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Annual review of biochemistry, ISSN 1545-4509, 2009, Volume 78, Issue 1, pp. 399 - 434
E3 ligases confer specificity to ubiquitination by recognizing target substrates and mediating transfer of ubiquitin from an E2 ubiquitin-conjugating enzyme to substrate... 
UPS | APC | Cbl | CRL | SCF | Protein Structure, Tertiary | Animals | Humans | Ubiquitin - metabolism | Ubiquitin-Protein Ligases - metabolism | Genome, Human | Ubiquitin-Protein Ligases - chemistry | Ubiquitin-Protein Ligases - genetics | Human genome | Ligases | Analysis | Enzyme binding | Research | Chemical properties | Ubiquitin-proteasome system
Journal Article
Nature (London), ISSN 1476-4687, 03/2011, Volume 471, Issue 7340, pp. 637 - 641
Journal Article
Biochimica et biophysica acta. Molecular cell research, ISSN 0167-4889, 01/2014, Volume 1843, Issue 1, pp. 75 - 85
Journal Article
Journal Article
Proceedings of the National Academy of Sciences - PNAS, ISSN 0027-8424, 10/2011, Volume 108, Issue 41, pp. 17004 - 17009
.... Here we show that the ubiquitin ligase Nedd4, which functions in the endosomal-lysosomal pathway, robustly ubiquitinates α... 
Proteins | Yeasts | Brain | Pathology | Neurons | Ubiquitins | Cell lines | Parkinson disease | Antibodies | Lewy bodies | Neurodegeneration | Protein misfolding | Science & Technology - Other Topics | Multidisciplinary Sciences | Science & Technology | 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 | neurodegeneration | Biological Sciences | protein misfolding
Journal Article
Nature (London), ISSN 1476-4687, 2011, Volume 472, Issue 7343, pp. 361 - 365
TRIM5 is a RING domain-E3 ubiquitin ligase that restricts infection by human immunodeficiency virus (HIV... 
Science & Technology - Other Topics | Multidisciplinary Sciences | Science & Technology | Capsid - chemistry | Receptors, Pattern Recognition - immunology | Humans | Ubiquitin - metabolism | NF-kappa B - metabolism | Lipopolysaccharides - immunology | Transcription Factor AP-1 - metabolism | Receptors, Pattern Recognition - metabolism | Signal Transduction - immunology | Ubiquitin-Protein Ligases - immunology | HIV-1 - chemistry | HEK293 Cells | Carrier Proteins - immunology | Cell Line | Retroviridae - chemistry | Ubiquitin-Protein Ligases - metabolism | Retroviridae - immunology | MAP Kinase Kinase Kinases - metabolism | Transcription Factors - metabolism | Capsid - immunology | Carrier Proteins - genetics | Immunity, Innate - immunology | HIV-1 - immunology | Carrier Proteins - metabolism | Signal Transduction - drug effects | Ubiquitin-Conjugating Enzymes - metabolism | Lipopolysaccharides - pharmacology | Protein Binding | Enzyme Activation | Ubiquitin-Protein Ligases - genetics | Signal transduction | Efficiency | RNA polymerase | Pattern recognition | Kinases | Evacuations & rescues | Immune system | HIV-1/immunology | Capsid/immunology | Life Sciences | MAP Kinase Kinase Kinases/metabolism | Carrier Proteins/immunology | Immunology | Transcription Factors/metabolism | Capsid/chemistry | HIV-1/chemistry | Ubiquitin/metabolism | Receptors, Pattern Recognition/immunology | Retroviridae/chemistry | Ubiquitin-Protein Ligases/immunology | Ubiquitin-Conjugating Enzymes/metabolism | HumansImmunity, Innate/immunology | Lipopolysaccharides/pharmacology | Signal Transduction/drug effects | Retroviridae/immunology | Transcription Factor AP-1/metabolism | Lipopolysaccharides/immunology | Ubiquitin-Protein Ligases/metabolism | Carrier Proteins/genetics | Signal Transduction/immunology | NF-kappa B/metabolism | Ubiquitin-Protein Ligases/genetics | Carrier Proteins/metabolism | Receptors, Pattern Recognition/metabolism
Journal Article
Nature (London), ISSN 1476-4687, 11/2018, Volume 563, Issue 7733, pp. 652 - 656
Journal Article