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nedd4 ubiquitin protein ligases (481) 481
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endosomal sorting complexes required for transport - metabolism (224) 224
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Molecular Cell, ISSN 1097-2765, 11/2009, Volume 36, Issue 3, pp. 457 - 468
Journal Article
Journal Article
Journal Article
Proceedings of the National Academy of Sciences of the United States of America, ISSN 0027-8424, 10/2011, Volume 108, Issue 41, pp. 17004 - 17009
α-Synuclein is an abundant brain protein that binds to lipid membranes and is involved in the recycling of presynaptic vesicles. In Parkinson disease,... 
Proteins | Yeasts | Brain | Pathology | Neurons | Ubiquitins | Cell lines | Parkinson disease | Antibodies | Lewy bodies | Neurodegeneration | Protein misfolding | CELLS | MULTIDISCIPLINARY SCIENCES | neurodegeneration | TOXICITY | AUTOPHAGY | PROTEIN-DEGRADATION | protein misfolding | IN-VIVO | PROTEASOME | EXPRESSION | DOMAINS | AGGREGATION | PARKINSONS-DISEASE | Saccharomyces cerevisiae - genetics | Humans | Endosomal Sorting Complexes Required for Transport - genetics | Molecular Sequence Data | Substrate Specificity | Ubiquitin-Protein Ligase Complexes - genetics | Substantia Nigra - metabolism | Endosomes - metabolism | Brain - metabolism | Saccharomyces cerevisiae - metabolism | Ubiquitination | Lysosomes - metabolism | HEK293 Cells | Nedd4 Ubiquitin Protein Ligases | Parkinson Disease - metabolism | alpha-Synuclein - genetics | Lewy Bodies - metabolism | Binding Sites | Recombinant Proteins - metabolism | Amino Acid Sequence | Cell Line | Endosomal Sorting Complexes Required for Transport - metabolism | Ubiquitin-Protein Ligases - metabolism | Rats | Recombinant Proteins - chemistry | Recombinant Proteins - genetics | Saccharomyces cerevisiae Proteins - genetics | alpha-Synuclein - chemistry | Animals | Ubiquitin-Protein Ligase Complexes - metabolism | Saccharomyces cerevisiae Proteins - metabolism | Mice | In Vitro Techniques | Lysine - chemistry | Ubiquitin-Protein Ligases - genetics | alpha-Synuclein - metabolism | Locus Coeruleus - metabolism | Parkinson Disease - etiology | Biological Sciences
Journal Article
Neuron, ISSN 0896-6273, 2010, Volume 65, Issue 3, pp. 341 - 357
Regulated protein degradation via the ubiquitin-proteasome system (UPS) plays a central role in building synaptic connections, yet little is known about either... 
DEVBIO | MOLNEURO | SIGNALING | RETINAL GROWTH CONES | UBIQUITIN LIGASE | IN-VIVO | RETINOTECTAL SYNAPTIC CONNECTIVITY | XENOPUS EMBRYOS | TUMOR-SUPPRESSOR | VISUAL-SYSTEM | PROTEIN-SYNTHESIS | NEUROSCIENCES | ZEBRAFISH RETINA | CHEMOTROPIC RESPONSES | Xenopus | Humans | Gene Expression Regulation, Developmental - genetics | Axons - physiology | Green Fluorescent Proteins - genetics | Phosphatidylinositol 3-Kinases - metabolism | Retinal Ganglion Cells - cytology | Retina - cytology | Arginine - genetics | Nedd4 Ubiquitin Protein Ligases | Transduction, Genetic - methods | Gene Expression Regulation, Developmental - physiology | Growth Cones - physiology | PTEN Phosphohydrolase - genetics | Retinal Ganglion Cells - physiology | Immunoprecipitation - methods | Tissue Culture Techniques | Endosomal Sorting Complexes Required for Transport - metabolism | Ubiquitin-Protein Ligases - metabolism | PTEN Phosphohydrolase - metabolism | Signal Transduction - genetics | Ubiquitin - genetics | Xenopus Proteins | Electroporation - methods | Mutation - genetics | Microscopy, Confocal - methods | Down-Regulation - genetics | Down-Regulation - physiology | Lysine - genetics | Animals | Embryo, Nonmammalian | Superior Colliculi - cytology | Signal Transduction - physiology | Ubiquitin-Protein Ligases - genetics | Cell Line, Transformed | Ubiquitin | Physiological aspects | Neurosciences | Proteolysis | Neurons | Ligases | Proteins | Enzymes | Insects | Kinases
Journal Article