The structural basis for unidirectional rotation of thermoalkaliphilic F1-ATPase
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Asymmetric Structure of the Yeast F1 ATPase in the Absence of Bound NucleotidesStructure of a thermophilic F1-ATPase inhibited by an ε-subunit: deeper insight into the ε-inhibition mechanismF1-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.Three-dimensional structure of A1A0 ATP synthase from the hyperthermophilic archaeon Pyrococcus furiosus by electron microscopy.F1F0-ATP synthases of alkaliphilic bacteria: lessons from their adaptations.The ATP synthase a-subunit of extreme alkaliphiles is a distinct variant: mutations in the critical alkaliphile-specific residue Lys-180 and other residues that support alkaliphile oxidative phosphorylation.Structure of the ATP synthase catalytic complex (F(1)) from Escherichia coli in an autoinhibited conformation.Draft genome sequence of the thermoalkaliphilic Caldalkalibacillus thermarum strain TA2.A1.Aerobic Growth of Escherichia coli Is Reduced, and ATP Synthesis Is Selectively Inhibited when Five C-terminal Residues Are Deleted from the ϵ Subunit of ATP Synthase.Purification, characterization and crystallization of the F-ATPase from Paracoccus denitrificansStructure of ATP synthase from Paracoccus denitrificans determined by X-ray crystallography at 4.0 Å resolution.Structural Basis for a Unique ATP Synthase Core Complex from Nanoarcheaum equitans.Improved crystallization of Escherichia coli ATP synthase catalytic complex (F1) by introducing a phosphomimetic mutation in subunit ε.A functionally important hydrogen-bonding network at the betaDP/alphaDP interface of ATP synthase.Regulation of the thermoalkaliphilic F1-ATPase from Caldalkalibacillus thermarumRegulation of the F1F0-ATP synthase rotary nanomotor in its monomeric-bacterial and dimeric-mitochondrial formsThe uniqueness of subunit α of mycobacterial F-ATP synthases: An evolutionary variant for niche adaptation.Structure of a Complete ATP Synthase Dimer Reveals the Molecular Basis of Inner Mitochondrial Membrane MorphologyStructure of a catalytic dimer of the α- and β-subunits of the F-ATPase from Paracoccus denitrificans at 2.3 Å resolution.Probing the rotor subunit interface of the ATP synthase from Ilyobacter tartaricus.Biophysical Characterization of a Thermoalkaliphilic Molecular Motor with a High Stepping Torque Gives Insight into Evolutionary ATP Synthase Adaptation.Deleting the IF1-like ζ subunit from Paracoccus denitrificans ATP synthase is not sufficient to activate ATP hydrolysis.Insights into the regulatory function of the ɛ subunit from bacterial F-type ATP synthases: a comparison of structural, biochemical and biophysical data.
P2860
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P2860
The structural basis for unidirectional rotation of thermoalkaliphilic F1-ATPase
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2007 nî lūn-bûn
@nan
2007 թուականի Օգոստոսին հրատարակուած գիտական յօդուած
@hyw
2007 թվականի օգոստոսին հրատարակված գիտական հոդված
@hy
2007年の論文
@ja
2007年論文
@yue
2007年論文
@zh-hant
2007年論文
@zh-hk
2007年論文
@zh-mo
2007年論文
@zh-tw
2007年论文
@wuu
name
The structural basis for unidirectional rotation of thermoalkaliphilic F1-ATPase
@ast
The structural basis for unidirectional rotation of thermoalkaliphilic F1-ATPase
@en
The structural basis for unidirectional rotation of thermoalkaliphilic F1-ATPase
@nl
type
label
The structural basis for unidirectional rotation of thermoalkaliphilic F1-ATPase
@ast
The structural basis for unidirectional rotation of thermoalkaliphilic F1-ATPase
@en
The structural basis for unidirectional rotation of thermoalkaliphilic F1-ATPase
@nl
prefLabel
The structural basis for unidirectional rotation of thermoalkaliphilic F1-ATPase
@ast
The structural basis for unidirectional rotation of thermoalkaliphilic F1-ATPase
@en
The structural basis for unidirectional rotation of thermoalkaliphilic F1-ATPase
@nl
P2093
P3181
P1433
P1476
The structural basis for unidirectional rotation of thermoalkaliphilic F1-ATPase
@en
P2093
Gregory M Cook
Janet Vonck
Stefanie Keis
P304
P3181
P356
10.1016/J.STR.2007.06.009
P577
2007-08-01T00:00:00Z