Discover Community Create You

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

How the N-terminal extremity of Saccharomyces cerevisiae IF1 interacts with ATP synthase: a kinetic approach.

Biochimica et biophysica acta - 1 Feb 2011

Andrianaivomananjaona Tiona, Moune-Dimala Martin, Herga Sameh, David Violaine, Haraux Francis

Abstract excerpt

The N-terminal part of the inhibitory peptide IF1 interacts with the central γ subunit of mitochondrial isolated extrinsic part of ATP synthase in the inhibited complex (J.R. Gledhill, M.G. Montgomery, G.W. Leslie, J.E. Walker, 2007). To explore its role in the different steps of IF1 binding, kinetics of inhibition of the isolated and membrane-bound enzymes were investigated using Saccharomyces cerevisiae IF1...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to Amino Acid Sequence
Share to Models, Molecular

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Molecular Sequence Data

Share to Peptides

Share to Protein Structure, Tertiary

Share to Proteins

Share to Saccharomyces cerevisiae

Share to Saccharomyces cerevisiae Proteins

Source

Identifiers

PMID: 20951672
DOI: 10.1016/j.bbabio.2010.10.002

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 5 Sept 2026. Manifest publication-graph-cohort-2026-09-05.1.

Source receipt: pubmed, retrieved 5 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

How the N-terminal extremity of Saccharomyces cerevisiae IF1 interacts with ATP synthase: a kinetic approach.PMID 20951672Read ↗

Interactions involved in grasping and locking of the inhibitory peptide IF1 by mitochondrial ATP synthase.Semantic proximity Read ↗

Insights into the regulatory function of the ɛ subunit from bacterial F-type ATP synthases: a comparison of structural, biochemical and biophysical data.Semantic proximity Read ↗

Alteration of apparent negative cooperativity of ATPase activity by alpha-subunit glutamine 173 mutation in yeast mitochondrial F1. Correlation with impaired nucleotide interaction at a regulatory site.Semantic proximity Read ↗

Identification of functional domains and critical residues in the adenosinetriphosphatase inhibitor protein of mitochondrial F0F1 ATP synthase.Semantic proximity Read ↗

Functional analysis of membranous Fo-a subunit of F1Fo-ATP synthase by in vitro protein synthesis.Semantic proximity Read ↗

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

Structure-function relationships based on ATP binding and cation occlusion at equilibrium in Na,K-ATPase.Semantic proximity Read ↗

Defining the pathogenesis of the human Atp12p W94R mutation using a Saccharomyces cerevisiae yeast model.Semantic proximity Read ↗

Comparison between single-molecule and X-ray crystallography data on yeast F1-ATPase.Semantic proximity Read ↗

Assembly of imported subunit 8 into the ATP synthase complex of isolated yeast mitochondria.Semantic proximity Read ↗

Movement of the helical domain of the epsilon subunit is required for the activation of thermophilic F1-ATPase.Semantic proximity Read ↗

Mechanism of inhibition by C-terminal alpha-helices of the epsilon subunit of Escherichia coli FoF1-ATP synthase.Semantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.