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160 related items for PubMed ID: 8662953
1. Nucleotide-dependent movement of the epsilon subunit between alpha and beta subunits in the Escherichia coli F1F0-type ATPase. Aggeler R, Capaldi RA. J Biol Chem; 1996 Jun 07; 271(23):13888-91. PubMed ID: 8662953 [Abstract] [Full Text] [Related]
2. 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]
3. Rotation of a gamma-epsilon subunit domain in the Escherichia coli F1F0-ATP synthase complex. The gamma-epsilon subunits are essentially randomly distributed relative to the alpha3beta3delta domain in the intact complex. Aggeler R, Ogilvie I, Capaldi RA. J Biol Chem; 1997 Aug 01; 272(31):19621-4. PubMed ID: 9235970 [Abstract] [Full Text] [Related]
12. Movement of the helical domain of the epsilon subunit is required for the activation of thermophilic F1-ATPase. Kato-Yamada Y, Yoshida M, Hisabori T. J Biol Chem; 2000 Nov 17; 275(46):35746-50. PubMed ID: 10958801 [Abstract] [Full Text] [Related]
14. Differentiation of catalytic sites on Escherichia coli F1ATPase by laser photoactivated labeling with [3H]-2-Azido-ATP using the mutant beta Glu381Cys:epsilonSer108Cys to identify different beta subunits by their interactions with gamma and epsilon subunits. Grüber G, Capaldi RA. Biochemistry; 1996 Apr 02; 35(13):3875-9. PubMed ID: 8672416 [Abstract] [Full Text] [Related]
15. Nucleotide-dependent and dicyclohexylcarbodiimide-sensitive conformational changes in the epsilon subunit of Escherichia coli ATP synthase. Mendel-Hartvig J, Capaldi RA. Biochemistry; 1991 Nov 12; 30(45):10987-91. PubMed ID: 1834172 [Abstract] [Full Text] [Related]
18. Cross-linking of chloroplast F0F1-ATPase subunit epsilon to gamma without effect on activity. Epsilon and gamma are parts of the rotor. Schulenberg B, Wellmer F, Lill H, Junge W, Engelbrecht S. Eur J Biochem; 1997 Oct 01; 249(1):134-41. PubMed ID: 9363764 [Abstract] [Full Text] [Related]