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

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

Biochimica et biophysica acta - 1 Jun 2014

Wu Qian, Andrianaivomananjaona Tiona, Tetaud Emmanuel, Corvest Vincent, Haraux Francis

Abstract excerpt

When mitochondria become deenergized, futile ATP hydrolysis is prevented by reversible binding of an endogenous inhibitory peptide called IF1 to ATP synthase. Between initial IF1 binding and IF1 locking the enzyme experiences large conformational changes. While structural studies give access to analysis of the dead-end inhibited state, transient states have thus far not been described. Here, we studied both...

Read the complete abstract on PubMed

Topics

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

Share to Kinetics
Share to Mitochondrial Proton-Translocating ATPases

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Mutation

Share to Peptides

Share to Saccharomyces cerevisiae

Source

Identifiers

PMID: 24513195
DOI: 10.1016/j.bbabio.2014.01.023

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Interactions involved in grasping and locking of the inhibitory peptide IF1 by mitochondrial ATP synthase.PMID 24513195Read ↗

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

Crystal structures of mutant forms of the yeast F1 ATPase reveal two modes of uncoupling.Semantic proximity Read ↗

A structure-based model for the synthesis and hydrolysis of ATP by F1-ATPase.Semantic proximity Read ↗

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

Torque generation and utilization in motor enzyme F0F1-ATP synthase: half-torque F1 with short-sized pushrod helix and reduced ATP Synthesis by half-torque F0F1.Semantic proximity Read ↗

Rotary catalysis of bovine mitochondrial F1-ATPase studied by single-molecule experiments.Semantic proximity Read ↗

Catalysis and rotation of F1 motor: cleavage of ATP at the catalytic site occurs in 1 ms before 40 degree substep rotation.Semantic proximity Read ↗

None of the rotor residues of F1-ATPase are essential for torque generation.Semantic proximity Read ↗

Structural Elements Involved in ATP Hydrolysis Inhibition and ATP Synthesis of Tuberculosis and Nontuberculous Mycobacterial F-ATP Synthase Decipher New Targets for InhibitorsSemantic proximity Read ↗

Mutations on the N-terminal edge of the DELSEED loop in either the α or β subunit of the mitochondrial F1-ATPase enhance ATP hydrolysis in the absence of the central γ rotor.Semantic proximity Read ↗

Role of α/β interface in F1 ATPase rotational catalysis probed by inhibitors and mutations.Semantic proximity Read ↗

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