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by Zhang, Bing and Zhang, Bing and Wang, Jing and Wang, Jing and Wang, Xiaojing and Wang, Xiaojing and Zhu, Jing and Zhu, Jing and Liu, Q and Liu, Qi and Shi, Zhiao and Shi, Zhiao and Chambers, Matthew C and Chambers, Matthew C and Zimmerman, Lisa J and Zimmerman, Lisa J and Shaddox, Kent F and Shaddox, Kent F and Kim, Sangtae and Kim, Sangtae and Davies, Sherri R and Davies, Sherri R and Wang, Sean and Wang, Sean and Wang, Pei and Wang, Pei and Kinsinger, Christopher R and Kinsinger, Christopher R and Rivers, Robert C and Rivers, Robert C and Rodriguez, Henry and Rodriguez, Henry and Townsend, R. Reid and Townsend, R Reid and Ellis, Matthew J. C and Ellis, Matthew J C and Carr, Steven A and Carr, Steven A and Tabb, David L and Tabb, David L and Coffey, Robert J and Coffey, Robert J and Slebos, Robbert J C and Slebos, Robbert J. C and Liebler, Daniel C and Liebler, Daniel C and NCI CPTAC, CPTAC and Gillette, Michael A and Klauser, Karl R and Kuhn, Eric and Mani, D.R and Mertins, Philipp and Ketchum, Karen A and Paulovich, Amanda G and Whiteaker, Jeffrey R and Edwards, Nathan J and McGarvey, Peter B and Madhavan, Subha and Chan, Daniel and Pandey, Akhilesh and Shih, Ie-Ming and Zhang, Hui and Zhang, Zhen and Zhu, Heng and Whiteley, Gordon A and Skates, Steven J and White, Forest M and Levine, Douglas A and Boja, Emily S and Hiltke, Tara and Mesri, Mehdi and Shaw, Kenna M and Stein, Stephen E and Fenyo, David and Liu, Tao and McDermott, Jason E and Payne, Samuel H and Rodland, Karin D and Smith, Richard D and Rudnick, Paul and Snyder, Michael and Zhao, Yingming and Chen, Xian and Ransohoff, David F and Hoofnagle, Andrew N and Sanders, Melinda E and Wang, Yue and Ding, Li and NCI CPTAC and the NCI CPTAC
Nature, ISSN 0028-0836, 2014, Volume 513, Issue 7518, pp. 382 - 387
Journal Article
Neuron, ISSN 0896-6273, 08/2012, Volume 75, Issue 4, pp. 618 - 632
Mitochondrial abnormalities have been documented in Alzheimer’s disease and related neurodegenerative disorders, but the causal relationship between... 
ALZHEIMERS-DISEASE BRAIN | DOMINANT OPTIC ATROPHY | MITOCHONDRIAL-FUNCTION | MOUSE MODEL | LIGHT-CHAIN | FRONTOTEMPORAL DEMENTIA | AXONAL-TRANSPORT | NEUROSCIENCES | DYNAMIN-RELATED PROTEIN | PHOSPHORYLATION SITES | TRANSGENIC MICE | Neurons - pathology | Microtubule-Associated Proteins - genetics | Tauopathies - genetics | Cytoskeletal Proteins - genetics | Gelsolin - metabolism | Microtubule-Associated Proteins - metabolism | Humans | Actins - metabolism | Tauopathies - pathology | Cytoplasm - metabolism | MicroRNAs - metabolism | Green Fluorescent Proteins - genetics | Mitochondrial Proteins - genetics | Drosophila Proteins - metabolism | GTP-Binding Proteins - genetics | Nerve Degeneration - metabolism | Neurons - ultrastructure | tau Proteins - genetics | Cell Death - genetics | Mitochondria - genetics | Mitochondrial Proteins - metabolism | ATP Synthetase Complexes - metabolism | Cell Cycle Proteins - genetics | Tauopathies - complications | Cytoskeletal Proteins - metabolism | Myosins - metabolism | Cytoplasm - genetics | RNA Interference - physiology | Disease Models, Animal | In Situ Nick-End Labeling | Green Fluorescent Proteins - metabolism | Animals, Genetically Modified | Gene Expression Regulation - genetics | Drosophila | Cell Cycle Proteins - metabolism | Mitochondria - metabolism | Mitochondria - pathology | Mutation - genetics | Animals | GTP Phosphohydrolases - metabolism | Analysis of Variance | GTP Phosphohydrolases - genetics | Gelsolin - genetics | Mice | Drosophila Proteins - genetics | Nerve Degeneration - etiology | Voltage-Dependent Anion Channels - metabolism | GTP-Binding Proteins - metabolism | Nervous system diseases | Actin | Neurons | Utrophin | Myosin | Mitochondrial DNA | Alzheimer's disease | Proteins | Phosphorylation | Mitochondria | Neurotoxicity | Insects | Microscopy | Neurodegeneration | Pathogenesis | Morphology | Mutation | Defects | Index Medicus | Neurodegenerative diseases | Tau protein | Cell death | Elongation
Journal Article
Neuron, ISSN 0896-6273, 04/2013, Volume 78, Issue 1, pp. 65 - 80
Mutations in VCP cause multisystem degeneration impacting the nervous system, muscle, and/or bone. Patients may present with ALS, Parkinsonism, frontotemporal... 
