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1. Full Text The metabolite α-ketoglutarate extends lifespan by inhibiting ATP synthase and TOR
by Chin, Randall M and Fu, Xudong and Pai, Melody Y and Vergnes, Laurent and Hwang, Heejun and Deng, Gang and Diep, Simon and Lomenick, Brett and Meli, Vijaykumar S and Monsalve, Gabriela C and Hu, Eileen and Whelan, Stephen A and Wang, Jennifer X and Jung, Gwanghyun and Solis, Gregory M and Fazlollahi, Farbod and Kaweeteerawat, Chitrada and Quach, Austin and Nili, Mahta and Krall, Abby S and Godwin, Hilary A and Chang, Helena R and Faull, Kym F and Guo, Feng and Jiang, Meisheng and Trauger, Sunia A and Saghatelian, Alan and Braas, Daniel and Christofk, Heather R and Clarke, Catherine F and Teitell, Michael A and Petrascheck, Michael and Reue, Karen and Jung, Michael E and Frand, Alison R and Huang, Jing
Nature, ISSN 0028-0836, 2014, Volume 510, Issue 7505, pp. 397 - 401
Metabolism and ageing are intimately linked. Compared with ad libitum feeding, dietary restriction consistently extends lifespan and delays age-related... 
DEVELOPMENTAL ARREST | LONGEVITY | CAENORHABDITIS-ELEGANS | RHESUS-MONKEYS | PHOSPHORYLATION | MULTIDISCIPLINARY SCIENCES | CALORIC RESTRICTION | MITOCHONDRIA | C-ELEGANS | DIETARY RESTRICTION | AUTOPHAGY | Cell Line | TOR Serine-Threonine Kinases - metabolism | Jurkat Cells | Longevity - drug effects | Humans | Enzyme Inhibitors - pharmacology | Longevity - genetics | Enzyme Activation - drug effects | Mitochondrial Proton-Translocating ATPases - metabolism | Gene Knockdown Techniques | Mitochondrial Proton-Translocating ATPases - genetics | Animals | Caenorhabditis elegans - drug effects | Ketoglutaric Acids - pharmacology | HEK293 Cells | Protein Binding | Mice | Longevity - physiology
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2. Full Text An early age increase in vacuolar pH limits mitochondrial function and lifespan in yeast
by Hughes, Adam L and Gottschling, Daniel E
Nature, ISSN 0028-0836, 12/2012, Volume 492, Issue 7428, pp. 261 - 265
Mitochondria have a central role in ageing. They are considered to be both a target of the ageing process and a contributor to it(1). Alterations in... 
TRANSPORT | BUDDING YEAST | MEMBRANE | MULTIDISCIPLINARY SCIENCES | H+-ATPASE | MECHANISMS | FLUORESCENT PROTEIN | INHERITANCE | SACCHAROMYCES-CEREVISIAE | MORPHOLOGY | CALORIE RESTRICTION | Gene Expression | Saccharomyces cerevisiae - physiology | Lysosomes - chemistry | Vacuoles - physiology | Mitochondria - metabolism | Microbial Viability | Saccharomyces cerevisiae Proteins - genetics | Lysosomes - physiology | Saccharomyces cerevisiae - chemistry | Proton-Translocating ATPases - metabolism | Saccharomyces cerevisiae - metabolism | Amino Acids - metabolism | Proton-Translocating ATPases - genetics | Homeostasis - physiology | Saccharomyces cerevisiae Proteins - metabolism | Vacuoles - chemistry | Hydrogen-Ion Concentration | Mitochondria | Cellular control mechanisms | Aging | Research | Observations | Brewer's yeast | Cells | Proteins | Daughters | Cell culture | Yeast | Rodents | Mitochondrial DNA | Age
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3. Full Text Structure of ATP synthase from Paracoccus denitrificans determined by X-ray crystallography at 4.0 Å resolution
by Edgar Morales-Rios and Martin G. Montgomery and Andrew G. W. Leslie and John E. Walker
Proceedings of the National Academy of Sciences, ISSN 0027-8424, 10/2015, Volume 112, Issue 43, pp. 13231 - 13236
The structure of the intact ATP synthase from the α-proteobacterium Paracoccus denitrificans, inhibited by its natural regulatory ζ-protein, has been solved by... 
