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

An uncoupling channel within the c-subunit ring of the F1FO ATP synthase is the mitochondrial permeability transition pore.

Proceedings of the National Academy of Sciences of the United States of America - 22 Jul 2014

Alavian Kambiz N, Beutner Gisela, Lazrove Emma, Sacchetti Silvio, Park Han-A, Licznerski Pawel, Li Hongmei, Nabili Panah, Hockensmith Kathryn, Graham Morven, Porter George A, Jonas Elizabeth A

Abstract excerpt

Mitochondria maintain tight regulation of inner mitochondrial membrane (IMM) permeability to sustain ATP production. Stressful events cause cellular calcium (Ca(2+)) dysregulation followed by rapid loss of IMM potential known as permeability transition (PT), which produces osmotic shifts, metabolic dysfunction, and cell death. The molecular identity of the mitochondrial PT pore (mPTP) was previously unknown. We...

Read the complete abstract on PubMed

Topics

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

Share to Cell Death
Share to Ion Channel Gating

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Ion Channels

Share to Liposomes

Share to Mitochondrial Membrane Transport Proteins

Share to Mitochondrial Membranes

Share to Protein Subunits

Share to Proton-Translocating ATPases

Source

Open in PubMed Open full text

Identifiers

PMID: 24979777
DOI: 10.1073/pnas.1401591111
PMCID: PMC4115574

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

An uncoupling channel within the c-subunit ring of the F1FO ATP synthase is the mitochondrial permeability transition pore.PMID 24979777Read ↗

Permeability transition in human mitochondria persists in the absence of peripheral stalk subunits of ATP synthase.Semantic proximity Read ↗

TMEM70 forms oligomeric scaffolds within mitochondrial cristae promoting <i>in situ</i> assembly of mammalian ATP synthase proton channelSemantic proximity Read ↗

The INA complex facilitates assembly of the peripheral stalk of the mitochondrial F1Fo-ATP synthase.Semantic proximity Read ↗

Role of SERCA1 truncated isoform in the proapoptotic calcium transfer from ER to mitochondria during ER stress.Semantic proximity Read ↗

The Mitochondrial Permeability Transition Pore Activates the Mitochondrial Unfolded Protein Response and Promotes AgingSemantic proximity Read ↗

A naturally occurring mutation in ATP synthase subunit c is associated with increased damage following hypoxia/reoxygenation in STEMI patients.Semantic proximity Read ↗

TMEM70 facilitates biogenesis of mammalian ATP synthase by promoting subunit c incorporation into the rotor structure of the enzyme.Semantic proximity Read ↗

Mitochondrial membrane potential is dependent on the oligomeric state of F1F0-ATP synthase supracomplexes.Semantic proximity Read ↗

Properties of the permeability transition pore in mitochondria devoid of Cyclophilin D.Semantic proximity Read ↗

Respiratory complex I dysfunction due to mitochondrial DNA mutations shifts the voltage threshold for opening of the permeability transition pore toward resting levels.Semantic proximity Read ↗

Mitofilin Heterozygote Mice Display an Increase in Myocardial Injury and Inflammation after Ischemia/ReperfusionSemantic proximity Read ↗

Msp1 Is a Membrane Protein Dislocase for Tail-Anchored Proteins.Semantic proximity Read ↗

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