Mitochondrial Membrane Potential Is Dependent on the Oligomeric State of F1F0-ATP Synthase Supracomplexes
Author:
Publisher
Elsevier BV
Subject
Cell Biology,Molecular Biology,Biochemistry
Reference27 articles.
1. The ATP synthase is involved in generating mitochondrial cristae morphology
2. The GxxxG motif of the transmembrane domain of subunit e is involved in the dimerization/oligomerization of the yeast ATP synthase complex in the mitochondrial membrane
3. In the Absence of the First Membrane-spanning Segment of Subunit4(b), the Yeast ATP Synthase Is Functional but Does Not Dimerize or Oligomerize
4. Is there a relationship between the supramolecular organization of the mitochondrial ATP synthase and the formation of cristae?
5. Yeast mitochondrial F1F0-ATP synthase exists as a dimer: identification of three dimer-specific subunits
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