OSCP subunit of mitochondrial ATP synthase: role in regulation of enzyme function and of its transition to a pore.


Journal

British journal of pharmacology
ISSN: 1476-5381
Titre abrégé: Br J Pharmacol
Pays: England
ID NLM: 7502536

Informations de publication

Date de publication:
11 2019
Historique:
received: 03 05 2018
revised: 20 06 2018
accepted: 04 09 2018
pubmed: 7 10 2018
medline: 25 9 2020
entrez: 7 10 2018
Statut: ppublish

Résumé

The permeability transition pore (PTP) is a latent, high-conductance channel of the inner mitochondrial membrane. When activated, it plays a key role in cell death and therefore in several diseases. The investigation of the PTP took an unexpected turn after the discovery that cyclophilin D (the target of the PTP inhibitory effect of cyclosporin A) binds to F

Identifiants

pubmed: 30291799
doi: 10.1111/bph.14513
pmc: PMC6887684
doi:

Substances chimiques

Mitochondrial Membrane Transport Proteins 0
Mitochondrial Permeability Transition Pore 0
Protein Subunits 0
Mitochondrial Proton-Translocating ATPases EC 3.6.3.-
oligomycin sensitivity-conferring protein EC 7.1.2.2

Types de publication

Journal Article Research Support, Non-U.S. Gov't Review

Langues

eng

Sous-ensembles de citation

IM

Pagination

4247-4257

Informations de copyright

© 2018 The British Pharmacological Society.

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Auteurs

Valentina Giorgio (V)

Consiglio Nazionale delle Ricerche Institute of Neuroscience and Department of Biomedical Sciences, University of Padova, Padova, Italy.

Federico Fogolari (F)

Department of Mathematics, Computer Sciences and Physics, University of Udine, Udine, Italy.

Giovanna Lippe (G)

Department of Agricultural, Food, Environmental and Animal Sciences, University of Udine, Udine, Italy.

Paolo Bernardi (P)

Consiglio Nazionale delle Ricerche Institute of Neuroscience and Department of Biomedical Sciences, University of Padova, Padova, Italy.

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Classifications MeSH