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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
Proceedings of the National Academy of Sciences of the United States of America, ISSN 0027-8424, 8/2012, Volume 109, Issue 35, pp. 13961 - 13965
We report the high-resolution (1.9 Å) crystal structure of oligomycin bound to the subunit c₁₀ ring of the yeast mitochondrial ATP synthase. Oligomycin binds... 
Protons | Molecules | Yeasts | Atomic interactions | Adenosine triphosphatases | Crystals | Atoms | Genetic mutation | Oligomycins | Binding sites | Proton pore | F1Fo ATP synthase | VENTURICIDIN | RESISTANT MUTANTS | MULTIDISCIPLINARY SCIENCES | AMINO-ACID SUBSTITUTIONS | ADENOSINE-TRIPHOSPHATASE | MITOCHONDRIAL ATPASE | SACCHAROMYCES-CEREVISIAE | SUBUNIT-9 | PARTIAL RESOLUTION | proton pore | INHIBITORS | CATALYZING OXIDATIVE PHOSPHORYLATION | Mitochondria - enzymology | Humans | Crystallography, X-Ray | Vacuolar Proton-Translocating ATPases - metabolism | Proton-Translocating ATPases - metabolism | Oligomycins - pharmacology | Hydrogen Bonding - drug effects | ATP Synthetase Complexes - metabolism | Drug Design | ATP Synthetase Complexes - chemistry | Binding Sites - drug effects | Escherichia coli - enzymology | Protein Structure, Secondary | Bacterial Proton-Translocating ATPases - chemistry | Bacterial Proton-Translocating ATPases - metabolism | Escherichia coli Proteins - metabolism | Mitochondria - drug effects | Proton-Translocating ATPases - chemistry | Animals | Mycobacterium tuberculosis - enzymology | Vacuolar Proton-Translocating ATPases - chemistry | Saccharomyces cerevisiae Proteins - metabolism | Saccharomyces cerevisiae - enzymology | Anti-Bacterial Agents - pharmacology | Escherichia coli Proteins - chemistry | Saccharomyces cerevisiae Proteins - chemistry | Clinical chemistry | Antibiotics | Yeast fungi | Physiological aspects | Microbiological chemistry | Chemical properties | Research | Structure | Identification and classification | Adenosine triphosphate | Protein binding | Bacteria | Yeast | Adenosine triphosphatase | Crystal structure | Index Medicus | Biological Sciences | Physical Sciences
Journal Article
Proceedings of the National Academy of Sciences of the United States of America, ISSN 0027-8424, 12/2018, Volume 115, Issue 50, pp. E11761 - E11770
Journal Article
Journal Article
Antimicrobial Agents and Chemotherapy, ISSN 0066-4804, 05/2012, Volume 56, Issue 5, pp. 2326 - 2334
Journal Article
Journal Article
Molecular Biology and Evolution, ISSN 0737-4038, 11/2013, Volume 30, Issue 11, pp. 2447 - 2462
Journal Article
PHYSICAL REVIEW LETTERS, ISSN 0031-9007, 03/2019, Volume 122, Issue 12, pp. 128101 - 128101
Journal Article