Epitope-specific anti-prion antibodies upregulate apolipoprotein E and disrupt membrane cholesterol homeostasis
Journal Article
Tayebi, M., David, M., Bate, C., Jones, D. R., Taylor, W., Morton, R., Pollard, J., & Hawke, S. Epitope-specific anti-prion antibodies upregulate apolipoprotein E and disrupt membrane cholesterol homeostasis. Journal of General Virology, 91(Pt12), 3105-3115. https://doi.org/10.1099/vir.0.023838-0
Outputs (65)
PrP-specific camel antibodies with the ability to immunodetect intracellular prion protein
Journal Article
Tayebi, M., Taylor, W. A., Jones, D. R., Bate, C., & David, M. PrP-specific camel antibodies with the ability to immunodetect intracellular prion protein. Journal of General Virology, 91, 2121-2131. https://doi.org/10.1099/vir.0.018754-0
Glimepiride Reduces the Expression of PrPC, Prevents PrPSc Formation and Protects against Prion Mediated Neurotoxicity
Journal Article
Bate, C., Tayebi, M., Diomede, L., Salmona, M., & Williams, A. Glimepiride Reduces the Expression of PrPC, Prevents PrPSc Formation and Protects against Prion Mediated Neurotoxicity. PLoS ONE, 4(12), e8221. https://doi.org/10.1371/journal.pone.0008221
LIPID RAFTS, CELL SIGNALLING, PRION FORMATION AND NEURODEGENERATION IN PRION DISEASES
Presentation / Conference Contribution
Williams, A., & Bate, C. LIPID RAFTS, CELL SIGNALLING, PRION FORMATION AND NEURODEGENERATION IN PRION DISEASES
Do prion-induced changes in cholesterol trigger neurodegeneration?
Journal Article
Bate, C., & Williams, A. Do prion-induced changes in cholesterol trigger neurodegeneration?. Future Neurology, 3(4), 367-370. https://doi.org/10.2217/14796708.3.4.367
Sequestration of free cholesterol in cell membranes by prions correlates with cytoplasmic phospholipase A(2) activation
Journal Article
Bate, C., Tayebi, M., & Williams, A. Sequestration of free cholesterol in cell membranes by prions correlates with cytoplasmic phospholipase A(2) activation. BMC Biology, 6, https://doi.org/10.1186/1741-7007-6-8Background: The transmissible spongiform encephalopathies (TSEs), otherwise known as the prion diseases, occur following the conversion of the normal cellular prion protein ( PrPC) to an alternatively folded isoform ( PrPSc). The accumulation of PrPS... Read More about Sequestration of free cholesterol in cell membranes by prions correlates with cytoplasmic phospholipase A(2) activation.
Ginkgolides protect against amyloid-beta(1-42)-mediated synapse damage in vitro
Journal Article
Bate, C., Tayebi, M., & Williams, A. Ginkgolides protect against amyloid-beta(1-42)-mediated synapse damage in vitro. Molecular Neurodegeneration, 3(1), https://doi.org/10.1186/1750-1326-3-1
Cholesterol esterification reduces the neurotoxicity of prions
Journal Article
Bate, C., Tayebi, M., & Williams, A. Cholesterol esterification reduces the neurotoxicity of prions. Neuropharmacology, 54(8), 1247-1253. https://doi.org/10.1016/j.neuropharm.2008.04.002The transmissible spongiform encephalopathies develop following the conversion of a host-encoded protein (PrPC) into abnormally folded, disease-related isoforms (PrPSc). Here we report that three acylcoenzyme A:cholesterol acyltransferase (ACAT) inhi... Read More about Cholesterol esterification reduces the neurotoxicity of prions.
Docosahexaenoic and eicosapentaenoic acids increase prion formation in neuronal cells
Journal Article
Bate, C., Tayebi, M., Diomede, L., Salmona, M., & Williams, A. Docosahexaenoic and eicosapentaenoic acids increase prion formation in neuronal cells. BMC Biology, 6, https://doi.org/10.1186/1741-7007-6-39Background: The transmissible spongiform encephalopathies, otherwise known as prion diseases, occur following the conversion of the cellular prion protein (PrPC) to an alternatively folded, disease-associated isoform (PrPSc). Recent studies suggest t... Read More about Docosahexaenoic and eicosapentaenoic acids increase prion formation in neuronal cells.
Role of glycosylphosphatidylinositols in the activation of phospholipase A(2) and the neurotoxicity of prions
Journal Article
Bate, C., & Williams, A. Role of glycosylphosphatidylinositols in the activation of phospholipase A(2) and the neurotoxicity of prions. Journal of General Virology, 85(85), 3797-3804. https://doi.org/10.1099/vir.0.80366-0