Inhibitory and anchoring domains in the ATPase inhibitor protein IF1 of bovine heart mitochondrial ATP synthase (Q80980949)

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4 January 2020

title

Inhibitory and anchoring domains in the ATPase inhibitor protein IF1 of bovine heart mitochondrial ATP synthase (English)

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4 January 2020

3

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4 January 2020

Sergio Papa

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4

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4 January 2020

author name string

Franco Zanotti

series ordinal

1

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4 January 2020

Gabriella Raho

series ordinal

2

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publication date

1 October 2004

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Journal of Bioenergetics and Biomembranes

4 January 2020

published in

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volume

36

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issue

5

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4 January 2020

page(s)

447-457

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The structure of bovine F1-ATPase in complex with its regulatory protein IF1

4 January 2020

cites work

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Modulation of the oligomerization state of the bovine F1-ATPase inhibitor protein, IF1, by pH

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Structure at 2.8 A resolution of F1-ATPase from bovine heart mitochondria

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

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

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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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Dimerization of F0F1ATP synthase from bovine heart is independent from the binding of the inhibitor protein IF1.

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The ATPase inhibitor protein from bovine heart mitochondria: the minimal inhibitory sequence

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Enhancement by N-hydroxysulfosuccinimide of water-soluble carbodiimide-mediated coupling reactions

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Sequence from picomole quantities of proteins electroblotted onto polyvinylidene difluoride membranes

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Binding of an intrinsic ATPase inhibitor to the interface between alpha- and beta-subunits of F1FoATPase upon de-energization of mitochondria

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

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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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ATP depletion and mitochondrial functional loss during ischemia in slow and fast heart-rate hearts

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

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Regulation of the mitochondrial ATP synthase/ATPase complex: cDNA cloning, sequence, overexpression, and secondary structural characterization of a functional protein inhibitor

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Genetic fusions of subunit c in the F0 sector of H -transporting ATP synthase. Functional dimers and trimers and determination of stoichiometry by cross-linking analysis

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The structural and functional connection between the catalytic and proton translocating sectors of the mitochondrial F1F0-ATP synthase.

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F1 and F0 connections in the bovine mitochondrial ATP synthase: the role of the of alpha subunit N-terminus, oligomycin-sensitivity conferring protein (OCSP) and subunit d

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The 2.8-A structure of rat liver F1-ATPase: configuration of a critical intermediate in ATP synthesis/hydrolysis

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Purification of membrane attachment and inhibitory subunits of the proton translocating adenosine triphosphatase from Escherichia coli

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Novel features in the structure of bovine ATP synthase

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A simple, non-chromatographic procedure to purify immunoglobulins from serum and ascites fluid

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ATP synthase complex. Proximities of subunits in bovine submitochondrial particles

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Activity and NMR structure of synthetic peptides of the bovine ATPase inhibitor protein, IF1

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Proton translocation by the H -ATPase of mitochondria. Effect of modification by monofunctional reagents of thiol residues in F0 polypeptides

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Preparation and characterization of homogeneous coupling factor 6 from bovine heart mitochondria

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A NATURALLY OCCURRING INHIBITOR OF MITOCHONDRIAL ADENOSINE TRIPHOSPHATASE

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Identification of nucleus-encoded F0I protein of bovine heart mitochondrial H -ATPase as a functional part of the F0 moiety

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12 December 2020