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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
Physical Sciences | Chemistry | Chemistry, Multidisciplinary | Science & Technology | 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 | Biochemistry | Pharmacology | Cancer therapies | Index Medicus
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2. Full Text Conformational switching of the 26S proteasome enables substrate degradation
by Matyskiela, Mary E and Lander, Gabriel C and Martin, Andreas
Nature structural & molecular biology, ISSN 1545-9993, 07/2013, Volume 20, Issue 7, pp. 781 - 788
Biochemistry & Molecular Biology | Biophysics | Life Sciences & Biomedicine | Science & Technology | Cell Biology | 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 | Index Medicus | 26S proteasome | 19S regulatory particle | Rpn11 | UPS | deubiquitination | AAA+ ATPase | cryo-EM | protein translocation
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3. Full Text An AAA Motor-Driven Mechanical Switch in Rpn11 Controls Deubiquitination at the 26S Proteasome
by Worden, Evan J and Dong, Ken C and Martin, Andreas
Molecular cell, ISSN 1097-2765, 09/2017, Volume 67, Issue 5, pp. 799 - 811.e8
DUB | 26S proteasome | energy-dependent protein degradation | mechanochemical coupling | Rpn11 | deubiquitination | ubiquitin | AAA ATPase | Biochemistry & Molecular Biology | Life Sciences & Biomedicine | Science & Technology | Cell Biology | Endopeptidases - metabolism | Protein Unfolding | Saccharomyces cerevisiae - genetics | Ubiquitin - chemistry | Ubiquitin - metabolism | Models, Molecular | Proteasome Endopeptidase Complex - chemistry | Crystallography, X-Ray | Structure-Activity Relationship | Saccharomyces cerevisiae Proteins - genetics | Proteasome Endopeptidase Complex - genetics | Endopeptidases - chemistry | Ubiquitination | Endopeptidases - genetics | Proteolysis | Saccharomyces cerevisiae Proteins - metabolism | Protein Binding | Saccharomyces cerevisiae - enzymology | Protein Conformation | Mutation | Proteasome Endopeptidase Complex - metabolism | Binding Sites | Saccharomyces cerevisiae Proteins - chemistry | Ubiquitin | Adenosine triphosphatase | Cells | Index Medicus
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4. Full Text Evidence for the existence in Arabidopsis thaliana of the proteasome proteolytic pathway: Activation in response to cadmium
by Polge, Cécile and Jaquinod, Michel and Holzer, Frances and Bourguignon, Jacques and Walling, Linda and Brouquisse, Renaud
The Journal of biological chemistry, ISSN 0021-9258, 12/2009, Volume 284, Issue 51, pp. 35412 - 35424
Life Sciences & Biomedicine | Biochemistry & Molecular Biology | Science & Technology | Gene Expression Regulation, Enzymologic - drug effects | Arabidopsis - enzymology | Serine Endopeptidases - biosynthesis | Muramidase - chemistry | Cadmium - pharmacology | Proteasome Endopeptidase Complex - chemistry | Serine Endopeptidases - chemistry | Dipeptidyl-Peptidases and Tripeptidyl-Peptidases - chemistry | Enzyme Activation - drug effects | Proteasome Endopeptidase Complex - biosynthesis | Up-Regulation - drug effects | Gene Expression Regulation, Plant - drug effects | Animals | Arabidopsis Proteins - chemistry | Cattle | Arabidopsis Proteins - biosynthesis | Aminopeptidases - chemistry | Serum Albumin, Bovine - chemistry | Stress, Physiological - drug effects | Plant Leaves - enzymology | Aminopeptidases - biosynthesis | Dipeptidyl-Peptidases and Tripeptidyl-Peptidases - biosynthesis | Index Medicus | Up-Regulation | Cadmium | Arabidopsis | Aminopeptidases | Plant Leaves | Biochemistry, Molecular Biology | Stress, Physiological | Proteasome Endopeptidase Complex | Dipeptidyl-Peptidases and Tripeptidyl-Peptidases | Gene Expression Regulation, Enzymologic | Life Sciences | Arabidopsis Proteins | Muramidase | Serum Albumin, Bovine | Gene Expression Regulation, Plant | Serine Endopeptidases | Enzyme Activation | Protein Synthesis, Post-Translational Modification, and Degradation
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5. Full Text Molecular Machines for Protein Degradation
by Groll, Michael and Bochtler, Matthias and Brandstetter, Hans and Clausen, Tim and Huber, Robert
Chembiochem : a European journal of chemical biology, ISSN 1439-4227, 02/2005, Volume 6, Issue 2, pp. 222 - 256
protein structures | molecular machines | structure–activity relationships | protein degradation | proteasomes | Molecular machines | Proteasomes | Protein degradation | Structure-acticity relationships | Protein structures | Pharmacology & Pharmacy | Biochemistry & Molecular Biology | Life Sciences & Biomedicine | Chemistry, Medicinal | Science & Technology | ATP-Dependent Proteases - genetics | Dipeptidyl Peptidase 4 - metabolism | Molecular Chaperones - metabolism | Allosteric Regulation | Dipeptidyl Peptidase 4 - chemistry | Multiprotein Complexes | Bacterial Proteins - chemistry | Molecular Sequence Data | Substrate Specificity | Molecular Chaperones - chemistry | Protein Subunits - metabolism | Heat-Shock Proteins - genetics | Endopeptidases - chemistry | ATP-Dependent Proteases - chemistry | Periplasmic Proteins - genetics | Serine Endopeptidases - genetics | Molecular Structure | Binding Sites | Protein Subunits - genetics | Amino Acid Sequence | Endopeptidases - metabolism | Periplasmic Proteins - chemistry | Heat-Shock Proteins - metabolism | Bacterial Proteins - genetics | Molecular Chaperones - genetics | Models, Molecular | Proteasome Endopeptidase Complex - chemistry | Dipeptidyl Peptidase 4 - genetics | Serine Endopeptidases - chemistry | Proteasome Endopeptidase Complex - genetics | Sequence Alignment | Endopeptidases - genetics | Bacterial Proteins - metabolism | Protein Conformation | Periplasmic Proteins - metabolism | Protein Subunits - chemistry | Serine Endopeptidases - metabolism | Proteasome Endopeptidase Complex - metabolism | Proteasome Inhibitors | ATP-Dependent Proteases - metabolism | Heat-Shock Proteins - chemistry | Index Medicus
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