Modeling and analysis of prion dynamics in the presence of a chaperone. Export

@article{citeulike:3658794, abstract = {Prions are infectious agents and are polymers called PrP(Sc)-Prion protein scrapies, of a normal protein, a monomer called PrP(c)-Prion protein cellular. These PrP(Sc)s cause TSEs-transmissible spongiform encephalopathies such as bovine spongiform encephalopathy (BSE) in cattle, scrapies in sheep, Kuru and Creutzfeld-Jacob diseases in humans. Cellular molecular chaperones, which are ubiquitous, stress-induced proteins, and newly found chemical and pharmacological chaperones have been found to be effective in preventing misfolding of different disease-causing proteins, essentially reducing the severity of several neurodegenerative disorders and many other protein-misfolding diseases. In this work, we propose a model for the replication of prions by nucleated polymerization in the presence of a chaperone. According to this model, the biological processes of coagulation, splitting and the inhibitory effects of the chaperone can be described by a coupled system consisting of ordinary differential equations and a partial differential equation. The model is converted into a system of ordinary differential equations and the equilibrium points are computed and their stability is studied. We give a numerical simulation of the model and we find that a disease free state can be achieved in the presence of a chaperone. The duration of the disease free state is found to increase with the amount of chaperone and this amount of chaperone can be computed from the model.}, author = {Kumar, R. and Murali, P.}, citeulike-article-id = {3658794}, citeulike-linkout-0 = {http://dx.doi.org/10.1016/j.mbs.2008.02.002}, citeulike-linkout-1 = {http://view.ncbi.nlm.nih.gov/pubmed/18362035}, citeulike-linkout-2 = {http://www.hubmed.org/display.cgi?uids=18362035}, doi = {10.1016/j.mbs.2008.02.002}, issn = {0025-5564}, journal = {Mathematical biosciences}, keywords = {dynamics, model, prion}, month = {May}, number = {1}, pages = {50--55}, posted-at = {2008-11-22 03:34:13}, priority = {2}, title = {Modeling and analysis of prion dynamics in the presence of a chaperone.}, url = {http://dx.doi.org/10.1016/j.mbs.2008.02.002}, volume = {213}, year = {2008} }

TY - JOUR ID - citeulike:3658794 L3 - citeulike-article-id:3658794 N2 - Prions are infectious agents and are polymers called PrP(Sc)-Prion protein scrapies, of a normal protein, a monomer called PrP(c)-Prion protein cellular. These PrP(Sc)s cause TSEs-transmissible spongiform encephalopathies such as bovine spongiform encephalopathy (BSE) in cattle, scrapies in sheep, Kuru and Creutzfeld-Jacob diseases in humans. Cellular molecular chaperones, which are ubiquitous, stress-induced proteins, and newly found chemical and pharmacological chaperones have been found to be effective in preventing misfolding of different disease-causing proteins, essentially reducing the severity of several neurodegenerative disorders and many other protein-misfolding diseases. In this work, we propose a model for the replication of prions by nucleated polymerization in the presence of a chaperone. According to this model, the biological processes of coagulation, splitting and the inhibitory effects of the chaperone can be described by a coupled system consisting of ordinary differential equations and a partial differential equation. The model is converted into a system of ordinary differential equations and the equilibrium points are computed and their stability is studied. We give a numerical simulation of the model and we find that a disease free state can be achieved in the presence of a chaperone. The duration of the disease free state is found to increase with the amount of chaperone and this amount of chaperone can be computed from the model. IS - 1 JF - Mathematical biosciences SN - 0025-5564 EP - 55 TI - Modeling and analysis of prion dynamics in the presence of a chaperone. VL - 213 SP - 50 KW - dynamics KW - model KW - prion AU - Kumar, R AU - Murali, P PY - 2008/05// UR - http://dx.doi.org/10.1016/j.mbs.2008.02.002 ER -