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Nature, ISSN 0028-0836, 2014, Volume 512, Issue 1, pp. 49 - 53
Journal Article
EMBO reports, ISSN 1469-221X, 12/2015, Volume 16, Issue 12, pp. 1699 - 1712
We describe a new class of reagents for identifying substrates, adaptors, and regulators of HECT and RING E3s. UBAITs (Ubiquitin‐Activated Interaction Traps)... 
Ubiquitin | RING E3s | HECT E3s | Ubiquitin ligases | YES-ASSOCIATED PROTEIN | RSP5 | COMPLEX | ECTOPIC LOCALIZATION | CRYSTAL-STRUCTURE | BIOCHEMISTRY & MOLECULAR BIOLOGY | CELL BIOLOGY | WW DOMAIN | YEAST URACIL PERMEASE | DEGRADATION | REVEALS | Peptide Elongation Factors - metabolism | Protein Binding - genetics | Saccharomyces cerevisiae - genetics | Humans | Ubiquitin - metabolism | Recombinant Fusion Proteins - metabolism | Endosomal Sorting Complexes Required for Transport - chemistry | Peptide Elongation Factors - genetics | Protein-Serine-Threonine Kinases - metabolism | Amino Acid Sequence | Endosomal Sorting Complexes Required for Transport - metabolism | Protein-Serine-Threonine Kinases - genetics | Ubiquitin - chemistry | Ubiquitin-Protein Ligases - metabolism | Ubiquitin-Conjugating Enzymes - genetics | Recombinant Fusion Proteins - chemistry | Saccharomyces cerevisiae Proteins - genetics | Ubiquitin-Protein Ligases - chemistry | Ubiquitin-Protein Ligase Complexes - chemistry | Peptide Elongation Factors - chemistry | Histones - genetics | Ubiquitin-Protein Ligase Complexes - metabolism | Ubiquitin-Conjugating Enzymes - metabolism | DNA Repair | Saccharomyces cerevisiae Proteins - metabolism | Saccharomyces cerevisiae - enzymology | Mutation | Ubiquitin-Protein Ligases - genetics | Saccharomyces cerevisiae Proteins - chemistry | Proteins | Molecular biology | DNA repair | Substrates | Methods & Resources | Post-translational Modifications, Proteolysis & Proteomics
Journal Article
NATURE, ISSN 0028-0836, 07/2016, Volume 535, Issue 7611, pp. 252 - 252
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 | PROTEIN-DEGRADATION | protein misfolding | MULTIDISCIPLINARY SCIENCES | neurodegeneration | EXPRESSION | DOMAINS | AGGREGATION | BRAIN | 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
Journal of Clinical Investigation, ISSN 0021-9738, 03/2009, Volume 119, Issue 3, pp. 650 - 660
Journal Article