Proton translocation | ATP synthase | Regulation | Paracoccus denitrificans | Structure | Mitochondrial Proton-Translocating ATPases - genetics | Protein Structure, Tertiary | Sequence Alignment | Species Specificity | Base Sequence | Molecular Sequence Data | Protein Binding | Crystallography, X-Ray | Catalysis | Mitochondrial Proton-Translocating ATPases - chemistry | Paracoccus denitrificans - enzymology | Physiological aspects | Mitochondria | Genetic aspects | Research | ATP synthases | Biological Sciences | regulation | proton translocation | structure
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4. Full Text Mitochondrial dysfunction in ATP13A2 carriers
by Finsterer, Josef and Scorza, Fulvio A and Scorza, Carla A and Fiorini, Ana C and de Almeida, Antonio Carlos
Brain and Development, ISSN 0387-7604, 02/2019, Volume 41, Issue 2, pp. 221 - 222
CLINICAL NEUROLOGY | Mitochondrial Diseases - genetics | Proton-Translocating ATPases - genetics | Mutation - genetics | Humans
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5. Full Text Visualization of ATP Levels inside Single Living Cells with Fluorescence Resonance Energy Transfer-Based Genetically Encoded Indicators
by Hiromi Imamura and Kim P. Huynh Nhat and Hiroko Togawa and Kenta Saito and Ryota Iino and Yasuyuki Kato-Yamada and Takeharu Nagai and Hiroyuki Noji and James A. Wells
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 | Nutrition | fluorescence resonance energy transfer | oligomycin A | ATP | Nuclei | Biological Sciences
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6. Full Text Structure and conformational states of the bovine mitochondrial ATP synthase by cryo-EM
by Zhou, Anna and Rohou, Alexis and Schep, Daniel G and Bason, John V and Montgomery, Martin G and Walker, John E and Grigorieffniko, Nikolaus and Rubinstein, John L
eLife, ISSN 2050-084X, 10/2015, Volume 4, Issue 2015
Adenosine triphosphate (ATP), the chemical energy currency of biology, is synthesized in eukaryotic cells primarily by the mitochondrial ATP synthase. ATP... 
COMPLEX I | REFINEMENT | ANISOTROPIC MAGNIFICATION | ELECTRON CRYOMICROSCOPY | DENSITY MAPS | PROTEIN | MEMBRANE | BIOLOGY | SUBUNITS | MICROSCOPY | PREDICTION | Physiological aspects | Mitochondria | Structure | Cryoelectron microscopy | Adenosine triphosphate | Methods | Enzymes | ATP synthase | Maps | Classification | Data processing | Lipids | ATP
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7. Full Text Mitochondrial ATP synthase: architecture, function and pathology
by Jonckheere, A.I and Smeitink, J.A.M and Rodenburg, R.J.T
Journal of Inherited Metabolic Disease, ISSN 0141-8955, 2012, Volume 35, Issue 2, pp. 211 - 225
Human mitochondrial (mt) ATP synthase, or complex V consists of two functional domains: F(1), situated in the mitochondrial matrix, and F(o), located in the... 
