Membrane integration and function of the three F0 subunits of the ATP synthase of Escherichia coli K12.
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Evidence for the involvement of coupling factor B in the H+ channel of the mitochondrial H+-ATPaseDNA sequence of a gene cluster coding for subunits of the F0 membrane sector of ATP synthase in Rhodospirillum rubrum. Support for modular evolution of the F1 and F0 sectorsHigh-resolution definition of the Vibrio cholerae essential gene set with hidden Markov model-based analyses of transposon-insertion sequencing dataLigand-dependent structural variations in Escherichia coli F1 ATPase revealed by cryoelectron microscopyEnergetics of Respiration and Oxidative Phosphorylation in Mycobacteria.Synthesis of a functional F0 sector of the Escherichia coli H+-ATPase does not require synthesis of the alpha or beta subunits of F1Physiology of mycobacteriaSubunit b of the membrane moiety (F0) of ATP synthase (F1F0) from Escherichia coli is indispensable for H+ translocation and binding of the water-soluble F1 moiety.An additional acidic residue in the membrane portion of the b-subunit of the energy-transducing adenosine triphosphatase of Escherichia coli affects both assembly and function.Oxidative Phosphorylation as a Target Space for Tuberculosis: Success, Caution, and Future Directions.Bacterial adenosine 5'-triphosphate synthase (F1F0): purification and reconstitution of F0 complexes and biochemical and functional characterization of their subunits.Hemin reconstitutes proton extrusion in an H(+)-ATPase-negative mutant of Lactococcus lactis.Limited differential mRNA inactivation in the atp (unc) operon of Escherichia coliCarbon and energy metabolism of atp mutants of Escherichia coli.Overproduction of truncated subunit a of H+-ATPase causes growth inhibition of Escherichia coli.Structure and function of proton-translocating adenosine triphosphatase (F0F1): biochemical and molecular biological approaches.All three subunits are required for the reconstitution of an active proton channel (F0) of Escherichia coli ATP synthase (F1F0).Proton conduction by subunit a of the membrane-bound ATP synthase of Escherichia coli revealed after induced overproduction.The topology of the proton translocating F0 component of the ATP synthase from E. coli K12: studies with proteases.The F1Fo-ATP synthase of Mycobacterium smegmatis is essential for growth.
P2860
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P2860
Membrane integration and function of the three F0 subunits of the ATP synthase of Escherichia coli K12.
description
1983 nî lūn-bûn
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1983年の論文
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1983年論文
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1983年論文
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1983年論文
@zh-hk
1983年論文
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1983年論文
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1983年论文
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1983年论文
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1983年论文
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name
Membrane integration and funct ...... thase of Escherichia coli K12.
@en
type
label
Membrane integration and funct ...... thase of Escherichia coli K12.
@en
prefLabel
Membrane integration and funct ...... thase of Escherichia coli K12.
@en
P2093
P2860
P1433
P1476
Membrane integration and funct ...... thase of Escherichia coli K12.
@en
P2093
Gunsalus RP
Michelsen O
Schairer HU
von Meyenburg K
P2860
P304
P407
P577
1983-01-01T00:00:00Z