S-nitrosylation of E3 ubiquitin-protein ligase RNF213 alters non-canonical Wnt/Ca+2 signaling in the P301S mouse model of tauopathy

Keyphrases

• Mouse Model 100%
• E3 Ubiquitin Ligase 100%
• Canonical Wnt Signaling 100%
• S-nitrosylation 100%
• RNF213 100%
• Ca+2 100%
• Tauopathy 100%
• P301S Mice 100%
• Ca++ 66%
• Frontotemporal Dementia 33%
• In(III) 16%
• Neurodegenerative Diseases 16%
• Path Analysis 16%
• Oxidative Stress 16%
• Transgenic 16%
• Missense mutation 16%
• Epilepsy 16%
• Brain Regions 16%
• Disease Progression 16%
• Tyrosine 16%
• Early Manifestation 16%
• Major Change 16%
• Cortex 16%
• Littermate Controls 16%
• Early Disease 16%
• Molecular Events 16%
• CaMKII 16%
• Entorhinal Cortex 16%
• S-nitrosylated Proteins 16%
• GO Analysis 16%
• Putative Drug Targets 16%
• Brain Hippocampus 16%
• MAPT Gene 16%
• Brain Cortex 16%
• Nuclear Factor of Activated T Cells 16%
• Microgliosis 16%
• Dementia with 16%
• Causes of Dementia 16%
• Calcium Regulation 16%
• Synaptic Function 16%
• MAPt 16%
• Nitric Oxide Production 16%
• P301S 16%
• Tau Protein 16%

Neuroscience

• Ubiquitin Protein Ligase E3 100%
• Tauopathy 100%
• Frontotemporal Dementia 66%
• Neurodegenerative Disorder 33%
• Hippocampus 33%
• Oxidative Stress 33%
• Missense Mutation 33%
• Nitric Oxide 33%
• Wnt Signaling Pathway 33%
• Gliosis 33%
• Calcium Signaling 33%
• Entorhinal Cortex 33%
• Nitrotyrosine 33%
• Transcription Factor NFAT 33%
• Tau Protein 33%