PATHOGENESIS | PARKIN | VALOSIN-CONTAINING-PROTEIN | INCLUSION-BODY MYOPATHY | DROSOPHILA MODEL | FRONTOTEMPORAL DEMENTIA | PAGETS-DISEASE | BONE | NEUROSCIENCES | P97 | DEGENERATION | Embryo, Mammalian | Humans | Ganglia, Spinal - cytology | Drosophila Proteins - metabolism | HSP72 Heat-Shock Proteins - genetics | Protein Tyrosine Phosphatases - genetics | Neurons - ultrastructure | Time Factors | Carbonyl Cyanide m-Chlorophenyl Hydrazone - pharmacology | Neuromuscular Junction - genetics | Neurons - metabolism | Protein-Serine-Threonine Kinases - metabolism | Mitochondrial Membrane Transport Proteins - metabolism | Cell Cycle Proteins - metabolism | Enzyme Inhibitors - pharmacology | Ubiquitin-Protein Ligases - metabolism | Adenosine Triphosphatases - metabolism | Mutation - genetics | Leupeptins - pharmacology | GTP Phosphohydrolases - metabolism | Luminescent Proteins - genetics | Adenosine Triphosphatases - genetics | Ubiquitin-Protein Ligases - genetics | RNA, Small Interfering - metabolism | Immunoprecipitation | Neuromuscular Junction - metabolism | Valosin Containing Protein | Mitochondria - ultrastructure | Transfection | Mitochondria - genetics | Proton Ionophores - pharmacology | Cell Cycle Proteins - genetics | Microscopy, Electron, Transmission | Animals, Genetically Modified | Gene Expression Regulation - genetics | Drosophila | RNA, Small Interfering - pharmacology | Cells, Cultured | Protein-Serine-Threonine Kinases - genetics | Nuclear Proteins - metabolism | Mitochondria - metabolism | Mitochondria - drug effects | Transcription Factors - genetics | Transcription Factors - metabolism | Animals | Proteins - metabolism | Drosophila Proteins - genetics | In Vitro Techniques | Ubiquitination - genetics | Luminescent Proteins - metabolism | Ubiquitin | Analysis | Genomics | Quality control | Amyotrophic lateral sclerosis | Genetic aspects | Mitochondrial DNA | Dementia | Neurons | Parkinsons disease | Biosynthesis | Digital cameras | Kinases | DNA repair | Proteins | Mitochondria | Brain research | Insects | Microscopy | Morphology | Mutation | Index Medicus
Journal Article
PLoS Genetics, ISSN 1553-7390, 01/2012, Volume 8, Issue 1, pp. e1002456 - e1002456
Pink1 is a mitochondrial kinase involved in Parkinson's disease, and loss of Pink1 function affects mitochondrial morphology via a pathway involving Parkin and... 
