The Subunit delta -Subunit b Domain of the Escherichia coli F1F0 ATPase. THE b SUBUNITS INTERACT WITH F1 AS A DIMER AND THROUGH THE delta SUBUNIT
Andrew Rodgers
Journal of Biological Chemistry, 1997
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The Second Stalk Composed of the b- and delta -subunits Connects F0 to F1 via an alpha -Subunit in the Escherichia coli ATP Synthase
Andrew Rodgers
Journal of Biological Chemistry, 1998
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Nucleotide Binding Drives Conformational Changes in the Isolated α and β Subunits of the F1-ATPase from Escherichia coli
Edgar Contreras
Biochemical and Biophysical Research Communications, 1999
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A Mutation in Which Alanine 128 Is Replaced by Aspartic Acid Abolishes Dimerization of the b-Subunit of the F(0)F(1)-ATPase from Escherichia coli
Andrew Rodgers
Journal of Biological Chemistry, 1996
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Molecular genetics of F1-ATPase fromEscherichia coli
Masamitsu Futai
Journal of Bioenergetics and Biomembranes, 1988
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F1TPase of Escherichia coli: A mutation (uncA401) located in the middle of the α subunit affects the conformation essential for F1 activity
Masamitsu Futai
Archives of Biochemistry and Biophysics, 1984
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Complete DNA sequence of the atp operon of the sodium-dependent F1Fo ATP synthase from Ilyobacter tartaricus and identification of the encoded subunits
Georg Kaim
Biochimica et Biophysica Acta (BBA) - Gene Structure and Expression, 2003
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Mutational replacements of conserved amino acid residues in the α subunit change the catalytic properties of Escherichia coli F1-ATPase
Masamitsu Futai
Archives of Biochemistry and Biophysics, 1989
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Mutations in the conserved proline 43 residue of the uncE protein (subunit c) of Escherichia coli F1F0-ATPase alter the coupling of F1 to F0
Dean Fraga
Journal of Biological Chemistry, 1989
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Mechanism of F1-ATPase studied by the genetic approach
Masamitsu Futai
Journal of Bioenergetics and Biomembranes, 1988
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The atp operon: nucleotide sequence of the genes for the γ, β, and ε subunits of Escherichia coli ATP synthase
Alex Eberle
Nucleic Acids Research, 1981
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Mapping of antigenic sites to monoclonal antibodies on the primary structure of the F1-ATPase β subunit from Escherichia coli: Concealed amino-terminal region of the subunit in the F1
Masamitsu Futai
Archives of Biochemistry and Biophysics, 1992
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Escherichia coli ATP synthase (F-ATPase): catalytic site and regulation of H+ translocation
Masamitsu Futai
The Journal of experimental biology, 1992
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Role of the amino terminal region of the ϵ subunit of Escherichia coli H+-ATPase (FoF1)
Masamitsu Futai
Archives of Biochemistry and Biophysics, 1992
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Molecular Mechanism of the ATP Synthase's Fo Motor Probed by Mutational Analyses of Subunit a
Georg Kaim
Journal of Molecular Biology, 2002
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Role of the carboxyl terminal region of H+-ATPase (F0F1 a subunit from Escherichia coli
Masamitsu Futai
Archives of Biochemistry and Biophysics, 1991
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Deletion of seven amino acid residues from the γ subunit of Escherichia coli H+-ATPase causes total loss of F1 assembly on membranes
Masamitsu Futai
Archives of Biochemistry and Biophysics, 1985
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A functional chimeric membrane subunit of an ion-translocating ATPase
DEXIAN DOU
Antonie van Leeuwenhoek, 1994
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An intermediate step in the evolution of ATPases - a hybrid F0-V0 rotor in a bacterial Na+ F1F0 ATP synthase
Nina Morgner
FEBS Journal, 2008
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The properties of hybrid F1-ATPase enzymes suggest that a cyclical catalytic mechanism involving three catalytic sites occurs.
Rajini Rao
Journal of Biological Chemistry, 1987
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Escherichia coli mutants defective in the γ subunit of proton-translocating ATPase: Intracistronic mapping of the defective site and the biochemical properties of the mutants
Masamitsu Futai
Archives of Biochemistry and Biophysics, 1983
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F1-ATPase of Escherichia coli: The epsilon-inhibited state forms after ATP hydrolysis, is distinct from the ADP-inhibited state, and responds dynamically to catalytic site ligands
Tom Duncan
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F1-ATPase of Escherichia coli: THE -INHIBITED STATE FORMS AFTER ATP HYDROLYSIS, IS DISTINCT FROM THE ADP-INHIBITED STATE, AND RESPONDS DYNAMICALLY TO CATALYTIC SITE LIGANDS
Tom Duncan
Journal of Biological Chemistry, 2013
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Structure–function relationships in an anion-translocating ATPase
Adrian Walmsley
2000
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Escherichia coli H+-ATPase: Role of the δ subunit in binding F1 to the F0 sector
Masamitsu Futai
Archives of Biochemistry and Biophysics, 1992
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Release of the α subunit of coupling factor F1 ATPase from membranes of an uncoupled mutant of Escherichia coli
Masamitsu Futai
FEBS Letters, 1980
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Charge Displacements during ATP-Hydrolysis and Synthesis of the Na+-Transporting FoF1-ATPase of Ilyobacter tartaricus
Georg Kaim
Biophysical Journal, 2003
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Directed mutagenesis of the strongly conserved lysine 175 in the proposed nucleotide-binding domain of alpha-subunit from Escherichia coli F1-ATPase.
Rajini Rao
Journal of Biological Chemistry, 1988
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Escherichia coli H+-ATPase: Loss of the carboxyl terminal region of the γ subunit causes defective assembly of the F1 portion
Masamitsu Futai
Archives of Biochemistry and Biophysics, 1986
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The ϵ subunit as an ATPase inhibitor of the F1-ATPase in Escherichia coli
Georges Dreyfus
Archives of Biochemistry and Biophysics, 1984
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Nucleotide sequence of the promoter region of the gene cluster for proton-translocating ATPase from Escherichiacoli and identification of the active promoter
MARINA FREGNI
Biochemical and Biophysical Research Communications, 1982
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Subunits of the H+-ATPase of Escherichia coli. Overproduction of an eight-subunit F1F0-ATPase following induction of a λ-transducing phage carrying the unc operon
Masamitsu Futai
Journal of Biological Chemistry
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Essential residues in the polar loop region of subunit c of Escherichia coli F1F0 ATP synthase defined by random oligonucleotide-primed mutagenesis
Dean Fraga
Journal of bacteriology, 1991
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Overproduction of subunit a of the F0 component of proton-translocating ATPase inhibits growth of Escherichia coli cells
Masamitsu Futai
Journal of bacteriology, 1984
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Sec/SRP Requirements and Energetics of Membrane Insertion of Subunits a, b, and c of the Escherichia coli F1F0 ATP Synthase
Minyong Chen
Journal of Biological Chemistry, 2004
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