Functional domains of the ATPase inhibitor protein from bovine heart mitochondria. (Q53978171)

23 May 2018

title

Functional domains of the ATPase inhibitor protein from bovine heart mitochondria. (English)

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4

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author name string

Zanotti F

1

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Raho G

2

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Vuolo R

3

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Papa F

5

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Papa S

6

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language of work or name

English

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publication date

1 September 2000

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23 May 2018

published in

FEBS Letters

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volume

482

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issue

1-2

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page(s)

163-166

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The ATP synthase--a splendid molecular machine

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Yeast mitochondrial F1F0-ATP synthase exists as a dimer: identification of three dimer-specific subunits

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Interaction between the mitochondrial ATP synthetase and ATPase inhibitor protein

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Inactivation of the mitochondrial ATPase inhibitor protein by chemical modification with diethylpyrocarbonate

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Binding of intrinsic ATPase inhibitor to mitochondrial ATPase--stoichiometry of binding of nucleotides, inhibitor, and enzyme

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The mitochondrial ATP synthase inhibitor protein binds near the C-terminus of the F1 beta-subunit

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Peptide analogs of the beef heart mitochondrial F1-ATPase inhibitor protein

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Identification of Functional Domains and Critical Residues in the Adenosinetriphosphatase Inhibitor Protein of Mitochondrial F0F1 ATP Synthase

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Cleavage of Bovine Mitochondrial ATPase Inhibitor with Endopeptidases, and Binding of the Resulting Peptides to the Interface between the α- and β-Subunits of F1 ATPase1

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Histidine-49 is necessary for the pH-dependent transition between active and inactive states of the bovine F1-ATPase inhibitor protein

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Studies of the energy-transfer system of submitochondrial particles. 2. Effects of oligomycin and aurovertin

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Functional regions of the H( )-ATPase inhibitory protein from ox heart mitochondria

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21 January 2018

Identifiers

DOI

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23 May 2018