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PloS one, ISSN 1932-6203, 2011, Volume 6, Issue 7, pp. e22336 - e22336
Journal Article
Journal Article
Journal Article
The Journal of cell biology, ISSN 1540-8140, 12/2010, Volume 191, Issue 7, pp. 1367 - 1380
Damage to mitochondria can lead to the depolarization of the inner mitochondrial membrane, thereby sensitizing impaired mitochondria for selective elimination... 
Depolarization | Mitochondria | Drosophila | Ubiquitins | Cell lines | HeLa cells | Antibodies | Parkinson disease | Opal | Standard deviation | Life Sciences & Biomedicine | Science & Technology | Cell Biology | RNA, Small Interfering - genetics | Protein Kinases - genetics | Microtubule-Associated Proteins - genetics | Humans | Autophagy - physiology | Mitochondrial Proteins - genetics | Membrane Potential, Mitochondrial - drug effects | Autophagy - drug effects | Mitochondrial Membrane Transport Proteins | Mitochondrial Proteins - metabolism | Carbonyl Cyanide m-Chlorophenyl Hydrazone - pharmacology | Membrane Transport Proteins - metabolism | Membrane Proteins - metabolism | Ubiquitination - physiology | Nuclear Proteins - genetics | Membrane Fusion - drug effects | Fibroblasts - metabolism | Membrane Proteins - genetics | HCT116 Cells | Ubiquitin-Protein Ligases - metabolism | Adenosine Triphosphatases - metabolism | Dynamins | Nuclear Proteins - metabolism | Mitochondria - drug effects | Mice, Knockout | Leupeptins - pharmacology | Animals | GTP Phosphohydrolases - metabolism | GTP Phosphohydrolases - genetics | Models, Biological | Ubiquitin-Conjugating Enzymes - metabolism | Fibroblasts - drug effects | Cell Line, Tumor | Adenosine Triphosphatases - genetics | Mice | HeLa Cells | Proteasome Endopeptidase Complex - metabolism | Membrane Fusion - physiology | Mitochondria - physiology | Proteasome Inhibitors | Ubiquitin-Protein Ligases - genetics | Protein Binding - physiology | Proteins | Ligases | Research | Properties | Ubiquitin-proteasome system | Guanosine triphosphatase | Adenosine triphosphatase | Membranes | Proteases | Index Medicus
Journal Article
Proceedings of the National Academy of Sciences - PNAS, ISSN 1091-6490, 09/2011, Volume 108, Issue 38, pp. 15798 - 15803
Protein release factor 3 (RF3), a guanosine triphosphatase, binds to ribosome after release of the nascent peptide and promotes dissociation of the class I release factors during the termination of protein synthesis... 
Messenger RNA | RNA | Ribosomes | Rotational states | Recycling | Hybridity | Rotation | Crystallography | Transfer RNA | Crystal structure | Ribosome structure | X-ray crystallography | Translation | Science & Technology - Other Topics | Multidisciplinary Sciences | Science & Technology | Protein Biosynthesis | Ribosomes - metabolism | Crystallography, X-Ray | Guanosine Triphosphate - metabolism | RNA, Messenger - metabolism | GTP Phosphohydrolases - chemistry | Base Sequence | Guanosine Triphosphate - chemistry | Nucleic Acid Conformation | RNA, Transfer - chemistry | Protein Structure, Tertiary | Peptide Termination Factors - genetics | RNA, Transfer - metabolism | Electrophoresis, Polyacrylamide Gel | Crystallization | Guanosine Triphosphate - analogs & derivatives | Ribosomes - chemistry | Models, Molecular | Escherichia coli Proteins - metabolism | Peptide Termination Factors - metabolism | GTP Phosphohydrolases - metabolism | GTP Phosphohydrolases - genetics | Escherichia coli Proteins - genetics | Protein Binding | RNA, Messenger - chemistry | Peptide Termination Factors - chemistry | Escherichia coli Proteins - chemistry | Physiological aspects | Protein biosynthesis | Research | Structure | Crystals | Peptides | Kinases | Protein synthesis | Index Medicus | GTP | Hybrids | Triphosphatase | Guanosine | release factor 3 | translation | Biological Sciences | ribosome structure
Journal Article
Nature (London), ISSN 1476-4687, 11/2011, Volume 480, Issue 7377, pp. 379 - 382
Journal Article