Human Genetics | Biochemistry, general | Pediatrics | Internal Medicine | Medicine & Public Health | Metabolic Diseases | DNA T8993G MUTATION | RESPIRATORY-CHAIN | OXIDATIVE-PHOSPHORYLATION | F-1 EPSILON-SUBUNIT | BILATERAL STRIATAL NECROSIS | LEIGH-SYNDROME | BLUE NATIVE ELECTROPHORESIS | ENDOCRINOLOGY & METABOLISM | GENETICS & HEREDITY | ADENOSINE-TRIPHOSPHATASE | HEREDITARY OPTIC NEUROPATHY | SACCHAROMYCES-CEREVISIAE | Mitochondrial Proton-Translocating ATPases - genetics | Mitochondria - enzymology | Animals | Mitochondria - genetics | Adenosine Triphosphate - metabolism | Humans | Adenosine Diphosphate - metabolism | Mitochondria - pathology | Mitochondrial Proton-Translocating ATPases - metabolism | Oligomers | Review
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8. Full Text Permeability transition in human mitochondria persists in the absence of peripheral stalk subunits of ATP synthase
by He, Jiuya and Carroll, Joe and Ding, Shujing and Fearnley, Ian M and Walker, John E
Proceedings of the National Academy of Sciences of the United States of America, ISSN 0027-8424, 08/2017, Volume 114, Issue 34, pp. 9086 - 9091
The opening of a nonspecific channel, known as the permeability transition pore (PTP), in the innermembranes of mitochondria can be triggered by calcium ions,... 
ATP5O oligomycin sensitivity conferral protein | Human mitochondria | ATP synthase | Permeability transition pore | ATP5F1 subunit b | INHIBITOR PROTEIN | C-SUBUNIT | MEMBRANE | MULTIDISCIPLINARY SCIENCES | human mitochondria | CELL-DEATH | HEART | CYCLOPHILIN-D | CYCLOSPORINE-A | CALCIUM UNIPORTER | PORE | permeability transition pore | COMPONENT | Cyclosporine - pharmacology | Humans | Cyclophilins - metabolism | Protein Subunits - metabolism | Mitochondrial Membrane Transport Proteins - genetics | Mitochondrial Membranes - drug effects | Mitochondrial Proton-Translocating ATPases - genetics | Mitochondria - genetics | Base Sequence | Membrane Proteins - metabolism | Protein Subunits - genetics | Catalytic Domain | Mitochondrial Membrane Transport Proteins - metabolism | Permeability - drug effects | Calcium - pharmacology | Membrane Proteins - genetics | Adenosine Triphosphatases - metabolism | Mitochondria - metabolism | Mitochondrial Proton-Translocating ATPases - chemistry | Sequence Homology, Nucleic Acid | Mitochondrial Proton-Translocating ATPases - metabolism | Mitochondrial Membranes - metabolism | Carrier Proteins - genetics | Carrier Proteins - metabolism | Cell Line, Tumor | Protein Binding | Adenosine Triphosphatases - genetics | Protein Subunits - chemistry | Mutation | Physiological aspects | Mitochondria | ATP synthases | Biological Sciences
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9. Full Text Formation of Cristae and Crista Junctions in Mitochondria Depends on Antagonism between Fcj1 and Su e/g
by Regina Rabl and Vincent Soubannier and Roland Scholz and Frank Vogel and Nadine Mendl and Andreja Vasiljev-Neumeyer and Christian Körner and Ravi Jagasia and Thomas Keil and Wolfgang Baumeister and Marek Cyrklaff and Walter Neupert and Andreas S. Reichert
The Journal of Cell Biology, ISSN 0021-9525, 6/2009, Volume 185, Issue 6, pp. 1047 - 1063
Crista junctions (CJs) are important for mitochondrial organization and function, but the molecular basis of their formation and architecture is obscure. We... 
