Electrophysiology clarifies the megariddles of the mitochondrial permeability transition pore. (Articolo in rivista)

Type
Label
  • Electrophysiology clarifies the megariddles of the mitochondrial permeability transition pore. (Articolo in rivista) (literal)
Anno
  • 2010-01-01T00:00:00+01:00 (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#doi
  • 10.1016/j.febslet.2010.01.012 (literal)
Alternative label
  • Zoratti M; U. De Marchi; L. Biasutto; I. Szabò. (2010)
    Electrophysiology clarifies the megariddles of the mitochondrial permeability transition pore.
    in FEBS letters (Print)
    (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#autori
  • Zoratti M; U. De Marchi; L. Biasutto; I. Szabò. (literal)
Pagina inizio
  • 1997 (literal)
Pagina fine
  • 2004 (literal)
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  • http://www.sciencedirect.com/science/article/pii/S0014579310000311 (literal)
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  • 584 (literal)
Rivista
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  • 8 (literal)
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  • 10 (literal)
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  • Scopu (literal)
  • ISI Web of Science (WOS) (literal)
  • PubMe (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#affiliazioni
  • Zoratti M: IN- Padova Zoratti M; Biasutto L: Dip. di Scienze Biomediche Sperimentali, Università di Padova De Marchi U: Dept. of Cellular Physiology and Metabolism, University of Geneva, Switzerland Szabò I: Dip. di Biologia, Università di Padova (literal)
Titolo
  • Electrophysiology clarifies the megariddles of the mitochondrial permeability transition pore. (literal)
Abstract
  • After a brief review of the early history of mitochondrial electrophysiology, the contribution of this approach to the study of the mitochondrial permeability transition (MPT) is recapitulated. It has for example provided evidence for a dimeric nature of the MPT pore, allowed the distinction between two levels of control of its activity, and underscored the relevance of redox events for the phenomenon. Single-channel recording provides a means to finally solve the riddle of the biochemical entity underlying it by comparing the characteristics of the pore with those of channels formed by candidate molecules or complexes. The possibility that this entity may be the protein import machinery of the inner mitochondrial membrane is emphasized. (literal)
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