Functional and stoichiometric analysis of subunit e in bovine heart mitochondrial F(0)F(1)ATP synthase (Q46287569)

21 December 2017

title

Functional and stoichiometric analysis of subunit e in bovine heart mitochondrial F(0)F(1)ATP synthase (English)

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21 December 2017

author

Valentina Giorgio

3

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21 December 2017

Paola Picotti

2

object named as

Paola Picotti

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21 December 2017

6

Giovanna Lippe

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21 December 2017

author name string

Elena Bisetto

1

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21 December 2017

Vera Alverdi

4

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21 December 2017

Irene Mavelli

5

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publication date

1 August 2008

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Journal of Bioenergetics and Biomembranes

published in

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21 December 2017

volume

40

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issue

4

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page(s)

257-267

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https://scigraph.springernature.com/pub.10.1007/s10863-008-9183-5

exact match

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cites work

The proximal N-terminal amino acid residues are required for the coupling activity of the bovine heart mitochondrial factor B

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The adenosine triphosphatase-inhibitor content of bovine heart submitochondrial particles. Influence of the inhibitor on adenosine triphosphate-dependent reactions

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Characterization of domain interfaces in monomeric and dimeric ATP synthase

21 January 2018

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Absolute quantification of the G protein-coupled receptor rhodopsin by LC/MS/MS using proteolysis product peptides and synthetic peptide standards

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Dimer ribbons of ATP synthase shape the inner mitochondrial membrane

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Supramolecular organization of the yeast F1Fo-ATP synthase

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On the structure of the stator of the mitochondrial ATP synthase

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Identification of the subunits of F1F0-ATPase from bovine heart mitochondria

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ATP synthase: motoring to the finish line

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The inhibitor protein (IF1) promotes dimerization of the mitochondrial F1F0-ATP synthase.

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Membrane topography and near-neighbor relationships of the mitochondrial ATP synthase subunits e, f, and g

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Transbilayer movement and distribution of spin-labelled phospholipids in the inner mitochondrial membrane

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

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12 December 2020

Formation of the yeast F1F0-ATP synthase dimeric complex does not require the ATPase inhibitor protein, Inh1.

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12 December 2020

Stoichiometry of subunit e in rat liver mitochondrial H(+)-ATP synthase and membrane topology of its putative Ca(2+)-dependent regulatory region

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Structure of the mitochondrial ATP synthase by electron cryomicroscopy

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Ground state structure of F1-ATPase from bovine heart mitochondria at 1.9 A resolution

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Regulation of mitochondrial structure and function by the F1Fo-ATPase inhibitor protein, IF1.

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Quantification of muscle mitochondrial oxidative phosphorylation enzymes via histochemical staining of blue native polyacrylamide gels.

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In vitro and in vivo studies of F(0)F(1)ATP synthase regulation by inhibitor protein IF(1) in goat heart.

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Characterization of dimeric ATP synthase and cristae membrane ultrastructure from Saccharomyces and Polytomella mitochondria

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Functional analysis of subunit e of the F1Fo-ATP synthase of the yeast Saccharomyces cerevisiae: importance of the N-terminal membrane anchor region

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The modification of the conserved GXXXG motif of the membrane-spanning segment of subunit g destabilizes the supramolecular species of yeast ATP synthase

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12 December 2020

Fo membrane domain of ATP synthase from bovine heart mitochondria: purification, subunit composition, and reconstitution with F1-ATPase.

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12 December 2020

The GxxxG motif of the transmembrane domain of subunit e is involved in the dimerization/oligomerization of the yeast ATP synthase complex in the mitochondrial membrane

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12 December 2020

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

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12 December 2020

Target-decoy search strategy for increased confidence in large-scale protein identifications by mass spectrometry

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12 December 2020

Identification of 491 proteins in the tear fluid proteome reveals a large number of proteases and protease inhibitors

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Identification of two proteins associated with mammalian ATP synthase

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12 December 2020

The modulation in subunits e and g amounts of yeast ATP synthase modifies mitochondrial cristae morphology

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12 December 2020

Absolute quantification of proteins and phosphoproteins from cell lysates by tandem MS

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12 December 2020

Differential steady-state tyrosine phosphorylation of two oligomeric forms of mitochondrial F0F1ATPsynthase: a structural proteomic analysis

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Mitochondrial ATP synthase. Crystal structure of the catalytic F1 unit in a vanadate-induced transition-like state and implications for mechanism

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Structural organization of mitochondrial ATP synthase

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The peripheral stalk participates in the yeast ATP synthase dimerization independently of e and g subunits.

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Yeast mitochondrial F1F0-ATPase: the novel subunit e is identical to Tim11.

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The ATP synthase is involved in generating mitochondrial cristae morphology

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Subunit E of mitochondrial ATP synthase: a bioinformatic analysis reveals a phosphopeptide binding motif supporting a multifunctional regulatory role and identifies a related human brain protein with the same motif

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Relative and absolute quantification of postsynaptic density proteome isolated from rat forebrain and cerebellum.

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Structure of dimeric mitochondrial ATP synthase: novel F0 bridging features and the structural basis of mitochondrial cristae biogenesis.

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Coupling of rotation and catalysis in F(1)-ATPase revealed by single-molecule imaging and manipulation.

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12 December 2020

Advantages and limitations of clear-native PAGE.

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12 December 2020

Mammalian ATPsynthase monomer versus dimer profiled by blue native PAGE and activity stain

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12 December 2020

10.1007/S10863-008-9183-5

Identifiers

DOI

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21 December 2017

PubMed ID

18958608

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21 December 2017