Oligomers | Proteins | Yeasts | Mitochondria | Plasmids | Lead | Tomography | Dimers | Curvature | Electrons | CONTACT SITES | CRYOELECTRON MICROSCOPY | INNER-MEMBRANE | DIMERIC ATP SYNTHASE | DYNAMIN-RELATED GTPASE | CELL-PROLIFERATION | RAT-LIVER MITOCHONDRIA | SACCHAROMYCES-CEREVISIAE | ELECTRON TOMOGRAPHY | PROTEIN COMPLEX | CELL BIOLOGY | DNA, Mitochondrial - metabolism | Humans | Mitochondria - metabolism | Mitochondrial Proteins - genetics | Saccharomyces cerevisiae Proteins - genetics | Mitochondria - ultrastructure | Mitochondrial Proton-Translocating ATPases - metabolism | Intracellular Membranes - ultrastructure | Proton-Translocating ATPases - chemistry | Mitochondrial Proton-Translocating ATPases - genetics | Proton-Translocating ATPases - metabolism | Saccharomyces cerevisiae - cytology | Saccharomyces cerevisiae - metabolism | DNA, Mitochondrial - genetics | Proton-Translocating ATPases - genetics | Mitochondrial Proteins - metabolism | Protein Structure, Quaternary | Saccharomyces cerevisiae Proteins - metabolism | Intracellular Membranes - metabolism | Models, Anatomic | Research | Properties | Membrane proteins
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10. Full Text Genome‐Wide Association Study in an Amerindian Ancestry Population Reveals Novel Systemic Lupus Erythematosus Risk Loci and the Role of European Admixture
by Alarcón‐Riquelme, Marta E and Ziegler, Julie T and Molineros, Julio and Howard, Timothy D and Moreno‐Estrada, Andrés and Sánchez‐Rodríguez, Elena and Ainsworth, Hannah C and Ortiz‐Tello, Patricia and Comeau, Mary E and Rasmussen, Astrid and Kelly, Jennifer A and Adler, Adam and Acevedo‐Vázquez, Eduardo M and Mariano Cucho-Venegas, Jorge and García‐De la Torre, Ignacio and Cardiel, Mario H and Miranda, Pedro and Catoggio, Luis J and Maradiaga‐Ceceña, Marco and Gaffney, Patrick M and Vyse, Timothy J and Criswell, Lindsey A and Tsao, Betty P and Sivils, Kathy L and Bae, Sang‐Cheol and James, Judith A and Kimberly, Robert P and Kaufman, Kenneth M and Harley, John B and Esquivel‐Valerio, Jorge A and Moctezuma, José F and García, Mercedes A and Berbotto, Guillermo A and Babini, Alejandra M and Scherbarth, Hugo and Toloza, Sergio and Baca, Vicente and Nath, Swapan K and Aguilar Salinas, Carlos and Orozco, Lorena and Tusié‐Luna, Teresa and Zidovetzki, Raphael and Pons‐Estel, Bernardo A and Langefeld, Carl D and Jacob, Chaim O
Arthritis & Rheumatology, ISSN 2326-5191, 04/2016, Volume 68, Issue 4, pp. 932 - 943
Objective Systemic lupus erythematosus (SLE) is a chronic autoimmune disease with a strong genetic component. We undertook the present work to perform the... 
IMPACT | GENETIC ASSOCIATION | VARIANTS | FREQUENCY | COMPONENTS | COMMON | IRF5 | HAPLOTYPE | RHEUMATOLOGY | INFERENCE | EXPRESSION | Haplotypes | Interferon Regulatory Factors | Interleukin-1 Receptor-Associated Kinases - genetics | United States | beta Karyopherins | Humans | Male | HLA-DQ beta-Chains - genetics | Case-Control Studies | Mitochondrial Proton-Translocating ATPases - genetics | CD11b Antigen - genetics | NADPH Oxidases - genetics | Female | Chile | Odds Ratio | Principal Component Analysis | Argentina | European Continental Ancestry Group - genetics | Genetic Predisposition to Disease | Genome-Wide Association Study | DNA-Binding Proteins - genetics | American Native Continental Ancestry Group - genetics | HLA-DQ Antigens - genetics | Lupus Erythematosus, Systemic - genetics | Mexico | STAT4 Transcription Factor - genetics | Chromosomes, Human, Pair 10 - genetics | Peru
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11. Full Text Post-translational modifications of the mitochondrial F 1 F O -ATPase
by Nesci, Salvatore and Trombetti, Fabiana and Ventrella, Vittoria and Pagliarani, Alessandra
Biochimica et biophysica acta. General subjects, ISSN 0304-4165, 11/2017, Volume 1861, Issue 11 Pt A, pp. 2902 - 2912
The mitochondrial F F -ATPase has the main role in synthesizing most of ATP, thus providing energy to living cells, but it also works in reverse and hydrolyzes... 
