Catalytic site nucleotide binding and hydrolysis in F1F0-ATP synthase.
about
Two ATPasesRole of Charged Residues in the Catalytic Sites of Escherichia coli ATP Synthase.The regulatory switch of F1-ATPase studied by single-molecule FRET in the ABEL Trap.Genetics of acid adaptation in oral streptococci.The cell-free integration of a polytopic mitochondrial membrane protein into liposomes occurs cotranslationally and in a lipid-dependent manner.ATP synthesis driven by proton transport in F1F0-ATP synthase.Significance of αThr-349 in the catalytic sites of Escherichia coli ATP synthase.Genetic and biochemical characterization of the F-ATPase operon from Streptococcus sanguis 10904.Studies of nucleotide binding to the catalytic sites of Escherichia coli betaY331W-F1-ATPase using fluorescence quenching.A model for the cooperative free energy transduction and kinetics of ATP hydrolysis by F1-ATPase.ATP synthase: a molecular therapeutic drug target for antimicrobial and antitumor peptidesMedicinal chemistry of ATP synthase: a potential drug target of dietary polyphenols and amphibian antimicrobial peptides.A functionally important hydrogen-bonding network at the betaDP/alphaDP interface of ATP synthase.The role of the betaDELSEED-loop of ATP synthase.A therapeutic connection between dietary phytochemicals and ATP synthase.Does F1-ATPase have a catalytic site that preferentially binds MgADP?The presence of phosphate at a catalytic site suppresses the formation of the MgADP-inhibited form of F(1)-ATPase.Role of {alpha}-subunit VISIT-DG sequence residues Ser-347 and Gly-351 in the catalytic sites of Escherichia coli ATP synthase.Bi-site catalysis in F1-ATPase: does it exist?Mutagenesis of residue betaArg-246 in the phosphate-binding subdomain of catalytic sites of Escherichia coli F1-ATPase.The binding mechanism of the yeast F1-ATPase inhibitory peptide: role of catalytic intermediates and enzyme turnover.Kinetics of the ATP hydrolysis cycle of the nucleotide-binding domain of Mdl1 studied by a novel site-specific labeling technique.ATP synthase: the right size base model for nanomotors in nanomedicine.Pi binding by the F1-ATPase of beef heart mitochondria and of the Escherichia coli plasma membrane.
P2860
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P2860
Catalytic site nucleotide binding and hydrolysis in F1F0-ATP synthase.
description
1998 nî lūn-bûn
@nan
1998年の論文
@ja
1998年学术文章
@wuu
1998年学术文章
@zh
1998年学术文章
@zh-cn
1998年学术文章
@zh-hans
1998年学术文章
@zh-my
1998年学术文章
@zh-sg
1998年學術文章
@yue
1998年學術文章
@zh-hant
name
Catalytic site nucleotide binding and hydrolysis in F1F0-ATP synthase.
@en
Catalytic site nucleotide binding and hydrolysis in F1F0-ATP synthase.
@nl
type
label
Catalytic site nucleotide binding and hydrolysis in F1F0-ATP synthase.
@en
Catalytic site nucleotide binding and hydrolysis in F1F0-ATP synthase.
@nl
prefLabel
Catalytic site nucleotide binding and hydrolysis in F1F0-ATP synthase.
@en
Catalytic site nucleotide binding and hydrolysis in F1F0-ATP synthase.
@nl
P2093
P356
P1433
P1476
Catalytic site nucleotide binding and hydrolysis in F1F0-ATP synthase.
@en
P2093
P304
10846-10853
P356
10.1021/BI9807153
P407
P577
1998-07-01T00:00:00Z