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Bioenergetics of the Archaea.Cloning, characterization and mapping of the human ATP5E gene, identification of pseudogene ATP5EP1, and definition of the ATP5E motifThe rotary mechanism of the ATP synthase.Two ATPasesSite-directed mutagenesis of the 100-kDa subunit (Vph1p) of the yeast vacuolar (H+)-ATPase.A novel secretion pathway of Salmonella enterica acts as an antivirulence modulator during salmonellosisThe ATP synthase gamma subunit. Suppressor mutagenesis reveals three helical regions involved in energy coupling.Energy coupling, turnover, and stability of the F0F1 ATP synthase are dependent on the energy of interaction between gamma and beta subunits.A mutation in the Escherichia coli F0F1-ATP synthase rotor, gammaE208K, perturbs conformational coupling between transport and catalysis.The regulator of the F1 motor: inhibition of rotation of cyanobacterial F1-ATPase by the epsilon subunit.The gamma subunit in chloroplast F(1)-ATPase can rotate in a unidirectional and counter-clockwise manner.The products of the mitochondrial orf25 and orfB genes are FO components in the plant F1FO ATP synthase.Salmonella typhimurium mutants defective in flagellar filament regrowth and sequence similarity of FliI to F0F1, vacuolar, and archaebacterial ATPase subunitsIdentification of an intragenic ribosome binding site that affects expression of the uncB gene of the Escherichia coli proton-translocating ATPase (unc) operon.Rotation of subunits during catalysis by Escherichia coli F1-ATPasePurification and characterization of the N-terminal domain of ExeA: a novel ATPase involved in the type II secretion pathway of Aeromonas hydrophilaThe phage shock protein PspA facilitates divalent metal transport and is required for virulence of Salmonella enterica sv. Typhimurium.The oxidative phosphorylation (OXPHOS) system: nuclear genes and human genetic diseases.Translation initiation rate determines the impact of ribosome stalling on bacterial protein synthesis.Proteomics and transcriptomics characterization of bile stress response in probiotic Lactobacillus rhamnosus GG.Functional genomic analysis of bile salt resistance in Enterococcus faeciumA bovine cDNA and a yeast gene (VMA8) encoding the subunit D of the vacuolar H(+)-ATPase.Characterization of the relationship between ADP- and epsilon-induced inhibition in cyanobacterial F1-ATPaseF-type ATPases: are nucleotide domains in adenylate kinase appropriate models for nucleotide domains in ATP synthase/ATPase complexes?A FRET-based DNA biosensor tracks OmpR-dependent acidification of Salmonella during macrophage infection.Construction and plasmid-borne complementation of strains lacking the epsilon subunit of the Escherichia coli F1F0 ATP synthaseMutagenic analysis of the a subunit of the F1F0 ATP synthase in Escherichia coli: Gln-252 through Tyr-263Complementation between nucleotide binding domains in an anion-translocating ATPase.Stepped versus continuous rotatory motors at the molecular scale.Role of the delta subunit in enhancing proton conduction through the F0 of the Escherichia coli F1F0 ATPase.Targeted mutagenesis of the b subunit of F1F0 ATP synthase in Escherichia coli: Glu-77 through Gln-85.Large conformational changes of the epsilon subunit in the bacterial F1F0 ATP synthase provide a ratchet action to regulate this rotary motor enzyme.Accumulation of newly synthesized F1 in vivo in arabidopsis mitochondria provides evidence for modular assembly of the plant F1Fo ATP synthase.Topographical structure of membrane-bound Escherichia coli F1F0 ATP synthase in aqueous buffer.Control of a Salmonella virulence locus by an ATP-sensing leader messenger RNAA bacterial virulence protein promotes pathogenicity by inhibiting the bacterium's own F1Fo ATP synthase.Second-site revertants of an arginine-210 to lysine mutation in the a subunit of the F0F1-ATPase from Escherichia coli: implications for structure.Mitochondrial Complex V α Subunit Is Critical for Candida albicans Pathogenicity through Modulating Multiple Virulence Properties.Bacterial Mg2+ homeostasis, transport, and virulence.Arginine residue at position 573 in Enterococcus hirae vacuolar-type ATPase NtpI subunit plays a crucial role in Na+ translocation.
P2860
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P2860
description
article científic
@ca
article scientifique
@fr
articolo scientifico
@it
artigo científico
@pt
bilimsel makale
@tr
scientific article published on January 1990
@en
vedecký článok
@sk
vetenskaplig artikel
@sv
videnskabelig artikel
@da
vědecký článek
@cs
name
The proton-translocating ATPase of Escherichia coli.
@en
The proton-translocating ATPase of Escherichia coli.
@nl
type
label
The proton-translocating ATPase of Escherichia coli.
@en
The proton-translocating ATPase of Escherichia coli.
@nl
prefLabel
The proton-translocating ATPase of Escherichia coli.
@en
The proton-translocating ATPase of Escherichia coli.
@nl
P1476
The proton-translocating ATPase of Escherichia coli.
@en
P2093
P356
10.1146/ANNUREV.BB.19.060190.000255
P577
1990-01-01T00:00:00Z