Channel Formation by Yeast F-ATP Synthase and the Role of Dimerization in the Mitochondrial Permeability Transition (Articolo in rivista)

Type

• Articolo in rivista (Classe)
• Prodotto della ricerca (Classe)

Label

• Channel Formation by Yeast F-ATP Synthase and the Role of Dimerization in the Mitochondrial Permeability Transition (Articolo in rivista) (literal)

Anno

• 2014-01-01T00:00:00+01:00 (literal)

Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#doi

• 10.1074/jbc.C114.559633 (literal)

Alternative label

• Carraro, Michela; Giorgio, Valentina; Sileikyte, Justina; Sartori, Geppo; Forte, Michael; Lippe, Giovanna; Zoratti, Mario; Szabo, Ildiko; Bernardi, Paolo (2014)
  Channel Formation by Yeast F-ATP Synthase and the Role of Dimerization in the Mitochondrial Permeability Transition
  in The Journal of biological chemistry (Print)
  (literal)

Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#autori

• Carraro, Michela; Giorgio, Valentina; Sileikyte, Justina; Sartori, Geppo; Forte, Michael; Lippe, Giovanna; Zoratti, Mario; Szabo, Ildiko; Bernardi, Paolo (literal)

Pagina inizio

• 15980 (literal)

Pagina fine

• 15985 (literal)

Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#numeroVolume

• 289 (literal)

Rivista

• ?The ?Journal of biological chemistry (Rivista)

Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#pagineTotali

• 6 (literal)

Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#numeroFascicolo

• 23 (literal)

Note

• PubMe (literal)
• ISI Web of Science (WOS) (literal)

Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#affiliazioni

• Consiglio Nazionale delle Ricerche (CNR); University of Padua; University of Padua; Oregon Health & Science University; University of Udine (literal)

Titolo

• Channel Formation by Yeast F-ATP Synthase and the Role of Dimerization in the Mitochondrial Permeability Transition (literal)

Abstract

• Purified F-ATP synthase dimers of yeast mitochondria display Ca2+ -dependent channel activity with properties resembling those of the permeability transition pore (PTP) of mammals. After treatment with the Ca2+ ionophore ETH129, which allows electrophoretic Ca2+ uptake, isolated yeast mitochondria undergo inner membrane permeabilization due to PTP opening. Yeast mutant strains Delta TIM11 and Delta ATP20 (lacking the e and g F-ATP synthase subunits, respectively, which are necessary for dimer formation) display a striking resistance to PTP opening. These results show that the yeast PTP originates from F-ATP synthase and indicate that dimerization is required for pore formation in situ. (literal)

Prodotto di

• Istituto di neuroscienze (IN) (Istituto)

Autore CNR

• MARIO ZORATTI (Persona)

Insieme di parole chiave

• Keywords of "Channel Formation by Yeast F-ATP Synthase and the Role of Dimerization in the Mitochondrial Permeability Transition" (Insieme di parole chiave)

Incoming links:

Autore CNR di

• MARIO ZORATTI (Persona)

Prodotto

• Istituto di neuroscienze (IN) (Istituto)

Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#rivistaDi

• ?The ?Journal of biological chemistry (Rivista)

Insieme di parole chiave di

• Keywords of "Channel Formation by Yeast F-ATP Synthase and the Role of Dimerization in the Mitochondrial Permeability Transition" (Insieme di parole chiave)