| scholarly article | Q13442814 |
| P356 | DOI | 10.1074/JBC.273.48.31765 |
| P698 | PubMed publication ID | 9822640 |
| P50 | author | Thomas M Duncan | Q61313175 |
| P2093 | author name string | R L Cross | |
| V V Bulygin | |||
| P2860 | cites work | Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: procedure and some applications | Q24561689 |
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| The ATP synthase--a splendid molecular machine | Q29617444 | ||
| Subunit organization and structure in the F0 sector of Escherichia coli F1F0 ATP synthase | Q32043519 | ||
| Direct observation of the rotation of epsilon subunit in F1-ATPase | Q32050424 | ||
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| The essential arginine residue at position 210 in the alpha subunit of the Escherichia coli ATP synthase can be transferred to position 252 with partial retention of activity | Q38466250 | ||
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| The stalk region of the Escherichia coli ATP synthase. Tyrosine 205 of the gamma subunit is in the interface between the F1 and F0 parts and can interact with both the epsilon and c oligomer. | Q54577299 | ||
| Probing interactions of the Escherichia coli F0F1 ATP synthase beta and gamma subunits with disulphide cross-links. | Q54600569 | ||
| Disulfide bond formation between the COOH-terminal domain of the beta subunits and the gamma and epsilon subunits of the Escherichia coli F1-ATPase. Structural implications and functional consequences. | Q54613743 | ||
| Introduction of reactive cysteine residues in the epsilon subunit of Escherichia coli F1 ATPase, modification of these sites with tetrafluorophenyl azide-maleimides, and examination of changes in the binding of the epsilon subunit when different nuc | Q54681961 | ||
| Intersubunit rotation in active F-ATPase | Q59065016 | ||
| Effect of dicyclohexylcarbodiimide on unisite and multisite catalytic activities of the adenosinetriphosphatase of Escherichia coli | Q69871179 | ||
| Characterization of the inhibitory (epsilon) subunit of the proton-translocating adenosine triphosphatase from Escherichia coli | Q70522864 | ||
| Cross-linking of chloroplast F0F1-ATPase subunit epsilon to gamma without effect on activity. Epsilon and gamma are parts of the rotor | Q73862685 | ||
| Three-stepped rotation of subunits gamma and epsilon in single molecules of F-ATPase as revealed by polarized, confocal fluorometry | Q74586417 | ||
| P433 | issue | 48 | |
| P407 | language of work or name | English | Q1860 |
| P921 | main subject | Escherichia coli | Q25419 |
| P304 | page(s) | 31765-31769 | |
| P577 | publication date | 1998-11-01 | |
| P1433 | published in | Journal of Biological Chemistry | Q867727 |
| P1476 | title | Rotation of the epsilon subunit during catalysis by Escherichia coli FOF1-ATP synthase | |
| P478 | volume | 273 |
| Q40101560 | Activation and stiffness of the inhibited states of F1-ATPase probed by single-molecule manipulation. |
| Q54446228 | Chemical modification of mono-cysteine mutants allows a more global look at conformations of the epsilon subunit of the ATP synthase from Escherichia coli. |
| Q77841244 | Defining the domain of binding of F1 subunit epsilon with the polar loop of F0 subunit c in the Escherichia coli ATP synthase |
| Q37103684 | Energy-driven subunit rotation at the interface between subunit a and the c oligomer in the F(O) sector of Escherichia coli ATP synthase |
| Q53819039 | Insights into the regulatory function of the ɛ subunit from bacterial F-type ATP synthases: a comparison of structural, biochemical and biophysical data. |
| Q42169415 | Integration of b subunits of unequal lengths into F1F0-ATP synthase |
| Q43014724 | Inverse regulation of rotation of F1-ATPase by the mutation at the regulatory region on the gamma subunit of chloroplast ATP synthase |
| Q73263431 | Lengthening the second stalk of F(1)F(0) ATP synthase in Escherichia coli |
| Q30305708 | Molecular mechanisms of rotational catalysis in the F(0)F(1) ATP synthase |
| Q43027868 | Movement of the helical domain of the epsilon subunit is required for the activation of thermophilic F1-ATPase |
| Q41839904 | Movements of the epsilon-subunit during catalysis and activation in single membrane-bound H(+)-ATP synthase |
| Q34478495 | Mutagenic analysis of the F0 stator subunits |
| Q73643345 | Mutations in single hairpin units of genetically fused subunit c provide support for a rotary catalytic mechanism in F(0)F(1) ATP synthase |
| Q33933678 | Operation of the F(0) motor of the ATP synthase |
| Q34478513 | Partial assembly of the yeast mitochondrial ATP synthase |
| Q39151141 | Regulatory conformational changes of the ε subunit in single FRET-labeled FoF1-ATP synthase. |
| Q73778707 | Secondary structure composition of reconstituted subunit b of the Escherichia coli ATP synthase |
| Q38141066 | Spotlighting motors and controls of single FoF1-ATP synthase |
| Q30788938 | Structural and functional features of the Escherichia coli F1-ATPase |
| Q34478502 | Structural changes during ATP hydrolysis activity of the ATP synthase from Escherichia coli as revealed by fluorescent probes. |
| Q27620439 | Structural features of the gamma subunit of the Escherichia coli F(1) ATPase revealed by a 4.4-A resolution map obtained by x-ray crystallography |
| Q27646164 | Structures of the thermophilic F1-ATPase subunit suggesting ATP-regulated arm motion of its C-terminal domain in F1 |
| Q33933673 | The ATP synthase of Escherichia coli: structure and function of F(0) subunits |
| Q34180478 | The Na(+)-translocating F(1)F(0) ATP synthase of Propionigenium modestum: mechanochemical insights into the F(0) motor that drives ATP synthesis |
| Q35313850 | The beta subunit loop that couples catalysis and rotation in ATP synthase has a critical length |
| Q33933627 | The epsilon subunit of bacterial and chloroplast F(1)F(0) ATPases. Structure, arrangement, and role of the epsilon subunit in energy coupling within the complex |
| Q73019327 | The epsilon subunit of the F(1)F(0) complex of Escherichia coli. cross-linking studies show the same structure in situ as when isolated |
| Q73195866 | The gammaepsilon-c subunit interface in the ATP synthase of Escherichia coli. cross-linking of the epsilon subunit to the c subunit ring does not impair enzyme function, that of gamma to c subunits leads to uncoupling |
| Q34303885 | The regulatory switch of F1-ATPase studied by single-molecule FRET in the ABEL Trap. |
| Q43028555 | The role of the betaDELSEED motif of F1-ATPase: propagation of the inhibitory effect of the epsilon subunit |
| Q33933633 | The rotary binding change mechanism of ATP synthases |
| Q54502988 | What is the role of epsilon in the Escherichia coli ATP synthase? |
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