Pages that link to "Q70522864"

The following pages link to Characterization of the inhibitory (epsilon) subunit of the proton-translocating adenosine triphosphatase from Escherichia coli (Q70522864):

Displaying 43 items.

• Structures of the thermophilic F1-ATPase   subunit suggesting ATP-regulated arm motion of its C-terminal domain in F1 (Q27646164) (← links)
• Crystal structure of the ϵ subunit of the proton-translocating ATP synthase from Escherichia coli (Q27745816) (← links)
• In vivo evidence for the role of the epsilon subunit as an inhibitor of the proton-translocating ATPase of Escherichia coli (Q28492864) (← links)
• F1-ATPase of Escherichia coli: the ε- inhibited state forms after ATP hydrolysis, is distinct from the ADP-inhibited state, and responds dynamically to catalytic site ligands. (Q30414148) (← links)
• A mutation in the Escherichia coli F0F1-ATP synthase rotor, gammaE208K, perturbs conformational coupling between transport and catalysis (Q30472484) (← links)
• Rapid hydrolysis of ATP by mitochondrial F1-ATPase correlates with the filling of the second of three catalytic sites (Q34048262) (← links)
• A functionally inactive, cold-stabilized form of the Escherichia coli F1Fo ATP synthase. (Q34974572) (← links)
• Construction and plasmid-borne complementation of strains lacking the epsilon subunit of the Escherichia coli F1F0 ATP synthase (Q35579242) (← links)
• ATP synthase and the actions of inhibitors utilized to study its roles in human health, disease, and other scientific areas (Q36995302) (← links)
• Protein translocation in vitro: biochemical characterization of genetically defined translocation components (Q37890390) (← links)
• Thermophilic F1-ATPase is activated without dissociation of an endogenous inhibitor, epsilon subunit. (Q38342855) (← links)
• Molecular genetics of F1-ATPase from Escherichia coli (Q39466617) (← links)
• Mutations at Glu-32 and His-39 in the epsilon subunit of the Escherichia coli F1F0 ATP synthase affect its inhibitory properties. (Q39933183) (← links)
• Properties and functions of the subunits of the Escherichia coli coupling factor ATPase (Q40101818) (← links)
• Polymorphism and conformational dynamics of F1-ATPases from bacterial membranes a model for the regulation of these enzymes on the basis of molecular plasticity (Q40103642) (← links)
• Inhibition of thermophilic F1-ATPase by the ε subunit takes different path from the ADP-Mg inhibition (Q41184268) (← links)
• Movements of the epsilon-subunit during catalysis and activation in single membrane-bound H(+)-ATP synthase (Q41839904) (← links)
• Mechanism of inhibition by C-terminal alpha-helices of the epsilon subunit of Escherichia coli FoF1-ATP synthase. (Q42675708) (← links)
• Structural features of the ε subunit of the Escherichia coli ATP synthase determined by NMR spectroscopy (Q42677702) (← links)
• Movement of the helical domain of the epsilon subunit is required for the activation of thermophilic F1-ATPase (Q43027868) (← links)
• The role of the betaDELSEED motif of F1-ATPase: propagation of the inhibitory effect of the epsilon subunit (Q43028555) (← links)
• Dynamic mechanisms driving conformational conversions of the β and ε subunits involved in rotational catalysis of F1-ATPase. (Q43032955) (← links)
• Isolated epsilon subunit of thermophilic F1-ATPase binds ATP. (Q43033766) (← links)
• Binding of dicyclohexylcarbodiimide to a native F1-ATPase-inhibitor protein complex isolated from bovine heart mitochondria (Q43935523) (← links)
• Nucleotide sequence of the genes for β and ε subunits of proton-translocating ATPase from Escherichia coli (Q48404922) (← links)
• Characterization of the alpha and beta-subunits of the F0F1-ATPase from the alga Polytomella spp., a colorless relative of Chlamydomonas reinhardtii. (Q54562312) (← links)
• A barrel in the stalk (Q54601135) (← links)
• Alanine-scanning mutagenesis of the epsilon subunit of the F1-F0 ATP synthase from Escherichia coli reveals two classes of mutants. (Q54601896) (← links)
• Nucleotide-dependent and dicyclohexylcarbodiimide-sensitive conformational changes in the .epsilon. subunit of Escherichia coli ATP synthase (Q54688965) (← links)
• Structure-function relationships of domains of the delta subunit in Escherichia coli adenosine triphosphatase. (Q54691519) (← links)
• An electrochemical study of energy-dependent potassium accumulation in E. coli (Q57768086) (← links)
• Catalytic site nucleotide and inorganic phosphate dependence of the conformation of the .epsilon. subunit in the Escherichia coli adenosinetriphosphatase (Q67897492) (← links)
• Molecular dissection of the epsilon subunit of the chloroplast ATP synthase of spinach (Q70831039) (← links)
• Characterization of the interface between gamma and epsilon subunits of Escherichia coli F1-ATPase (Q71058953) (← links)
• Subunit specific antisera to the Escherichia coli ATP synthase: Effects on ATPase activity, energy transduction, and enzyme assembly (Q72677924) (← links)
• Sulfhydryl groups of the F1 adenosine triphosphatase of Escherichia coli and the stoichiometry of the subunits (Q72809551) (← links)
• Stoichiometry of proton movements coupled to ATP synthesis driven by a pH gradient inStreptococcus lactis (Q72927047) (← links)
• 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 (Q73019327) (← links)
• Functional Consequences of Deletions of the N Terminus of the [epsilon] Subunit of the Chloroplast ATP Synthase (Q74770391) (← links)
• Overexpression, purification, and characterization of human and bovine mitochondrial ATPase inhibitors: comparison of the properties of mammalian and yeast ATPase inhibitors (Q75324551) (← links)
• Rotation of the epsilon subunit during catalysis by Escherichia coli FOF1-ATP synthase (Q77580862) (← links)
• Effect of the epsilon-subunit on nucleotide binding to Escherichia coli F1-ATPase catalytic sites (Q77926922) (← links)
• The regulatory subunit ε in Escherichia coli FOF1-ATP synthase (Q89187364) (← links)