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1. Full Text Advances in copper complexes as anticancer agents
by Santini, Carlo and Pellei, Maura and Gandin, Valentina and Porchia, Marina and Tisato, Francesco and Marzano, Cristina
Chemical Reviews, ISSN 0009-2665, 01/2014, Volume 114, Issue 1, pp. 815 - 862
APOPTOSIS-INDUCING ACTIVITIES | MIXED-LIGAND COMPLEXES | METAL ION COMPLEXES | TOPOISOMERASE-II-ALPHA | EHRLICH ASCITES-CARCINOMA | DNA-BINDING PROPERTIES | CELL-CYCLE ARREST | SELECTIVE ANTITUMOR-ACTIVITY | IN-VITRO CYTOTOXICITY | PHOSPHATASE-LIKE ACTIVITY | CHEMISTRY, MULTIDISCIPLINARY | Neoplasms - metabolism | Quinones - chemistry | Proteasome Endopeptidase Complex - chemistry | Coordination Complexes - metabolism | Antineoplastic Agents - therapeutic use | DNA Topoisomerases - metabolism | DNA Topoisomerases - chemistry | Antineoplastic Agents - chemistry | Coordination Complexes - chemistry | Neoplasms - drug therapy | Antineoplastic Agents - metabolism | Coordination Complexes - therapeutic use | Pyrazoles - chemistry | Animals | Copper - chemistry | Carboxylic Acids - chemistry | Schiff Bases - chemistry | Sulfhydryl Compounds - chemistry | Proteasome Endopeptidase Complex - metabolism | Neoplasms - pathology | Indoles - chemistry | Antimitotic agents | Copper compounds | Research | Chemical properties | Antineoplastic agents | Health aspects | Schiff bases | Copper
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2. Full Text MotionCor2: Anisotropic correction of beam-induced motion for improved cryo-electron microscopy
by Zheng, Shawn Q and Palovcak, Eugene and Armache, Jean-Paul and Verba, Kliment A and Cheng, Yifan and Agard, David A
Nature Methods, ISSN 1548-7091, 2017, Volume 14, Issue 4, pp. 331 - 332
CRYO-EM | BIOCHEMICAL RESEARCH METHODS | Motion | Algorithms | Macromolecular Substances - chemistry | Archaeal Proteins - chemistry | Imaging, Three-Dimensional - methods | Models, Molecular | Proteasome Endopeptidase Complex - chemistry | TRPV Cation Channels - chemistry | Cryoelectron Microscopy - methods | Electron microscopy
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3. Full Text Complete subunit architecture of the proteasome regulatory particle
by Lander, Gabriel C and Estrin, Eric and Matyskiela, Mary E and Bashore, Charlene and Nogales, Eva and Martin, Andreas
Nature, ISSN 0028-0836, 02/2012, Volume 482, Issue 7384, pp. 186 - 191
The proteasome is the major ATP-dependent protease in eukaryotic cells, but limited structural information restricts a mechanistic understanding of its... 
TRANSLOCATION | UBIQUITIN CHAINS | MULTIDISCIPLINARY SCIENCES | ELECTRON-MICROSCOPY | DEGRADATION | 26S PROTEASOME | NEW-GENERATION | PROTEINS | SACCHAROMYCES-CEREVISIAE | CORE PARTICLE | ATPASES | Recombinant Proteins - metabolism | Endopeptidases - metabolism | Saccharomyces cerevisiae - genetics | Ubiquitin - metabolism | Adenosine Triphosphatases - metabolism | Models, Molecular | Proteasome Endopeptidase Complex - chemistry | Recombinant Proteins - chemistry | Holoenzymes - chemistry | Recombinant Proteins - genetics | Protein Subunits - metabolism | Proteasome Endopeptidase Complex - genetics | Holoenzymes - metabolism | Adenosine Triphosphate - metabolism | Escherichia coli - metabolism | Saccharomyces cerevisiae Proteins - metabolism | Protein Binding | Saccharomyces cerevisiae - enzymology | Protein Conformation | Holoenzymes - genetics | Protein Subunits - chemistry | Proteasome Endopeptidase Complex - metabolism | Binding Sites | Protein Subunits - genetics | Physiological aspects | Eukaryotes | Research | Ubiquitin-proteasome system | Proteases | Adenosine triphosphatase | Proteins | Atoms & subatomic particles | Yeast | E coli | Cell cycle
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4. Full Text Rpn1 provides adjacent receptor sites for substrate binding and deubiquitination by the proteasome
by Shi, Yuan and Chen, Xiang and Elsasser, Suzanne and Stocks, Bradley B and Tian, Geng and Lee, Byung-Hoon and Shi, Yanhong and Zhang, Naixia and De Poot, Stefanie A. H and Tuebing, Fabian and Sun, Shuangwu and Vannoy, Jacob and Tarasov, Sergey G and Engen, John R and Finley, Daniel and Walters, Kylie J
Science, ISSN 0036-8075, 02/2016, Volume 351, Issue 6275, pp. aad9421 - aad9421
Hundreds of pathways for degradation converge at ubiquitin recognition by a proteasome. Here, we found that the five known proteasomal ubiquitin receptors in... 
