Engineering rotor ring stoichiometries in the ATP synthase. - Wikidata - awgldk - TriplyDB

Engineering rotor ring stoichiometries in the ATP synthase.

Engineering rotor ring stoichiometries in the ATP synthase.

http://www.wikidata.org/entity/Q36056515

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Alkaliphilic Bacteria with Impact on Industrial Applications, Concepts of Early Life Forms, and Bioenergetics of ATP Synthesis Life under extreme energy limitation: a synthesis of laboratory- and field-based investigations The c-ring stoichiometry of ATP synthase is adapted to cell physiological requirements of alkaliphilic Bacillus pseudofirmus OF4 A new type of Na(+)-driven ATP synthase membrane rotor with a two-carboxylate ion-coupling motif The c-ring ion binding site of the ATP synthase fromBacillus pseudofirmus OF4 is adapted to alkaliphilic lifestyle Rotary ATPases: models, machine elements and technical specifications The function of the Na+-driven flagellum of Vibrio cholerae is determined by osmolality and pH High-resolution structure and mechanism of an F/V-hybrid rotor ring in a Na⁺-coupled ATP synthase Three distinct isoforms of ATP synthase subunit c are expressed in T. brucei and assembled into the mitochondrial ATP synthase complex On the principle of ion selectivity in Na+/H+-coupled membrane proteins: experimental and theoretical studies of an ATP synthase rotor.Spatio-temporal resolution of primary processes of photosynthesis.Serine 26 in the PomB subunit of the flagellar motor is essential for hypermotility of Vibrio cholerae.Diverse high-torque bacterial flagellar motors assemble wider stator rings using a conserved protein scaffold The Phylogenetic Signature Underlying ATP Synthase c-Ring Compliance.Biophysical comparison of ATP-driven proton pumping mechanisms suggests a kinetic advantage for the rotary process depending on coupling ratio.Biophysical comparison of ATP synthesis mechanisms shows a kinetic advantage for the rotary process.Structure and mechanism of the ATP synthase membrane motor inferred from quantitative integrative modeling.Atomistic simulations indicate the c-subunit ring of the F1Fo ATP synthase is not the mitochondrial permeability transition pore.Evolution of Na(+) and H(+) bioenergetics in methanogenic archaea.Half a century of molecular bioenergetics.Evolution of peroxisomes illustrates symbiogenesis.Catalytic robustness and torque generation of the F1-ATPase Predicted Structures of the Proton-Bound Membrane-Embedded Rotor Rings of the Saccharomyces cerevisiae and Escherichia coli ATP Synthases.Tuning the size and properties of ClyA nanopores assisted by directed evolution.Molecular architecture of the N-type ATPase rotor ring from Burkholderia pseudomallei.A mechano-chemiosmotic model for the coupling of electron and proton transfer to ATP synthesis in energy-transforming membranes: a personal perspective.The Minimum Biological Energy Quantum.Role of the N-terminal signal peptide in the membrane insertion of Aquifex aeolicus F1F0 ATP synthase c-subunit.In silico analysis of the regulation of the photosynthetic electron transport chain in C3 plants.Energy costs of carbon dioxide concentrating mechanisms in aquatic organisms.Horizontal membrane-intrinsic α-helices in the stator a-subunit of an F-type ATP synthase.Mitochondrial permeability transition involves dissociation of F1FO ATP synthase dimers and C-ring conformation.An exploration of how the thermodynamic efficiency of bioenergetic membrane systems varies with c-subunit stoichiometry of F₁F₀ ATP synthases.Mussel and mammalian ATP synthase share the same bioenergetic cost of ATP.Enhanced biofuel production using optimality, pathway modification and waste minimization The Peripheral Stalk of Rotary ATPases

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P2860

Engineering rotor ring stoichiometries in the ATP synthase.

http://www.wikidata.org/entity/Q36056515

description

2012 nî lūn-bûn

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2012年の論文

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2012年論文

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2012年論文

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2012年論文

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2012年論文

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2012年論文

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2012年论文

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2012年论文

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2012年论文

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name

Engineering rotor ring stoichiometries in the ATP synthase.

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Engineering rotor ring stoichiometries in the ATP synthase.

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Engineering rotor ring stoichiometries in the ATP synthase.

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Engineering rotor ring stoichiometries in the ATP synthase.

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Engineering rotor ring stoichiometries in the ATP synthase.

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Engineering rotor ring stoichiometries in the ATP synthase.

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PNAS.1120027109

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Proceedings of the National Academy of Sciences of the United States of America

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Engineering rotor ring stoichiometries in the ATP synthase.

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Adriana L Klyszejko

http://www.w3.org/2001/XMLSchema#string

Daniel J Müller

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Denys Pogoryelov

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Eva-Maria Heller

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Ganna O Krasnoselska

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Janet Vonck

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José D Faraldo-Gómez

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Julian D Langer

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Thomas Meier

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Vanessa Leone

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P2860

A new type of proton coordination in an F(1)F(o)-ATP synthase rotor ring

Effects of carbon source on expression of F0 genes and on the stoichiometry of the c subunit in the F1F0 ATPase of Escherichia coli

Molecular architecture of the rotary motor in ATP synthase

Complete ion-coordination structure in the rotor ring of Na+-dependent F-ATP synthases

High-resolution structure of the rotor ring of a proton-dependent ATP synthase

Bioenergetic cost of making an adenosine triphosphate molecule in animal mitochondria

Microscopic rotary mechanism of ion translocation in the F(o) complex of ATP synthases

Structure at 2.8 A resolution of F1-ATPase from bovine heart mitochondria

A transmembrane helix dimer: structure and implications

Solution structure of the transmembrane H+-transporting subunit c of the F1F0 ATP synthase

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10.1073/PNAS.1120027109

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25

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109

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2012-05-24T00:00:00Z

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225044552

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22628564

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3382517

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