LIFE-SPAN | OXIDATIVE STRESS | DROSOPHILA-PARKIN MUTANTS | ALTERNATIVE OXIDASE | QUINONE OXIDOREDUCTASE | NDI1 GENE | HUMAN-CELLS | INCREASED SENSITIVITY | GENETICS & HEREDITY | MITOCHONDRIAL-DYSFUNCTION | RESERVE POOL | Electron Transport Complex III - genetics | Electron Transport Complex III - metabolism | Cytoskeletal Proteins - genetics | Saccharomyces cerevisiae - genetics | Humans | Male | Drosophila Proteins - metabolism | Ciona intestinalis - genetics | Drosophila melanogaster - genetics | Electron Transport Complex I - metabolism | GTP-Binding Proteins - genetics | Electron Transport Complex IV - metabolism | Drosophila melanogaster - metabolism | Mitochondria - genetics | Electron Transport Complex I - genetics | Mitochondrial Proteins - metabolism | Cytoskeletal Proteins - metabolism | Membrane Proteins - metabolism | Plant Proteins - metabolism | Protein-Serine-Threonine Kinases - metabolism | Oxidoreductases - metabolism | Membrane Proteins - genetics | Gene Expression Regulation | Protein-Serine-Threonine Kinases - genetics | Ubiquitin-Protein Ligases - metabolism | Mitochondria - metabolism | Electron Transport Complex IV - genetics | Parkinson Disease - genetics | Saccharomyces cerevisiae Proteins - genetics | Animals, Genetically Modified - metabolism | Animals | Animals, Genetically Modified - genetics | Saccharomyces cerevisiae Proteins - metabolism | Drosophila Proteins - genetics | Mutation | Ubiquitin-Protein Ligases - genetics | GTP-Binding Proteins - metabolism | Parkinson's disease | Physiological aspects | NADH dehydrogenase | Genetic aspects | Mitochondrial DNA | Research | Electron transport | Risk factors | Enzymes | Mitochondria | Yeast | Insects | Parkinsons disease | Genetic engineering | Grants | Experiments | Evacuations & rescues | Deoxyribonucleic acid--DNA | Defects | Index Medicus | Deoxyribonucleic acid | DNA
Journal Article
Science, ISSN 0036-8075, 12/2010, Volume 330, Issue 6012, pp. 1820 - 1824
How can species remain unaltered for long periods yet also undergo rapid diversification? By linking genetic variation to phenotypic variation via... 
Quantitative trait loci | Oxidative stress | Phenotypes | Genetic variation | Capacitors | REPORTS | Evolutionary genetics | Evolution | Genomes | Genotypes | Phenotypic traits | MORPHOLOGICAL EVOLUTION | YEAST | PHENOTYPIC VARIATION | PROTEIN | MULTIDISCIPLINARY SCIENCES | CAPACITOR | DRUG-RESISTANCE | CHAPERONE | SACCHAROMYCES-CEREVISIAE | ACTS | Adaptation, Physiological | Hydroxyurea - pharmacology | Microtubule-Associated Proteins - genetics | Microtubule-Associated Proteins - metabolism | Saccharomyces cerevisiae - genetics | Open Reading Frames | Stress, Physiological | Intracellular Signaling Peptides and Proteins - metabolism | Mitochondrial Proteins - genetics | Genetic Variation | Mitochondrial Proteins - metabolism | HSP90 Heat-Shock Proteins - genetics | Drug Resistance, Fungal | Intracellular Signaling Peptides and Proteins - genetics | Protein-Serine-Threonine Kinases - metabolism | Saccharomyces cerevisiae - physiology | Protein-Serine-Threonine Kinases - genetics | Sulfurtransferases - genetics | Saccharomyces cerevisiae Proteins - genetics | Sirolimus - pharmacology | Polymorphism, Genetic | Biological Evolution | Deoxycholic Acid - pharmacology | Saccharomyces cerevisiae Proteins - metabolism | HSP90 Heat-Shock Proteins - metabolism | Quantitative Trait Loci | Saccharomyces cerevisiae - growth & development | Sulfurtransferases - metabolism | Crosses, Genetic | Phenotype | Heat shock proteins | Genotype | Research | Properties | Genotype & phenotype | Genetic diversity | Yeast | Cellular biology | Molecular biology | Index Medicus
Journal Article
EMBO reports, ISSN 1469-221X, 01/2010, Volume 11, Issue 1, pp. 45 - 51
Autophagy is the cellular homeostatic pathway that delivers large cytosolic materials for degradation in the lysosome. Recent evidence indicates that autophagy... 
