| scholarly article | Q13442814 |
| P2093 | author name string | Nelli Mnatsakanyan | |
| Toshiharu Suzuki | |||
| Joachim Weber | |||
| Arathianand M Krishnakumar | |||
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| Rotary molecular motors | Q36288571 | ||
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| The alpha3(betaMet222Ser/Tyr345Trp)3gamma subcomplex of the TF1-ATPase does not hydolyze ATP at a significant rate until the substrate binds to the catalytic site of the lowest affinity | Q43020316 | ||
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| Expression of the wild-type and the Cys-/Trp-less α3β3γ complex of thermophilic F1-ATPase in Escherichia coli | Q43022320 | ||
| The alpha 3(beta Y341W)3 gamma subcomplex of the F1-ATPase from the thermophilic Bacillus PS3 fails to dissociate ADP when MgATP is hydrolyzed at a single catalytic site and attains maximal velocity when three catalytic sites are saturated with MgAT | Q43026078 | ||
| The role of the DELSEED motif of the beta subunit in rotation of F1-ATPase | Q43027538 | ||
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| The presence of phosphate at a catalytic site suppresses the formation of the MgADP-inhibited form of F(1)-ATPase | Q43029702 | ||
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| The beta G156C substitution in the F1-ATPase from the thermophilic Bacillus PS3 affects catalytic site cooperativity by destabilizing the closed conformation of the catalytic site | Q43031801 | ||
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| F0F1-ATPase/synthase is geared to the synthesis mode by conformational rearrangement of epsilon subunit in response to proton motive force and ADP/ATP balance | Q44526070 | ||
| Fluorescent probes applied to catalytic cooperativity in ATP synthase | Q44819918 | ||
| Highly coupled ATP synthesis by F1-ATPase single molecules | Q45270373 | ||
| Interactions between beta D372 and gamma subunit N-terminus residues gamma K9 and gamma S12 are important to catalytic activity catalyzed by Escherichia coli F1F0-ATP synthase | Q46480206 | ||
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| Catalytic site nucleotide binding and hydrolysis in F1F0-ATP synthase | Q47732557 | ||
| Complete kinetic and thermodynamic characterization of the unisite catalytic pathway of Escherichia coli F1-ATPase. Comparison with mitochondrial F1-ATPase and application to the study of mutant enzymes. | Q52488807 | ||
| Further examination of seventeen mutations in Escherichia coli F1-ATPase beta-subunit | Q54671636 | ||
| F1-ATPase, roles of three catalytic site residues | Q73025369 | ||
| A microcolorimetric method for the determination of inorganic phosphorus | Q73182371 | ||
| Effect of the epsilon-subunit on nucleotide binding to Escherichia coli F1-ATPase catalytic sites | Q77926922 | ||
| The role of beta-Arg-182, an essential catalytic site residue in Escherichia coli F1-ATPase | Q77937444 | ||
| P4510 | describes a project that uses | ImageJ | Q1659584 |
| P433 | issue | 17 | |
| P407 | language of work or name | English | Q1860 |
| P304 | page(s) | 11336-11345 | |
| P577 | publication date | 2009-02-25 | |
| P1433 | published in | Journal of Biological Chemistry | Q867727 |
| P1476 | title | The role of the betaDELSEED-loop of ATP synthase | |
| P478 | volume | 284 |
| Q41311853 | A conformational change of the γ subunit indirectly regulates the activity of cyanobacterial F1-ATPase |
| Q40083367 | A therapeutic connection between dietary phytochemicals and ATP synthase |
| Q37446710 | ATP synthase with its gamma subunit reduced to the N-terminal helix can still catalyze ATP synthesis |
| Q35978276 | Aerobic Growth of Escherichia coli Is Reduced, and ATP Synthesis Is Selectively Inhibited when Five C-terminal Residues Are Deleted from the ϵ Subunit of ATP Synthase. |
| Q36165353 | Asp residues of βDELSEED-motif are required for peptide binding in the Escherichia coli ATP synthase |
| Q34721063 | Double-lock ratchet mechanism revealing the role of alphaSER-344 in FoF1 ATP synthase |
| Q43187793 | Energy complexes are apparently associated with the switch-motor complex of bacterial flagella |
| Q37168333 | Escherichia coli F1Fo-ATP synthase with a b/δ fusion protein allows analysis of the function of the individual b subunits |
| Q54569713 | High-speed atomic force microscopy reveals rotary catalysis of rotorless F₁-ATPase. |
| Q90227278 | Identification of two segments of the γ subunit of ATP synthase responsible for the different affinities of the catalytic nucleotide-binding sites |
| Q36658989 | Load-dependent destabilization of the γ-rotor shaft in FOF1 ATP synthase revealed by hydrogen/deuterium-exchange mass spectrometry. |
| Q37335919 | Mutations on the N-terminal edge of the DELSEED loop in either the α or β subunit of the mitochondrial F1-ATPase enhance ATP hydrolysis in the absence of the central γ rotor |
| Q36598084 | Rate of hydrolysis in ATP synthase is fine-tuned by α-subunit motif controlling active site conformation |
| Q42140180 | Role of the DELSEED loop in torque transmission of F1-ATPase |
| Q98906811 | Structural basis of redox modulation on chloroplast ATP synthase |
| Q30435062 | Temperature dependence of single molecule rotation of the Escherichia coli ATP synthase F1 sector reveals the importance of gamma-beta subunit interactions in the catalytic dwell |
| Q35313850 | The beta subunit loop that couples catalysis and rotation in ATP synthase has a critical length |
| Q40648734 | Torque generation and utilization in motor enzyme F0F1-ATP synthase: half-torque F1 with short-sized pushrod helix and reduced ATP Synthesis by half-torque F0F1. |
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