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Science, ISSN 0036-8075, 10/2011, Volume 334, Issue 6054, pp. 380 - 385
The ability of electrospray to propel large viruses into a mass spectrometer is established and is rationalized by analogy to the atmospheric transmission of... 
Protons | Pumping | Vapor phases | REPORTS | Adenosine triphosphatases | Lead | Lipids | Mass spectroscopy | Dimers | Nucleotides | Mass spectra | ATP SYNTHESIS | NA+-ATPASE | ENTEROCOCCUS-HIRAE | CRYSTAL-STRUCTURE | MULTIDISCIPLINARY SCIENCES | MACROMOLECULAR ASSEMBLIES | THERMOPHILUS H+-ATPASE/SYNTHASE | PERIPHERAL STALK | ROTOR RING | THERMUS-THERMOPHILUS | VACUOLAR ATPASE | Protein Multimerization | Bacterial Proteins - chemistry | Vacuolar Proton-Translocating ATPases - metabolism | Protein Subunits - metabolism | Enterococcus - enzymology | Spectrometry, Mass, Electrospray Ionization | Adenosine Triphosphate - metabolism | Mass Spectrometry | Membrane Lipids - analysis | Binding Sites | Protein Structure, Tertiary | Thermus thermophilus - enzymology | Phosphatidylethanolamines - analysis | Adenosine Triphosphatases - metabolism | Models, Molecular | Cardiolipins - metabolism | Hydrolysis | Cardiolipins - analysis | Vacuolar Proton-Translocating ATPases - chemistry | Hydrophobic and Hydrophilic Interactions | Membrane Lipids - metabolism | Adenosine Triphosphatases - chemistry | Bacterial Proteins - metabolism | Protein Conformation | Protein Subunits - chemistry | Phosphatidylethanolamines - metabolism | Physiological aspects | Identification and classification | Mass spectrometry | Methods | Adenosine triphosphatase | Binding sites | Index Medicus
Journal Article
Nature Structural and Molecular Biology, ISSN 1545-9993, 12/2012, Volume 19, Issue 12, pp. 1356 - 1362
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
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