| review article | Q7318358 |
| scholarly article | Q13442814 |
| P356 | DOI | 10.1017/S0033583517000129 |
| P698 | PubMed publication ID | 29233226 |
| P2093 | author name string | Rudolph A Marcus | |
| Sándor Volkán-Kacso | |||
| P2860 | cites work | Structure of bovine mitochondrial F(1)-ATPase inhibited by Mg(2+) ADP and aluminium fluoride | Q27625106 |
| The binding change mechanism for ATP synthase--some probabilities and possibilities | Q28265156 | ||
| F1-ATPase conformational cycle from simultaneous single-molecule FRET and rotation measurements | Q28829498 | ||
| High-speed atomic force microscopy reveals rotary catalysis of rotorless F₁-ATPase. | Q54569713 | ||
| Turnover number of Escherichia coli F0F1 ATP synthase for ATP synthesis in membrane vesicles. | Q54572105 | ||
| Electron transfers in chemistry and biology | Q56002451 | ||
| Ion motive ATPases. I. Ubiquity, properties, and significance to cell function | Q61889649 | ||
| ATP synthase: motoring to the finish line | Q80700451 | ||
| Free energy and temperature dependence of electron transfer at the metal-electrolyte interface | Q81231642 | ||
| Cooperative three-step motions in catalytic subunits of F(1)-ATPase correlate with 80 degrees and 40 degrees substep rotations | Q82619781 | ||
| Direct observation of the rotation of F1-ATPase | Q29615360 | ||
| Controlled rotation of the F₁-ATPase reveals differential and continuous binding changes for ATP synthesis. | Q30525177 | ||
| Chemomechanical coupling in F1-ATPase revealed by simultaneous observation of nucleotide kinetics and rotation | Q33196928 | ||
| One rotary mechanism for F1-ATPase over ATP concentrations from millimolar down to nanomolar | Q33210480 | ||
| Reverse engineering a protein: the mechanochemistry of ATP synthase | Q33933719 | ||
| Resolution of distinct rotational substeps by submillisecond kinetic analysis of F1-ATPase | Q33942984 | ||
| ATP synthase | Q34470136 | ||
| Dissecting the role of the γ-subunit in the rotary-chemical coupling and torque generation of F1-ATPase | Q35156989 | ||
| How release of phosphate from mammalian F1-ATPase generates a rotary substep | Q35616100 | ||
| Electrostatic origin of the mechanochemical rotary mechanism and the catalytic dwell of F1-ATPase | Q35651241 | ||
| Theory for rates, equilibrium constants, and Brønsted slopes in F1-ATPase single molecule imaging experiments | Q36306129 | ||
| On artifacts in single-molecule force spectroscopy | Q36306139 | ||
| Rate of hydrolysis in ATP synthase is fine-tuned by α-subunit motif controlling active site conformation | Q36598084 | ||
| Single molecule measurements of F1-ATPase reveal an interdependence between the power stroke and the dwell duration | Q37331232 | ||
| Theory of single-molecule controlled rotation experiments, predictions, tests, and comparison with stalling experiments in F1-ATPase | Q37379896 | ||
| Why nature really chose phosphate | Q38073986 | ||
| The ATP synthase: the understood, the uncertain and the unknown. | Q38077205 | ||
| Theory of long binding events in single-molecule-controlled rotation experiments on F1-ATPase | Q38708042 | ||
| Timing of inorganic phosphate release modulates the catalytic activity of ATP-driven rotary motor protein | Q38785918 | ||
| Viscoelastic dynamics of actin filaments coupled to rotary F-ATPase: angular torque profile of the enzyme | Q40189247 | ||
| Catalytic mechanism of F1-ATPase | Q41434371 | ||
| Functional halt positions of rotary FOF1-ATPase correlated with crystal structures. | Q41839337 | ||
| Movements of the epsilon-subunit during catalysis and activation in single membrane-bound H(+)-ATP synthase | Q41839904 | ||
| Structural biology: Toward the ATP synthase mechanism | Q42855081 | ||
| Phosphate release in F1-ATPase catalytic cycle follows ADP release. | Q42876375 | ||
| Power Stroke Angular Velocity Profiles of Archaeal A-ATP Synthase Versus Thermophilic and Mesophilic F-ATP Synthase Molecular Motors | Q43028804 | ||
| Mechanical modulation of catalytic power on F1-ATPase | Q43033513 | ||
| Axle-less F1-ATPase rotates in the correct direction | Q46752462 | ||
| Coupling of rotation and catalysis in F(1)-ATPase revealed by single-molecule imaging and manipulation. | Q50335878 | ||
| P275 | copyright license | Creative Commons Attribution 4.0 International | Q20007257 |
| P6216 | copyright status | copyrighted | Q50423863 |
| P304 | page(s) | e14 | |
| P577 | publication date | 2017-01-01 | |
| P1433 | published in | Quarterly Reviews of Biophysics | Q2361372 |
| P1476 | title | What can be learned about the enzyme ATPase from single-molecule studies of its subunit F1? | |
| P478 | volume | 50 |
| Q89187364 | The regulatory subunit ε in Escherichia coli FOF1-ATP synthase | cites work | P2860 |
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