mitophagy | Nix | LC3 | GABARAP | selective autophagy | Selective autophagy | Mitophagy | APOPTOSIS | PROTEIN | RETICULOCYTE MATURATION | UBIQUITIN | BNIP3 | BIOCHEMISTRY & MOLECULAR BIOLOGY | CELL-DEATH | CELL BIOLOGY | STRUCTURAL BASIS | DEGRADATION | Microtubule-Associated Proteins - genetics | Microtubule-Associated Proteins - metabolism | Humans | Cercopithecus aethiops | Molecular Sequence Data | Substrate Specificity | Autophagy - physiology | Mitochondrial Proteins - genetics | Proto-Oncogene Proteins - chemistry | Mitochondrial Proteins - metabolism | Tumor Suppressor Proteins - chemistry | Tumor Suppressor Proteins - genetics | Membrane Proteins - metabolism | Binding Sites | Proto-Oncogene Proteins - metabolism | Amino Acid Sequence | Tumor Suppressor Proteins - metabolism | Membrane Proteins - genetics | Cells, Cultured | Ubiquitin-Protein Ligases - metabolism | Proto-Oncogene Proteins - genetics | Mitochondria - metabolism | Saccharomyces cerevisiae Proteins - genetics | Blotting, Western | Amino Acid Motifs | Autophagy-Related Protein 8 Family | Animals | Membrane Proteins - chemistry | Reticulocytes - cytology | Mitochondrial Proteins - chemistry | Saccharomyces cerevisiae Proteins - metabolism | Protein Binding | Mice | Receptors, GABA-A - metabolism | COS Cells | Proteins | Mitochondria | Cellular biology | Cytoplasm | Index Medicus | Scientific Report
Journal Article
Science, ISSN 0036-8075, 7/2012, Volume 337, Issue 6090, pp. 96 - 100
Pyruvate constitutes a critical branch point in cellular carbon metabolism. We have identified two proteins, Mpc1 and Mpc2, as essential for mitochondrial... 
Yeasts | Mitochondria | Diet | Plasmids | Drosophila | REPORTS | Amino acids | Oxidation | Respiration | Sugars | Medical schools | RAT-LIVER | TRANSPORT | COMPLEX | MECHANISM | IDENTIFICATION | MULTIDISCIPLINARY SCIENCES | Metabolomics | Humans | Molecular Sequence Data | Mitochondrial Proteins - genetics | Drosophila Proteins - metabolism | Drosophila melanogaster - genetics | Anion Transport Proteins - chemistry | Mitochondrial Membrane Transport Proteins - genetics | Drosophila melanogaster - metabolism | Saccharomyces cerevisiae - metabolism | Amino Acids - metabolism | Biological Transport | Mitochondrial Proteins - metabolism | Pyruvic Acid - metabolism | Amino Acid Sequence | Mitochondrial Membrane Transport Proteins - chemistry | Mitochondrial Membrane Transport Proteins - metabolism | Oxidation-Reduction | Carbohydrate Metabolism | Mitochondria - metabolism | Drosophila Proteins - chemistry | Saccharomyces cerevisiae Proteins - genetics | Anion Transport Proteins - metabolism | Citric Acid Cycle | Mitochondrial Membranes - metabolism | Point Mutation | Animals | Drosophila melanogaster - chemistry | Mitochondrial Proteins - chemistry | Saccharomyces cerevisiae Proteins - metabolism | Drosophila Proteins - genetics | Anion Transport Proteins - genetics | Saccharomyces cerevisiae Proteins - chemistry | Cell metabolism | Pyruvates | Chemical properties | Research | Molecular biology | Proteins | Yeast | Metabolism | Index Medicus | Carriers | Human | Bacteria | Transport | Transporter
Journal Article
The American Journal of Human Genetics, ISSN 0002-9297, 11/2011, Volume 89, Issue 5, pp. 656 - 667
Journal Article