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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
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
Journal of Biological Chemistry, ISSN 0021-9258, 10/2014, Volume 289, Issue 41, pp. 28070 - 28086
In eukaryotes, mitochondrial iron-sulfur cluster (ISC), export and cytosolic iron-sulfur cluster assembly (CIA) machineries carry out biogenesis of iron-sulfur... 
IRON-SULFUR CLUSTER | MITOCHONDRIAL-MEMBRANE PROTEIN | OXIDATIVE STRESS | AZOTOBACTER-VINELANDII (NIF)ISCA | BIOCHEMISTRY & MOLECULAR BIOLOGY | ESCHERICHIA-COLI | NITRIC-OXIDE | 2FE-2S CLUSTER | FUNCTIONAL-CHARACTERIZATION | SCAFFOLD PROTEIN | INSULIN SENSITIVITY | Humans | Homeostasis | Mitochondrial Proteins - genetics | Mitochondrial Membrane Transport Proteins - genetics | Hydrogen Peroxide - chemistry | Mitochondrial Proteins - metabolism | Mitochondrial Membranes - chemistry | Escherichia coli - metabolism | Protein Stability | Mitochondria - chemistry | Protein Structure, Tertiary | Recombinant Proteins - metabolism | Iron Regulatory Protein 1 - genetics | Mitochondrial Membrane Transport Proteins - chemistry | Mitochondrial Membrane Transport Proteins - metabolism | Nitric Oxide - chemistry | Oxidation-Reduction | Signal Transduction | Iron Regulatory Protein 1 - chemistry | Gene Expression Regulation | Recombinant Proteins - chemistry | Mice, Transgenic | Mitochondria - metabolism | Recombinant Proteins - genetics | Iron - metabolism | Protein Folding | Hep G2 Cells | Mitochondrial Membranes - metabolism | Protein Transport | Animals | Iron Regulatory Protein 1 - metabolism | Escherichia coli - genetics | Mitochondrial Proteins - chemistry | Mice | HeLa Cells | Index Medicus | Organic chemistry | Chemical Sciences | Mitochondria | Iron Metabolism | Oxidative Stress | MitoNEET | Fe-S Transfer | Small Interfering RNA (siRNA) | Iron-Sulfur Protein | Nitric Oxide | Iron Regulatory Protein 1 | Protein Degradation | Cell Biology
Journal Article
Nature Communications, ISSN 2041-1723, 12/2017, Volume 8, Issue 1, pp. 1287 - 15
Iron-sulfur (Fe/S) clusters are essential protein cofactors crucial for many cellular functions including DNA maintenance, protein translation, and energy... 
IRON-SULFUR CLUSTER | ACYL CARRIER PROTEIN | CYSTEINE DESULFURASE | FRATAXIN | ARABIDOPSIS-THALIANA | BIOGENESIS | CRYSTAL-STRUCTURE | MULTIDISCIPLINARY SCIENCES | ESCHERICHIA-COLI | X-RAY | SCAFFOLD PROTEIN | Fungal Proteins - chemistry | Humans | Protein Multimerization | Iron-Sulfur Proteins - genetics | Crystallography, X-Ray | Iron-Binding Proteins - chemistry | Mitochondrial Proteins - genetics | Iron-Sulfur Proteins - chemistry | Iron-Binding Proteins - metabolism | Multiprotein Complexes - metabolism | Carbon-Sulfur Lyases - genetics | Mitochondrial Proteins - metabolism | X-Ray Diffraction | Iron-Regulatory Proteins - chemistry | Protein Stability | Amino Acid Sequence | Chaetomium - chemistry | Mutagenesis, Site-Directed | Acyl Carrier Protein - metabolism | Models, Molecular | Scattering, Small Angle | Iron-Regulatory Proteins - metabolism | Mitochondria - metabolism | Fungal Proteins - genetics | Saccharomyces cerevisiae Proteins - genetics | Static Electricity | Carbon-Sulfur Lyases - metabolism | Chaetomium - genetics | Iron-Regulatory Proteins - genetics | Molecular Dynamics Simulation | Sequence Homology, Amino Acid | Acyl Carrier Protein - chemistry | Multiprotein Complexes - chemistry | Acyl Carrier Protein - genetics | Mitochondrial Proteins - chemistry | Saccharomyces cerevisiae Proteins - metabolism | Iron-Binding Proteins - genetics | Protein Conformation | Iron-Sulfur Proteins - metabolism | Carbon-Sulfur Lyases - chemistry | Amino Acid Substitution | Fungal Proteins - metabolism | Saccharomyces cerevisiae Proteins - chemistry | Iron | Small angle X ray scattering | Crystallography | Cofactors | Proteins | Energy balance | Mitochondria | X-ray scattering | Frataxin | Energy conversion | Acyl carrier protein | Clusters | X ray scattering | Catalysis | Ferredoxin | Sulfur | Chemical synthesis | Deoxyribonucleic acid--DNA | Crystal structure | Lipids | Index Medicus
Journal Article
Proceedings of the National Academy of Sciences of the United States of America, ISSN 0027-8424, 9/2009, Volume 106, Issue 37, pp. 15651 - 15656
Adenosine 5'-triphosphate (ATP) is the major energy currency of cells and is involved in many cellular processes. However, there is no method for real-time... 
Proteins | Pollutant emissions | Mitochondria | Ratios | HeLa cells | Fluorescence | Glycolysis | Dynamic range | Cytoplasm | Oligomycins | Fluorescent indicator | FRET | Live imaging | Oxidative phosphorylation | CANCER-CELLS | F-1-ATPASE BINDS ATP | MITOCHONDRIAL | MULTIDISCIPLINARY SCIENCES | THERMOPHILIC F-1-ATPASE | oxidative phosphorylation | live imaging | MICRODOMAINS | fluorescent indicator | ISOLATED EPSILON-SUBUNIT | CA2 | DYNAMICS | PROTEINS | Humans | Bacterial Proteins - chemistry | Fluorescent Dyes - metabolism | Green Fluorescent Proteins - genetics | Recombinant Fusion Proteins - metabolism | Cell Compartmentation | Adenosine Triphosphate - metabolism | Luminescent Proteins - chemistry | Green Fluorescent Proteins - chemistry | Fluorescent Dyes - chemistry | Green Fluorescent Proteins - metabolism | Bacterial Proton-Translocating ATPases - chemistry | Bacterial Proton-Translocating ATPases - genetics | Bacterial Proton-Translocating ATPases - metabolism | Bacterial Proteins - genetics | Oxidative Phosphorylation | Models, Molecular | Recombinant Fusion Proteins - chemistry | Recombinant Fusion Proteins - genetics | Bacterial Proteins - metabolism | Fluorescence Resonance Energy Transfer - methods | Luminescent Proteins - genetics | HeLa Cells | Microscopy, Fluorescence | Luminescent Proteins - metabolism | Physiological aspects | Research | Adenosine triphosphate | ATP synthases | Glucose | Adenosine triphosphatase | Cells | Nutrition | fluorescence resonance energy transfer | oligomycin A | ATP | Nuclei | Index Medicus | Biological Sciences
Journal Article
Science, ISSN 0036-8075, 11/2018, Volume 362, Issue 6416, pp. 829 - 834
Membrane proteins reside in lipid bilayers and are typically extracted from this environment for study, which often compromises their integrity. In this work,... 
