Dimer ribbons of ATP synthase shape the inner mitochondrial membrane
By M. Strauss, G. Hofhaus, Rasmus R. Schröder, W. Kühlbrandt. EMBO Journal, 2008
656 citations recorded by the source corpus.
Subfields: Molecular Biology
View Paper: https://www.semanticscholar.org/paper/c7bee5f770e9af36bc1e45e6e3e8d350756ae642
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In Molecular Biology
- L. Scorrano
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- C. Frezza
- J. Nunnari
Citations in the corpus
- Mitochondrial Cristae: Where Beauty Meets Functionality. (2016, background): “Studies with in vitro vesicles demonstrated that the dimer ribbons of ATP synthase enforce the highly positive local curvature observed at the apex of the cristae [19].”
- Mitochondrial Cristae Shape Determines Respiratory Chain Supercomplexes Assembly and Respiratory Efficiency (2013, background): “Interestingly, cristae shape and ATPase dimers are linked: in yeast mutants where the ATPase cannot dimerize, cristae are disorganized (Paumard et al., 2002; Minauro-Sanmiguel et al., 2005; Strauss et al., 2008), whereas in mammalian cells, increased cristae density favors ATPase dimerization during”
- Mitochondrial ATP synthase: architecture, function and pathology (2011, background): “Next to structure and function of the monocomplex, also the role of di- and oligomerization of complex V, shaping the inner mitochondrial membrane, has been addressed in many studies both in yeast and in mammalian mitochondria (Paumard et al. 2002; Strauss et al. 2008).”
- Mitochondria: In Sickness and in Health (2012, background): “tionally and functionally distinct regions (Reichert and Neupert, 2002): the inner boundary region is in close apposition to the OM and facilitates lipid trafficking, mitochondrial protein import, and respiratory complex assembly, the cristae are invaginations that penetrate into the matrix and hous”