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145 related items for PubMed ID: 6329170
1. The DCCD-reactive aspartyl-residue of subunit C from the Escherichia coli ATP-synthase is important for the conformation of F0. Friedl P, Hoppe J, Schairer HU. Biochem Biophys Res Commun; 1984 Apr 30; 120(2):527-33. PubMed ID: 6329170 [Abstract] [Full Text] [Related]
2. Identification of amino-acid substitutions in the proteolipid subunit of the ATP synthase from dicyclohexylcarbodiimide-resistant mutants of Escherichia coli. Hoppe J, Schairer HU, Sebald W. Eur J Biochem; 1980 Nov 30; 112(1):17-24. PubMed ID: 6256167 [Abstract] [Full Text] [Related]
8. Modification of the F0 portion of the H+-translocating adenosinetriphosphatase complex of Escherichia coli by the water-soluble carbodiimide 1-ethyl-3-[3-(dimethylamino)propyl]carbodiimide and effect on the proton channeling function. Lötscher HR, deJong C, Capaldi RA. Biochemistry; 1984 Aug 28; 23(18):4128-34. PubMed ID: 6237682 [Abstract] [Full Text] [Related]
15. Mutation of alanine 24 to serine in subunit c of the Escherichia coli F1F0-ATP synthase reduces reactivity of aspartyl 61 with dicyclohexylcarbodiimide. Fillingame RH, Oldenburg M, Fraga D. J Biol Chem; 1991 Nov 05; 266(31):20934-9. PubMed ID: 1834653 [Abstract] [Full Text] [Related]
16. Labeling of individual amino acid residues in the membrane-embedded F0 part of the F1 F0 ATP synthase from Neurospora crassa. Influence of oligomycin and dicyclohexylcarbodiimide. Hoppe J, Gatti D, Weber H, Sebald W. Eur J Biochem; 1986 Mar 03; 155(2):259-64. PubMed ID: 2869944 [Abstract] [Full Text] [Related]
17. An Asp-Asn substitution in the proteolipid subunit of the ATP-synthase from Escherichia coli leads to a non-functional proton channel. Hoppe J, Schairer HU, Friedl P, Sebald W. FEBS Lett; 1982 Aug 16; 145(1):21-9. PubMed ID: 6290265 [No Abstract] [Full Text] [Related]