EXCHANGE MASS-SPECTROMETRY | MULTIUBIQUITIN-CHAIN-BINDING | H/D EXCHANGE | MULTIDISCIPLINARY SCIENCES | CYCLIN B1 | DEGRADATION | UBIQUITIN RECEPTORS | 26S PROTEASOME | SACCHAROMYCES-CEREVISIAE | PROTEIN DDI1 | SUBUNIT | Endopeptidases - metabolism | Models, Molecular | Proteasome Endopeptidase Complex - chemistry | Saccharomyces cerevisiae Proteins - genetics | DNA-Binding Proteins - metabolism | Proteasome Endopeptidase Complex - genetics | Saccharomyces cerevisiae - metabolism | Ubiquitination | Metabolic Networks and Pathways | Saccharomyces cerevisiae Proteins - metabolism | Mutation | Proteasome Endopeptidase Complex - metabolism | Ubiquitin-Specific Proteases - metabolism | Saccharomyces cerevisiae Proteins - chemistry | Neurons | Proteases | Binding sites | Substrates
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5. Full Text The Logic of the 26S Proteasome
by Collins, Galen Andrew and Goldberg, Alfred L
Cell, ISSN 0092-8674, 05/2017, Volume 169, Issue 5, pp. 792 - 806
The ubiquitin proteasome pathway is responsible for most of the protein degradation in mammalian cells. Rates of degradation by this pathway have generally... 
ubiquitin proteasome system | protein turnover | protein degradation | proteasome phosphorylation | DEUBIQUITINATING ENZYME | REGULATORY PARTICLE | EUKARYOTIC PROTEASOME | 20 S PROTEASOMES | PROTEIN-DEGRADATION | BIOCHEMISTRY & MOLECULAR BIOLOGY | MOLECULAR-WEIGHT PROTEASES | MEDIATED DEGRADATION | MISFOLDED PROTEINS | FUNCTIONAL ASYMMETRIES | BRANCHED UBIQUITIN CHAINS | CELL BIOLOGY | Phosphorylation | Ubiquitination | Animals | Proteolysis | Allosteric Regulation | Humans | Eukaryota - chemistry | Adenosine Triphosphatases - metabolism | Proteasome Endopeptidase Complex - chemistry | Proteasome Endopeptidase Complex - metabolism | Eukaryota - metabolism | Ubiquitin | Cells
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6. Full Text Structure of the human 26S proteasome at a resolution of 3.9 Å
by Andreas Schweitzer and Antje Aufderheide and Till Rudack and Florian Beck and Günter Pfeifer and Jürgen M. Plitzko and Eri Sakata and Klaus Schulten and Friedrich Förster and Wolfgang Baumeister
Proceedings of the National Academy of Sciences of the United States of America, ISSN 0027-8424, 7/2016, Volume 113, Issue 28, pp. 7816 - 7821
Protein degradation in eukaryotic cells is performed by the Ubiquitin-Proteasome System (UPS). The 26S proteasome holocomplex consists of a core particle (CP)... 
AAA-ATPase | Proteostasis | Cryo-electron microscopy | Integrative modeling | Microscopy, Electron, Transmission | Yeasts | Proteasome Endopeptidase Complex - isolation & purification | Humans | Models, Molecular | Proteasome Endopeptidase Complex - chemistry | Protein Conformation | Proteasome Endopeptidase Complex - metabolism | Proteins | Physiological aspects | Ubiquitin-proteasome system | Structure | Observations | integrative modeling | Biological Sciences | proteostasis | cryo-electron microscopy
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7. Full Text Conformational switching of the 26S proteasome enables substrate degradation
by Matyskiela, Mary E and Lander, Gabriel C and Martin, Andreas
Nature Structural and Molecular Biology, ISSN 1545-9993, 07/2013, Volume 20, Issue 7, pp. 781 - 788
The 26S proteasome is the major eukaryotic ATP-dependent protease, responsible for regulating the proteome through degradation of ubiquitin-tagged substrates.... 
