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Journal Article
Nature, ISSN 0028-0836, 06/2015, Volume 522, Issue 7557, pp. 450 - 454
The anaphase-promoting complex (APC/C) is a multimeric RING E3 ubiquitin ligase that controls chromosome segregation and mitotic exit. Its regulation by... 
E3 LIGASE | SPINDLE CHECKPOINT | ANAPHASE-PROMOTING COMPLEX | CRYSTAL-STRUCTURE | MULTIDISCIPLINARY SCIENCES | MITOTIC REGULATION | EM STRUCTURE DETERMINATION | CRYO-EM | ELECTRON-MICROSCOPY | CONJUGATING ENZYME | CHAIN ELONGATION | Phosphorylation | Ubiquitin - ultrastructure | Cadherins - metabolism | Humans | Apc11 Subunit, Anaphase-Promoting Complex-Cyclosome - chemistry | Ubiquitin - metabolism | Cell Cycle Proteins - ultrastructure | Substrate Specificity | Apc10 Subunit, Anaphase-Promoting Complex-Cyclosome - ultrastructure | Structure-Activity Relationship | Anaphase-Promoting Complex-Cyclosome - ultrastructure | Protein Subunits - metabolism | Ubiquitin-Conjugating Enzymes - chemistry | Apc1 Subunit, Anaphase-Promoting Complex-Cyclosome - metabolism | Cell Cycle Proteins - chemistry | Apc3 Subunit, Anaphase-Promoting Complex-Cyclosome - chemistry | Ubiquitination | Apc8 Subunit, Anaphase-Promoting Complex-Cyclosome - metabolism | Cadherins - chemistry | Cytoskeletal Proteins - metabolism | Lysine - metabolism | Anaphase-Promoting Complex-Cyclosome - chemistry | Cadherins - ultrastructure | Apc10 Subunit, Anaphase-Promoting Complex-Cyclosome - metabolism | Catalytic Domain | F-Box Proteins - metabolism | Apc3 Subunit, Anaphase-Promoting Complex-Cyclosome - metabolism | F-Box Proteins - chemistry | Cell Cycle Proteins - metabolism | Ubiquitin - chemistry | Models, Molecular | Ubiquitin-Conjugating Enzymes - ultrastructure | Cytoskeletal Proteins - chemistry | Apc1 Subunit, Anaphase-Promoting Complex-Cyclosome - chemistry | Apc8 Subunit, Anaphase-Promoting Complex-Cyclosome - chemistry | Cryoelectron Microscopy | F-Box Proteins - ultrastructure | Ubiquitin-Conjugating Enzymes - metabolism | Protein Binding | Protein Subunits - chemistry | Apc10 Subunit, Anaphase-Promoting Complex-Cyclosome - chemistry | Anaphase-Promoting Complex-Cyclosome - metabolism | Apc11 Subunit, Anaphase-Promoting Complex-Cyclosome - metabolism | Apc1 Subunit, Anaphase-Promoting Complex-Cyclosome - ultrastructure | Apc8 Subunit, Anaphase-Promoting Complex-Cyclosome - ultrastructure | Ubiquitin | Physiological aspects | Structure | Ubiquitin-proteasome system | Ligases | Proteins | Peptides | Molecular structure | Cyclin-dependent kinases | Cell division | Kinases | Gene expression
Journal Article
Nature, ISSN 0028-0836, 11/2010, Volume 468, Issue 7322, pp. 400 - 407
Journal Article
Analytical Chemistry, ISSN 0003-2700, 11/2003, Volume 75, Issue 21, pp. 6023 - 6028
Improved in-solution tryptic digestion of proteins in terms of speed and peptide coverage was achieved with the aid of a novel acid-labile anionic surfactant... 
