Proteolipid domains form in biomimetic and cardiac mitochondrial vesicles and are regulated by cardiolipin concentration but not monolyso-cardiolipin.
Pennington, Edward Ross; Sullivan, E Madison; Fix, Amy; Dadoo, Sahil; Zeczycki, Tonya N; DeSantis, Anita; Schlattner, Uwe; Coleman, Rosalind A; Chicco, Adam J; Brown, David A; Shaikh, Saame Raza.
J Biol Chem
; 293(41): 15933-15946, 2018 10 12.
Artigo em Inglês | MEDLINE | ID: mdl-30158245
Electrostatic Constituents of the Interaction of Cardiolipin with Site A of Cytochrome c.
The Role of Water Distribution Controlled by Transmembrane Potentials in the Cytochromeâ c-Cardiolipin Interaction: Revealing from Surface-Enhanced Infrared Absorption Spectroscopy.
Structural characterization of cardiolipin-driven activation of cytochrome c into a peroxidase and membrane perturbation.
Analyzing Structural Properties of Heterogeneous Cardiolipin-Bound Cytochrome C and Their Regulation by Surface-Enhanced Infrared Absorption Spectroscopy.
Known unknowns of cardiolipin signaling: The best is yet to come.
Characterization of the Cytochromeâ c Membrane-Binding Site Using Cardiolipin-Containing Bicelles with NMR.
The key role played by charge in the interaction of cytochrome c with cardiolipin.
Immobilized cytochrome c bound to cardiolipin exhibits peculiar oxidation state-dependent axial heme ligation and catalytically reduces dioxygen.
Cytochrome c-Cardiolipin Complex in a Nonpolar Environment.
Cytochrome-c-assisted escape of cardiolipin from a model mitochondrial membrane.