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Proceedings of the National Academy of Sciences of the United States of America, ISSN 0027-8424, 03/2018, Volume 115, Issue 12, pp. 2850 - 2852
Journal Article
Journal Article
Molecular Cell, ISSN 1097-2765, 08/2016, Volume 63, Issue 3, pp. 445 - 456
Journal Article
FEBS Letters, ISSN 0014-5793, 02/2018, Volume 592, Issue 3, pp. 343 - 355
Journal Article
Proceedings of the National Academy of Sciences of the United States of America, ISSN 0027-8424, 8/2011, Volume 108, Issue 34, pp. 14121 - 14126
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 | ANTIBIOTICS | MULTIDISCIPLINARY SCIENCES | SENSITIVITY | AMINO-ACID SUBSTITUTIONS | MITOCHONDRIAL ATPASE | 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 | Biological Sciences | Physical Sciences
Journal Article
Proceedings of the National Academy of Sciences, ISSN 0027-8424, 06/2012, Volume 109, Issue 25, pp. E1599 - E1608
Journal Article
Proceedings of the National Academy of Sciences of the United States of America, ISSN 0027-8424, 03/2018, Volume 115, Issue 12, pp. 2988 - 2993
The ATP synthase in human mitochondria is a membrane-bound assembly of 29 proteins of 18 kinds. All but two membrane components are encoded in nuclear genes,... 
Membrane subunits | Human mitochondria | ATP synthase | Assembly | COMPLEX I | BOVINE HEART-MITOCHONDRIA | MULTIDISCIPLINARY SCIENCES | F-1-ATPASE | SUBUNITS | IDENTIFICATION | human mitochondria | ORGANIZATION | GENE | BIOGENESIS | F1FO-ATP SYNTHASE | assembly | membrane subunits | F1F0-ATP SYNTHASE | Physiological aspects | Mitochondria | Cell membranes | ATP synthases | Biological Sciences
Journal Article
The FEBS Journal, ISSN 1742-464X, 05/2010, Volume 277, Issue 9, pp. 2192 - 2205
Pigment epithelium‐derived factor (PEDF), a potent blocker of angiogenesis in vivo, and of endothelial cell migration and tubule formation, binds with high... 
endothelial cells | PEDF | surface plasmon resonance | F1Fo‐ATP synthase | F1‐ATPase | ATP synthase | Surface plasmon resonance | ATPase | Endothelial cells | Proteins | Retina | Biochemistry | Binding sites | Cell adhesion & migration | ligand | F1-ATP synthase | protein-protein interactions
Journal Article
Current Medicinal Chemistry, ISSN 0929-8673, 10/2017, Volume 24, Issue 35, pp. 3894 - 3906
For centuries, phytochemicals have been used to prevent and cure multiple health ailments. Phytochemicals have been reported to have antioxidant, antidiabetic,... 
Enzyme inhibition | Polyphenols | Molecular drug target | Microbial and mammalian F1Fo ATP synthase | Antimicrobial phytochemicals | MYCOBACTERIUM-TUBERCULOSIS | polyphenols | OXIDATIVE-PHOSPHORYLATION | ANTIMICROBIAL PROPERTIES | CHEMISTRY, MEDICINAL | MITOCHONDRIAL F1F0-ATPASE | 3 CATALYTIC SITES | ENDOTHELIAL-CELL SURFACE | BIOCHEMISTRY & MOLECULAR BIOLOGY | BETA-DELSEED-MOTIF | molecular drug target | EPSILON-SUBUNIT | Microbial and mammalian F1F0 ATP synthase | enzyme inhibition | ESCHERICHIA-COLI F-1-ATPASE | antimicrobial phytochemicals | F1FO-ATP SYNTHASE | PHARMACOLOGY & PHARMACY | Phytochemicals - chemistry | Bacterial Proteins - antagonists & inhibitors | Drug Resistance, Microbial - drug effects | Enzyme Inhibitors - metabolism | Anti-Infective Agents - metabolism | Anti-Infective Agents - pharmacology | Humans | Enzyme Inhibitors - pharmacology | Mitochondrial Proton-Translocating ATPases - metabolism | Anti-Infective Agents - chemistry | Enzyme Inhibitors - chemistry | Bacteria - enzymology | Bacterial Proteins - metabolism | Phytochemicals - metabolism | Binding Sites | Dietary Supplements | Mitochondrial Proton-Translocating ATPases - antagonists & inhibitors | Phytochemicals - pharmacology | Health care | Plants (botany) | Vegetables | Diabetes mellitus | Amino acids | Infections | Antiinfectives and antibacterials | Anticancer properties | Antioxidants | ATP synthase | Microorganisms | Phytochemicals | Diet | Antibiotics | Cell death | Selective binding | Antibiotic resistance | Spices | Inhibition | ATP | Binding sites
Journal Article
Journal of Molecular Biology, ISSN 0022-2836, 10/2011, Volume 413, Issue 3, pp. 593 - 603
Cell-free (CF) expression technologies have emerged as promising methods for the production of individual membrane proteins of different types and origin.... 
cell-free expression | F1Fo-ATP synthase | Caldalkalibacillus thermarum strain TA2.A1 | in vitro protein synthesis and assembly | membrane protein complex | ATP synthase | ROTATION