Recent Publications on Bacterial Proton-Translocating Atpases: |  |
Protein disorder is positively correlated with gene expression in Escherichia coli.
We considered, on a global scale, the relationship between the predicted...
Direct Link | 22nd August, 2008
| Department of Biochemistry and Molecular Biology, Wright State University,
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Regulatory mechanisms of proton-translocating F(O)F (1)-ATP synthase.
H(+)-F(O)F(1)-ATP synthase catalyzes synthesis of ATP from ADP and...
Direct Link | 15th August, 2008
| Exploratory Research for Advanced Technology, Japan Science and Technology
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The stoichiometry of subunit c of Escherichia coli ATP synthase is independent of its rate of synthesis.
Immunoblot quantitation of Escherichia coli ATP synthase isolated from atp...
Direct Link | 22nd July, 2008
| Abteilung Mikrobiologie, Fachbereich Biologie/Chemie, Universitat
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Arginine-induced conformational change in the c-ring/a-subunit interface of ATP synthase.
The rotational mechanism of ATP synthases requires a unique interface...
Direct Link | 10th July, 2008
| Institut fur Mikrobiologie, ETH Zurich Honggerberg, Switzerland.
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An intermediate step in the evolution of ATPases: a hybrid F(0)-V(0) rotor in a bacterial Na(+) F(1)F(0) ATP synthase.
The Na(+) F(1)F(0) ATP synthase operon of the anaerobic, acetogenic...
Direct Link | 10th July, 2008
| Molecular Microbiology & Bioenergetics, Institute of Molecular
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GFT projection NMR based resonance assignment of membrane proteins: application to subunit C of E. coli F(1)F (0) ATP synthase in LPPG micelles.
G-matrix FT projection NMR spectroscopy was employed for resonance...
Direct Link | 13th June, 2008
| Department of Chemistry, State University of New York at Buffalo, Buffalo,
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Remarkable stability of the proton translocating F1FO-ATP synthase from the thermophilic cyanobacterium Thermosynechococcus elongatus BP-1.
For functional characterization, we isolated the F1FO-ATP synthase of the...
Direct Link | 10th June, 2008
| Physical Biochemistry, Department of Chemistry, Darmstadt University of
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The charge distribution in the cytoplasmic loop of subunit C of the F1F0 ATPase is a determinant for YidC targeting.
YidC is a member of the Oxa1 family of proteins that facilitates the...
Direct Link | 29th May, 2008
| Department of Molecular Microbiology, Groningen Biomolecular Sciences and
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Interaction of transmembrane helices in ATP synthase subunit a in solution as revealed by spin label difference NMR.
Subunit a in the membrane traversing F0 sector of Escherichia coli ATP...
Direct Link | 9th April, 2008
| Department of Biomolecular Chemistry, University of Wisconsin School of
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Stoichiometry and localization of the stator subunits E and G in Thermus thermophilus H+-ATPase/synthase.
Proton-translocating ATPases are central to biological energy conversion....
Direct Link | 3rd April, 2008
| Laboratory of Molecular Biology, Medical Research Council, Hills Road,
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UncI protein can mediate ring-assembly of c-subunits of FoF1-ATP synthase in vitro.
In F(o)F(1)-ATP synthase, multimeric c-subunits are assembled to a ring...
Direct Link | 5th March, 2008
| Chemical Resources Laboratory, Tokyo Institute of Technology, 4259
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Phylogenetic analysis of vibrios and related species by means of atpA gene sequences.
We investigated the use of atpA gene sequences as alternative phylogenetic...
Direct Link | 8th January, 2008
| Instituto Oswaldo
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Heterogeneity of photosynthetic membranes from Rhodobacter capsulatus: size dispersion and ATP synthase distribution.
The density distribution of photosynthetic membrane vesicles...
Direct Link | 20th December, 2007
| Department of Biology, University of Bologna, Laboratory of Biochemistry
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| Regulation of the phage-shock-protein stress response in Yersinia enterocolitica.
| 8th December, 2007
| Department of Microbiology, New York University School of Medicine, New
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Two distinct proton binding sites in the ATP synthase family.
The F1F0 ATP synthase utilizes energy stored in an electrochemical...
Direct Link | 6th December, 2007
| Institut fur Mikrobiologie, ETH Zurich, Wolfgang-Pauli-Strasse 10, CH-8093
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