REGULATORY PARTICLE | TRANSLOCATION | RECOGNITION | MECHANISM | BIOCHEMISTRY & MOLECULAR BIOLOGY | ATPASES | CELL BIOLOGY | BIOPHYSICS | STRUCTURAL BASIS | MOLECULAR ARCHITECTURE | NEW-GENERATION | DEUBIQUITINATION | SUBUNIT | Protein Structure, Tertiary | Saccharomyces cerevisiae Proteins - ultrastructure | Endopeptidases - metabolism | Catalytic Domain | Mutagenesis, Site-Directed | Saccharomyces cerevisiae - genetics | Models, Molecular | Proteasome Endopeptidase Complex - chemistry | Substrate Specificity | Structure-Activity Relationship | Saccharomyces cerevisiae Proteins - genetics | Cryoelectron Microscopy | Proteasome Endopeptidase Complex - genetics | Proteasome Endopeptidase Complex - ultrastructure | Proteolysis | Adenosine Triphosphate - metabolism | Saccharomyces cerevisiae Proteins - metabolism | Protein Binding | Saccharomyces cerevisiae - enzymology | Protein Conformation | Proteasome Endopeptidase Complex - metabolism | Ubiquitinated Proteins - metabolism | Saccharomyces cerevisiae Proteins - chemistry | Hydrolysis | Proteases | Physiological aspects | Genetic aspects | Research | Structure | Ubiquitin-proteasome system | Protease inhibitors | Mutagenesis | Molecular biology | Proteomics | 26S proteasome | 19S regulatory particle | Rpn11 | UPS | deubiquitination | AAA+ ATPase | cryo-EM | protein translocation
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8. Full Text The ubiquitin-26S proteasome system at the nexus of plant biology
by Vierstra, Richard D
Nature Reviews Molecular Cell Biology, ISSN 1471-0072, 06/2009, Volume 10, Issue 6, pp. 385 - 397
Plants, like other eukaryotes, rely on proteolysis to control the abundance of key regulatory proteins and enzymes. Strikingly, genome-wide studies have... 
SELF-INCOMPATIBILITY | ARABIDOPSIS-THALIANA | RAPID DEGRADATION | COP9 SIGNALOSOME | F-BOX PROTEINS | GENE FAMILY | 26S PROTEASOME | GIBBERELLIN RECEPTOR | AUXIN RECEPTOR | ETHYLENE BIOSYNTHESIS | CELL BIOLOGY | Chromatin - metabolism | Indoleacetic Acids - metabolism | Arabidopsis - growth & development | Ubiquitin - chemistry | Ubiquitin - metabolism | Models, Molecular | Proteasome Endopeptidase Complex - chemistry | Photoperiod | Ubiquitin - genetics | Phylogeny | Proteome - analysis | Arabidopsis - metabolism | Ethylenes - metabolism | Morphogenesis | Proteasome Endopeptidase Complex - genetics | Plant Proteins - genetics | Plant Proteins - classification | Plant Proteins - chemistry | Arabidopsis - parasitology | Protein Conformation | Signal Transduction - physiology | Plant Proteins - metabolism | Proteasome Endopeptidase Complex - metabolism | Plant Growth Regulators - metabolism | Arabidopsis thaliana | Physiological aspects | Genetic aspects | Research | Ubiquitin-proteasome system | Proteolysis
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9. Full Text Atypical ubiquitylation-the unexplored world of polyubiquitin beyond Lys48 and Lys63 linkages
by Kulathu, Yogesh and Komander, David
Nature Reviews Molecular Cell Biology, ISSN 1471-0072, 08/2012, Volume 13, Issue 8, pp. 508 - 523
Ubiquitylation is one of the most abundant and versatile post-translational modifications (PTMs) in cells. Its versatility arises from the ability of ubiquitin... 
UBIQUITIN-CONJUGATING ENZYME | K11-LINKED POLYUBIQUITINATION | ESSENTIAL MODULATOR NEMO | MULTIUBIQUITIN CHAIN | STRUCTURAL BASIS | SITE-SPECIFIC UBIQUITINATION | CRYSTAL-STRUCTURE | LINEAR UBIQUITINATION | CHEMICAL-SYNTHESIS | TNF-ALPHA | CELL BIOLOGY | Polyubiquitin - metabolism | Signal Transduction | Humans | Ubiquitin-Protein Ligases - metabolism | Proteasome Endopeptidase Complex - chemistry | NF-kappa B - metabolism | Ubiquitin-Protein Ligases - chemistry | Hydrolysis | Ubiquitination | Proteolysis | Cell Cycle - physiology | Lysine - metabolism | Proteasome Endopeptidase Complex - metabolism | Lysine - chemistry | Polyubiquitin - chemistry | Ubiquitin | Post-translational modification | Research | Properties | Cell cycle
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