Modulation of charge in the phosphate binding site of Escherichia coli ATP synthase. - Wikidata - awgldk - TriplyDB

Modulation of charge in the phosphate binding site of Escherichia coli ATP synthase.

Modulation of charge in the phosphate binding site of Escherichia coli ATP synthase.

http://www.wikidata.org/entity/Q46531306

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Two ATPases Inhibition of Escherichia coli ATP synthase by amphibian antimicrobial peptides.Dietary bioflavonoids inhibit Escherichia coli ATP synthase in a differential manner.Role of Charged Residues in the Catalytic Sites of Escherichia coli ATP Synthase.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 synthase Residue propensities, discrimination and binding site prediction of adenine and guanine phosphates.Thymoquinone Inhibits Escherichia coli ATP Synthase and Cell Growth.Asp residues of βDELSEED-motif are required for peptide binding in the Escherichia coli ATP synthase ATP synthase: a molecular therapeutic drug target for antimicrobial and antitumor peptides Medicinal chemistry of ATP synthase: a potential drug target of dietary polyphenols and amphibian antimicrobial peptides.Conformational transitions of subunit epsilon in ATP synthase from thermophilic Bacillus PS3 Role of {alpha}-subunit VISIT-DG sequence residues Ser-347 and Gly-351 in the catalytic sites of Escherichia coli ATP synthase.Functional importance of αIle-346 and αIle-348 in the catalytic sites of Escherichia coli ATP synthase.ATP synthase: the right size base model for nanomotors in nanomedicine.

P2860

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P2860

Modulation of charge in the phosphate binding site of Escherichia coli ATP synthase.

http://www.wikidata.org/entity/Q46531306

description

2005 nî lūn-bûn

@nan

2005年の論文

@ja

2005年学术文章

@wuu

2005年学术文章

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2005年学术文章

@zh-cn

2005年学术文章

@zh-hans

2005年学术文章

@zh-my

2005年学术文章

@zh-sg

2005年學術文章

@yue

2005年學術文章

@zh-hant

name

Modulation of charge in the phosphate binding site of Escherichia coli ATP synthase.

@en

Modulation of charge in the phosphate binding site of Escherichia coli ATP synthase.

@nl

type

label

Modulation of charge in the phosphate binding site of Escherichia coli ATP synthase.

@en

Modulation of charge in the phosphate binding site of Escherichia coli ATP synthase.

@nl

prefLabel

Modulation of charge in the phosphate binding site of Escherichia coli ATP synthase.

@en

Modulation of charge in the phosphate binding site of Escherichia coli ATP synthase.

@nl

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P1433

Journal of Biological Chemistry

P1476

Modulation of charge in the phosphate binding site of Escherichia coli ATP synthase.

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P2093

Alan E Senior

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P2860

Structural model of F1-ATPase and the implications for rotary catalysis

Cleavage of structural proteins during the assembly of the head of bacteriophage T4

Structure of bovine mitochondrial F(1)-ATPase inhibited by Mg(2+) ADP and aluminium fluoride

Structure of bovine mitochondrial F(1)-ATPase with nucleotide bound to all three catalytic sites: implications for the mechanism of rotary catalysis

Bovine F1-ATPase covalently inhibited with 4-chloro-7-nitrobenzofurazan: the structure provides further support for a rotary catalytic mechanism

The mitochondrial ATPase. Selective modification of a nitrogen residue in the beta subunit

The Escherichia coli FOF1 gammaM23K uncoupling mutant has a higher K0.5 for Pi. Transition state analysis of this mutant and others reveals that synthesis and hydrolysis utilize the same kinetic pathway.

Intergenic suppression of the gammaM23K uncoupling mutation in F0F1 ATP synthase by betaGlu-381 substitutions: the role of the beta380DELSEED386 segment in energy coupling.

Chemomechanical coupling in F1-ATPase revealed by simultaneous observation of nucleotide kinetics and rotation.

The rotary machine in the cell, ATP synthase.

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27981-27989

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scholarly article

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10.1074/JBC.M503955200

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30

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280

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15939739

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