Oxidative phosphorylation in Escherichia coli. Characterization of mutant strains in which F1-ATPase contains abnormal beta-subunits.
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Two ATPasesInhibition of Escherichia coli ATP synthase by amphibian antimicrobial peptides.Dietary bioflavonoids inhibit Escherichia coli ATP synthase in a differential manner.Significance of αThr-349 in the catalytic sites of Escherichia coli ATP synthase.Effect of structural modulation of polyphenolic compounds on the inhibition of Escherichia coli ATP synthaseA model for the catalytic site of F1-ATPase based on analogies to nucleotide-binding domains of known structure.Thymoquinone Inhibits Escherichia coli ATP Synthase and Cell Growth.Asp residues of βDELSEED-motif are required for peptide binding in the Escherichia coli ATP synthaseA functionally important hydrogen-bonding network at the betaDP/alphaDP interface of ATP synthase.The role of the betaDELSEED-loop of ATP synthase.Escherichia coli F1Fo-ATP synthase with a b/δ fusion protein allows analysis of the function of the individual b subunits.ATP synthase with its gamma subunit reduced to the N-terminal helix can still catalyze ATP synthesisThe proton-ATPase of bacteria and mitochondria.Structure and function of proton-translocating adenosine triphosphatase (F0F1): biochemical and molecular biological approaches.Random mutagenesis of the gene for the beta-subunit of F1-ATPase from Escherichia coli.Assembly of the stator in Escherichia coli ATP synthase. Complexation of alpha subunit with other F1 subunits is prerequisite for delta subunit binding to the N-terminal region of alpha.Properties of F1-ATPase from the uncD412 mutant of Escherichia coli.Role of {alpha}-subunit VISIT-DG sequence residues Ser-347 and Gly-351 in the catalytic sites of Escherichia coli ATP synthase.Mutagenesis of residue betaArg-246 in the phosphate-binding subdomain of catalytic sites of Escherichia coli F1-ATPase.Functional importance of αIle-346 and αIle-348 in the catalytic sites of Escherichia coli ATP synthase.Modulation of charge in the phosphate binding site of Escherichia coli ATP synthase.Photosynthetic ATPases: purification, properties, subunit isolation and function.Safranal and its analogs inhibit Escherichia coli ATP synthase and cell growth.Understanding the link between antimicrobial properties of dietary olive phenolics and bacterial ATP synthase.Venom peptides cathelicidin and lycotoxin cause strong inhibition of Escherichia coli ATP synthase.
P2860
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P2860
Oxidative phosphorylation in Escherichia coli. Characterization of mutant strains in which F1-ATPase contains abnormal beta-subunits.
description
1983 nî lūn-bûn
@nan
1983年の論文
@ja
1983年学术文章
@wuu
1983年学术文章
@zh-cn
1983年学术文章
@zh-hans
1983年学术文章
@zh-my
1983年学术文章
@zh-sg
1983年學術文章
@yue
1983年學術文章
@zh
1983年學術文章
@zh-hant
name
Oxidative phosphorylation in E ...... ntains abnormal beta-subunits.
@en
Oxidative phosphorylation in E ...... ntains abnormal beta-subunits.
@nl
type
label
Oxidative phosphorylation in E ...... ntains abnormal beta-subunits.
@en
Oxidative phosphorylation in E ...... ntains abnormal beta-subunits.
@nl
prefLabel
Oxidative phosphorylation in E ...... ntains abnormal beta-subunits.
@en
Oxidative phosphorylation in E ...... ntains abnormal beta-subunits.
@nl
P2093
P2860
P356
P1433
P1476
Oxidative phosphorylation in E ...... ntains abnormal beta-subunits.
@en
P2093
P2860
P304
P356
10.1042/BJ2100395
P407
P577
1983-02-01T00:00:00Z