MIXTURES | CHEMISTRY, ANALYTICAL | PEPTIDES | POLYACRYLAMIDE-GEL ELECTROPHORESIS | LIQUID-CHROMATOGRAPHY | SEPARATION | IDENTIFICATION | Myoglobin - metabolism | Chymotrypsin - metabolism | Ubiquitin - metabolism | Myoglobin - chemistry | Chromatography, High Pressure Liquid | Arginine - analogs & derivatives | Urea - chemistry | Neurotensin - metabolism | Ovalbumin - metabolism | Neurotensin - chemistry | Spectrometry, Mass, Electrospray Ionization | Membrane Proteins - metabolism | Molecular Structure | Ovalbumin - chemistry | Endopeptidases - metabolism | Angiotensin II - metabolism | Muramidase - chemistry | Solubility | Ubiquitin - chemistry | Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization - methods | Muramidase - metabolism | Trypsin - metabolism | Dioxolanes - chemistry | Arginine - chemistry | Angiotensin II - chemistry | Proteins - metabolism | Membrane Proteins - chemistry | Alkanesulfonates - chemistry | Sodium Dodecyl Sulfate - chemistry | Bacteriorhodopsins - metabolism | Hydrophobic and Hydrophilic Interactions | Surface-Active Agents - chemistry | Proteins - chemistry | Bacteriorhodopsins - chemistry | Arginine - metabolism | Hydrogen-Ion Concentration | Enzymes | Usage | Composition | Chemistry, Analytic | Solution (Chemistry) | Liquid chromatography | Research | Chemical compounds | Proteins | Trypsin | Surface active agents | Acids | Proteolysis | Analysis | Mass spectrometry
Journal Article
Science, ISSN 0036-8075, 5/2010, Volume 328, Issue 5981, pp. 1025 - 1029
SAGA is a transcriptional coactivator complex that is conserved across eukaryotes and performs multiple functions during transcriptional activation and... 
Proteins | Yeasts | Active sites | Ubiquitins | REPORTS | Histones | Atoms | Amino acids | Nucleosomes | Aldehydes | Zinc | COMPLEX | DOMAIN | UBP8 | CHROMATIN | NUCLEAR-PORE | UBIQUITIN | MULTIDISCIPLINARY SCIENCES | SUS1 | DEUBIQUITYLATION | MESSENGER-RNA EXPORT | ASSOCIATION | Transcription Factors - chemistry | Histone Acetyltransferases - chemistry | Nucleosomes - chemistry | Zinc - metabolism | Ubiquitin - metabolism | Crystallography, X-Ray | Ubiquitins - chemistry | Aldehydes - metabolism | Trans-Activators - chemistry | Zinc - chemistry | Endopeptidases - chemistry | Ubiquitination | Histone Acetyltransferases - metabolism | Ubiquitinated Proteins - metabolism | Ubiquitins - metabolism | Protein Structure, Tertiary | Endopeptidases - metabolism | Zinc Fingers | RNA-Binding Proteins - chemistry | Ubiquitin - chemistry | Models, Molecular | Nucleosomes - metabolism | Nuclear Proteins - metabolism | Nuclear Proteins - chemistry | Transcription Factors - metabolism | Models, Biological | Saccharomyces cerevisiae Proteins - metabolism | Protein Binding | Protein Conformation | Trans-Activators - metabolism | Histones - metabolism | RNA-Binding Proteins - metabolism | Aldehydes - chemistry | Saccharomyces cerevisiae Proteins - chemistry | Ubiquitin | Physiological aspects | Transcription factors | Research | Eukaryotes | Biochemistry | Cellular biology | Proteases | Crystal structure | Modules | Mathematical models | Assembly | Elongation
Journal Article
Journal Article
Journal Article
Molecular Cell, ISSN 1097-2765, 10/2009, Volume 36, Issue 1, pp. 39 - 50
In the largest E3 ligase subfamily, Cul3 binds a BTB domain, and an associated protein-interaction domain such as MATH recruits substrates for ubiquitination.... 
