(Q45216879)

10 December 2017

title

The binding mechanism of the yeast F1-ATPase inhibitory peptide: role of catalytic intermediates and enzyme turnover (English)

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10 December 2017

Vincent Corvest

1

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10 December 2017

Claude Sigalat

2

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10 December 2017

Renée Venard

3

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10 December 2017

Pierre Falson

4

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10 December 2017

David M Mueller

5

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10 December 2017

Francis Haraux

6

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10 December 2017

language of work or name

English

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publication date

6 January 2005

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Journal of Biological Chemistry

10 December 2017

number of pages

10

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based on heuristic

inferred from page(s)

published in

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10 December 2017

volume

280

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10 December 2017

issue

11

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10 December 2017

page(s)

9927-9936

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The ATP synthase--a splendid molecular machine

10 December 2017

cites work

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ATP synthase: an electrochemical transducer with rotatory mechanics

21 January 2018

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Catalytic and noncatalytic nucleotide binding sites of the Escherichia coli F1 ATPase. Amino acid sequences of beta-subunit tryptic peptides labeled with 2-azido-ATP.

21 January 2018

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

21 January 2018

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Direct observation of the rotation of F1-ATPase

21 January 2018

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Mechanically driven ATP synthesis by F1-ATPase

21 January 2018

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Resolution of distinct rotational substeps by submillisecond kinetic analysis of F1-ATPase

21 January 2018

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

21 January 2018

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Bi-site activation occurs with the native and nucleotide-depleted mitochondrial F1-ATPase

21 January 2018

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Catalytic site occupancy during ATP synthase catalysis

21 January 2018

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Regulation of the mitochondrial ATP synthase/ATPase complex

21 January 2018

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Effect of the protonmotive force on ATP-linked processes and mobilization of the bound natural ATPase inhibitor in beef heart submitochondrial particles

21 January 2018

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Cross-linking of the endogenous inhibitor protein (IF1) with rotor (gamma, epsilon) and stator (alpha) subunits of the mitochondrial ATP synthase.

21 January 2018

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

21 January 2018

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Natural protein ATPase inhibitor from Candida utilis mitochondria binding properties of the radiolabeled inhibitor

21 January 2018

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Studies on the transformation of intact yeast cells by the LiAc/SS-DNA/PEG procedure

21 January 2018

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Catalytic properties of Escherichia coli F1-ATPase depleted of endogenous nucleotides.

21 January 2018

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Investigation of the role and mechanism of IF1 and STF1 proteins, twin inhibitory peptides which interact with the yeast mitochondrial ATP synthase

21 January 2018

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Catalytic mechanism of F1-ATPase

21 January 2018

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Functional transitions of F0F1-ATPase mediated by the inhibitory peptide IF1 in yeast coupled submitochondrial particles

21 January 2018

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A thermodynamic analysis of the interaction between the mitochondrial coupling adenosine triphosphatase and its naturally occurring inhibitor protein

21 January 2018

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The IF(1) inhibitor protein of the mitochondrial F(1)F(0)-ATPase

21 January 2018

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Binding of the transition state analog MgADP-fluoroaluminate to F1-ATPase

21 January 2018

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Catalytic site nucleotide binding and hydrolysis in F1F0-ATP synthase

21 January 2018

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Specific tryptophan substitution in catalytic sites of Escherichia coli F1-ATPase allows differentiation between bound substrate ATP and product ADP in steady-state catalysis

21 January 2018

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Bi-site catalysis in F1-ATPase: does it exist?

21 January 2018

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

21 January 2018

1 reference

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Radiolabeling of natural adenosine triphosphatase inhibitor with phenyl (14C)isothiocyanate and study of its interaction with mitochondrial adenosine triphosphatase. Localization of inhibitor binding sites and stoichiometry of binding

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M414098200

21 January 2018

Identifiers

DOI

10.1074/JBC.M414098200

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10 December 2017

1 reference