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Publication : european journal of biochemistry

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The absence of the mitochondrial ATP synthase δ subunit promotes a slow growth phenotype of rho- yeast cells by a lack of assembly of the catalytic sector F1.

Authors : Giraud, Marie-France¹; Velours, Jean¹

Source: European Journal of Biochemistry. 5/1/97, Vol. 245 Issue 3, p813-818. 6p.

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Membrane embedded location of Na+ or H+ binding sites on the rotor ring of F1 F0 ATP synthases.

Authors : von Ballmoos, Christoph¹; Meier, Thomas¹; Dimroth, Peter¹

Source: European Journal of Biochemistry. Nov2002, Vol. 269 Issue 22, p5581-5589. 9p.

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The presence of phosphate at a catalytic site suppresses the formation of the MgADP-inhibited form of F1 -ATPase.

Authors : Mitome, Noriyo¹; Ono, Sakurako¹; Suzuki, Toshiharu¹

Source: European Journal of Biochemistry. Jan2002, Vol. 269 Issue 1, p53-60. 8p.

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The N-termini of the α and β subunits at the top of F1 stabilize the energy-transfer function in the mitochondrial F1Fo ATP synthase.

Authors : Xu, Ting¹; Candita, Cosimo¹; Amoruso, Giovanna¹

Source: European Journal of Biochemistry. Feb98 Part 2, Vol. 252 Issue 1, p155-161. 7p. 3 Diagrams, 2 Charts, 11 Graphs.

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Synthesis and release of ATP by soluble mitochondrial F1 in complex with its inhibitor protein during dimethylsulfoxide-water transitions.

Authors : Tuena de Gómez-Puyou, Marietta¹; Sandoval, Francisca¹; García, José J.¹

Source: European Journal of Biochemistry. Jul98 Part 1, Vol. 255 Issue 1, p303-308. 6p. 1 Chart, 3 Graphs.

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Fluorescence resonance energy transfer mapping of subunit δ in spinach chloroplast F1 ATPase.

Authors : Engelbrecht, Siegfried¹; Giakas, Enrico¹; Marx, Olaf¹

Source: European Journal of Biochemistry. Mar98 Part 1, Vol. 252 Issue 2, p277-283. 7p. 2 Diagrams, 4 Charts, 10 Graphs.

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The three-dimensional structure of guanine-specific ribonuclease F1 in solution determined by NMR spectroscopy and distance geometry.

Authors : Nakai, Takahisa¹; Yoshikawa, Wataru¹; Nakamura, Haruki¹

Source: European Journal of Biochemistry. 8/15/92, Vol. 208 Issue 1, p41-51. 11p.

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Role of Fo and F1 subunits in the gating and coupling function of mitochondrial H+-ATP synthase.

Authors : Zanotti, Franco¹; Guerrieri, Ferruccio¹; Capozza, Giuseppe¹

Source: European Journal of Biochemistry. 8/15/92, Vol. 208 Issue 1, p9-16. 8p.

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Purification and characterization of the F1 portion of the ATP synthase (F1F0) of Streptomyces lividans.

Authors : Hensel, Michael¹; Deckers-Hebestreit, Gabriele¹; Altendorf, Karlheinz¹

Source: European Journal of Biochemistry. 12/18/91, Vol. 202 Issue 3, p1313-1319. 7p.

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Localization on the mitochondrial F1 ATPase α subunit of an epitope masked in the membrane-bound enzyme using a monoclonal antibody and synthetic peptides.

Authors : Moradi-Améli, Mahnaz¹; Clerc, François Frédéric¹; Cieur, Franck¹

Source: European Journal of Biochemistry. 8/1/91, Vol. 199 Issue 3, p671-676. 6p.

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نتائج البحث

فلترة النتائج

The absence of the mitochondrial ATP synthase δ subunit promotes a slow growth phenotype of rho- yeast cells by a lack of assembly of the catalytic sector F1.

Membrane embedded location of Na+ or H+ binding sites on the rotor ring of F1 F0 ATP synthases.

The presence of phosphate at a catalytic site suppresses the formation of the MgADP-inhibited form of F1 -ATPase.

The N-termini of the α and β subunits at the top of F1 stabilize the energy-transfer function in the mitochondrial F1Fo ATP synthase.

Synthesis and release of ATP by soluble mitochondrial F1 in complex with its inhibitor protein during dimethylsulfoxide-water transitions.

Fluorescence resonance energy transfer mapping of subunit δ in spinach chloroplast F1 ATPase.

The three-dimensional structure of guanine-specific ribonuclease F1 in solution determined by NMR spectroscopy and distance geometry.

Role of Fo and F1 subunits in the gating and coupling function of mitochondrial H+-ATP synthase.

Purification and characterization of the F1 portion of the ATP synthase (F1F0) of Streptomyces lividans.

Localization on the mitochondrial F1 ATPase α subunit of an epitope masked in the membrane-bound enzyme using a monoclonal antibody and synthetic peptides.

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