODEL; CATALYSIS; CHEMICAL REACTION KINETICS; CONCENTRATION (PARAMETERS); DISEASE COURSE; MOLECULAR DYNAMICS; MONTE CARLO METHOD; NONHUMAN; NUCLEATED POLYMERIZATION MODEL; POLYMERIZATION; PRION; PRION DISEASE; PRIORITY JOURNAL; PROTEIN AGGREGATION; PROTEIN FOLDING; PROTEIN STRUCTURE; SIMULATION; TIME; VIRUS REPLICATION;

ANIMALS; HUMANS; MODELS, CHEMICAL; MONTE CARLO METHOD; PARTICLE SIZE; POLYMERS; PRIONS; PROTEIN FOLDING; PRPC PROTEINS; PRPSC PROTEINS;

EID: 33846328750     PISSN: 03014622     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bpc.2006.09.011     Document Type: Article

References (17)

1. Cohen F.E., Pan K.M., Huang Z., Baldwin M., Fletterick R.J., and Prusiner S.B. Structural clues of prion replication. Science 264 (1994) 530
2. Landsbury P.T. Mechanism of scrapie replication. Science 265 (1994) 1510
3. Eigen M. Prionics or the kinetic basis of prion diseases. Biophys. Chem. 63 (1996) A1-A18
4. Weissmann C. Molecular genetics of transmissible spongiform encephalopathies. J. Biol. Chem. 274 1 (1999) 3-6
5. Bueler H., Aguzzi A., Sailer A., Greiner R.A., Autenried P., Aguet N., and Weissmann C. Mice devoid of prp are resistant to scrapie. Cell 73 (1993) 1339
6. Masel J., Jansen V.A.A., and Nowak M.A. Quantifying the parameters of prion replication. Biophys. Chem. 77 (1999) 139-152
7. Nowak M.A., Krakaur D.C., Klug A., and May R.M. Prion infection dynamics. Integr. Biol. 1 (1998) 3-15
8. 2. J. Mol. Biol. 345 (2005) 1243-1251
9. Gillespie D.T. A general method for numerically simulating the stochastic time evolution of coupled chemical reactions. J. Comp. Phys. 22 (1976) 403-434
10. Gibson M.A., and Bruck J. Efficient exact stochastic simulation of chemical systems with many species and many channels. J. Phys. Chem., A 104 (2000) 1876-1889
11. Roberts R.M., Cleland T.J., Gray P.C., and Ambrosiano J.J. Hidden Markov model for competitive binding and chain elongation. J. Phys. Chem., B 108 20 (2004) 6228-6232
12. Blinov M.L., Faeder J.R., Goldstein B., and Hlavacek W.S. BioNetGen: software for rule-based modeling of signal transduction based on the interactions of molecular domains. Bioinformatics 20 (2004) 3289-3291
13. Faeder J.R., Blinov M.L., Goldstein B., and Hlavacek W.S. Rule-based modeling of biochemical networks. Complexity 10 (2005) 22-41
14. Cohen S.D., and Hindmarsh A.C. CVODE users guide. LLNL Report UCRL-MA-118618 (October 1994)
15. Gillespie D.T. A rigorous derivation of the chemical master equation. Physica, A 188 (1992) 404-425
16. Saborio G.P., Permanne B., and Soto C. Sensitive detection of pathological prion protein by cyclic amplification of protein misfolding. Nature 411 (2001) 810-813
17. Mabbott N.A., and Bruce M.E. The immunobiology of TSE diseases. J. Gen. Virol. 82 (2001) 2307-2318