about
Interacting cytoplasmic loops of subunits a and c of Escherichia coli F1F0 ATP synthase gate H+ transport to the cytoplasm.Na⁺-substrate coupling in the multidrug antiporter norm probed with a spin-labeled substrate.Structure and pH-induced structural rearrangements of the putative multidrug efflux pump EmrD in liposomes probed by site-directed spin labeling.Residues in the polar loop of subunit c in Escherichia coli ATP synthase function in gating proton transport to the cytoplasm.Half channels mediating H(+) transport and the mechanism of gating in the Fo sector of Escherichia coli F1Fo ATP synthase.Subunit a facilitates aqueous access to a membrane-embedded region of subunit c in Escherichia coli F1F0 ATP synthase.Sodium and proton coupling in the conformational cycle of a MATE antiporter from Vibrio cholerae
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description
investigador
@es
researcher
@en
wetenschapper
@nl
name
P Ryan Steed
@en
P Ryan Steed
@nl
type
label
P Ryan Steed
@en
P Ryan Steed
@nl
prefLabel
P Ryan Steed
@en
P Ryan Steed
@nl
P108
P31
P496
0000-0001-5445-0080