OUTER-MEMBRANE | NMR | OXIDASE | STRUCTURAL BASIS | MULTIDISCIPLINARY SCIENCES | LIPIDS | SUBUNIT | Molecular Chaperones - metabolism | Bacterial Proteins - chemistry | Porins - metabolism | Molecular Chaperones - chemistry | Proteome - chemistry | Adenine Nucleotide Translocator 1 - chemistry | Cattle | Mass Spectrometry | Mitochondrial Membranes - chemistry | Porins - chemistry | Membrane Proteins - metabolism | SEC Translocation Channels - chemistry | SEC Translocation Channels - metabolism | Bacterial Outer Membrane Proteins - chemistry | Escherichia coli Proteins - metabolism | Adenine Nucleotide Translocator 1 - metabolism | Mitochondrial Proton-Translocating ATPases - chemistry | Mitochondrial Proton-Translocating ATPases - metabolism | Mitochondrial Membranes - metabolism | Animals | Bacterial Outer Membrane Proteins - metabolism | Membrane Proteins - chemistry | Protein Conformation, beta-Strand | Bacterial Proteins - metabolism | Lipid Bilayers - chemistry | Lipid Bilayers - metabolism | Escherichia coli Proteins - chemistry | Proteome - metabolism | Physiological aspects | Mass spectrometry | Methods | Membrane proteins | Escherichia coli | Muscle proteins | Fatty acids | Porins | Adenosine triphosphate | Adenosine triphosphatase | Stoichiometry | Membranes | Outer membranes | Lipids | Translocase | Chaperones | ADP | Lipid bilayers | Proteins | Mitochondria | E coli | Bacteria | Assemblies | Efflux | Inner membranes | Adenosine | Adenosine diphosphate | Membrane vesicles | Mass spectroscopy | Electron microscopy | Organic chemistry | Scientific imaging | Dimers | Disruption | ATP | Ejection | Index Medicus
Journal Article
Molecular Cell, ISSN 1097-2765, 10/2017, Volume 68, Issue 1, pp. 233 - 246.e5
Several ubiquitin chain types have remained unstudied, mainly because tools and techniques to detect these posttranslational modifications are scarce.... 
X-ray crystallography | mitophagy | HUWE1 | microscale thermophoresis | Mfn2 | Lys6-linked ubiquitin chains | affimer | Parkin | PARKIN | POLYUBIQUITIN | PROTEIN | RECOGNITION | PHOSPHORYLATION | BIOCHEMISTRY & MOLECULAR BIOLOGY | REPLACEMENT STRATEGY | CHAINS | DEUBIQUITINASE | LIGASE | CELL BIOLOGY | Humans | Ubiquitin - metabolism | Substrate Specificity | Crystallography, X-Ray | Mitochondrial Proteins - genetics | GTP Phosphohydrolases - chemistry | Ubiquitination | Mitochondrial Proteins - metabolism | Cloning, Molecular | Escherichia coli - metabolism | HEK293 Cells | Carrier Proteins - chemistry | Lysine - metabolism | Protein Interaction Domains and Motifs | Binding Sites | Recombinant Proteins - metabolism | Gene Expression | Protein Structure, Secondary | Signal Transduction | Ubiquitin - chemistry | Ubiquitin-Protein Ligases - metabolism | Models, Molecular | Recombinant Proteins - chemistry | Recombinant Proteins - genetics | Ubiquitin - genetics | Ubiquitin-Protein Ligases - chemistry | Amino Acid Motifs | Carrier Proteins - genetics | Molecular Probes - chemistry | Carrier Proteins - metabolism | GTP Phosphohydrolases - metabolism | Escherichia coli - genetics | GTP Phosphohydrolases - genetics | Mitochondrial Proteins - chemistry | Cell Line, Tumor | Protein Binding | Protein Processing, Post-Translational | HeLa Cells | Kinetics | Lysine - chemistry | Ubiquitin-Protein Ligases - genetics | Tumor Suppressor Proteins | Ubiquitin | Structure | Ligases | Fluorescence microscopy | Crystals | Viral antibodies | Chemical tests and reagents | Fluorescence | Antibodies | Nucleic acids | Molecular biology | Index Medicus
Journal Article
Nucleic Acids Research, ISSN 0305-1048, 2016, Volume 44, Issue 1, pp. D1251 - D1257
Journal Article
Science, ISSN 0036-8075, 2/2008, Volume 319, Issue 5867, pp. 1247 - 1250
Journal Article