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The defective proton-ATPase of uncA mutants of Escherichia coli. Studies of nucleotide binding sites, bound aurovertin fluorescence, and labeling of essential residues of the purified F1-ATPase.

Data up to Jan 2025

Published1981
Citations110
References38

Total Citations Per Year

Abstract

References (38)

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1980 • 118 citations

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1981 • 118 citations

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1980 • 59 citations

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1980 • 57 citations

Reactivity of the .beta. subunit of Escherichia coli adenosine triphosphatase with 4-chloro-7-nitrobenzofurazan

1979 • 50 citations

Identfication of the altered subunit in the inactive F1ATPase of an Escherichia coli uncA mutant

1978 • 49 citations

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1978 • 46 citations

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1977 • 40 citations

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1980 • 40 citations

The binding of aurovertin to isolated F1 (mitochondrial ATPase)

1977 • 40 citations

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1981 • 37 citations

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1980 • 30 citations

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1979 • 25 citations

Effect of ATP on the translational diffusion coefficient of the α‐subunit of Escherichia coli F1‐ATPase

1980 • 20 citations

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1980 • 11 citations

The uncA401 mutation alters a nucleotide‐binding site in the α‐subunit of the F1 adenosine triphosphatase from Escherichia coli

1980 • 6 citations

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The defective proton-ATPase of uncA mutants of Escherichia coli. Studies of nucleotide… (1981) – Journal of Biological Chemistry | Metascience Observatory Explorer