Mitochondrial Proton-Translocating ATPases - genetics | Mitochondria - genetics | Adenosine Triphosphate - metabolism | Humans | Protein Processing, Post-Translational - genetics | Mitochondria - metabolism | Mitochondrial Proton-Translocating ATPases - metabolism
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12. Full Text Incompatibility of Nuclear and Mitochondrial Genomes Causes Hybrid Sterility between Two Yeast Species
by Lee, Hsin-Yi and Chou, Jui-Yu and Cheong, Liplee and Chang, Nai-Hsin and Yang, Shi-Yow and Leu, Jun-Yi
Cell, ISSN 0092-8674, 2008, Volume 135, Issue 6, pp. 1065 - 1073
Hybrids between species are usually unviable or sterile. One possible mechanism causing reproductive isolation is incompatibility between genes from different... 
CELLBIO | MICROBIO | EVO_ECOL | SUBSTITUTION | GENETIC MATERIAL | EVOLUTION | ATP SYNTHASE | GENUS SACCHAROMYCES | SPECIATION | BIOCHEMISTRY & MOLECULAR BIOLOGY | EPISTASIS | SACCHAROMYCES-CEREVISIAE | DROSOPHILA | DEFICIENCY | CELL BIOLOGY | Carbon - metabolism | Protein Biosynthesis | Saccharomyces cerevisiae - genetics | Mitochondria - metabolism | Fungal Proteins - genetics | Saccharomyces cerevisiae Proteins - genetics | Saccharomyces - genetics | Mitochondrial Proton-Translocating ATPases - genetics | Saccharomyces cerevisiae - metabolism | Genome, Fungal | Genetic Speciation | Genome, Mitochondrial | Saccharomyces cerevisiae - growth & development | Chimera | Mitochondrial DNA | Genomes | Messenger RNA | Genomics
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13. Full Text Cardiolipin binds selectively but transiently to conserved lysine residues in the rotor of metazoan ATP synthases
by Anna L. Duncan and Alan J. Robinson and John E. Walker
Proceedings of the National Academy of Sciences of the United States of America, ISSN 0027-8424, 8/2016, Volume 113, Issue 31, pp. 8687 - 8692
The anionic lipid cardiolipin is an essential component of active ATP synthases. In metazoans, their rotors contain a ring of eight c-subunits consisting of... 
RAT-LIVER | mitochondria | MEMBRANE | MULTIDISCIPLINARY SCIENCES | molecular dynamics simulation | F-ATPASE | MITOCHONDRIAL ATPASE | cardiolipin | CYTOCHROME-C-OXIDASE | ANGSTROM RESOLUTION | ATP synthase | RING | COARSE-GRAINED MODEL | FORCE-FIELD | MOLECULAR-DYNAMICS SIMULATIONS | trimethyllysine | Amino Acid Sequence | Bacterial Proteins - chemistry | Bacterial Proteins - genetics | Cardiolipins - metabolism | Binding Sites - genetics | Saccharomyces cerevisiae Proteins - genetics | Cardiolipins - chemistry | Molecular Dynamics Simulation | Proton-Translocating ATPases - chemistry | Proton-Translocating ATPases - metabolism | Sequence Homology, Amino Acid | Lysine - genetics | Animals | Proton-Translocating ATPases - genetics | Cattle | Saccharomyces cerevisiae Proteins - metabolism | Protein Binding | Bacterial Proteins - metabolism | Lysine - metabolism | Lipid Bilayers - chemistry | Lipid Bilayers - metabolism | Lysine - chemistry | Methylation | Saccharomyces cerevisiae Proteins - chemistry | Biological Sciences
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