a-Synuclein-Induced Synapse Damage in Cultured Neurons Is Mediated by Cholesterol-Sensitive Activation of Cytoplasmic Phospholipase A2

Bate, C; Williams, A

doi:10.3390/biom5010178

A role for B lymphocytes in anti-infective prion therapies?
Journal Article
Tayebi, M., Bate, C., Hawke, S., & Williams, A. A role for B lymphocytes in anti-infective prion therapies?. Expert Review of Anti-infective Therapy, 5(4), 631-638. https://doi.org/10.1586/14787210.5.4.631

Squalestatin alters the intracellular trafficking of a neurotoxic prion peptide
Journal Article
Wilson, R., Bate, C., Boshuizen, R., Williams, A., & Brewer, J. Squalestatin alters the intracellular trafficking of a neurotoxic prion peptide. BMC Neuroscience, 8,

Background: Neurotoxic peptides derived from the protease-resistant core of the prion protein are used to model the pathogenesis of prion diseases. The current study characterised the ingestion, internalization and intracellular trafficking of a neur... Read More about Squalestatin alters the intracellular trafficking of a neurotoxic prion peptide.

Interferon-gamma increases neuronal death in response to amyloid-beta(1-42)
Journal Article
Bate, C., Kempster, S., Last, V., & Williams, A. Interferon-gamma increases neuronal death in response to amyloid-beta(1-42). https://doi.org/10.1186/1742-2094-3-7

Platelet-activating factor antagonists protect amyloid-beta damaged neurons from microglia-mediated death
Journal Article
Bate, C., Kempster, S., & Williams, A. Platelet-activating factor antagonists protect amyloid-beta damaged neurons from microglia-mediated death. Neuropharmacology, 51(2), 173-181. https://doi.org/10.1016/j.neuropharm.2006.02.015

Prostaglandin D-2 mediates neuronal damage by amyloid-beta or prions which activates microglial cells
Journal Article
Bate, C., Kempster, S., & Williams, A. Prostaglandin D-2 mediates neuronal damage by amyloid-beta or prions which activates microglial cells. Neuropharmacology, 50(2), 229-237. https://doi.org/10.1016/j.neuropharm.2005.09.008

Microglial cells kill prion-damaged neurons in vitro by a CD14-dependent process
Journal Article
Bate, C., Boshuizen, R., & Williams, A. Microglial cells kill prion-damaged neurons in vitro by a CD14-dependent process. Journal of Neuroimmunology, 170(1-2), 62-70. https://doi.org/10.1016/j.jneuroim.2005.08.021

Manipulation of PrPres production in scrapie-infected neuroblastoma cells
Journal Article
Bate, C., Langeveld, J., & Williams, A. Manipulation of PrPres production in scrapie-infected neuroblastoma cells. Journal of Neuroscience Methods, 138(1-2), 217-223. https://doi.org/10.1016/j.jneumeth.2004.04.001

Phospholipase A(2) inhibitors or platelet-activating factor antagonists prevent prion replication
Journal Article
Bate, C., Reid, S. W. J., & Williams, A. Phospholipase A(2) inhibitors or platelet-activating factor antagonists prevent prion replication. Journal of Biological Chemistry, 279(35), 36405-36411. https://doi.org/10.1074/jbc.M404086200

Squalestatin cures prion-infected neurons and protects against prion neurotoxicity
Journal Article
Bate, C., Salmona, M., Diomede, L., & Williams, A. Squalestatin cures prion-infected neurons and protects against prion neurotoxicity. Journal of Biological Chemistry, 279(15), 14983-14990. https://doi.org/10.1074/jbc.M313061200

The role of platelet activating factor in prion and amyloid-beta neurotoxicity
Journal Article
Bate, C., Salmona, M., & Williams, A. The role of platelet activating factor in prion and amyloid-beta neurotoxicity. NeuroReport, 15(3), 509-513. https://doi.org/10.1097/01.wnr.0000113065.17279.7b

Microglia kill amyloid-beta(1-42) damaged neurons by a CD14-dependent process
Journal Article
Bate, C., Veerhuis, R., Eikelenboom, P., & Williams, A. E. Microglia kill amyloid-beta(1-42) damaged neurons by a CD14-dependent process. NeuroReport, 15(9), 1427-1430. https://doi.org/10.1097/01.wnr.0000132203.76836.16

