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2. 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. Watts SD, Tang C, Capaldi RA. J Biol Chem; 1996 Nov 08; 271(45):28341-7. PubMed ID: 8910457 [Abstract] [Full Text] [Related]
3. Subunits coupling H+ transport and ATP synthesis in the Escherichia coli ATP synthase. Cys-Cys cross-linking of F1 subunit epsilon to the polar loop of F0 subunit c. Zhang Y, Fillingame RH. J Biol Chem; 1995 Oct 13; 270(41):24609-14. PubMed ID: 7592682 [Abstract] [Full Text] [Related]
10. Crystal structure of the epsilon subunit of the proton-translocating ATP synthase from Escherichia coli. Uhlin U, Cox GB, Guss JM. Structure; 1997 Sep 15; 5(9):1219-30. PubMed ID: 9331422 [Abstract] [Full Text] [Related]
13. The second stalk composed of the b- and delta-subunits connects F0 to F1 via an alpha-subunit in the Escherichia coli ATP synthase. Rodgers AJ, Capaldi RA. J Biol Chem; 1998 Nov 06; 273(45):29406-10. PubMed ID: 9792643 [Abstract] [Full Text] [Related]
15. Site-directed cross-linking of b to the alpha, beta, and a subunits of the Escherichia coli ATP synthase. McLachlin DT, Coveny AM, Clark SM, Dunn SD. J Biol Chem; 2000 Jun 09; 275(23):17571-7. PubMed ID: 10747904 [Abstract] [Full Text] [Related]
16. 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. Aggeler R, Haughton MA, Capaldi RA. J Biol Chem; 1995 Apr 21; 270(16):9185-91. PubMed ID: 7721834 [Abstract] [Full Text] [Related]
17. The trapping of different conformations of the Escherichia coli F1 ATPase by disulfide bond formation. Effect on nucleotide binding affinities of the catalytic sites. Grüber G, Capaldi RA. J Biol Chem; 1996 Dec 20; 271(51):32623-8. PubMed ID: 8955091 [Abstract] [Full Text] [Related]