PROTEINS | E3 LIGASE | OXIDATIVE STRESS | PROTEIN SPOP | NRF2 | BIOCHEMISTRY & MOLECULAR BIOLOGY | SCF | ADAPTER | DEGRADATION | BTB DOMAIN | F-BOX | TRANSCRIPTION FACTOR | CELL BIOLOGY | Transcription Factors - chemistry | Humans | Crystallography, X-Ray | Drosophila Proteins - metabolism | Mutation - physiology | Protein Multimerization - physiology | Protein Structure, Quaternary - physiology | Ubiquitination - physiology | Peptide Fragments - genetics | Repressor Proteins - metabolism | Amino Acid Sequence | Ubiquitin-Protein Ligases - metabolism | Models, Molecular | Repressor Proteins - genetics | Recombinant Fusion Proteins - chemistry | Nuclear Proteins - chemistry | Ubiquitin-Protein Ligases - chemistry | DNA-Binding Proteins - chemistry | Cullin Proteins - chemistry | Peptide Fragments - chemistry | Phosphoprotein Phosphatases - genetics | Consensus Sequence - physiology | Recombinant Fusion Proteins - genetics | Histones - metabolism | Ubiquitin-Protein Ligases - genetics | Drosophila melanogaster | Phosphoprotein Phosphatases - chemistry | Protein Binding - physiology | Adaptor Proteins, Signal Transducing - chemistry | Histones - chemistry | Protein Interaction Domains and Motifs - physiology | Phosphoprotein Phosphatases - metabolism | Recombinant Fusion Proteins - metabolism | DNA-Binding Proteins - metabolism | Cullin Proteins - metabolism | Nuclear Proteins - genetics | Peptide Fragments - metabolism | Repressor Proteins - chemistry | Nuclear Proteins - metabolism | Drosophila Proteins - chemistry | Transcription Factors - genetics | DNA-Binding Proteins - genetics | Cullin Proteins - genetics | Transcription Factors - metabolism | Animals | Histones - genetics | Adaptor Proteins, Signal Transducing - genetics | Drosophila Proteins - genetics | Adaptor Proteins, Signal Transducing - metabolism | Ubiquitin | Chromatin | Phosphatases | Ligases | CHROMATIN | BASIC BIOLOGICAL SCIENCES | SUBSTRATES | FLEXIBILITY | GENERAL AND MISCELLANEOUS//MATHEMATICS, COMPUTING, AND INFORMATION SCIENCE | LIGASES | DIMERIZATION | DIMERS | PHOSPHATASES
Journal Article
PLoS ONE, ISSN 1932-6203, 09/2009, Volume 4, Issue 9, pp. e7052 - e7052
Neurodegenerative disorders share common features comprising aggregation of misfolded proteins, failure of the ubiquitin-proteasome system, and increased... 
BIOLOGY | Protein Structure, Tertiary | Protein Structure, Secondary | Microscopy, Electron, Transmission - methods | Solvents - chemistry | Humans | Molecular Conformation | Chelating Agents - chemistry | Ubiquitin - chemistry | Ubiquitin - metabolism | Spectroscopy, Fourier Transform Infrared | Copper - chemistry | Alzheimer Disease - metabolism | Copper - metabolism | Microscopy, Atomic Force | Protein Binding | Cell Membrane - metabolism | Proteasome Endopeptidase Complex - metabolism | Electrochemistry - methods | Oligomers | Ubiquitin | Development and progression | Nervous system diseases | Analysis | Electric properties | Brain | Atomic force microscopy | Parkinson's disease | Aluminum | Disorders | Conglomerates | Risk factors | Proteins | Ring structures | Particle physics | Dichroism | Chelation | Copper | Alzheimer's disease | Movement disorders | Cadmium | Dielectric constant | Trifluoroethanol | Neurodegenerative diseases | Infrared spectra | Electron microscopy | Fatty acids | Substrates | Circular dichroism | Studies | Aggregates | Proteasomes | Dismantling | Parkinsons disease | Chain branching | Lipids | Agglomeration | Infrared analysis | Protein folding | Spectrum analysis | Amyloid | Incubation | Gel electrophoresis | Health risks | Particulates | Amyotrophic lateral sclerosis | Clustering | Phosphocholine | Zinc | Coalescing | Transmission electron microscopy | N-Terminus | Nickel | Dimers | Liposomes | Alzheimers disease | Coalescence | Index Medicus
Journal Article
Journal Article