Detoxified lipopolysaccharide reduces microglial cell killing of prion-infected neurons
Journal Article
Bate, C., & Williams, A. Detoxified lipopolysaccharide reduces microglial cell killing of prion-infected neurons. NeuroReport, 15(18), 2765-2768

The N-Methylated Peptide SEN304 Powerfully Inhibits A beta(1-42) Toxicity by Perturbing Oligomer Formation
Journal Article
Amijee, H., Bate, C., Williams, A., Virdee, J., Jeggo, R., Spanswick, D., Scopes, D. I. C., Treherne, J. M., Mazzitelli, S., Chawner, R., Eyers, C. E., & Doig, A. J. The N-Methylated Peptide SEN304 Powerfully Inhibits A beta(1-42) Toxicity by Perturbing Oligomer Formation. Biochemistry, 51(42), 8338-8352. https://doi.org/10.1021/bi300415v

Simvastatin treatment prolongs the survival of scrapie-infected mice
Journal Article
Kempster, S., Bate, C., & Williams, A. Simvastatin treatment prolongs the survival of scrapie-infected mice. NeuroReport, 18(5), 479-482

Squalestatin protects neurons and reduces the activation of cytoplasmic phospholipase A(2) by A beta(1-42)
Journal Article
Bate, C., & Williams, A. Squalestatin protects neurons and reduces the activation of cytoplasmic phospholipase A(2) by A beta(1-42). Neuropharmacology, 53(2), 222-231. https://doi.org/10.1016/j.neuropharm.2007.05.003

Statins reduce the neurotoxicity of platelet-activating factor
Journal Article
Bate, C., Rumbold, L., & Williams, A. Statins reduce the neurotoxicity of platelet-activating factor

Cholesterol synthesis inhibitors protect against platelet-activating factor-induced neuronal damage
Journal Article
Bate, C., Rumbold, L., & Williams, A. Cholesterol synthesis inhibitors protect against platelet-activating factor-induced neuronal damage. https://doi.org/10.1186/1742-2094-4-5

Glycosylphosphatidylinositols: More than just an anchor?
Journal Article
Bate, C., Nolan, W., & Williams, A. (in press). Glycosylphosphatidylinositols: More than just an anchor?. https://doi.org/10.1080/19420889.2016.1149671

Monoacylated Cellular Prion Proteins Reduce Amyloid-beta-Induced Activation of Cytoplasmic Phospholipase A2 and Synapse Damage
Journal Article
West, E., Osborne, C., Nolan, W., & Bate, C. (in press). Monoacylated Cellular Prion Proteins Reduce Amyloid-beta-Induced Activation of Cytoplasmic Phospholipase A2 and Synapse Damage. Biology, 4(2), 367-82. https://doi.org/10.3390/biology4020367

Alzheimer’s disease (AD) is a progressive neurodegenerative disease characterized by the accumulation of amyloid-β (Aβ) and the loss of synapses. Aggregation of the cellular prion protein (PrPC) by Aβ oligomers induced synapse damage in cultured neur... Read More about Monoacylated Cellular Prion Proteins Reduce Amyloid-beta-Induced Activation of Cytoplasmic Phospholipase A2 and Synapse Damage.

a-Synuclein-Induced Synapse Damage in Cultured Neurons Is Mediated by Cholesterol-Sensitive Activation of Cytoplasmic Phospholipase A2
Journal Article
Bate, C., & Williams, A. (in press). a-Synuclein-Induced Synapse Damage in Cultured Neurons Is Mediated by Cholesterol-Sensitive Activation of Cytoplasmic Phospholipase A2. Biomolecules, 5(1), 178-93. https://doi.org/10.3390/biom5010178

The accumulation of aggregated forms of the α-synuclein (αSN) is associated with the pathogenesis of Parkinson’s disease (PD) and Dementia with Lewy Bodies. The loss of synapses is an important event in the pathogenesis of these diseases. Here we sho... Read More about a-Synuclein-Induced Synapse Damage in Cultured Neurons Is Mediated by Cholesterol-Sensitive Activation of Cytoplasmic Phospholipase A2.

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